sequence stringlengths 13 8.92k | annotation listlengths 2 214 | description stringlengths 61 12.1k | labels int64 0 0 |
|---|---|---|---|
MEEQQWSSFPELPQFLIENLQNNDYNAPFPVQVAVLEKFFASDVDLAIGFPTGSGKTLAYLIPIISCLYKRIVQRLRAIIVVPNRELAIQVYNVVCALIQNSKLTCAILSSNYWCGESSSYTNVPDIYICSSLSLSSYLLDVDDKLLSDIEYIVLDEGDVILEQPLENWLDHVQRSLNSDPIPEKFTIPLVTAPPKDRRIRKILCSATLSRNSKQSEDFKMQFPEILISSDKSRYVIPNHLKEEFIIAERQNKPAILQSLTTRFQFILCFVSTTKRAVALANIMRTLLAKTDFQVIEFAASLKSDKKNQAFESVDQNSSRLIICTDSLARGINLPYIDAVINFDAPASARTYIHRIGRTARGGNSGTCVTFLLDSELILFRDIISKIDGANPQKTEPKMVGLTGKFYRETVKGFDSLKPRKLPQKKMAKYQEMEEEEMNEIEEEEKNENGEEERNEGESNNDTEGDYNQNEEE | [
5174,
24974,
27925,
28298,
29033,
30332,
37314,
45692,
47717,
58239,
87110,
87539,
87601,
87855,
88001,
88008
] | The following text describes a protein:
Function:
RNA helicase.
Domain:
The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis. | 0 |
MTAFGVEPYGQPKYLEIAGKRMAYIDEGKGDAIVFQHGNPTSSYLWRNIMPHLEGLGRLVACDLIGMGASDKLSPSGPDRYSYGEQRDFLFALWDALDLGDHVVLVLHDWGSALGFDWANQHRDRVQGIAFMEAIVTPMTWADWPPAVRGVFQGFRSPQGEPMALEHNIFVERVLPGAILRQLSDEEMNHYRRPFVNGGEDRRPTLSWPRNLPIDGEPAEVVALVNEYRSWLEETDMPKLFINAEPGAIITGRIRDYVRSWPNQTEITVPGVHFVQEDSPEEIGAAIAQFVRRLRSAAGV | [
5225,
14110,
25079,
25163,
30332,
30652,
36010,
36465,
55360,
59224,
87103,
87115,
87601,
88008
] | The following text describes a protein:
Function:
Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. | 0 |
MINTNDMFYAKSSDAEIAEAGEYGGAVTTLLKFLLKEGIVDAVLAVDSSADLYDVVPILIEDPEDVVKAAGSLHFGTLNLAKVVTRYLDGAQDMKIAVTVKPCDAMTMVELMKREKVNADNVIMVGLNCGGTMPPVKGRQMMEEFYEVDPDSVVKEEIAKGKLIVETEDGTEKEIPIDELEDEGFGRRTNCRRCEVNIPRMADLACGNWGVIGPLAGKATFIEVCSPKGAEVLEKAKEAGVIDLEDPIPKGIEIREKIDGAMVKLADKWQGNDWEDKAGREIFSVLTEYMDDFSRCLKCYGCREACPICYCEDCCLEANNGPDWLSKGEIPPSPMFHLERMLHMVESCTNCGQCEEVCPGEIPLAKIWHEVNAKMKDTFGYVKGTGDEKPPIAYFPVGK | [
1337,
29486,
32236,
32536,
33780,
33855,
42339,
42346,
43620,
50754,
50758,
71435,
87004,
87039,
87042,
87105,
87411,
87425,
87455,
87470,
87678,
87681,
87767,
87873,
88009,
88162,
88261
] | The following text describes a protein:
Function:
Catalyzes the oxidation of formate to carbon dioxide, with coenzyme F420 as the electron acceptor. In vitro can also use methyl viologen, 7,8-didemethyl-8-hydroxy-5-deazariboflavin (or FO, a hydrolytic derivative of coenzyme F420), FMN and FAD as electron acceptors, but not NAD(+) or NADP(+). | 0 |
MSRNRAAMVSAFRLFLRPATTTTHRSLALRLAPGTTFALHLRPCHELQQHRSFASTAEDGETDKHKKPTTGEDIYVEYVNGMPHMTVRLPSRNELCQFALKPISHNVGDLLAMLRAEDRGIDRAAVINKHGVRIASSCTIESLLDDSFSIQINNRTLDVNPPKRDKVTLESMDKVGDVRKVIAQLYEAFNVGEYQLEKSNQLAKELETLRYELEPLEEKKLELSKKAARRTNFMTWMGLGLMSVQFGILARLTWWEYSWDIMEPVTYFVTYGTTMAMYAYYCVTKREYMMEDVKNREFSLSLYRNAKKVQFDVEHYNELKRKSAELEYNLRRINDPLNMQLPSHLVRTQENTPPTLTEEKAERKYT | [
8466,
8552,
8977,
13785,
16900,
19354,
24979,
27469,
28922,
29919,
41694,
66481,
87139,
87244,
87245,
87247,
87326,
87674,
87676,
87760,
87785,
87786,
88008,
88154,
88159,
88161,
88162
] | The following text describes a protein:
Function:
Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. Together with Itpr, has a role in oxidative stress-induced ER-mitochondria calcium transfer. During pupation, required for memory function in mushroom body neurons.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
Domain:
The selectivity filter, in which calcium ions are arranged in single file, is composed of two acidic rings separated by one helical turn along the central axis of the channel pore. | 0 |
MLRLIKQPLFRCASSGHLMKESLVFIHQTRTFQVGKFTSNEKYNEKIEDINERSNPQWDNAGLENLLNQLQDSVEQSASDDFMGELEKKIEVENEEPPLMGTNLWPSPSSSIVGLIDRPFQVDSTVQHLVNLIMRDGKKAKAEKIVATALSIIQKETGENPIDVLKQAIAEISPLMKLVSAKRFNKSVEFPMPLKERQRRRIALQWILGECKSSSPKRLSDRIVKEIIAIRSKTSNCFKKKDHLHRMCLVNRGNAPVRI | [
6649,
8138,
12385,
24979,
24992,
25047,
27930,
27932,
30795,
36135,
52850,
55541,
64556,
73890,
87785,
87914,
88008,
88020,
88022,
88154
] | The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion. | 0 |
MSYFLASCLGVGLLSTVSCSLQGLTSHYRENIPRFKHVANERYEVFLGDEIKFDCQTAASKISAFVEWYRNDKLLKNDQIDKDKIRKDNNRMMLHLKNIDVSDQGLWSCRVHNAYGQISRNFTVEVIDFCDYFLFPDIHHLNIPMECVCLWKYNKEAKRSDVNYAAVTGEVCSKYASRMINRARKPLPMIPCFGDHCKEFDTTPVSDFGLPGKPEDDPLVKRVVLKKDDVIVPVHDSEESPSESRTEFINADEKENKEDEEEDYSVSQPVAPDAGLTELNITAEEPPYFKSNDNIVLFNETHALPAGRTLKLNCRAKGYPEPQIIWYKNGKMLKKSSARSGGYEFKFNRWSLEVEDAVVADSGEFHCEALNKVGSAKKYFHVIIVNRMRRPPIIVPNILANQSVNINDTATFHCKVVSDLLPHIIWVRINKINGSYSYYNNSAEEYMFNYTEMDTFDKAHVHHVGDESTLTIFNVSLDDQGIYACLSGNSLGMSMANATLTVNEFMAIHLLTGDEPKIDRWTTSDYIFTTILLFLLLAATLFGILFMVCKQTLHKKGFMDDTVGLVARKKRVVVSKRPMNEDNENSDDEPSPYQIQIIETPITKKEAARKQRKRMNSENTVLSEYEVDSDPVWEVERSKLSLVHMLGEGAFGEVWKATYKETENNEIAVAVKKLKMSAHEKELIDLVSEMETFKVIGEHENVLRLIGCCTGAGPLYVVVELCKHGNLRDFLRAHRPKEEKAKKSSQELTDYLEPRKASDKDDIELIPNLTQRHLVQFAWQVAQGMNFLASKKIIHRDLAARNVLVGDGHVLKISDFGLSRDVHCNDYYRKRGNGRLPIKWMALEALDSNVYTVESDVWSYGVLLWEIMTLGGTPYPTIAMPELYANLKEGYRMEPPHLCPQEVYHLMCSCWREKLEERPSFKTIVDYLDWMLTMTNETIEGSQEFNDQFFSERSTASGPVSPMESFQKKRKHRPLSAPVNLPSEPQHTICDDYESNFSVEPPNDPNHLYCNDNMLKNHIITPETSQRIPSNNNSMSKPEF | [
3601,
7198,
8918,
9051,
9091,
10729,
10902,
12013,
12115,
14622,
15811,
16172,
25079,
26232,
28522,
28550,
29033,
32536,
36535,
36977,
38877,
38878,
41979,
42970,
45290,
46939,
47529,
50333,
52872,
63951,
75777,
87016,
87110,
87139,
87402,
87413,... | The following text describes a protein:
Function:
Receptor tyrosine kinase required for larval development. May phosphorylate adapter protein soc-1 which in turn may result in the recruitment and/or activation of phosphatase ptp-2. May activate the Ras/MAPK kinase signaling pathway which includes sem-5, sos-1, let-60/Ras, lin-45/Raf, mek-2 and mpk-1. Acts in the hypodermis to regulate axon growth and fluid homeostasis. Activates protein degradation in muscles. Probably following interaction with ligand let-756, negatively regulates membrane protrusion from body wall muscles during larval development. Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine. Regulates synaptic levels of nAChR subunit lev-1 in the nerve cord; [Isoform b]: Affects the maintenance of axon position without affecting axon growth. Interaction with egl-17 is required for the guidance of sex myoblast migration during gonad development; [Isoform a]: Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures; [Isoform c]: Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures; [Isoform d]: Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures; [Isoform e]: Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. | 0 |
MAALNLSDQRQSPDDVLASGEYPLTRRDLSEIAAMIYADAGIYLNDTKASLVYSRLSKHIRNLGLSGFREYCALVSSSEGAQPRREMLSHLTTNFTRFFRENHHFEHLRDEVLPGLIARAKSGGRVRIWSAACSDGQEPYSIALTVLAMFPNAADYDFKILATDIDPKILAQARAGVYDDNALETVSPAMRKQWFTEVDAGGRRKFRIDDKVKRLITFNELNLMTQWPFKGNFDVIFCRNVVIYFDEPTQVRIWSRFAGLLPEGGHLYIGHSERVSGDAKNVFDNTGITTYRFIGHASGRKA | [
2395,
8522,
12244,
29580,
36586,
54585,
54586,
57416,
59229,
64538,
76558,
87777,
88008,
88026,
88153
] | The following text describes a protein:
Function:
Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. | 0 |
MKFDKPAGENPIDQLKVVGRPHDRIDGPLKTTGTARYAYEWHEEAPNAAYGYIVGSAIAKGRLTALDTDAAQKAPGVLAVITASNAGALGKGDKNTARLLGGPTIEHYHQAIALVVAETFEQARAAASLVQAHYRRNKGAYSLADEKQAVNQPPEDTPDKNVGDFDGAFTSAAVKIDATYTTPDQSHMAMEPHASMAVWDGNKLTLWTSNQMIDWCRTDLAKTLKVPVENVRIISPYIGGGFGGKLFLRSDALLAALAARAVKRPVKVMLPRPSIPNNTTHRPATLQHLRIGADQSGKITAISHESWSGNLPGGTPETAVQQSELLYAGANRHTGLRLATLDLPEGNAMRAPGEAPGLMALEIAIDELAEKAGIDPVEFRILNDTQVDPADPTRCFSRRQLIECLRTGADKFGWKQRNATPGQVRDGEWLVGHGVAAGFRNNLLEKSGARVHLEQNGTVTVETDMTDIGTGSYTILAQTAAEMLGVPLEQVAVHLGDSSFPVSAGSGGQWGANTSTSGVYAACMKLREMIASAVGFDPEQSQFADGKITNGTRSATLHEATAGGRLTAEESIEFGTLSKEYQQSTFAGHFVEVGVHSATGEVRVRRMLAVCAAGRILNPKTARSQVIGAMTMGMGAALMEELAVDDRLGYFVNHDMAGYEVPVHADIPKQEVIFLDDTDPISSPMKAKGVGELGLCGVSAAIANAVYNATGIRVRDYPITLDKLLDKLPDVV | [
1492,
8549,
9133,
20714,
25488,
26161,
27455,
29023,
30200,
30409,
30888,
33053,
36495,
42976,
49252,
64586,
64868,
72865,
75376,
87020,
87103,
87767,
87806,
87873,
87892,
88008
] | The following text describes a protein:
Function:
Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage.
Subcellular Localization:
Periplasm. | 0 |
MNTTMNSQPSDECAICYQKMVLPLMLTCNHSFCFLCIKGVHETMNPPLCPMCRDDISPDLFKKPRQVGKIDMKDPEDSPRRQSAGPTVKQDPGSHVQITRDAQGNIVAQTSSTPVVKTDPDQAKSYWLYQSGSDRWWRFDPRCEKDLDEKRAAGERQFDMMIVGHSYRIDLDRMTQMRLDRLGGQPIGNGRHRELLHVESVEELKALDVRGIAGVILTTN | [
2741,
8202,
10615,
17018,
24917,
24978,
25040,
28656,
29166,
34103,
34458,
37468,
39360,
46929,
50763,
50924,
61838,
64892,
87367,
87767,
88008,
88153,
88181,
88261,
88263
] | The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated proteins and mediates their ubiquitination and subsequent degradation.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The WWE domain mediates non-covalent poly(ADP-ribose)-binding. | 0 |
MTVTLCSPTEDDWPGMFLLAAASFTDFIGPESATAWRTLVPTDGAVVVRDGAGPGSEVVGMALYMDLRLTVPGEVVLPTAGLSFVAVAPTHRRRGLLRAMCAELHRRIADSGYPVAALHASEGGIYGRFGYGPATTLHELTVDRRFARFHADAPGGGLGGSSVRLVRPTEHRGEFEAIYERWRQQVPGGLLRPQVLWDELLAECKAAPGGDRESFALLHPDGYALYRVDRTDLKLARVSELRAVTADAHCALWRALIGLDSMERISIITHPQDPLPHLLTDTRLARTTWRQDGLWLRIMNVPAALEARGYAHEVGEFSTVLEVSDGGRFALKIGDGRARCTPTDAAAEIEMDRDVLGSLYLGAHRASTLAAANRLRTKDSQLLRRLDAAFASDVPVQTAFEF | [
2459,
11791,
12826,
15790,
16976,
17094,
17098,
17099,
17111,
25040,
26272,
26294,
26985,
29071,
31649,
32073,
34131,
36091,
49230,
54801,
57010,
64273,
68424,
77207,
87103,
87125,
87160,
87411,
87578,
88008,
88038,
88153
] | The following text describes a protein:
Function:
Effector that is released into the host cell and affects host immune responses; it negatively modulates inflammation, macrophage autophagy, and cell death through redox-dependent signaling. Acts as an acetyltransferase. Acetylates 'Lys-55' of dual-specificity protein phosphatase 16 (DUSP16)/mitogen-activated protein kinase phosphatase-7 (MKP-7), a JNK-specific phosphatase; this leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS (reactive oxygen species) generation for enhanced intracellular survival of M.tuberculosis. Inhibits Con A-mediated T-cell proliferation in vitro. Treatment of T-cells with Eis inhibits ERK1/2, JAK pathway, and subsequent production of tumor necrosis factor-alpha (TNF-alpha) and interleukin-4 (IL-4); on the contrary, there is increased production of interferon-gamma (IFN-gamma) and interleukin-10 (IL-10), which indicates that immunity in response to Eis treatment is skewed away from a protective T(H)1 response and Eis disturbs the cross regulation of T-cells. When expressed in M.smegmatis, enhances intracellular survival of the bacteria in host macrophages during infection; Can also acetylate multiple amine groups of many aminoglycoside (AG) antibiotics, leading to their inactivation, and thus contributes to drug resistance. Is also able to acetylate and deactivate the cyclic peptide antibiotic capreomycin, but not the other anti-tuberculous drugs isoniazid and pyrazinamide. Acetylates kanamycin (KAN) more efficiently than amikacin (AMK), even though Eis seems to bind AMK with higher affinity. Does not acetylate and inactivate streptomycin, apramycin and spectinomycin; Acetylates DNA-binding protein HupB.
Miscellaneous:
MISCELLANEOUS: Increased expression of eis due to point mutations in the promoter region of eis is responsible for resistance to the second-line injectable drug kanamycin in a number of M.tuberculosis clinical isolates, through acetylation of its amino groups, which leads to inactivation of the drug.
Subcellular Localization:
Secreted. Host cytoplasmic vesicle, host phagosome. Extracellular vesicle, bacterial extracellular vesicle. Host extracellular space. Note=Eis is present in the macrophage cytoplasm from 4 to 96 hours post-infection.
Domain:
The Eis monomer consists of three regions that are assembled into a heart-shaped molecule. This shape is formed by an unusual fusion of two general control non-derepressible 5 (GCN5)-related N-acetyltransferase (GNAT) regions and a C-terminal region. The N-acetyltransferase domain of Eis is responsible for its modulation of ROS generation and pro-inflammatory responses in macrophages. | 0 |
MQDNTSEPSTSITQLLRESYLAENSHQGNSERSRSEPSPHSFHCGDTSGTSDEVPGQDDLPDLSAFLSQEELDQSVNLARQAISQDPLESKPDEQVHVFYPSELKNSGNTVSKKPQFQPSSSPTLDSSQKKQTSSSEAESKKEFLNKAADFIEELSSLFKAHNSKRIRPRTCKNYKSKLESKNKAAQESSCAFSNLSENRERPCAPVTQDLDKTEHTLEQPDKLLQADLEAVTTLEISGLTTESPAASFNSDEPLGQPPHFTQKLKSREVLEGTKVQLDCIVVGIPTPEIRWYCEGKELENSPDIQIIQSGDLHSLTIVEAFEEDTGRYSCFASNIYGTDSTSAEIFVEGASSSESEPDSSKEEMDQYQTHRKVSSDVPPPPVNTIVSHQESPKPQPSIIQPVSIPVHCQSPTNYLQGLDGRPIIAAPVFTKMLQNISASEGQLVVFECRVKGAPSPKVEWYREGTLIEDSPDFRILQKKPRSMSEPEEICTLVIAEVFSEDSGSFTCTASNKYGTVSSSAHLTVKGPEDQNNNAVLHSVSSISLFAAEHTPSAPVPSLPLVDHTPKPKLEGVLINHNEPRSSSKAGLHVHFKLPEDDKGSEASSEDGGGPGNQIRPNSFPDKLNGQIFKIQEPTSPSKEPPPVLAKPKLDPTQLKQLHNQVMLEQQQIQQPSPPPPRETLFNFATPNFSPLPNQQQQSPPPPSSAAYKQNKAPPTQAFNYTRPKQFLSSQSSLAAVSSPSSSPMPSFTNVSQGTQRTANKESFLGSPPPSQTKSSGGMMNQTEQLLTSPKETVLPPLLLSVSSTNQFQPQNVPSTPLSPTGRIQNPVAFLSSVLPSLPSTPPKNAMGLPKSAPAVGNQGTVKRNHRTSHLATEDSIRDHKATVVKDLEKRLHQRDDVFSQSLQRTNYDENLACRLQGPSNDATTFNFTAQDVSKEYKISSFEQRLMNEIEFRLERTPVDESDDEIEHDEIPTGKCIAPIFDKRLKHFRVLEGYPAAFTCKIVGIPIPKVYWFKDGKQISKRNEHFQMNREGDGTCSLHIETTTNDDDGNYTIMAANPQGRISCSGHLMVQTPPLRGRLTTAEQSHRGRSRIPEGDKEPLQERFFRPYFLQAPGDMVAHEGRLCRLDCKVSGLPPPELMWLLNGRPILPDITHKMLVRETGVHSLLIDPLTRNDAGTYTCIATNKTGQNSFSLELSVVAKEVKKAPVILEKLQNCGVPEGHPVRLECRVIGMPPPVFYWKKDNETIPPNRERTSMHQDATGYVCLLIQPAKKVDAGWYTLSAKNEVGIVSCTARLDIYAQWHQQIPQPIKIRPGGTRYASLSGQGLDIFSAFSPVETPVRFSSPPQPVVESEEL | [
8654,
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25040,
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25494,
27940,
30483,
33751,
34712,
38877,
38878,
41979,
46939,
47529,
63951,
87118,
87326,
87367,
87413,
87618,
87857,
87914,
88008,
88009
] | The following text describes a protein:
Function:
Component of the sarcomere that tethers together nebulin (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at the Z lines.
Subcellular Localization:
Cytoplasm, myofibril, sarcomere, Z line. Nucleus. | 0 |
MVQEEIRRGPWTEQEDLQLVFYVKLFGDRRWDFLAKVSGLKRTGKSCRLRWVNYLNPDLKRGKMTPQEERLVLELHSKWGNRWSRIARKIPGRTDNEIKNYWRTHMRKKAQEQRKKATSISPSSSFSNCSSSSSITNEENERNFYDTGGIELLQIEEQKKANDQEQAGESTKVYSMDEIWKDIELLEENETINKPIMGSISPLWDYCPDPMWKDFDWSNFR | [
8101,
9963,
24917,
27731,
27918,
32185,
36776,
43624,
50779,
70929,
87384,
87857,
88008,
88009,
88148,
88150
] | The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus. | 0 |
KTESTQTCFDCICTSFVKFFVFLFFLVTFPISGFFCLKIAHQYERIIIYRLGRLIPIKGPGVVLVLPCIDHWKKVDMRTKAFNVPPSKLCTSDGCIISIGAIVHFSIQDPRLMSLSVQNMNHSIRDASQGCMMNLLCKKTYNDIKTKRQGLSYDLQVDINQSAKEWGLAVSRVELSDITLIMAPQNKTPAFMPMYGAPPPPETGDAFTGSGVDNFGGIAQFATQLFAQVANAQSQQANDAEPPTSSTMDNLLRVLKTAVNEELVQEVDTLYQFNITGIQDGNFFADLRTGSGVVGLGVCSESPDVTFSLSMSTLQKIIAGSVTPYNAYIGGQLHMDGDTDKAMKLEKVVKDIK | [
25079,
25272,
29140,
36860,
37582,
38424,
63803,
64273,
69883,
87760,
88008,
88159,
88161
] | The following text describes a protein:
Function:
Plays a role in the regulation of glomerular permeability, acting probably as a linker between the plasma membrane and the cytoskeleton. | 0 |
MGRVKLKIKKLENTNGRQSTFAKRKNGILKKANELSILCDIDIVLLMFSPTGKAAICCGTRSSMEEVIAKFSQVTPQERTKRKFESLENLKKTFQKLDHDVNIREFIASSNSTVEDLSTQARILQARISEIHGRLSYWTEPDKINNVEHLGQLEISIRQSLDQLRAHKEHFGQQQQAMQIENANFVKDWSTCSMQDGIQIPLEQQLQSMSWILNSNTTNIVTEEHNSIPQREVECSASSSFGSYPGYFGTGKSPEMTIPGQETSFLDELNTGQLKQDTSSQQQFTNNNNITAYNPNLHNDMNHHQTLPPPPLPLTLPHAQVYIPMNQREYHMNGFFEAPPPDSSAYNDNTNQTRFGSSSSSLPCSISMFDEYLFSQVTKTKLSQRF | [
9325,
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15427,
19531,
24917,
27735,
27736,
27918,
32578,
37681,
62120,
64609,
75797,
87139,
87384,
87857,
88008,
88148,
88150
] | The following text describes a protein:
Function:
Probable transcription factor that forms heterodimers with the MADS-box proteins AGL66 and AGL104 and is involved in the regulation of pollen maturation at the late stages of pollen development and pollen tube growth.
Subcellular Localization:
Nucleus. | 0 |
MHLIFLLFLAPFCSAAVFQLPTKSTGSLRAKLIRAGKYQEFLITQHAARLNTISQPISDYSDEVYLGNFTVGTPPQPVSLVLDTGSANMWVIDASCDNMFCNGWIGSNYTRQKFDTSKSSSFSRENRKFSIQYGKGLCSGYLGTDTVGLGGGLTIRKQELGIANKLDVDFAVQPMDGIFGLAWPALAVDQITPPMQNLISQLDVPVFSVWLDRKIQASHGGSAGMITYGGIDTKNCDAGVTYVPLTAKTYWQFKMDGFAVGTYSQYGYNQVISDTGSSWISAPYAMINDIATQTHATWDEMNEIYTVKCSTMKTQPDLVFTIGGALFPVKSVEYILDIGLDEGKCALAISPLMASGFGPSWILGDVFIRQYCNIYDIGNARIGFANAHHSF | [
4723,
8200,
8512,
24878,
24993,
28222,
37159,
37579,
53178,
61636,
62344,
87183,
87413,
87522,
87601,
87965,
88008,
88038,
88058
] | The following text describes a protein:
Function:
Aspartic proteinase.
Subcellular Localization:
Secreted. | 0 |
MPPKKGVSAAEKRDRVLEIFHESSDVFQGKDIEKLATKKGVISQAVKDVLQSLVDDNLVHMEKIGISNYYWAFPSEASVMVENDVKRLETDLAATRKRRAEVEASLEQHKAANPDTESRAQALAELNKLKKRATEVSFKLEAYRDNDPETVQAMHNIAESCKLAANRWLDNTYSLLSWCKKRFAGNEAELAKFFEEVRARPLAPRVQNTWAAS | [
8643,
24917,
27912,
40692,
67591,
67763,
87326,
87379,
87757,
87857,
88008
] | The following text describes a protein:
Function:
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis.
Subcellular Localization:
Nucleus. | 0 |
MFTSEEYLPTKPLDSPITITNKSAKFAAFKVWSKYPDLFRADPQCGIIPAGGTQTVNINYQNPVKPTVEYYVRVFAALVDKEVLPEEFRAEKTATPKNYDGENFLPVQFRRAAAITPLPKEVVIIPGDKIPLNFECKPIGAEPAYSVMTITNNHPQKNLTGSVIPTGSQIFNVKWRSGVLRPGKSAHLPCMFTNLKEEKEEHWFLTFVVFIDSTTLPDDFRKRIAPPFVYDGARAIEITFSKSTSTEPSPYHLKWQALFTKKATVPSAEKAASAEKTEDGGGPPSQTGAPTVTDADNPAPVPAPVPVPAAAPTTTAA | [
18205,
19747,
25014,
25057,
25079,
32172,
36380,
43551,
47529,
87367,
87371,
88008
] | The following text describes a protein:
Function:
Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod. | 0 |
MHTLSSAHNSFEAWNQALRQVCGRFESQPALNRTLFIGDISRQDLGGLELAQIRTNAGRIARQATHADHDDDRHCFLVVQRSGHAQLRQGGDSIELAPGEMALMDSAGGCEIIPHGLIEHTSFHLSREEVCRHLPPSQRAFGKLSPNCASGRLLSLLVQQVCAGELQPWAVADEGGALQEALIALLGPALQHAGEELEGPLAGLYGYSLRRHAERLIEQSLQEPRLSPDMLAGRLRISVRQLYRLFEEQGDSVCRYILRQRLSRSAADLGNPRLRGESITSIAFKWGFSDSAHFSRAFKKQFEVSPKDYRAGALPA | [
8101,
9526,
24978,
27731,
27918,
43624,
50869,
50871,
52747,
63271,
75859,
87123,
87384,
88008,
88148,
88150
] | The following text describes a protein:
Function:
Regulatory protein of the TOL plasmid xyl operons. XylS activates the xylXYZLTEGFJQKIH operon required for the degradation of toluene, m-xylene and p-xylene.
Subcellular Localization:
Cytoplasm. | 0 |
MTRRCSHCNHNGHNSRTCPNRGVKLFGVRLTEGSIRKSASMGNLSHYTGSGSGGHGTGSNTPGSPGDVPDHVAGDGYASEDFVAGSSSSRERKKGTPWTEEEHRMFLLGLQKLGKGDWRGISRNYVTTRTPTQVASHAQKYFIRQSNVSRRKRRSSLFDMVPDEVGDIPMDLQEPEEDNIPVETEMQGADSIHQTLAPSSLHAPSILEIEECESMDSTNSTTGEPTATAAAASSSSRLEETTQLQSQLQPQPQLPGSFPILYPTYFSPYYPFPFPIWPAGYVPEPPKKEETHEILRPTAVHSKAPINVDELLGMSKLSLAESNKHGESDQSLSLKLGGGSSSRQSAFHPNPSSDSSDIKSVIHAL | [
6673,
8101,
9374,
9420,
9429,
9701,
11694,
15387,
16085,
16155,
20029,
21042,
24917,
27731,
27918,
29166,
36776,
37501,
41410,
43624,
50745,
50779,
77895,
87384,
87767,
87857,
88008,
88010,
88148,
88150,
88261,
88263
] | The following text describes a protein:
Function:
Transcriptional repressor. Direct regulator of the transcription of peroxidase (Prxs) and reactive oxygen species (ROS)-related genes via the recognition of 5'-ATCACA-3' motif. Binds to 5'-TATCCA-3' motif (TA box) and represses the activity of corresponding promoters (e.g. sugar response genes). Regulates hypocotyl elongation in response to darkness by enhancing auxin accumulation in a phytochrome-interacting factor (PIF) proteins-dependent manner. Promotes lateral roots formation. Promotes cell expansion during leaves development via the modulation of cell wall-located Prxs. Plays a critical role in developmentally regulated and dark-induced onset of leaf senescence by repressing the transcription of several genes involved in chloroplast function and responses to light and auxin. Promotes responses to auxin, abscisic acid (ABA), and ethylene.
Miscellaneous:
MISCELLANEOUS: 'Kuoda' means 'enlarge' or 'expand' in Chinese.
Subcellular Localization:
Nucleus.
Domain:
Contains a R/KLFGV repression motif, which may be involved in the activity of transcriptional repression. | 0 |
MRFLPLLGGLLPLLGLVGAAPSCNHECNRACWTSRFNVNTDYENEWPVTGVTRKFDFEITEVDEWVGPDGHIKKGAMLINGGYPGPLIKADWGDRIEVTVTNKLKTNGTSMHWHGFHQLNSNNQDGVAGVTECLIVPGASKVYSFLATQHGTSWYHSHISSQYANGIVGPIQINGPSSYPYDTDLGVFPISDWYYDSAEHIVDRMMDPNDPFLKGVPGSPPPSNNILFNGMNIAPNGTGGEYARLKFTKNKRHRLRLVNTSADNTFVVSIVGHNMTVIETDFVPVEPYAVHQLYLTVGQRYDVVIKADQEVDNYWINATLSSTPLCGVSLNPYPAAIVSYEGSDESRLPTNRGPRAIDQFCEDDVSSKPLTSRTAPKADFSDTKVDTLSVTLDVKEVNKGISKVLWSVDGSAIDVQWDKPTLEYVVEGNFTFPRQANIIQLPEAVKWSFWVIQNNSPSPHPMHLHGHDFLILGRSRFPANPLVDPGQPILFDPVVDGPHLKFDNPTRRDTTVVPSFGWLVIAFEAGRNPGSWVFHCHIPWHMSQGLSVQFLERVDRINDGAIPNLMPDLQEKCDEWRRYADNDPEFRMKKVDSGI | [
472,
15590,
29024,
30200,
36869,
37900,
43559,
45808,
45809,
61653,
71310,
87000,
87346,
87413,
87522,
87725,
87767,
87873,
88008,
88058
] | The following text describes a protein:
Function:
Lignin degradation and detoxification of lignin-derived products. | 0 |
MEKSPAMHFLLELESQEPVCLLILFTMFTWFISKVQMILPSSCQHCNYAVTKVTSTPVLADRKISKNLSKHKDDGIEMTHEDVESVMTKMGPDFDHGKTMVYKEIGSNCMSELFDDDEPSLDEVKQAFLVFDEDNDGYIDALDLYRVLRNLGLREGVGVDECEQMIAKYDMNRDRRIDMVEFIRVLEASFF | [
29025,
37640,
46081,
51011,
87244,
87767,
88008,
88009
] | The following text describes a protein:
Function:
Potential calcium sensor. | 0 |
MPDETNFTIEDIEPRPDALRGLDTQFLQDNTALVQAYRGLDWSDISSLTQMVDVIEQTVVKYGNPNDSIKLALETILWQILRKYPLLFGFWKRFATIEYQLFGLKKSIAVLATSVKWFPTSLELWCDYLNVLCVNNPNETDFIRNNFEIAKDLIGKQFLSHPFWDKFIEFEVGQKNWHNVQRIYEYIIEVPLHQYARFFTSYKKFLNEKNLKTTRNIDIVLRKTQTTVNEIWQFESKIKQPFFNLGQVLNDDLENWSRYLKFVTDPSKSLDKEFVMSVFDRCLIPCLYHENTWMMYIKWLTKKNISDEVVVDIYQKANTFLPLDFKTLRYDFLRFLKRKYRSNNTLFNNIFNETVSRYLKIWPNDILLMTEYLCMLKRHSFKNSLDQSPKEILEKQTSFTKILETSITNYINNQIDAKVHLQTLINDKNLSIVVVELIKTTWLVLKNNMQTRKYFNLYQKNILIKNSVPFWLTYYKFEKSNVNFTKLNKFIRELGVEIYLPTTVMNDILTDYKTFYLTHSNIVTYESSIIDSNTFDPILYPELKMSNPKYDPVLNTTANVDWHKKTEWKEAGHIGITTERPQISNSIIECNSGTLIQKPISLPNFRNLEKINQVKINDLYTEEFLKEGK | [
6735,
6736,
24744,
24917,
24945,
24949,
26699,
38482,
46079,
87103,
87411,
87857,
88008,
88009,
88273,
88274
] | The following text describes a protein:
Function:
Function prior to stable branch point recognition by the U1 snRNP particle to facilitate or stabilize the U1 snRNP/5'-splice site interaction. Has a direct role in the assembly or function of a catalytically active spliceosome.
Miscellaneous:
MISCELLANEOUS: Present with 4460 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. | 0 |
MADLLDKIMGSSSSNRIPKRDNRMNQDKDEPTSKRSAPMFSTPKSTTPIGRDSFATMDTMNVQMNMFPVDIKDMPHKIQRFQVDVIVCSSNGKQINANLGVLAAKGDVNSHNRRLAQYYIMRTVHDKLLVKFSGKSHHFLAYDCAATLYLPEGVYTGDDQEEVTLTIDDFPKEEWKFVSKLSRRKDDSYLVVLKPAGFVYTQGEVAQEEANRMELTRIIEIVTSQKLNNEDYLQFGNATFPRLSPPHSEPDAISEIRSGFAKVSRLSQNGGGKAFMTVDTKISPFYKDTSVIKFSSNKLSEMKGGGGGRGGYGRSDSRDSRGGYRGGRSDSRDFRGVYGNRGGNDRYRDESRGRRDMYDSRRDSGSSNGADYSPSDAAELEHAFGERGNTKRCIEEALKGLDVECTHLKGNLIRVSSIAENNAENTSFMMKDDKGEREVTVAEYFLLQYNIKLKYPRLPLVVSKRFKHESFFPMELLRIAPGQRIKVNKMSPTVQSAMTGRNASMPQHHVKLVQDILRDNLKLEQNKYMDAFGIKLMSTEPIQMTAKLLPPAQIKFKGQTYMPDMSRPAFRTQDKFVEPARIRKIGIVVFDNCIQMRQAEDFCDKLSNFCRDNGITVEKDSRDWSIRELNSSDSVAIQNLMKKWLDDRVDILVGIAREKKPDVHDILKYFEESIGLQTIQLCQQTVDKMMGGQGGRQTIDNVMRKFNLKCGGTNFFVEIPNAVRGKAVCSNNETLRKKLLEHVQFIGFEISHGASRTLFDRSRSQMDGEPSVVGVSYSLTNSTQLGGFTYLQTQKEYKLQKLDEFFPKCVRSYKEHSKTLPTRIVIYRVGAGEGNFNRVKEEVEEMRRTFDKIQPGYRPHLVVIIAQRASHARVFPSCISGNRATDQNIPSGTCVENVLTSYGYDEFILSSQTPLIGTVRPCKYTILVNDAKWSKNELMHLTYFRAFGHQVSYQPPSVPDVLYAAENLAKRGRNNYKIHQRYVNLQAVENRIIKDHSELINEDMREELAAAIVDEMSVAMNGMTIPKRNFWA | [
8740,
13236,
24917,
24978,
25342,
25627,
26098,
27929,
28403,
31759,
38476,
38534,
46274,
63866,
64155,
87367,
87857,
88008
] | The following text describes a protein:
Function:
Argonaute protein which is involved in the endogenous small interfering RNA (endo-siRNA) pathway and is required for RNA-mediated gene silencing (RNAi) in the germline. Interacts with secondary 22G-RNAs in an hrde-2-dependent manner; 22G-RNAs are RNA-dependent RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length with a 5'-guanosine residue. Plays a key role in transgenerational epigenetic inheritance and germline immortality. May be involved in transgenerational gene silencing both by inducing subnuclear-co-localization of target genes into heterochromatin and by activation of small RNA amplification in the nuage.
Subcellular Localization:
Cytoplasm, Cytoplasmic ribonucleoprotein granule. Nucleus. Note=Shuttles to and from the nucleus to the peri-nuclear region of the cytoplasm called nuage. Co-localizes with mut-16, probably to subdomains of the nuage known as Mutator foci. | 0 |
MATVQGAVVTEDGNETKLSKNELKRRLKAEKKLAEKEAKHKELSEKQLNQASTTNHSIDNGVLADEEILDPNQYYKIRSQAIQQLKISGEDPYPHKFHVDTSLTHFIEQYNNLQPGDHLTDITVRVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRDFKSEEEFFPINNKLPRGDIFGVPGNPGRTKRGELSLIPHEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFITRSKIITYIRSFLDELGFLEIETPMMNVIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMISGMVKNITGSYKVSYHPDGPEGQAYDIDFTPPFRRISMVEELEKALGMKLPETSLFETEETRKILDDICVARDVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKNGLTERFELFVMKKEICNAYTELNDPVRQRQLFEEQAKAKAAGDDEAMVIDDNFCTALEYGLPPTAGWGMGIDRLTMFLTDSNNIKEVLLFPAMKPEEKKEASSHSGVSEGTVATATN | [
6314,
7279,
8155,
10579,
14456,
24878,
24917,
24978,
24979,
25040,
25079,
25382,
27640,
27995,
28640,
29033,
37863,
39536,
39537,
41180,
46277,
50938,
62795,
70436,
72021,
87110,
87115,
87145,
87276,
87367,
87722,
87760,
87855,
87857,
87914,
8796... | The following text describes a protein:
Function:
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm, cytosol. Nucleus. Secreted. | 0 |
MVQLRKLLRVLTLMKFPCCVLEVLLCALAAAARGQEMYAPHSIRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPGLSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTRISKEAGGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNVWFAEYWEENFNCKLTIGGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVCPEMEQAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTSNPGYRLIGQWTDELQLNIEDMQWGKGVREIPPSVCTLPCKPGQRKKTQKGTPCCWTCEPCDGYQYQFDEMTCQHCPYDQRPNENRTGCQDIPIIKLEWHSPWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRVFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVFIWFGVDPPNIIIDYDEHKTMNPEQARGVLKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEKLYIQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSFKAVVTAATMSSRLSHKPSDRPNGEAKTELCENVDPNNCIPPVRKSVQKSVTWYTIPPTV | [
8688,
18127,
25079,
27828,
29067,
32578,
36077,
36219,
37459,
37505,
45658,
50811,
50812,
58725,
66036,
76381,
87276,
87413,
87484,
87522,
87760,
88006,
88008,
88045,
88058,
88152,
88159,
88161
] | The following text describes a protein:
Function:
G-protein coupled receptor activated by glutamate that regulates axon outgrowth through the MAPK-cAMP-PKA signaling pathway during neuronal development (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase that it inhibits (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. | 0 |
MVKISEIARTSTFAWSSKNLPLLAAGTVAGAVDINFSSSATLELWDIFSPTNKTEPIFSATVDNRFYALAWSKPFEGRPQGLLAGAFENGTVEFWDADVLIKTKDLAKASVHKSNKHTGAVKSLQFNPIQNHVLVTGGSNGQIFIWDTKTFSEPFAPGQAMTPMDEITSVSWNNSVSHILASTGNGGYTSIWDLKTKREVLHLSYTGAGGRANFSYVSWHPSQSTKLITASDNDSCPLILTWDLRNSNAPEKILEGHKKGVLSLDWCKQDPTLLLSSGKDNSTFLWNPIEGIKLGEYPTTANWAFETKFAPAAPDIFATASFDGKVVVQTIQDTSPSVSTKVASTDDNEFWSELSTTETQQPVFEVKQAPNWLKNPSNVSFGFGSKLVIINTDSSGKSTVKVDKFVAKGQEKTEKLFKDLKNDNYSSLIQDKLEGETVNENNKSDWEVLKRLSETGKESLFEDANNDEKEATSPETKKENGEDDFFEHLGNGETAKKEEVFVPEGNFKIFTNNENEDSKKLINLILRNKTEEAVSSCLEQKKLVEALVLALDGSDDVKQQVKNAYFKKNKENNLSRVIYNASTKNVTDLVAHANVENWKEVAVGISSFTTDSSEYNSKMSELGDRILKAKDGKRNDAVVCYLAGGALDKISNLWLQELPDYESELLSLKSEEITSPSDARLQALTNFVEKVATYRYITKSTGEFSGPMVEPLAKAILEFVNLVAGSGDFDLANKFLQLLPSEFSGTEKERILKATSKAVEPASAVKSSANAKIAKPASSSGQTRASINAVPAPAYAPPVQAPPVQAPQPPLVQQQQQQQQQQQPNRYGYAQPTYAGAAPKTNPYARTNPYAPSNNIYKPASPVATPSSLSGTTSGVPPPPPKASYKHETEGWNDLPDTFKAKTAAPRRAAAAATPPVSTPTPVSAPAFGSPGQPPSAPSQPGSVGSVSSAGYPKKTFSATNVLPPPPKSISRSTSRTTVPTSSTVPASPKPTPVSNKYAPAVTSDASQPPSSGFASPTLNSSPRLAKNPYAPSVTEQLPPKISYATPPAHHLANNGPSTPSYAPPKNPYAVPPSTSVSHAGIAPPPPAPKLGSAAPPPPQPFGSSMSMPVQPAFNGVPPPPPPVGRAVSTPAAAKIEQPPAREPELPVQSKHPKGDRTHIPENSLPIYNSLTNVLEAIKPNIPEKYAKHGTDMEQRLNILFDHLNNEEISNGVIELLLKVATSLESKDFANATAVNLQIATEHSDEIGNWHTGLKRLITMAEAMY | [
8581,
8653,
10368,
18654,
19715,
22285,
25014,
25314,
25468,
26695,
28885,
36460,
37341,
44347,
49061,
52270,
64085,
67421,
87369,
87420,
87432,
87760,
87974,
88008,
88009,
88162,
88252
] | The following text describes a protein:
Function:
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity).
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. | 0 |
MDRSREAEMELRRGPSPPRAGRSHEVDGDKAACHSCCICGKSFPFQSSLSQHMRKHTGEKPYKCPYCDHRASQKGNLKIHIRSHRTGTLIQGHEPEVGEAQLGELRVSEGLDGCASPTKSTSACNRVLNGAVPTDGSKILLRSSRKEAEGAASAQEDAEAMVQCSFCKSRFERKKDLELHVHQAHKPFKCRLCSYVTLREESLLSHIERDHITAQVPNGSEACVENGKPELSPGEFPCEVCGQAFSQTWFLKAHMKKHRGSFDHGCHICGRRFKEPWFLKNHMKAHGPKAGSKNRPKSDLDPIATINNVVQEEVIVTGLSLYEICTKCGNLFTDLDSLNAHNTVHRKVEASRNPAPAEEGDTEDPPDTKQFFLQCLNLTPCVAGDVSPSGQAGRRVAELDPVNSYQAWQLATRGKVAEPAEYLKYGTWDEALAGDVAFDKDKREYILVSQEKRKRESDAPSTQAPPRKRASVPGDPMLSGHLDPRPASRPNRRAAATTGQGKSSECFECGKIFRTYHQMVLHSRVHRRARRDRDPEGDRAVRARCGSLSEGDSASQPSSPGSACATADSPGLAEEVVDDSGEEAVSEPASGGQPGHCCSSGEVAPILLSNGDPSHKLGNNLPEEDISEPTVGIATPSVSILENSSRETTKGPEQHRHSLDLKMPAFHPRQEASTPERVDFPSSMEIASLQHTLDSQAGHSKEKLSDLHKEHCGVGKRASAPDLVPLDLSMKSSREDPSSKEASSLQTALVIHPCPYCNHKTYYPEVLWMHKRIWHRISCGSIAPPWTQPSGHKSICSNLAFLARSGRTGPPPALGGKDCQPLLLARFTRTQVPGGVPGSKGSSSPLGVTTKAASIPKNKESPSGGPCAPWAPGPDGYRQTRAGHGQDPPSAAVQGPLPKPKQEASSRLAPSPGSGGLSRSATPTPSVITRVGAQPSANSKPVEKLGVPAVGTGFTPPNKHSAPDSLKAKFSPQPQGQPPSKGEGGSPLPPREAPVKPAQELRTLATCAAGPRGDAALQAPPGAPPTLHSIQQEPAAAEGQEKRLDILSIFKYIPKDFATLYQGWGVSSPGPEHRGTPRTQARQGDFVCVECGKSFHQPSQLRAHLRAHTGERPHCPRDCAGRAPPKGDLETHLQHPARDSVDCGLTGDWKAPSSDHGHFGEEDPRSPDQTP | [
9296,
15388,
16544,
17650,
20782,
24917,
27736,
29166,
35342,
46932,
64003,
77619,
87384,
87684,
87767,
87857,
88008,
88009,
88148,
88150,
88180,
88261,
88263
] | The following text describes a protein:
Function:
Transcriptional regulator that binds to the promoter and activates the transcription of genes promoting brown adipose tissue (BAT) differentiation. Among brown adipose tissue-specific genes, binds the proximal region of the promoter of the UCP1 gene to activate its transcription and thereby regulate thermogenesis. May also play a role in the cellular response to replication stress.
Subcellular Localization:
Nucleus. | 0 |
MTSLIQPEPQATNTKENQTTVKTTTNQITTVETKTTVAILKTNPKQQQQQQQLLVNFTPRLSTLDPHNQLLHQNPLRGLYALFWILLGFHIIATLHASGSLVIQSPLARLFSKHLPQLALVDLCLVASTFSALGFAKLLSNRYFDYCHTGLILQHLFQFSWLGAWILYIFYREWPWIQSGFLTLHSITMLMKIHSYCATNGEYSVQLKSLESKMKELKRSKVIEIKEDDQQHHKTLVSTVVKTGIYQKLQQFVDQKKEQPTTIDQSLGSNSQSDQGPEKPMNDEMMEQQVHETIDLLDQLGARNLRDSHDDDDQKEDQYSGQPWPENLTISNFTDYLLIPTLVYRLRYPRTKEIRIFFVVEKVFAVVGIFGLIYMITQYYIWDQVTNIKAFDRDHRSSALHLVDNVIRLVVPFTINYLLIFYIIFECICNAFAELTRFADREFYSDWWNSCSFDEFSRKWNKPVHHFLLKHVYASTISSYGVSRSAAAIMTLFLSSLVHELLMVIVTRKLRLYLFLAQMTQLPLTYIGRSKLFKTRPALANAFFWVGLISGFPLLAVWLVSP | [
9033,
25014,
31730,
39478,
48055,
87125,
87326,
87432,
87760,
88008,
88153,
88159,
88161
] | The following text describes a protein:
Function:
Sterol O-acyltransferase that catalyzes the formation of stery esters.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. | 0 |
MNAESCSLILSYISSAPAGNLVLNCTATTNKQTLEANLKSAVYQRYPEFLEDWTNVCVHIIHSYFPKDADYWNVDKLYTSVNRITTLEQSKVVGKEIKNGFTFDAENSTASLENDLQPQFRSHALFMVGSAGPLFSSTARTSRLDSRLPDGGIIAKPVALLPTPSVANSQEYTLDKLSPPSTAKPPASVIEFNPSLAKLPTVKYLQSGPFSSIAPYKNSSSSVIPDSSFHSVACYRASSHYKEAPVEKSIDIDIIQNNLSLLEEDSWTSVPIQGELVELNKLLQHLQLLQNQRITSHNVLSDEERQISVQVQNLILKLAKDYDMSPEDFLMDDFTLSLTQYGAFYRGTLPLSAQPLELPSQQLLRSQSNAALRSNSLSMNGSLSPSSTNVPLQSYRRTTKSRR | [
8095,
8103,
15340,
24788,
24917,
25040,
25356,
87302,
87367,
87857,
87914,
88008,
88148,
88150
] | The following text describes a protein:
Function:
Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes.
Subcellular Localization:
Cytoplasm. Nucleus. | 0 |
MGQRGSRVSPVVASASDPPSPNPTERLSLVAPSAAVVGAGVAGVHVAYELAKLGFKVTVFERRGDIAGGETRFSLPFVGVGLIEPSLARTAFRTEVLRGMLFPTACPDLIAREHLFNTLLNPVVYRWMWGRLRSCFSDSEVMAYTNNLSCVSHSVVCELVNKYPHLHQHVFAGPVTVLNERKEAAVTAHAEPLMVDPVGWTRALAEVCRRDYDVQFALGERLEDAVTYLKYDVESTRSIRVSKPDPSHPEQRLFASEGYDVVILAAGASTGTMTLPNSRLPVLGLSGLSAVVQQPSGALKDAVWSLFQCRPHRSPAAAASSSSPEVDAPSSHEGVADPLARPAPGTLALLSSHCSLYGYTWPSSLTLSANRNGGPPSRSSAVASMMQSKVLPTPQDVVLQGLLSLDSTVKTKTHALVSRQLDRLESYLRIKCGWSVPLSSSSTSAEAGCGSNVVRVSEYVRAFTPDGVPIVDRNGGSFNCFVCCGFGDHAMDFAPGAAKVLGKLVEHQAQHLREEDIEKTKTWGLLTSKLSPSRRAAVEEELQLLFNGVDSDAVKRKGSRTPSEASALALLRHEDNPYSTNRFANMVRKEVKMDSSPPILSRLCALEDVFLTHLEPLRRRFHAKATELALRENTPDWLRTFVFCFMYEEDDDPAAQARKEQHVRSLQRLASQYETPVTDAKTTGDGAEELPLTPAEQSKRKQAELERRAREVFAKRV | [
24978,
24981,
30200,
41080,
63960,
87873,
88008
] | The following text describes a protein:
Function:
Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). Involved in mid-late stages of complex I assembly. | 0 |
MQRAVSVVARLGFRLQAFPPALCRPLSCAQEVLRRTPLYDFHLAHGGKMVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQGPTAAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK | [
2414,
8233,
24926,
24979,
25130,
28111,
29269,
41203,
41204,
47701,
58150,
59087,
59210,
87147,
87785,
87976,
88008,
88153,
88154
] | The following text describes a protein:
Function:
The glycine cleavage system catalyzes the degradation of glycine.
Subcellular Localization:
Mitochondrion. | 0 |
MLACDLPEAGVRRVSALPTAAEPAGFWSGVAVWVDKPHVVNRRLTGAKEVARIWTNHRVISTMLQQPRVFAGLSEESLQKRLADMKMEGRNEAEGDDLELIIRDLLPRQLERAKVVREVVVLDHPRITAWFIPLGSSCHGDTESEQSYKSYRFVYSEDQTGKTIALDILSPPGVAAAHSPDRNCSTGGAAVHSPDRNCSTGGAAVHTAEDDRKCSPGGAAVHSAEDDGICSPTTKWLCDHLLPKIAKWSADVAPGGRRRVQALVPIDRYNIRYQQLKRKYGRRMMQVWPDVTTTDPEKFVYEDIAIATYLLLLWEEERSRLRLEEKQSFVDLGCGNGLLVYILAQEGHPGKGIDVRKRTTWDIFGQGTVLQEEPITPSDSCLFPDSDWLIGNHSDELTPWIPVIAARSSYTARYFVLPCCPHDFHGRFARTHTATSHYRNYLDYVCSIGQACGFTVEEDSLRIPSTKRICQIGRTRIYPEDEMQKIDKQISDFIISRPREQPKNPPKSQTERTGATTEFLQGGRNVFTDDPSADSKLTSDRRRSKVDGTTANGSALWVDGFQPRSKVELVRNCNRLEEGLKERIVNTVGLALLSQTGTASGAVLNQT | [
2180,
11739,
24978,
30158,
45777,
59229,
87367,
87777,
88008,
88026,
88153,
88278
] | The following text describes a protein:
Function:
Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase; Probable adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular Localization:
Cytoplasm. | 0 |
MKERIKDKAWRPQFIKLNNPDTSKKIVSQKSKKPEIVDLSSPGNNDLVTISILCVLLCFQLAISLNPHSGESQPPMYGDYEAQRHWMEITVNLPIEQWYLNGTHNDLLYWGLDYPPITAYHHYLLGVISNKINKKWVELTTSRGYESIAHKLFMRLSAIIPFYIFYLPPLIFYFTRSKKMSPILYALALLYPSLLVIDNGHFQYNSISLGLFLATYMFLTKNFTIIGSILFVAALNYKQMELYHALPVFVFILARSINKTQLFNSFRRILTIGLFVVGTFLIIWLPFLLTGTAKDVIIRVFPFNRGLYEDKVASFWCAFSFILKRLPLQSVQIYISTALVLAGSAPSLLVLFLRPTEKQFRISLTATGLSFFLFSFHVHEKTILLAAVPALLLISEYTSLVIWFLNITNISIFSLCVKDNFALSLSFFFAYFVVSYAYTAPRKISHILTILIGFAICILELYGPSNQRFPHIYQLANAFFSCVHFIYFLLYLSFASFEKTKKE | [
2908,
8190,
25014,
32019,
39982,
87432,
87525,
87760,
88008,
88153,
88159,
88161
] | The following text describes a protein:
Function:
Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation (By similarity). Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man(9)GlcNAc(2)-PP-Dol (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. | 0 |
MAEVVQVHKDWVGSLPSGKKITVVFVIGGPGSGKGTQCAKIVSQFGFTHLSAGDLLREEVKSDTEQGAMIKNLMHEGKLVPSEIIVRLLLKAMLASGNDKFLIDGFPRNEENREAYEKIIKIEPEFVLLIDCSREEMERRILHRNQGRDDDNMETIRRRFEVFQQSTLPVIQHYEKMGKLRRVDGDRQPDMVFEDVKAIFAQLNTQANEGSNISRAQINPFKRWFLDLFCSCFDLQDRRN | [
3665,
8013,
8028,
15806,
24917,
24978,
28087,
29033,
31521,
31936,
31937,
36650,
41244,
58239,
61941,
87016,
87110,
87367,
87694,
87855,
87857,
87988,
88008,
88153
] | The following text describes a protein:
Function:
Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. | 0 |
MFATPLRQPAAANHQTPKNSAGMDEHGKPYQYEITDHGYGKDAVKVLHVSRNGPVHAIQEFEVGTHLKLYSKKDYYQGNNSDIVATDSQKNTVYLLAKKHGIESPEKFALLLARHFINKYSHVEEAHVHVEAYPWQRVCQEETRTNVNGKCENGVQGNCDFSSIDNRSLHNHAFIFTPTALHYCDVVIRRTDPKQTVITGIKGLRVLKTTQSSFVNFVNDEFRSLPDQYDRIFSTVVDCSWEYSDTENLDFLRAWQTVKNIIIRNFAGDPQVGVSSPSVQHTLYLSERQVLDVLPQVSVISMTMPNKHYFNFDTKPFQKIAPGDNNEVFIPVDKPHGTIYAQLARKNINSHL | [
1967,
7975,
11060,
11155,
25004,
28660,
37635,
52330,
87873,
87894,
87982,
88008
] | The following text describes a protein:
Function:
Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular Localization:
Peroxisome. | 0 |
MLEEAGEVLENMLKASCLPLGFIVFLPAVLLLVAPPLPAADAAHEFTVYRMQQYDLQGQPYGTRNAVLNTEARTMAAEVLSRRCVLMRLLDFSYEQYQKALRQSAGAVVIILPRAMAAVPQDVVRQFMEIEPEMLAMETIVPVYFAVEDEALLSIYEQTQAASASQGSASAAEVLLRTATANGFQMVTSGVQSKAVSDWLIASVEGRLTGLGGEDLPTIVIVAHYDAFGVAPWLSLGADSNGSGVSVLLELARLFSRLYTYKRTHAAYNLLFFASGGGKFNYQGTKRWLEDNLDHTDSSLLQDNVAFVLCLDTVGRGSSLHLHVSKPPREGTLQHAFLRELETVAAHQFPEVRFSMVHKRINLAEDVLAWEHERFAIRRLPAFTLSHLESHRDGQRSSIMDVRSRVDSKTLTRNTRIIAEALTRVIYNLTEKVTPALPPVPQIQQEQLDSVMDWLTNQPRAAQLVDKDSTFLSTLEHHLSRYLKDVKQHHVKADKRDPEFVFYDQLKQVMNAYRVKPAVFDLLLAVGIAAYLGMAYVAVQHFSLLYKTVQRLLVKAKTQ | [
9575,
14547,
16511,
18151,
21160,
25014,
27303,
32118,
42312,
49564,
87432,
87522,
87760,
88008,
88058,
88159,
88161
] | The following text describes a protein:
Function:
Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning, via its interaction with NOMO; May antagonize Nodal signaling and subsequent organization of axial structures during mesodermal patterning.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. | 0 |
MRRKCNLELTLSPSNLLMEDKRLENEQSQQLTIFYNGKFVASHVTQLQAKAIIYLASREMEEKTNKLSEPSSPLLQPQTVKKSLQRFLQKRKNRIQITSPYHH | [
9350,
12016,
23998,
24917,
44782,
51147,
67538,
87686,
87857,
88008
] | The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1. | 0 |
MASSGSNSKSSMVNGTKQFALLPKIINGGIAGIIGVSCVFPLDLVKTRLQNQQVGPNGEKMYNSMLDCFKKTYRAEGYFGMYRGSAVNILLITPEKAIKLAANDFFRHHLTTSNGTLPITRQMAAGGLAGLCQIVITTPMELLKIQMQDAGRVAAQAKAIGKTIPKVSATSIAMELIRTKGITGLYKGTGATMLRDVSFSIVYFPLFATLNSLGPRRDDGSNEAVFWCSFLSGCAAGSMAALAVNPFDVVKTRLQALKKVEGEMQFNGVADCIGKTLKYEGVTAFFKGGLCRMIVIAPLFGIAQMVYFLGVAEALLGVKSGNK | [
10476,
10479,
14665,
24983,
28946,
29854,
29920,
37655,
50913,
55191,
76682,
87760,
87785,
87786,
87914,
88008,
88009,
88096,
88159,
88161,
88162
] | The following text describes a protein:
Function:
Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein. | 0 |
MVELTITGDDDDILSMFFDEEFVPHAFVDILLSNALNEDQIQTQSVSSLLLTRLDFYTKNLTKELESTIWNLDKLSQTLPRTWASSRYHKEAEQNDSSLYSTESLKSSKLEYYLDTLASAVRALETGMHNVTEKLSDLDNENNRNTNVRQQLQSLMLIKERIEKVVYYLEQVRTVTNISTVRENNTTSTGTDLSITDFRTSLKALEDTIDESLSSAIDNEAKDETNKDLIGRIDSLSELKCLFKGLDKFFAEYSNFSESIKSKAQSYLSTKNIDDGMIS | [
6705,
8494,
12243,
24724,
24979,
25040,
25386,
87528,
87760,
87974,
88008,
88162
] | The following text describes a protein:
Function:
Acts as a component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Miscellaneous:
MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus membrane; Peripheral membrane protein. | 0 |
MDKSKRPFIKSKRSFRRRLPPIQSGDRIDYRNMSLISRFISEQGKILSRRVNRLTLKQQRLITSAIKQARILSLLPFLNNEKQFERTESTTRTANFRTKNK | [
8138,
24992,
25225,
27932,
34266,
37313,
51037,
64600,
87103,
87296,
87411,
87930,
88001,
88008,
88020,
88022,
88277
] | The following text describes a protein:
Function:
Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus.
Miscellaneous:
MISCELLANEOUS: Two forms, which differ in pI, are produced, S18 alpha and S18 beta.
Subcellular Localization:
Plastid, chloroplast. | 0 |
MALSSRLLAACGAALLLLSLSVDAALNVNMKLASSRVTLTADALEVAVVVTPKQPKLKQLTLETLVDTSGASVLSGLTLKGDGSKFVTKLSGDNKLQAGMYKLKVSAVDEETKQSAYEVLQLKVTTPVNVASAKVNGKALKPGDKLSGQSFNAAAEDALKMEVALQQTHDKTPVAAHQAFLRFTHATEKTETYFVLTADKGLAHSTTLQFAALSKKFGYNSGKHHVELILGASTFEKAIVWDLGNVELQLGAAPPETPSPLYKKPLLYESDTTLKALPEIAHVMREQDPRPPVTVSMAFMGAVLAPFAFFLLFVARLGLNVKRLFEGSVFVFGCVFLASLGGILALFGFYWLELTMFRTLGYLSVLGSVNLWSGHLTLKRLAEAPAKKTTKVE | [
8189,
25147,
43429,
87432,
87760,
88008,
88058,
88159,
88161
] | The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. | 0 |
MENGEILLTSWLNRSVHIEIFDERKFIGKFLCTDREGAAILSNTTEYNKGFSRALGLVVIPGKHIKSFSVRA | [
16923,
25008,
25325,
25640,
27925,
36906,
45220,
62297,
73532,
76569,
87103,
87432,
88008
] | The following text describes a protein:
Function:
Component of the NatC N-terminal acetyltransferase, which associates with the ribosome to acetylate nascent protein chains in a cotranslational manner. NatC acetylates protein N-termini starting with methionine, followed by a hydrophobic or amphipathic amino acid, with amino acids at positions 3 and 4 also contributing to NatC recognition. The first 4 amino acids of cognate substrates are recognized at the Naa30-Naa35 interface. NatC-dependent acetylation targets various substrate proteins to specific subcellular sites (By similarity).
Subcellular Localization:
Endoplasmic reticulum. | 0 |
MTEALYFLDCYMKEFEATVEKVTDDKFVVLDRTVFYPESGGQPSDTGKLVRESDGAEFNVLYVRKFNGDISHEIDGENVSNGLKAGDKVKGFIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEVFDRDKFAEYEKIANDLIAQKSPVNLYLVSRKEAEEKLSRLTTLAKGFSDEIKEVRIVEIEGVTIEACGGTHVKNTEEIKGVKIIKLQNKGKSNRRMYFTLVD | [
8144,
24978,
27893,
27903,
28629,
29033,
32536,
43581,
46837,
50946,
50947,
50948,
76988,
79071,
87039,
87367,
87767,
88261
] | The following text describes a protein:
Function:
Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala). Has no activity on incorrectly charged Ser-tRNA(Thr), nor on correctly charged Ala-tRNA(Ala) or Ser-tRNA(Ser).
Subcellular Localization:
Cytoplasm. | 0 |
MSAVESPVIVTEPGSLKPQGLTQTATGGKFGAAATVKTTPTKAKPYVKPQNANNLQNNFNPRKIFTEYISKEETDAGIEDGSMFKGVLRINPKNYQECFLDHPKGTNHPDVLVLGQDRNRAMQGDVVAVKIKPKEDWLVNYVEYVKWWAEHKKGDRNSGKTDNNSPNKTEKRCLRNEIQDNGVTSDEVPDSCLITIGAIVHILEKKHFRVAAGKLQLMPNSANPNVLFVATDSRVPRILIPKSDVDKEFFSRPKDFERFLYTAKITDWRAESVYADGRLVKLLGMSGEIDTETERIVYEHQIDHREFSDECLESLPITTAENWKVPDAEFEYRRDFRSDIVFTIDPKTARDLDDALHAKHIDDCDGKGTPGLEIGVHIADVTFFLKEGTELDKWASERGNSTYLSQTVIPMLPRILCEQLCSLNPGVDRLSFSTVFKMSYEAELYDVWFGRSVIRSRVKLAYEHAQDFIENPEKDFTCDELPDISDGNTPFEIKEKTLMLHRIAQVLRQKREDSGALRIELPRLKFALDEDKKPQGVSIYEIKDSNKLVEEFMLLANMEVAKKIAENFPEHALLRNHPPPKEKMIKDVAEQCARIGFPLDGRTSGLLSTSLRKYQGKSRLDMCIRQVISSLTIKPMQQAKYFCTFEMPLSFYHHFALNVDHYTHFTSPIRRYPDVIVHRQLAAALGYNERSERVPEEIQEICTRCNDTKLASKEASDESAMLYFGVFIHQTGPMKCQAVVLGVMDLSFDVLIVEYGVVKRVYVDKMKRDFNKSTEKLTIYWPADPNAESGNREEFSSSIQMCNVVYVILVPYKSIEVSATIVRPSLEQRNILKSTLKDMKETGSTILQ | [
4026,
6843,
8131,
9953,
14027,
14295,
23758,
24818,
27659,
27925,
32536,
37520,
46277,
54855,
58981,
62008,
68157,
68543,
75835,
87016,
87017,
87367,
87449,
87601,
87747,
87752,
87767,
87850,
88001,
88008
] | The following text describes a protein:
Function:
3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.
Subcellular Localization:
Cytoplasm. Cytoplasm, P-body. | 0 |
MTETVTDQGKQRSSKLQKNEAAKDEQVEGKGKETLESGTDKSAEQNSSLLVGQPDVIDNDNVQTVDDFKNLMYKMQETRRAIVFALLNEKDLTKDDVEILKRAYEKLTDNQTHSFQREMCTLTTKLSVNIGDETRGLEKDLKYLDALMNIRREEPNLLWPIIMSRVDLFSILANYHPKGKETFLKEYEDTVKFLKTFISSEAITGKKPIFITDWDGTMKDYCSQYATNLQPVYSAVGMTRFAASFTRISAVLTAGPLRGPGILDLTAMPIDGPVMFSGSWGREWWLSGKRVVHQDGITDEGFNALQRLDDEMKDLLHTSDYAPFALVGSGVQRKVDRLTLGVQTVCHHVTSELSNRYQMAVKERMHRVDPNSQILVFDPSTELEVEVVAHNSGIIWNKGNGVERLIKSLGDSLQSPGKILICGDTLSDIPMVRQAVKQNPDGVLAIFVGAKMSLREEVKQVIGDESRCCFVSCPDVIHAAMSQILNEHCIGK | [
4105,
7871,
10701,
21558,
24978,
27681,
28623,
55054,
64168,
68129,
74864,
87016,
87103,
87601,
87747,
87767,
88008
] | The following text describes a protein:
Function:
Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate. | 0 |
MASKLFVLAFLCLALVVVVQSAPQYARGDVPTYDEEDFDEESLKPHSSSSSDDGEEEFDPSLLEEHADAPTARDPGRNPEFLRNSNTDEQASAPAASSSESDE | [
24878,
34624,
35457,
51562,
87103,
87226,
87550,
88008,
88038,
88058,
88146
] | The following text describes a protein:
Function:
Salivary protein with anticoagulant activity that inhibits host thrombin (F2); binds to the proteinase in a reverse orientation (opposite to substrates).
Miscellaneous:
MISCELLANEOUS: Does not inhibit host coagulation factor Xa (F10), factor XIa (F11), factor XIIa (F12), kallikrein, chymase, trypsin, chymotrypsin, elastase, tryptase, cathepsin G (CTSG), plasmin (PLG), urokinase-type plasminogen activator (PLAU), tissue plasminogen activator (PLAT) and matriptase.
Subcellular Localization:
Secreted. | 0 |
MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPPENSDIGTGKKEKEKKNRKGKDKENGSVSTSETPPPPPPNEISPPHAVEEEEDDDWGEDTTEEAQRRRMDEISDHAKGLTLSDDLERTVEERVNILFDFVKKKKEEGIIDSSDKEIVAEAERLDVKAMGPLVLTEVLFDEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKTASVPKVETVKSDNKDDDIDIDAI | [
8164,
14125,
25040,
25079,
26413,
27933,
28816,
29034,
38200,
38628,
49116,
49238,
49239,
71415,
87367,
87491,
87492,
87661,
87684,
87855,
87914,
87968,
88008,
88180
] | The following text describes a protein:
Function:
Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon. In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3). During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD). This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC. When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP. Start codon recognition also induces a conformational change of the PIC to a closed state. This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC. Finally, EIF5 stabilizes the PIC in its closed conformation.
Subcellular Localization:
Cytoplasm. | 0 |
MLSFLQKLGKSFMLPIAVLPAVGIILALGREDVFNIPFVYQAGTAVFDHLPLIFAIGIAIGISKDSNGAAGLSGAISYLMLDAATKTIDKTNNMAVFGGIIAGLIAGYTYNRFKDTKLPEYLGFFSGRRLVPILTAIITIILAGIFGVVWPPIQSCINSFGEWMLGLGGIGAGIFGLFNRLLIPLGLHHVLNNIFWFQFGEYNGVTGDLARFFAKDPTAGTYMTGFFPIMMFGLPAACLAMVVTAKPSKRKATAGMMIGFALTAFITGITEPIEFAFMFLSPLLYAVHAVLTGLSLFIVNWLGIRSGFSFSAGAIDYVLSYGIAEKPLLLLLVGICYAAVYFIVFYVLIKALNLKTPGREDDDVDEVLDENTVQDVNENIMLKGLGGKENLQTIDHCATRLRLTVKDTALVDEALLKKAGAKGVVKSGGQSVQVIIGPNVEFAAEELRAAVK | [
3484,
9291,
10443,
25079,
25408,
26403,
29579,
30043,
30159,
34600,
35096,
37598,
38665,
45264,
46891,
50916,
64608,
76084,
87276,
87694,
87760,
87915,
88008,
88087,
88153,
88159,
88161,
88162
] | The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (By similarity). This system is involved in N-acetylglucosamine transport.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion.
Domain:
The EIIC domain type-1 forms the PTS system translocation channel and contains the specific substrate-binding site; The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-1 domain. | 0 |
MGNQSTKSTHGTTRVSHSKSAHHNSSRVTSDVIPRSASAISSHERFFSDSQSSSPPAVCPVSAPGKYRNFPGKDVPPICLTDEYNNSDDEVFCSTRTSKQSPLATGCPRQNLGSPGNRRSVDSTNSDLLEAVTPRSHISVKRTVSSGTEHAPDHANMQKSSSLKFTRPGVRSETKETTPSTSSNPTMFPCIHQFLHLTQPQILFVRKTWNHARNQGALEPAISIFRNSFFKNPEIRQMIMFGTKNEGHERLKKHAQLFTVLMDDLIANLDSPSATVAGLREAGEKHVWPTRNQYGCPFHAHLLDQFATAMIERTLEWGEKKDRTETTQRGWTKIVLFVTEQLKEGFQDEQKRARRIKAQIKTSAGSSSFEISTKTKQSDMKRFHTLDNM | [
6932,
10372,
28962,
29023,
30786,
30838,
36744,
43619,
46244,
70675,
76187,
87103,
87541,
87678,
87767,
87874,
88008,
88162
] | The following text describes a protein:
Function:
May play a role as physiological sensor for oxygen via redox signaling and/or electron transport.
Miscellaneous:
MISCELLANEOUS: Does not bind carbon monoxide (CO), nitric oxide (NO) or CN(-). | 0 |
MNEITLFIKSSSANAERRINPQWTVSQLKTKLVPIVGTPEQYQKLTYEPASSTVPGHVFTSEEENLDLGEFKLQPLGTIVVEDTRPPHLRLDFDDLSQVDKYVMPREQYENRTDSVYAWKKRNQLGRFNPDFEASKASRQESLKRELVDLQKNLNSRCCAAGERYGTIRYIGLVPEINNDNLWVGVEFDEPVGKNDGTVSGKRYFNAKNKHGSFLRSSEVEVGDFPPEDILEGL | [
8577,
11935,
24917,
24978,
25040,
25114,
26011,
33715,
36454,
36722,
59237,
64589,
87285,
87367,
87371,
87782,
87914,
88008
] | The following text describes a protein:
Function:
Required for microtubule function and cell polarity. Involved in the proper folding of alpha-tubulin.
Subcellular Localization:
Cytoplasm, cytoskeleton. | 0 |
MAKPFFRLQKFLRRTQFLLFFLTAAYLMTGSLLLLQRVRVALPQGPRAPGPLQTLPVAAVALGVGLLDSRALHDPRVSPELLLGVDMLQSPLTRPRPGPRWLRSRNSELRQLRRRWFHHFMSDSQGPPALGPEAARPAIHSRGTYIGCFSDDGHERTLKGAVFYDLRKMTVSHCQDACAERSYVYAGLEAGAECYCGNRLPAVSVGLEECNHECKGEKGSVCGAVDRLSVYRVDELQPGSRKRRTATYRGCFRLPENITHAFPSSLIQANVTVGTCSGFCSQKEFPLAILRGWECYCAYPTPRFNLRDAMDSSVCGQDPEAQRLAEYCEVYQTPVQDTRCTDRRFLPNKSKVFVALSSFPGAGNTWARHLIEHATGFYTGSYYFDGTLYNKGFKGEKDHWRSRRTICVKTHESGRREIEMFDSAILLIRNPYRSLVAEFNRKCAGHLGYAADRNWKSKEWPDFVNSYASWWSSHVLDWLKYGKRLLVVHYEELRRSLVPTLREMVAFLNVSVSEERLLCVENNKEGSFRRRGRRSHDPEPFTPEMKDLINGYIRTVDQALRDHNWTGLPREYVPR | [
24724,
29111,
36659,
38319,
58239,
77242,
87522,
87528,
87760,
87976,
88008,
88009,
88061,
88159,
88161
] | The following text describes a protein:
Function:
Sialate:O-sulfotransferase which catalyzes 8-O-sulfation at the Sia-glycan level using 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a donor, forming 8-O-sulfated Sia (Sia8S)-glycans. Displays selectivity toward glycolipids such as GM1 gangliosides.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein. | 0 |
MAASGWGWGCDILIFYSPDAEEWCQYLQDLFVSCRQVRSQKIQTYRLVPDACFSSQDLSVFRDARCVLVLLSAGLVECFVQPGLLPVLQRACHPPQRVVRLLCGVQPNDEDFQAFFPDWAHWQELTCDDEPETYLAAVRKAISEDSGCDSVTDTEPEDERALPFSKHTDLPLETSPGNLMVVQPDRIRCGAETTVYVIVRCKLDEKVSTEVEFSPEDSPSVRMEGTLENEYTVSVKAPDLSSGNVSLKVYSGDLVVCETTISYYTDMEEIGNLLSSAANPVEFMCQAFKIVPYNTETLDKLLTESLKNNIPASGLHLFGINQLEEDDMMTNQRDEELPTLLHFAAKYGLKNLTALLLTCPGALQAYSVANKHGHYPNTIAEKHGFRDLRQFIDEYVETVDMLKSHIKEELMQGEEADDVYESMAHLSTDLLMKCSLNPGCDDELYESMAAFAPAATEDLYVEMLQASAGNPVSGESFSRPTKDSMIRKFLEGNSMKLASLEREQHPPHGEELYHTVEEDETFSVDLANRPPVPVPRPETSTPGPHPLPDNEPYISKEPLVRPWRDRPPSSIYDPFAGMKTPGQRQLITLQEQVKLGIVNVDEAVLHFKEWQLNQKKRSESFRFQQENLKRLRDSITRRQREKQKSGKHADLEITVPIRHSQHLPGKVEFGVYESGPRKSVFPARTELRRGDWKTDSTSSTASSTSNRSSTRSLLSVSSGMEGDNEDNEVPEITRSRGPGPTQVDGAPVVTGTPVGILERPPRVPPRAASQRPLTREPFHHPPPPVPPRGR | [
12898,
12905,
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17039,
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30159,
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32073,
36072,
50751,
63698,
68385,
78096,
87276,
87367,
87694,
87760,
87914,
88153
] | The following text describes a protein:
Function:
Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Cytoplasm. | 0 |
MSNVAPGVTPDAPAPSAVSNRPDVKRDTHPFSRSQLEVLMTKRFFYIQSFEIYGGVGGLYDYGPTGAALQANIINQWRNHFIIEEEMLELDTTIMTLSDVLKTSGHVDKFADWMCKDTKTGEIFRADHLVEGVLEARLEGDKQARAIEAGQTAAVPAEAASGDSKKSNKKKVKSSAVKLDDALVDEYTSTLAQIDNFNGEQLGELVRKYDIRSPESGNEVSEPVEFNLMFESYIGPTGQIKGYLRPETAQGHFVNFQRLLEFNNGRVPFASAQIGKSFRNEISPRAGLLRVREFTMAEIEHFVDPEDKNHDRFDEVKHINVPLLAKDVQESGKTDITIKTIGEAVSAGIIDNQTLGYFIGRIYLFLVKIGIDATRLRFRQHMSNEMAHYASDCWDAEIHTSYGWIECVGCADRSAYDLTVHSKRTKKDLVVQKAHKEPKVYDALVPTIVKKNLGPKFKKDAKFVEEAILEMNQQQLAKLQRKLKNGSARLSICTGETYVLTTDVVTVEMKTIRETVREFTPNVIEPSFGIGRIFYSLLEHSFWTRAEDQDRGVLSLPPLVAPIKASIVPISSNEKLSPLVKQVSRKLRSAGVASRVDDSNASIGRRYARNDELGTPFACTLDFASLSKGTMTLRERDTTAQRIGPIDQVIDVIRQLCDGSLDWEGACKILPEYSGQQDVEG | [
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24979,
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58077,
61977,
64364,
72021,
87110,
87145,
87367,
87722,
87855,
87968,
88008,
88153
] | The following text describes a protein:
Function:
Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.
Subcellular Localization:
Cytoplasm. | 0 |
MKGTRAIGSVPERSPAGVDLSLTGLPPPVSRRPGSAATTKPIVRSVSVVTGSEQKRKVLEATGPGGSQAINNLRRSNSTTQVSQPRSGSPRPTEPTDFLMLFEGSPSGKKRPASLSTAPSEKGATWNVLDDQPRGFTLPSNARSSSALDSPAGPRRKECTVALAPNFTANNRSNKGAVGNCVTTMVHNRYTPSERAPPLKSSNQTAPSLNNIIKAATCEGSESSGFGKLPKNVSSATHSARNNTGGSTGLPRRKEVTEEEAERFIHQVNQATVTIQRWYRHQVQRRGAGAARLEHLLQAKREEQRQRSGEGTLLDLHQQKEAARRKAREEKARQARRAAIQELQQKRALRAQKASTAERGPPENPRETRVPGMRQPAQELSPTPGGTAHQALKANNTGGGLPAAGPGDRCLPTSDSSPEPQQPPEDRTQDVLAQDAAGDNLEMMAPSRGSAKSRGPLEELLHTLQLLEKEPDVLPRPRTHHRGRYAWASEVTTEDDASSLTADNLEKFGKLSAFPEPPEDGTLLSEAKLQSIMSFLDEMEKSGQDQLDSQQEGWVPEAGPGPLELGSEVSTSVMRLKLEVEEKKQAMLLLQRALAQQRDLTARRVKETEKALSRQLQRQREHYEATIQRHLAFIDQLIEDKKVLSEKCEAVVAELKQEDQRCTERVAQAQAQHELEIKKLKELMSATEKARREKWISEKTKKIKEVTVRGLEPEIQKLIARHKQEVRRLKSLHEAELLQSDERASQRCLRQAEELREQLEREKEALGQQERERARQRFQQHLEQEQWALQQQRQRLYSEVAEERERLGQQAARQRAELEELRQQLEESSSALTRALRAEFEKGREEQERRHQMELNTLKQQLELERQAWEAGRTRKEEAWLLNREQELREEIRKGRDKEIELVIHRLEADMALAKEESEKAAESRIKRLRDKYEAELSELEQSERKLQERCSELKGQLGEAEGENLRLQGLVRQKERALEDAQAVNEQLSSERSNLAQVIRQEFEDRLAASEEETRQAKAELATLQARQQLELEEVHRRVKTALARKEEAVSSLRTQHEAAVKRADHLEELLEQHRRPTPSTK | [
8747,
9051,
10112,
13491,
17404,
18977,
19866,
23397,
23543,
23969,
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24869,
25026,
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25315,
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26048,
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32074,
32382,
59823,
87139,
87272,
87278,
87312,
87367,
87369,
87371,
87402,
87407,
879... | The following text describes a protein:
Function:
Component of centriolar satellites contributing to the building of a complex and dynamic network required to regulate cilia/flagellum formation. In proliferating cells, MIB1-mediated ubiquitination induces its sequestration within centriolar satellites, precluding untimely cilia formation initiation. In contrast, during normal and ultraviolet or heat shock cellular stress-induced ciliogenesis, its non-ubiquitinated form is rapidly displaced from centriolar satellites and recruited to centrosome/basal bodies in a microtubule- and p38 MAPK-dependent manner. Also acts as a negative regulator of BBSome ciliary trafficking. Plays a role in sperm flagellar formation; may be involved in the regulation of intraflagellar transport (IFT) and/or intramanchette (IMT) trafficking, which are important for axoneme extension and/or cargo delivery to the nascent sperm tail (By similarity). Required for optimal cell proliferation and cell cycle progression; may play a role in the regulation of genome stability in non-ciliogenic cells. Involved in centriole duplication (By similarity). Required for CEP152, WDR62 and CEP63 centrosomal localization and promotes the centrosomal localization of CDK2. Essential for maintaining proper centriolar satellite integrity.
Miscellaneous:
MISCELLANEOUS: Transient cell cultured-based knock-down (by RNAi) of CEP131 leads to a reduction in ciliogenesis. However, analysis of mice with chronic absence of CEP131 following genetic deletion (knockout) shows that cilia develop and function normally in vivo. This suggests that CEP131 is not essential for ciliogenesis, except for the modified cilia of the developing sperm flagella, and that there is an alternative mechanism to compensate for the lack of CEP131.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasmic vesicle, secretory vesicle, acrosome. Note=Colocalized with pericentriolar material protein PCM1 at centriolar satellites. During spermiogenesis, becomes enriched with nephrocystin NPHP1 at the transition zone, a structure at the base of the ciliary axoneme important for regulating traffic into the ciliary compartment. Traffics towards and away from the centrosome/basal body and the transition zone of the ciliary axoneme in a microtubule-dependent manner. Localized at the Golgi-derived acrosome and the centrosome-containing head-tail coupling apparatus (HTCA) (By similarity). Ubiquitinated form is sequestered and colocalized with BBS4, CEP290, PCM1 and PCNT at centriolar satellites in proliferating cells. Colocalized with the pericentriolar material protein PCM1 at centrosome. Traffics towards and away from centriolar satellites and centrosome in a microtubule- and dynein-dependent manner in interphase cells. Displaced from centriolar satellites but still remains associated with the centrosome in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, in a process that requires p38 MAPK signaling. | 0 |
MAAAQAMAKMSVGSPACNRAAGSLCRWRGAVAVRLGGSWSWRKSPFLGGRMAVGPRRSRPVSRNPVASPVQMNLSFGKTMKWWEKGLQPNMRAIHTAQELVDSLINAGDGLVIVDFFSPGCAGCHALHPKICQFAERNPDVQFLQVNFEEHKSMCHSLHVHVFPFFRFYRGAQGRLCSFSCTNATIKKFKDALAKHKPDRCSLGPIKGLEESELLALAANRDLQFTYTKEQDLAPSMEDGAEVITHDHPRLPAAAKPLVRQGSEDRAVVSSGR | [
15142,
25225,
47521,
64016,
87413,
87425,
88007,
88008,
88162
] | The following text describes a protein:
Function:
Probable thiol-disulfide oxidoreductase that may participate in various redox reactions. | 0 |
MDMFPLTWIFLALYFSGHEVRGQADQPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPDKYPHNLDCTFTILAKPKMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSELRSATGILSLTFHTDMAVAKDGFSARYYLVHQEPLENFQCNVPLGMESGRIANEQISASSMYSDGRWTPQQSRLHGDDNGWTPNLDSSKEYLQVDLRFLTVLTAIATQGAISRETQNGYYVKSYKLEVSTNGEDWMVYRHGKNHKVFQANNDATEVVLNKLHSPLLTRFVRVRPQTWHTGIALRLELFGCRVTDAPCSNMLGMLSGLIADSQISASSTREYLWSPSAARLVSSRSGWFPRIPQAQPGEEWLQVDLGAPKTVKGVIIQGARGGDSITAVEARAFVRKFKVSYSLNGKDWEHIQDPRTQQPKLFEGNMHYDTPDIRRFDPVLAQYVRVYPERWSPAGIGMRLEVLGCDWTDSKPTVETLGPTVKSEETTTPYPTDEEATDCGENCSFEDDKDLQLPSGFNCNFDFPEEPCGWMYDHAKWLRSTWASSSSPDDRTFPDDRNFLRLQSDGRREGQYARLISPPVHLPRSPVCMEFQYQATGGRGVALQVVREASQESKLLWVIREDQGGEWKHGRIILPSYDMEYQIVFEGVIGKGRAGEIAIDDIRISTDVPLENCMEPISAFAGENFQVDIPEIHGREGYEDEIDDDYEVDWSNSSSPTSGSGAPLADKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYSGLSSRSCTTLENYNFELYDGLKHKVKMNHQKCCSEA | [
6890,
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26414,
27093,
28788,
29141,
30495,
32536,
36286,
36657,
36769,
43563,
47128,
48237,
54532,... | The following text describes a protein:
Function:
High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
Subcellular Localization:
Membrane; Single-pass type I membrane protein. | 0 |
METIAKHRHARSSAQKVRLVADLIRGKKVSQALETLTYTNKKAAGLVKKVLESAIANAEHNDGADIDDLKVTKIFVDEGPSMKRIMPRAKGRADRILKRTSHITVVVSDR | [
8138,
25435,
27932,
30795,
36823,
40768,
51022,
64152,
73776,
88001,
88008,
88020,
88022,
88277
] | The following text describes a protein:
Function:
This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity); The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. | 0 |
MKVKEETLKNLGDGVVLRPVDHCSSIWSMKMNMKNFLKKLHISPNQSDEAEGSISTTKSNHHKSIDVSSSSSPRSHHSNSPEIKPFSGLSNWLSSVGHRKIPSPPNSFNAKNRAATVDDTVVVNGSEHVDLGSKDPAVEEENQIQLALELSAREDPEATQIEAIKQFSLGSCAPENSPAELIAYRYWNYNCLGYDDKILDGFYDLYGVLNASSAERIPPLLDLQGTPVSDGVTWEAVLVNRSGDSNLLRLEQMALDIAAKSRSVSSSGFVNSELVRKLAILVGDYMGGPVVHPESMLRAWRSLSYSLKATLGSMVLPLGSLTIGLARHRALLFKVLCDSVGVPCRIVKGQQYTGSEDVAMNFIKADDGREYIVDLMGDPGTLIPADAAGLQIDYDESAYSASPGDNDSIHVASSSNGIESSYEENTEFRTGEHRSSTKSSGERNQSGGGGDLIVHPNISREDVKNQKKVEKAPFQNLSSRPIHSFTHMRSPSWTEGVSSPAAQRMKVKDVSQYMIDAAKENPRLAQKLHDVLLESGVVAPPNLFSEVYPQQLEATVESKNSTEAKKERGKDLETTQEGRHQNGFGPVRFLPPLPRVQSKTNAHDQRDNGKVVSQSDSSHSEASSTEYARTVPAAVAAAAVVASSMVAAAAAKSANSDSSPIELPAAAAATATAAAVVATAAAVSRQLELGSNSDGDDGSGGHEPQGSGDSNHGPNSGGERISDKSIGNESSKSDCDDVSDCEILWEEITVGERIGLGSYGEVYRGDWHGTEVAVKKFLDQDLTGEALEEFRSEVRIMKKLRHPNIVLFMGAVTRPPNLSIVTEFLPRGSLYRLIHRPNNQLDERRRLRMALDAARGMNYLHSCNPMIVHRDLKSPNLLVDKNWVVKVCDFGLSRMKHSTYLSSKSTAGTAEWMAPEVLRNEPADEKCDVYSYGVILWELFTLQQPWGKMNPMQVVGAVGFQHRRLDIPDFVDPAIADLISKCWQTDSKLRPSFAEIMASLKRLQKPVTGSNIPRPVPSSSSLPTEHEQKD | [
3604,
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9717,
24917,
24979,
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28548,
29033,
35176,
36535,
36977,
39128,
42974,
45290,
50333,
77334,
80685,
87110,
87694,
87855,
87857,
88008,
88052,
88086,
88153
] | The following text describes a protein:
Function:
Acts as a negative regulator of salt tolerance. Mediates sugar response during early seedling development.
Subcellular Localization:
Nucleus. Note=Colocalizes with UGT72E1 in the nucleus. | 0 |
MAGPGWGPPRLDGFILTERLGSGTYATVYKAYAKKDTREVVAIKCVAKKSLNKASVENLLTEIEILKGIRHPHIVQLRDFQWDSDHIYLIMEFCAGGDLSRFIHTRRLLPEKVARVFMQQLASALQFLHEQNISHLDLKPQNILLSSLEKPHLKLADFGFAQHMSPWDEKHVLRGSPLYMAPEMVCQRQYDARVDLWSVGVILYEALFGQPPFASRSFTELEEKIRSNRVIELPLRPPLSRDCRDLLQRLLERDPNRRISFQDFFAHPWVDLEHMPSGESLARATALVVQAVKKDQDGDAAAALSLYCKALDFFVPALHYEVDAQRKEAIKAKVGQYVSRAEELKAIVSSSNQALLRQGTSAQDLLRDGPGQTSAPRGPGSGFGCHGQGGGGWWGAGCPGPVPACPGGVAGAAGSGAHRPEAGAASHRGSEPHGSSRIPEGAGQDEGVSLGSRDPGQGGTVRVRSYLVHPAVTPEG | [
3604,
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45290,
50333,
63953,
71481,
87110,
87194,
87367,
87694,
87855,
88008,
88009,
88052,
88153
] | The following text describes a protein:
Function:
Serine/threonine protein kinase that acts as a regulator of Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative regulator of SHH signaling in the absence of SHH ligand: interacts with SUFU, thereby inactivating the protein kinase activity and preventing phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively regulates SHH signaling in the presence of SHH: dissociates from SUFU, autophosphorylates and mediates phosphorylation of GLI2, activating it and promoting its nuclear translocation. Phosphorylates in vitro GLI2, as well as GLI1 and GLI3, although less efficiently. Also acts as a regulator of autophagy: following cellular senescence, able to induce autophagy.
Subcellular Localization:
Cytoplasm. | 0 |
MHLQNTHNTMESNAAMDAASPASRDVRQFHDLITCRLCRGYMIDPTTVDYCYHTYCRSCILKHLLRAVYCPECKASGGKEINELNLKSDDTLRSLIYKLVPGLYQRECKELADFKEQHDLVDEQTTDEPEFFTTTELISLSLEYHPAMLHQCGPGEVPPTIYLQCAAGLPVELLKRFLCSKYNIETDNGLVEVEVTYKDEVLPTNFTLMDVAYCYNWSRESPMAFCYRILLYDNEQTKNDENNLSRINQDIEPEHSVRRSKSAKSVTFAEDLESEIDSGSPRSKVRCKTPPKVSPSSKNKRLTSSKREAEPESPVSNFKSLRSNDMRYSDYAVSKVKSEPEQEQFLLPREREQQPLEANTNIVVSIPPSQLRKSYVDAEDFELKTANRKGVGHLPKLKIELNSMKSKLSMPLSAGPRLEDTSCSLSCSAQQLDLETYAKNIGLKPIEQPLQQSASNPDSKYSPNASPMSSCSSSTNGSSSSLGTADASTSTSTSSSHRKRKKKHSKEPKDANGKRKKLHAEISSQTDGKMKVKITAKPNHKLDFKRSHSLASGELDLQKLKLDSTSTSEALNRTLGEEARSINSLVVGGAPTPPPTPTAEPEQQQQQQQQQQQPQQQQQQQQQQQQQQQFVVLPKIKDLTLPTSPPLPPSLFKAYTPSTTPTAPHTVAGGKPKQQQQQMPQQPQAVLQQSLAKTNPAKPPLSSNNNRKPNSGHFAVPQAPTHRNMYHMQRYQSTPSSIASAANKMPKRSMSLDESHPAKQARLSQAQAMASSYAAKLHMQTSNQAKSQAAAFLPNPQMRSYGLPDLGSKPTLPMLCPASSSSQVTITPRPRATPSIYSFSEPNIHVPALEIVRLPVNKQSAGGKGLTMPPLSPPATSSARLMGPPAALPKHAGHGHGAAKRSCQMPTMPMPLPLPLPMPMTTIPAIVKSPPLSVALSGQRNNKGNSSNSNAYRTSPPALINLRNTAAPQHSFPSKSSPKVEANSKKSPPAAGCQGKTNGTAALDKSKTSLREFRPAVQSAVTATATTSVTTAAGAGAGAGTGTGTALAKDADILDLSANPGRSNNDAKLAPNSPPAGNNNNNNNNNNNNNNNNNNNNNNSTSNSLEAALNKIKQNISANSNGGPSTTSGSNSNGTTNGDDLQNLHMLSESATAREKISIKAASSGNGSGSTSSSSAKPKNANALVRPQNASVRSIPNPSALAFRNQPAAASTAASISKPLTVRAEEKPKVSTSNPGSLSPTNTSSSSSSSSSGSSGCSAATSPRAMTKKPTTIDQVAANLNIRAEAKAAALAEEAPPVLSSNAAKSPELAKTTTAVALRPEPKETPITVSAASTLLTIPSAVSSVSAVPETMAKPPVQIANAPVASSA | [
6673,
12057,
24917,
25996,
27904,
29166,
35929,
37468,
46929,
50763,
51583,
61204,
87384,
87402,
87767,
87857,
88008,
88261,
88263
] | The following text describes a protein:
Function:
Regulates expression of the homeotic selector genes by influencing higher-order chromatin structure through interaction with other proteins.
Subcellular Localization:
Nucleus. | 0 |
MLRTIRPARTTLVRAVRPVRPVSGRVGRLGRHVTTGTTSSTTSASSPDLSTTLAMAIEQQGPMSVATFMKHCLTNPSGGYYIDKDPLGAKGDFTTSPEISQMFGELVGLWLAAQWLYYGQKQPFRVIEYGPGRGTLMDDSLRALVSAKSTGAKEALKEVLLVEASPVLRDAQRKKLCGAESQFKTEEDGSITCVTKYGVPIRWYEDSKMLDKLASSNDPLHNYIVAHEFFDALPIYQFEKTDKGWRELMVNYGVENKTKESSILLPGQTHIKSSDLDKDKKKTFHLVTAPTWTVASKVIPQSHKRYRDLPEWSKIEVCPDAWDVANQMGRLVAKGGAAFIVDYAVKPGVPVNTLRGIRDHKICSPFEEPGKVDLSADVDFTAIGIASRSKNKENVSAFGPINQATWLKNMGIEMRTEKLMEGKEEYIKKRIESQYKRLVDIGINGMGKIYKAFFLTHSSHGYPVGFPIPEPKDLKEPHQKPEKDPKDTEPKVVEV | [
2291,
12244,
12589,
24979,
31766,
39033,
59229,
65875,
87777,
87785,
88008,
88153
] | The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion. | 0 |
MDFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIECSKGISTGAGIVLWNDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKGIVGVSEITNHTKTNMWVVKHFLDVDFEIKEYKENNCNGFTIEVV | [
6530,
8125,
24978,
28053,
29033,
36129,
47537,
47538,
50641,
52882,
55540,
64296,
64840,
87110,
87367,
87722,
87855,
88008
] | The following text describes a protein:
Function:
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Subcellular Localization:
Cytoplasm. | 0 |
MLTDPDLPQEFERMSSKRPASPYGETDGEVAMVTSRQKVEEEESERLPAFHLPLHVSFPNKPHSEEFQPVSLLTQEACGPRTPAAQHSTMEVDGNKVMSSLAPYNSSTSPQKAEEGGRQSGESVSSAALGTPERRKGSLADVVDTLKQRKMEELIKNEPEDTPSIEKLLSKDWKDKLLAMGSGNFGEIKGTPESLAEKERQLMGMINQLTSLREQLLAAHDEQKKLAASQIEKQRQQMELAKQQQEQIARQQQQLLQQQHKINLLQQQIQVQGQLPPLMIPVFPPDQRTLAAAAQQGFLLPPGFSYKAGCSDPYPVQLIPTTMAAAAAATPGLGPLQLQQFYAAQLAAMQVSPGGKLLGLPQGNLGAAVSPTSIHTDKSTNSPPPKSKDEVAQPLNLSAKPKTSDGKSPASPTSPHMPALRINSGAGPLKASVPAALASPSARVSTIGYLNDHDAVTKAIQEARQMKEQLRREQQALDGKVAVVNSIGISNCRTEKEKTTLESLTQQLAVKQNEEGKFSHGMMDFNMSGDSDGSAGVSESRIYRESRGRGSNEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKAMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFNVGQQAQIPIATAGVVYPGAIAMAGMPSPHLPSEHSSVSSSPEPGMPVIQSTYGVKGEEPHIKEEIQAEDINGEIYEEYEEEEEDPDVDYGSDSENHIAGQAN | [
6879,
6947,
7163,
8103,
11496,
12276,
15076,
15387,
16288,
16732,
17178,
17338,
17899,
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24446,
24917,
24936,
27731,
27733,
27735,
27736,
27918,
43634,
64639,
77009,
87123,
87139,
87326,
87384,
87407,
87857,
87914,
88008,
88148,
88150
] | The following text describes a protein:
Function:
Transcription factor involved in chondrocytes differentiation and cartilage formation (By similarity). Specifically binds the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes, such as COL2A1 and AGC1 (By similarity). Required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active enhancers and super-enhancers associated with cartilage-specific genes, and thereby potentiate SOX9's ability to transactivate. Not involved in precartilaginous condensation, the first step in chondrogenesis, during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX6, required to form and maintain a pool of highly proliferating chondroblasts between epiphyses and metaphyses, to form columnar chondroblasts, delay chondrocyte prehypertrophy but promote hypertrophy, and to delay terminal differentiation of chondrocytes on contact with ossification fronts (By similarity). Binds to the proximal promoter region of the myelin protein MPZ gene (By similarity).
Subcellular Localization:
Nucleus. | 0 |
MERVALYILTMDAINFCFWPVSEAKDATNSVKNGLEYEHLAIGLRKLAELDDGNSQVNVKTSESGVYELPDMQIRCQLLNELGKGLLEQHGGSALQMISKANQSADALVRIIMDTFPGFRDYVDTDASGEWETVKASLTAIHLHKRAQIATADIWAALGRCNDQSVQTTNTTNPEHAKLFTCCHFTDMDAVTTFPDYRVPQILRHVAVLRYGSQLANLIDNQLELEKSGMDEVSIRASTVVAVEELLSDDVSAVTIDWYLWQKGERLDRANQLEPHHRVRTTFY | [
4437,
8129,
30332,
51982,
87601,
88008
] | The following text describes a protein:
Function:
Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly. | 0 |
MNIVKLQRKFPILTQEDLFSTIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDDYVGLVAKLRESKTGAAPQTTFNVAPNSTPIVSTAATGLQHKGKGTQAKIIVAGSQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDIKLHPELYRLLEDDETLEQFLRLPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFNTHPGLEPIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASGAEISRFKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGALIWLVPEDINEVRARLIITFIASLMTLNK | [
8572,
16631,
16939,
18575,
24978,
25077,
25079,
25111,
25503,
25771,
26245,
31013,
32536,
33717,
37264,
37370,
46081,
64602,
67202,
87118,
87244,
87767,
88008,
88009
] | The following text describes a protein:
Function:
Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity.
Miscellaneous:
MISCELLANEOUS: Present with 3510 molecules/cell in log phase SD medium. | 0 |
MRFRPSIVALLSVCFGLLTFLYSGSAFAVDKSQLTYDDIVNTGLANVCPEISSFTRGTIEVEPNTKYFVSDFCMEPQEYFVKEEPVNKRQKAEYVKGKVLTRQTTSLEQIRGSIAVGADGTLTFKEKDGIDFQPITVLLPGGEEVPFFFTVKNFTGTTEPGFTSINSSTDFVGDFNVPSYRGAGFLDPKARGLYTGYDNAVALPSAADKFRTNKKETPLGKGTLSLQVTQVDGSTGEIAGIFESEQPSDTDLGAKEPLDVKVRGIFYGRVDTDV | [
9738,
14268,
25262,
25455,
25692,
29683,
38111,
45476,
87103,
87411,
87752,
87760,
87919,
87921,
88008,
88058,
88139
] | The following text describes a protein:
Function:
One of the extrinsic, lumenal subunits of photosystem II (PSII), which stabilize and protect the oxygen-evolving complex. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation. Required for dimerization of PSII and for binding of PsbQ to PSII.
Subcellular Localization:
Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side. Note=CyanoQ (PsbQ) binds to the large lumenal domain of PsbC (CP43) between PsbO and PsbV. | 0 |
MATYQPYNEYSSVTGGGFENSESRPGSGESETNTRVNTLTPVTIKQILESKQDIQDGPFVSHNQELHHVCFVGVVRNITDHTANIFLTIEDGTGQIEVRKWSEDANDLAAGNDDSSGKGYGSQVAQQFEIGGYVKVFGALKEFGGKKNIQYAVIKPIDSFNEVLTHHLEVIKCHSIASGMMKQPLESASNNNGQSLFVKDDNDTSSGSSPLQRILEFCKKQCEGKDANSFAVPIPLISQSLNLDETTVRNCCTTLTDQGFIYPTFDDNNFFAL | [
6794,
6795,
6796,
8047,
8050,
8065,
8072,
8086,
8564,
8643,
10121,
10753,
11741,
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24793,
24931,
26044,
27912,
27917,
32009,
32185,
39537,
46277,
48235,
48394,
64146,
64148,
67426,
87103,
87381,
87384,
87411,
87857,
87914,
88008
] | The following text describes a protein:
Function:
Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Miscellaneous:
MISCELLANEOUS: Present with 6080 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. | 0 |
MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN | [
14256,
24878,
25325,
25414,
26161,
27319,
29037,
32528,
34624,
37464,
43575,
87103,
87411,
87413,
87436,
87573,
87586,
87760,
88008,
88038,
88058,
88146,
88240
] | The following text describes a protein:
Function:
The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.
Subcellular Localization:
Secreted. Host cell membrane. | 0 |
MEVDEDIELQKHQEQQSRKLQRFSEDNTGLMRNWNNPSSRIIRVSRASGGKDRHSKVLTSKGLRDRRIRLSVATAIQFYDLQDRLGFDQPSKAVEWLINAASDSITDLPLLNTNFDHLDQNQNQTKSACSSGTSESSLLSLSRTEIRGKARERARERTAKDRDKDLQNAHSSFTQLLTGGFDQQPSNRNWTGGSDCFNPVQLQIPNSSSQEPMNHPFSFVPDYNFGISSSSSAINGGYSSRGTLQSNSQSLFLNNNNNITQRSSISSSSSSSSPMDSQSISFFMATPPPLDHHNHQLPETFDGRLYLYYGEGNRSSDDKAKERR | [
8101,
9052,
16085,
24917,
27904,
27918,
40409,
50746,
50747,
87384,
87402,
87857,
88008,
88148,
88150
] | The following text describes a protein:
Function:
Plays a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164). In association with ABAP1, exerts a negative role in cell proliferation in leaves, possibly by inhibiting mitotic DNA replication. Participates in ovule development.
Subcellular Localization:
Nucleus. | 0 |
MLNHWFVLLNTNHFFSFPKTCLRFLMVKFEKKTKYTENSFPVKFEKKIKYTGNKIPDELPHAFFLGIVLLTAVFILYFVGFIFYSAIPVFESQGIINFITGDSWNNGNFGIRNFIVGTLIITAVTIILAVPPSIFTAIFLSEFASPKVVSVFRPLIELLVGIPSVVYGIFGLYVLADILKHVDPIISSIFYFIPFMRDTTPGQGDGVFLSSVVLSIMILPTIITISEDSIRAVPGVYREASFALGATKWETIRHVVLPAASGGILSAVVLGIMRAMGETMAVVMLIGNINRIPSSIFGYTLPMTTKIVTSVGENIGNPDVLSALFGIAAVLFALEILLAGFAKLLVRRCKY | [
13356,
25079,
28948,
36363,
45955,
63707,
76778,
87276,
87760,
87907,
88008,
88159,
88161,
88162
] | The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. | 0 |
MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEDRRVIADDEIISLSIEFFHPSRSDRKVTKEKPKEEVNDKRYLRCPAALTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSQQRDGLTAAGELESDSGSDKANSPAGGAPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSGNHQSSFASRPRKSSVNGSSATSSG | [
6673,
6878,
6947,
8091,
8095,
8096,
8538,
8844,
9888,
11475,
11608,
11854,
12639,
15339,
15969,
15984,
16283,
16285,
18848,
18983,
19769,
20123,
23989,
24654,
24729,
24791,
24917,
25040,
25365,
25671,
25996,
27908,
29166,
34401,
34635,
35929,
3... | The following text describes a protein:
Function:
Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2.
Subcellular Localization:
Nucleus. | 0 |
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCESPDDQRYFEEETFSKLIEDSDFVFKRDPALNKKENRGCDSPDPDGSYVLTPHTEEKYKKINEEFDNMMRSHKISPGLPQQTFPMSVTVPVSNPNTLPYSSPGNTMVTASLAASASLTDARMLSPPPTTLHRNVVSPGLPQRPPSTGNAGVMLCSSDLSVPNGAGTSPVGNGFVNPRASPSHLGPTGGNVLGKVMPTKSPPPPGGNLVMNSRKPDLRVVIPPSSKGMMPPLNTQRVTSSQGTQPLATPIVSVATPSLAPQGLIYSAMPTAYNTDYPLTSADLSMLQGFNSPGILPLGQVSAWQQHHVGQAALSSFVATGQLSQGSNLSINTNQNINIKSEPISPPRDRITPSGFQSHQHHQHQPRPEMDSLSSSSSSYDGSDREDVRNDFHSPIGLGRPANNEDRDSPSVKRMRMDAWVT | [
9561,
11620,
15427,
24917,
27733,
27735,
30811,
32079,
32185,
32578,
37681,
54083,
62119,
64609,
87123,
87384,
87402,
87857,
87914,
88008,
88148,
88150
] | The following text describes a protein:
Function:
May regulate muscle-specific transcription in the embryo and may regulate transcription of a variety of cell types in the adult. Binds to the sequence 5'-CTA[TA]4TAR-3'. Acts downstream of nlk2 in anterior neural development, including eye formation.
Subcellular Localization:
Nucleus. | 0 |
MRTTLPRCLVLSVCICLECNVALASFGVLSRSKPLVLDSDQNQSVKKFCQQHRKEARLRRFCSVDPGLVQAIVHGTRLTVDSCQSLFQWEPWQCDLLQDKRRHLLKKVYRETALVYALAAAGLTHSVARGCSSGRLSSRCSCNESGSRTLSATESDQNWKWGGCGDNYSFSAKFSRKLLARNKSRRPRTLRRPVDNHNLVVGIRVLRHGIRRVCKCHGLSGSCSAKTCWEELAHFPDVAKALKRKYSKAIMAQVENKPDFASTEVVSKLKKTLLTRTTQKPKWLRAVTAELQRLGRDRLVYLEESPSFCERNVLTGGMSQRRCRDHAHCEQVCCGRGHRSFSETVQERCHCRVVWCCQLECKTCTVLKYSHSCH | [
11632,
15076,
17278,
24907,
28820,
28832,
40849,
50944,
69846,
87402,
87413,
87453,
87735,
88008,
88038,
88058,
88256
] | The following text describes a protein:
Function:
Ligand for members of the frizzled family of seven transmembrane receptors.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. | 0 |
MWREAMMELLDQLEAENPEDPALAPKDLSEWACIYIKYLQIMRKLETAYDQMVHPQKRQDMRKALEACIGRMLEIRHWMVKLNRGLDFINLDDILVDLKLGPEVLEVPVPKYFIEDRAKELDDRDKFLEALIEKYNVKGPAASPIIRIGAPLGEDEAILMIQKNERGRQARERARLAAITKRQRQIEDRRVRLGVTLSHEEAARKIQAAIRGFLWRRRIKKEADKELMFIGMKPKPRDPKRDPQMGEAKNLMRRKRVQLEHGREYDEAIVNLKGKVRELEGQDMRETIQDKVNAWFVEKRNPDTGEYPDFPDPDDGGSRAILNPPPPSLASLLEDAAGDGKGKGKDGKGDAKKDAKKDPKKDKKGGGDEPQAEEQKIGAVFIPAIEAAVQEFVAKWQDRDEADNFHQKYDAELVKDELRPIVFEEIRLQVDGEMRVLLQNLKDLVEAERAAKLGKKGKKKKGKKKEPFSRIKKELLKEAKTLAPGERVLVLGNSREPYLCAKKDEKDAAGDGKGKGKDGKGGGKPGTAGSKPGTADKKKKGGKKKSLCSDWSCGA | [
25109,
25668,
35989,
77917,
87278,
87311,
87367,
87371,
87468
] | The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. | 0 |
MSPWIKHICLVLVAAFMLVKTTESKKDEALYCSACMAIADEINYSISQTDPKKMIHVGGFRLKPDGSLTDKKVPLARSETYLTELLEEVCKSMSDYALYENPDTKEKSYKRFAPRDNDGGNFPDFKNFKFDGPESSSALKFACESIVEELEDDIISLFASDSDHVAKTLCSEVSDHCKSSVFQHSEL | [
8802,
9091,
11864,
14028,
18338,
25008,
53848,
69346,
87402,
87413,
87432,
88008,
88058
] | The following text describes a protein:
Function:
Involved in the maintenance of the midbrain-hindbrain boundary (MHB) organizer. Contributes to a positive-feedback loop of FGF signaling in the MHB, enabling the MHB to exert its role as an organizer for the tectal and cerebellar development.
Subcellular Localization:
Endoplasmic reticulum. | 0 |
MASVPCSFKLSAHRRSSSKLDGNNKQCSSLVERLRDKTKSQVPKSITCINRLEISRIAPLHATMNSPKGFGPPPKKTKKSKKPKPGNQSDEDDDDEDEDDDDEEDERERGVIPEIVTNRMISRMGFTVGLPLFIGLLFFPFFYYLKVGLKVDVPTWVPFIVSFVFFGTALAGVSYGIVSSSWDPLREGSLLGWNEAKKNWPVFWQSFWNSSDKR | [
9738,
25225,
25238,
25248,
53851,
87296,
87760,
87919,
87921,
87930,
88008,
88139,
88154,
88159,
88161
] | The following text describes a protein:
Function:
Involved in early steps in photosystem II (PSII) biogenesis and in maturation and stability of newly synthesized psbA protein.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | 0 |
MALRLAGVSLRLLWVLVIAVTGLKPRKPSDTCFVTKELPFHVSTSSITESKAGNFMASIANGYVGTVVMSNSVHVSGLFNGKGWPKRYPIYPIYMSEHAHRARLPSTASISFKVHDNDVVYINGTRSYALDVKTGVFYSWFEETNENGSLFIEMRYYAHRERRNLLINEITIKNDLNKEITLDLSNNYGNFSKDVKLTQHTVSEKEELEIAFGKVNIPEEKFGLQPQVALAFRDIKEHIFINASEWRTWYYITAIATSIDTKFDPWRQAEGAWKEAMRDKRHLLWHHTKAWEELWESGKVDVVTKDKSSHLGQAIYGSLYYLLSSTRADWPYGLSPGGLPGGEEYMGHTFWDQDIWMYPVMVLLYPDLARASLRYRYDRLPAARRIARKWGYKGAMFPWESSLSGIETSPGEKYGRYQNHITGDIAYAAQLYWHATKDYQWLKEIGYALAYQTAEYWASRVSFDNRKEKYVIEYVMPPDEYQFPVDNSVYTNVVAKINLEFAVKVCTLLGRYYPKMWVKIAEQMYIPFDSDRNFHPEFDLYDLGYQAKQADTILIGYPLMYNMSRQVRYNDLLTYENRTDPEGPAMTHAMFAIGWLEVGEEERAAKAFLKNYEHIEQPFQVWTEQRRKRGAINFITGAGGFLQAVLFGYGGFRIREDQLYFDPKLPPTSNTFTITGVDYLGSSLKFIIKNKKMRITLTEREQIAPALELVIYKKVYPLEHKNTLLLLRGPGFIRMRRD | [
4276,
7854,
28423,
32824,
40287,
40288,
43533,
46278,
87523,
87601,
88008,
88058
] | The following text describes a protein:
Function:
Catalyzes the hydrolysis of glucose from the disaccharide unit linked to hydroxylysine residues of collagen and collagen-like proteins. | 0 |
MNNDHASKKSFCIKAPSNWEKSYLEVWPLVTVPRQCICLRWCISKEYHEFTCSSLQFIVIRPAGTSVLLGRVKSSKANQLVGIEHVEGSRYALIFLSEKLDFKSLKVIANHQLTKSSKSLSNVSNKPLGDQLFRSNSLMSPSLLKKELHRIQSDASQANERESQAPHSFVTHDLISSSKDGNSLTHEFANDSVTEMVQDYTPSCSRDVKSLLDHLYNSYFYQLLMTKTPVVFYVKQMVGKTRQLAVEVHNHVEEKALVDELLKFLDNLKSVDDRKSRLLQCFESHLNYKAWHLEFENEAHQYEIKGYRLWLQNILNRENCQITKLDFEREFSQLKLKEYEIRVLLYFEILYLFLKWDPEYARRRANDNSLLDSRDSGKRKSRKKNAKTLNPFETAQLKLEFTFDGLCIRRTIEQNATERSEDLLLKFCKETIVPYYSSKFPRITRNLLEKCNGLDLLPERSHKHRHSAPPRSKLISSKSEAGRALPGNTSGASISNTSSPHSEASISKDYEILKRRRSNSGVHSLTRSDSSFNGFERDTRRRSSDIARIKNREINLPSSSLSKQRNSMHDISTNFPRRNLSFTEKLTMASLQGQSEESVQPKTTSSLSRSKTLSILEGSVSKRSEPSMDSILVQATPRKSSSVITELPDTPIKMNSLDKASACTVENHIVTESPAHKSNKAQLFVCVPTTPVKKKSASP | [
8055,
16800,
22297,
24788,
25617,
47672,
69414,
87103,
87272,
87381,
87757,
87857,
87914,
88008
] | The following text describes a protein:
Function:
Required for loading and maintenance of stable association of cdc45 with chromatin during initiation and elongation of DNA replication. Also involved in temporal regulation of origin firing. Plays a role in meiosis.
Subcellular Localization:
Nucleus. | 0 |
MSRGTNLFVAFSISGIVWIVTLFLSTGYVNEVAKSMPTYALILYFSYALFKVGGDLARLKDYPEEAQSLQKEVEEAKRFYKEKGLKL | [
8188,
25014,
25853,
47001,
87432,
87760,
88008,
88159,
88161
] | The following text describes a protein:
Function:
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. | 0 |
MAHSSDTARKDMTNGAHPSAQPGPSGTSTLPRYLHKKQQRQRGVRSSSPMGRVILINAPVDGGDDSEDIHTITVDKSEDGHLGFSVRGGSEHGLGIFVSKVEDDSTAEMAGLCVGDKLVEVNGISLESITMSSAVKVLTGNNRLRMVVRRVGKVPGIRYSKEKTTWVDLIHRRMVVEESGRTPSEASSDGALRRIVHLYTTSDDYCLGFNIRGGKEFGLGIYVSKLDPGGLAEQNGIKMGDQILAANGVSFEDITHSNAVEVLKSHTHVMLTIKEAGRYPAYKEMVAEYSWLNKLANGGQPSSSQGSDSYSSTSSLSSGTPVSSLSGLSQVTFPPAFGSEMVDVCISTEDRSRRPSSERIETAIQTDPQDPDTISRTSRVMSTETSRMVGETVLLKDTVIRRGTAHSRTRTFSAGDKETLDSPKTAVLMALSKPRKAIRRSQSHITVSEFWFATERASCLCGCTSRSRQEDKQKKRKHQKGKVETEGSTLQRSKTFVTLPFKSGRRRERSSSRDRKDTGREDGHKGRSKSPKHLDNEPGKERGRPIINLLSSPRETRAGLREQSPMPSPETMALLEDVARKLLNEDEVAAVMRHCKRFLVDRVVEDLVRPLLAILDKPEKLLLLREVRMIIPATDLGRFDSMVLPFELEAYDILKSRSVRSPVLRSPRHGGTPRRHLITPIPDYRGGFHLQPVQDLERERQLIEDLERMRLAGLPTGRLPPPRAFTPLLDVPVDTYITDSLRNRSLSPARSGFSHSESPYSTERTGRSPLRRDNGFPHDSLSSRGDSVPERGRSPYRNGHRMKTDKSLNGKEVKYTVMSAHRRSRTPLSQVFAPSPEQHWKEPVNGHSDSQDRTEQDYVLTTVTISKTKQSLGISISGGIESKVQPMVKIEKIFPGGAASTSDVLKAGFELVSVDGESLQGVTHQHAVDAIRRAFSNKAKEPMEFIVKVPKRLT | [
8970,
14230,
17293,
17306,
24866,
24917,
25079,
25108,
25770,
37172,
63819,
69581,
77497,
87278,
87311,
87857,
88008,
88009
] | The following text describes a protein:
Function:
In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links. Blocks inhibition of adenylate cyclase activity mediated by ADGRV1.
Subcellular Localization:
Cell projection, cilium. Cell projection, stereocilium. Nucleus. | 0 |
MRSYGKEKKLVFPYVFIACCFFLAIFGFCFFNLFSQGISFSEIPTTRRSVNDETDSLDHGSSVSNIPFHGLSWNPRVFYLPNFATKQQCEAVIDMAKPKLKPSTLALRKGETAETTQNYRSLHQHTDEDESGVLAAIEEKIALATRFPKDYYESFNILRYQLGQKYDSHYDAFHSAEYGPLISQRVVTFLLFLSSVEEGGETMFPFENGRNMNGRYDYEKCVGLKVKPRQGDAIFFYNLFPNGTIDQTSLHGSCPVIKGEKWVATKWIRDQTYD | [
647,
19553,
25014,
28508,
29023,
31115,
40223,
41567,
71101,
71278,
87008,
87013,
87409,
87432,
87522,
87678,
87760,
87767,
87873,
88008,
88061,
88159,
88161
] | The following text describes a protein:
Function:
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein. | 0 |
MLWVLDRVGFMDMSKFWDEDAIVQRVFIWIIMVNATKGIFISCDIPMAQFIINLNATQPASSKFIIHVLDSTHLFVQPNVTEMIRSAISEFRDLNSYEKPA | [
8074,
8110,
8111,
24775,
24942,
43904,
63734,
87374,
87380,
87857,
88008,
88148,
88150
] | The following text describes a protein:
Function:
In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape.
Subcellular Localization:
Nucleus. | 0 |
MADAAAAAPAQEEDPPPPCDPETLARGYQLEALERAVAGNTVAFLETGAGKTLIAVLLLRAYAHRIRSAPPPCFAVFLVPTVVLVGQQARVIEHHTDLRVEQFYGEMGVDYWNADTWRRAVDGAEVLVMTPQILLDNLRHCFFRLRDIALLIFDECHHAHGNSPYANILKEFYHPQLNSRPSDPIPRIFGMTASLINSKTLQRSDYSVKISELENLMNAKVYTVESESALSQYIPFATTKVVQYDDSIISSELYCHAIGCLNRLERKHLEFLKGKLHDSSLENAEKRIKQLSATFLYCIDNLGVWLAAKAAEVLQSRKESCLSFWGEKLDEKVEEFVRNYMEDAYSDLSEIISKMTKRGIQRHIGEDFAADLQDGLLTPKVHFLIKSLLEYRHKQDLRCIVFVERVVTSIVLESFLSTIHQMSGWIIRYMAGKNCGLQHQSRKEHTEIVDSFRRGKVHLIVATQILEEGLDVPTCNLIIRFDPSATVCSFIQGDAVALSKTQKFLAGGQIMREESLRLASTSCQPLPNTMCQEESYCVQSTGAVVTLNSSVQLIYFFCSKLPSDEYFKPVPRFNIDKALGTCTLHLPKSSPIQTIYAEGEGSVLKRVVCLKACRELHAIGALSDSLLPELSVPYEDGPDIVVDKYQKEQPNYFPEQLVDSWLSFSRLGLYHCYEISLEWCSKTANSPAEIVLAVKCDMGSDFISNSFKMWGVQDHVSVTMRYIGIIHLNQEQVIVARRFQTAILSLLISNNQLEVRDSIKNSLEMQASPGVVYLVLPLVSGKIDWCSIKFSASPMLEVTNKDMRHCHSCKDTNLVQTKDGPLCQCMLQHAIVCTPHNGMLYAVSGFLDLNANSLLHRSDGSVVSYKTHFKTRHGLDLTCEDQPLLAASMLLKVRNFLHKCNYKNEKESTSTNAVELPPELCVVVMSPVSSDTLRSFLFIPSIMYRIQCMLLSVKLKIQLSQRMGQFDIPALKILEALTTKKCQEEFSQESLETLGDSFLKYITTQHLFNKYRHQHEGLLTEMKKNLISNAALCQLACSNNLVGYIRGEAFNPKTWIIPGIDHDACSDSKLILLSPNMYSVRKMSIKSKRIADSVEALIGAYLSAGGEQAAYLFLISLGMDIEFHKMPVERKITIKSEEFINLRSLEVMLGYDFNDPSLLVEAMTHGSYQIAGTTACYQRLEFLGDAVLDHIFTDYFYRQYPECTPELLTDLRSASVNNNCYAHAAVKAGLHKHILHSSSALHKRMADYLENFKQSFSGPSHGWEAGIGLPKVLGDVIESIAGAIYIDSKCDKEVVWRSMKRLLEPLATPDTLDVDPVKELQELCGREAYSITYNVIREDRVTSVVAEVQTKGTAFKAARTGLSKLDAKKLAAKAVLQDMKAADGAK | [
9783,
11724,
24917,
24978,
27925,
28298,
28406,
29033,
32536,
36770,
37314,
38476,
40138,
45692,
47717,
48249,
58239,
63866,
64147,
65758,
87016,
87017,
87110,
87431,
87539,
87601,
87747,
87752,
87767,
87850,
87855,
88001,
88008,
88009
] | The following text describes a protein:
Function:
Probably involved in the RNA silencing pathway. May cleave double-stranded RNA to produce short 21-24 nucleotides (nt) RNAs which target the selective destruction of complementary RNAs. | 0 |
MLPTPYVKCDYDKVYEPAEDSFLILDCLEKEHDFLKQKFGNRLAIVCEIGSGSGIVTTFLMQNKIIPQENSIHLAVDINPWALEATLDTAKLNSCKSSFLEVIQADLNSSIRNNQVDVLIFNPPYVPAECVPDVPGSREEADQWLDLALLGGKDGMAITDKLLRQLEQILSPDGVAYILFCARNKPKEVIKRFVDTYKWNVKLIETRKAGWEVLSVYSFTR | [
2266,
8142,
12244,
14134,
17620,
24917,
24978,
25047,
25316,
26026,
27903,
29169,
29404,
34958,
37643,
39709,
42637,
59229,
77841,
87367,
87777,
87857,
88008,
88026,
88153
] | The following text describes a protein:
Function:
Methylates eRF1 on 'Gln-182' using S-adenosyl L-methionine as methyl donor. eRF1 needs to be complexed to eRF3 in its GTP-bound form to be efficiently methylated.
Miscellaneous:
MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus. | 0 |
MDITTDTQQPAPSRTPQPPATEDTRPGRGVTRPGDRIFVGLSRGSGILVLVIMAAIAAFLTYRAVLAIGEDEANFFTSFEWNPTGSPPEFGIAVLAYGTVVSSIIAMAIAVPVSVGIALFITHYAPRKLGGLIGYVIDLLAAVPSIVYGLWGALVLVPHLNGLYGWLDEYLGWTGIFEWNGGAGRSLLTVGILLAIMILPIITNVSREVFRQVPRMHEEAALALGATRWEVIRMSVLPFGRSGVISASMLGLGRALGETMAVAMVLSPTFDITPSLLDPGGGTFAQNIASKFNEATQMGRDALIASGLVLFVITLLVNGGARMIIARRKEYSGANA | [
13356,
25079,
28948,
36363,
45955,
63707,
76778,
87276,
87760,
87907,
88008,
88159,
88161,
88162
] | The following text describes a protein:
Function:
Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. | 0 |
MSWRFPLFGSSQQQQADPSFQDIPTQSWYPPSVVGSSSRPSTPTSSSASLHQRASDSPQSSSRGQPSPAEAAGIIARLKDKSIEELQRLLKDREAYNAFFNSLDQVKTQNNVRDELKKETLQLARENLEKEQRILELRNQCTIIRTTELAAAQDRLTDLERQKDDIMRSYSPAALLNKLQTSMAKLDEESEELHQKFLEKDIDLPTFVQKYKKLRTAYHKQALLHLAGQTSLR | [
8290,
8298,
14522,
24805,
44290,
59183,
64897,
87326,
87434,
87974,
87976,
88008,
88162
] | The following text describes a protein:
Function:
Component of the ESCRT-I complex (endosomal sorting complex required for transport I), a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs).
Subcellular Localization:
Endosome. | 0 |
MAKQTFLKGTLILIAAGMVTRMLGFVNRVVIARFIGEEGVGLYMMAAPTFFLATTLTQFGLPVAISKLVAEASARGDHQKTKNILVMSLTITGVLSLIFTPLFLFFAPVMAETMLTDKRTLYPLLAITPVVPIIAISSVLRGYFQGKQNMNPLAMSQVLEQVVRISLVAVCTTIFLPYGIEYAAAGAMLSSVAGELASLLYLFVCFKYKKTIKIRKHFLQSIKNGKQTFTQLMSVSLPTTGSRFIGNLSWFFEPIVVAQSLAIAGVATVAATKQYGELTGFAMTLLTLPSFITYSLSTALVPAISEGMEQKKLQVVEYRLEQAMRLCLLSGGISVVILFVFADELMRVMYGSSGAAVFIKVMAPFFLLYYFQGPLQAVLQALNLAGAAMMNSLIGALVKTGLIFVLATRPSLGIMGAALAIVTGMVLVTLLHAATVSKVLPISIKIKEYALSFAVIVICGFISSAIKQYISFGASEAVNLAGWIAASAAIYMILLLVFRLIKKDELRRIPIIGRLIIR | [
11727,
25079,
38248,
47949,
56457,
76488,
87276,
87760,
88008,
88074,
88159,
88161
] | The following text describes a protein:
Function:
Involved, directly or indirectly, in spore cortex biosynthesis. Affects only indirectly the expression of late sporulation genes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. | 0 |
MQWKKKFTRLKAATGNSRVRRMLCCGRRKENGRSVPDVTASPGRAPPGPLPANQMPAMGNQQHHGNQQHHGNQQQHHGNQHSNHRGQSGSLSNAAGVKDPVMLQGDFRKVSGISSEIFRQIEAVENDHDPNTAAALEAVERRGEMIVRVLEPRCMGSKQAVDAAHKLMNKADARHTVQLVEIVKRPGQTLGLYIREGNGADRTDGVFISRIALESAVYNSGCLRVGDEILAVNLVDVTHMSLDDVVIIMSIPRRLVLAIRQRRGNRGTGSPGPPTLSRPEQKPPPVVVIKRDLRDEDLDETDRMPRPRSSRDRRTGDGREMTESRSRLGLGLNNYSPQSEQLDMYYNTRGGGGGAMGEPPNWGYKPPPPPSSVITEQPTKAHAFAPSHAYYQNAGTLESLAEKVHAFYPGQPGGPPVGPSRRMSTGTGNVGLAQQHARFPRSGSDQHLPRVEYSDYSNSLGRHSLLRSSLKPGTTGGAPMQVGVGGTLGRYGRYDQQRAGVSKYGPPSGGAQSLTRRSRPNLDYSSDTEATIGPRPSYYYYNRPAIGSMSRGSGGAGGGVGAASTAALLAGAADLNKFNSLPRERPGTRLQGIRSRMGDRLVDENDGNTSAPEFDVRRGRDLRQRITASPSIFTADEYRAWLRRAPSSSAIAEQMRMTRDMFAQPRAQRFSCSAENIHDALRNTESIYSSRNHILGTGTLDRNMGLTRPISALPVRSMSSQHIGGAGSIRSPSIRRMRQLLELSAGPASPSGSILSTGGHQSPAPTPSATLPRPHRQIDINPAEFAKYKLDKPIVDIGGISGMLWIHLLAGRGLRTAPEGAAGTATQGQTRDLYCVIECDRVHKARTVVRSGDLQFDWDESFELDLVGNKQLDVLVYSWDPQHRHKLCYRGAISLSSILRQSPLHQLALKVEPRGTIYIRMRHTDPLALYKRRGLPSLRAGYPTLFGADLETVVNRESKNAPGSAPVPIVLRRCVEEVERRGLDIIGLYRLCGSATKKRLLREAFERNSRAVELTPEHVPDINVITGVLKDYLRELPEPLFTRCLFQMTVDALAVCLPDDPEGNAKLMLSILDCLPRANRATLVFLLDHLSLVVSNSERNKMSAQALATVMGPPLMLHSASAQPGADIDHAQPIAVLKYLLQIWPQPQAQHQQMAQHMGGAAGAMMGGLVTAGSMSNMAGVASGRRGESTGQRGSKVSALPADRQQLLLQQQAQLMAAGNLLRSSTSVTNILSQGHPQLSATANNHLYQSVVGQLAQSHRALQQAVQQPYQLGGSVGSAIPDPSPLPLPGTPSPGSSSASTGSGSGSGKSTDTIKRGASPVSVKQVKIVDQPSSPYSIVMKKPPLQKDAPVEITTPTTQADTESTLGCKESNGTASRRGNVDFYDTHKTQAKSVVNEESSYSSKYTGSETKKIIPGNSSYTPSKANASGLSGGEDYKAMRNKSSATSSSSSSQATVLSAGSTATSAPTTSSDDSDDLVSYKSSASTNALLAQSQAMTTSQLMSKYLKREPRVQFTPIKSPESPSPPGSGDGLPKGTYQLVTPISGSSSKPGATTGAISKYTTGSVESSINANSQKLSSPSRLCNSKDSNSRTGTASSTTPATSMVSTGRRLFDSLASSSSSETETKTYIGGTTAASGAITTTIYTNDTKNSGSSSSKSGIGGGSGTGLGAVSGASSETRSFGSTLFGSSGLGNGNGSSHNHSSASPSPFTTTNGNGNHNTMHLYGTLPKNGTSTGAALFGGSANSSSYHSSASGSGAGTASSSGVSSMTGSTNSYDFYTSTSSTVSSSRPFANGGNNYHTLGTYRAQYAATNPFLDAFDEKPGSNGGNAHGEEKLGADKGHHRAAVMAFQSSGDSKNGSDEYDDIK | [
8727,
8840,
10729,
11587,
15152,
15730,
16328,
16329,
16370,
20005,
20215,
23906,
25685,
26194,
26471,
26851,
27062,
28816,
35959,
36104,
37172,
43538,
63695,
63819,
77770,
87139,
87278,
87492,
87914,
88008,
88097
] | The following text describes a protein:
Function:
GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state (By similarity). Promotes the anchoring of Liprin-alpha clusters at synapses. Recruits and keeps Nrx-1 levels high in active zones in the presynapse opposite the postsynaptic region.
Subcellular Localization:
Presynapse. Note=Localized in the active zone of the presynapse. | 0 |
MSVVGTPKSAEQIQQEWDTNPRWKDVTRTYSAEDVVALQGSVVEEHTLARRGAEVLWEQLHDLEWVNALGALTGNMAVQQVRAGLKAIYLSGWQVAGDANLSGHTYPDQSLYPANSVPQVVRRINNALQRADQIAKIEGDTSVENWLAPIVADGEAGFGGALNVYELQKALIAAGVAGSHWEDQLASEKKCGHLGGKVLIPTQQHIRTLTSARLAADVADVPTVVIARTDAEAATLITSDVDERDQPFITGERTREGFYRTKNGIEPCIARAKAYAPFADLIWMETGTPDLEAARQFSEAVKAEYPDQMLAYNCSPSFNWKKHLDDATIAKFQKELAAMGFKFQFITLAGFHALNYSMFDLAYGYAQNQMSAYVELQEREFAAEERGYTATKHQREVGAGYFDRIATTVDPNSSTTALTGSTEEGQFH | [
5392,
7945,
7947,
7949,
18926,
24878,
25040,
25079,
28339,
31786,
32475,
32536,
41233,
48977,
51194,
67580,
87016,
87103,
87526,
87684,
87741,
87747,
87752,
87767,
88008,
88165,
88180
] | The following text describes a protein:
Function:
Involved in the persistence and virulence of M.tuberculosis. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. It could also catalyze the formation of pyruvate and succinate from 2-methylisocitrate, a key step in the methylcitrate cycle (propionate degradation route) (By similarity).
Miscellaneous:
MISCELLANEOUS: Was identified as a natural substrate of the M.tuberculosis proteasome. | 0 |
MATGDLKRSLRNLEQVLRSLNYPREVDCVGLVKGDIAASLPIISYSLTSYSPYVAELLVESNVELIAKNDLRFIDTVYKLLRDHFNYKPILTKKQFLQCGFAEWKIQIICDILNCVMKKHKELSGLEKTPSQQRKKISSIKSEPCSGAEKTSAEPVGIDVTGRFVTSGKKKAVVIRHLYSEDGVNIPEDPSADVHEAFDVCDLKTADLKIPELQVPEINCEQQDVKVNPEITALQVMLAECQEKLRKLTCLENRLDSLETKMKGKVMVNEKTWTNLLSRVTLLETEMLLSKKNDNYIEFNEMSEEYASSSDMDSLNPDRKSQEERQANIPLSSGYSTVSSDSTPRTSTVNYYGLKEISEETTIQKMERMKKMFEETAELLKCPNH | [
8624,
9880,
24814,
25026,
25027,
25040,
25506,
26070,
29056,
59317,
61880,
87326,
87367,
87371,
88008
] | The following text describes a protein:
Function:
Centriole-enriched microtubule-binding protein involved in centriole biogenesis. In collaboration with CEP295 and POC1B, is required for the centriole-to-centrosome conversion by ensuring the formation of bona fide centriole wall. Functions as a linker component that maintains centrosome cohesion. Associates with CROCC and regulates its stability and localization to the centrosome.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole. Midbody. | 0 |
MDGKEKGSKKKKKSLSSFSAISNETNSSFMSSNVTNEEPNDEGDKTPENPEEESHMRILSLHRDLTAALINIQTAAVAIVATTKLENAQGTIAELQEKNEQSSQKIFEELIEGWSTAHQKEAHQDLLEALESQQHLCAAVIRDKKILINDLKQELNRRHESYVRTLRKNAEELNLVTVMMEEKMKIMTDVYREESEQMERIHQQEVEILLTKDKDQWEKQIKALCDKELQLLTERKKKVKEYEEKCHDKILGDVINNAKSKVSVKNLHKKVPSDLLVPKNNLHAQLAKQSKEMSTFLNGRIFSLKNDIKKLRETYTEKERELKNCTDKLYGEYQRSYQRVQRCNQMQMKTRHNSVDAKQFKELQQMIDGELNQLAQRALTIDSLICQYLGLPWKQDNMAMLELLSPIQEQVPNFGQLNYETDKCNQGMIESDNKEKEKLCKEALETSVDPLWDEMKSSAGCSGMMKAVEASPPTNSSIHHKPFLPPLKLHPGLKRESRESSEKQISSSWHGQVLDASEVGARWERLANVIPEEKVRMWEIAQKQLLQHHSVLREISDLSLETENLRQKNLQLKKQLQERGISVTNSCAFDPKEG | [
7805,
17414,
18426,
25058,
25109,
25668,
59592,
66833,
67049,
87278,
87311,
87326,
87468,
88008
] | The following text describes a protein:
Function:
Component of the nexin-dynein regulatory complex (N-DRC) a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays a critical role in the assembly of N-DRC and also stabilizes the assembly of multiple inner dynein arms and radial spokes. Coassembles with CCDC65/DRC2 to form a central scaffold needed for assembly of the N-DRC and its attachment to the outer doublet microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme. | 0 |
MESTVPFLSPVSQSPENHFSFYHNFELFYMENIAQNNSFDQTQTLESPFSGLNVSGYPDLPDSGYQFGGGFARAGQDRNNNVIGEGTKVGPDVESWGAFMYSSYQLGSSRNTEFSILPSSNQTRLLSAAASAAGCTMPFGLNNNINRPSFNTSKLCNNNQTRPHWLHEPLNCLSLGDLRGRLVALAKDQYGCKFLQKSVEKASKEEIDMVFMEVIDHVCELMSNSFANFVVQKVVDVCSEEQRNQILLMVIKNRFRLVEICLNLHGARAVQKLLEKLTTQQQISLFMSALSPGAVALSKDLNGHRVIQYCLKNFSDEDNKYFLTVVANNCYQIAIDKCGCCALKHCLDHSNGEARSRLFQEIIANALNLAEDQYGNYVVQHILELKETQTTESLLRQLQGNYASLSCNRYGSNVVERCLLESEEPLTTRIIVELLRSPIVSTLLLDPFGNYVIQSALSVSKGFVFDALLNLVQDHYPIMRSHSYGKWVLAWFSRRKQLHM | [
8142,
9972,
24978,
27930,
37035,
46078,
49116,
61648,
61959,
87367,
88001,
88008,
88009,
88155
] | The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Subcellular Localization:
Cytoplasm. | 0 |
MSSPSEFYKSLPPITKAYGTICLMTTVASHLGLYRLENIALIHELVFSEFQVWRLLTNFFFLGNFSMNFGIRLLMIARYGVQLEQGPFQRRTADFLWMMIFGAISLLALSIVPILRGAFLGISLVFMLLYICSREFPNAQVNIYGLVALKAFYLPWAMLALDVIFGSPLVPDLMGIIAGHLYYFLTVLHPLAGGRNIISTPRLVHKLVARARLEYPTNARVPQERTTGVAFTGRSYRLNSSTGRGFSLRRFWSS | [
11875,
13808,
25014,
28801,
42411,
63750,
87432,
87760,
88008,
88159,
88161
] | The following text describes a protein:
Function:
May be involved in the degradation of misfolded endoplasmic reticulum (ER) luminal proteins; May be involved in the degradation process of specific misfolded endoplasmic reticulum (ER) luminal proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. | 0 |
MNHAELRRLFAACDGNQSGRVEYEDFTTVCRELNVPADDIRTLFNKFDLDGDGYINFNDFSSSFQEVSEALNLASLGNCLHSQRRAWDEFENTLDGDVAFYLGRQWDALSELYEGIHSTSDELLLQQFEDLIRALVTEIREHRMESEQLETSLRRTEEVSSSQLAEMEEDLQQQLIHTERRVREEEQKKLDESIAMLQIKHENELADLQTTIERLTKQYQEESKLNTPREDSVKLRAQIKDLMEENEELRASLMKAQMNVSILQVELDKLKNAFTDQKRQHERESDDLKKMVMEFQSYSSHIEMLQEMNKSLYDSNDGLRSALSQENASTKRQLSPRNEVLPRKMKPIRQSTMNQSSFTNEEDTLALVKCWAEKYLDSGVSVQSEMDAMSGIDYDSDDSHHSVETVHHSYSCVPSELEVSEVKPEALRSVARSTVGSISSSLRRRLSAFPVKQNEEDLLDTQDLAPVYRLVLAGDAGSGKSSFLLRLSLNEFRGDIQTTLGVDFQIKKMLVDGEKTNLQIWDTAGQERFRSIARSYFRKAHGVLLLYDVTSESSFLNVREWVEQIRESTDEDIPMCIIGNKVDLRAARPEGSCVSSIHGEKLAMNYNALFCEASAKEGTNVIEAVLHLAREVKKHVKLGRRSESQVKLSLHKRRKTLSNCCGV | [
10671,
26465,
28025,
29025,
29034,
37443,
37640,
40315,
46081,
51011,
58239,
75882,
87244,
87326,
87367,
87491,
87767,
87855,
88008,
88009
] | The following text describes a protein:
Function:
Binds predominantly GDP, and also GTP.
Subcellular Localization:
Cytoplasm, perinuclear region. | 0 |
MFKKSRHLKNVSNAIKSARVHDVSNGINSKFFDTKKICTYGINGRITVTTFDYTQSLLAVATTAGEIHVYGQKQIEVVFTLKNRPQIKHMRFIKGIYLIAVDEKSNIIVLSVHSKQILTTVFCPNSITCIETDPSLDWMLIGLESGSILIYDVDRNQMSKLKIENFQKSVFLPKERLSPVISIQWNPRDIGTILISYEHITVIYSFIDYKVKQHFFYQLEPYAPGGDLSTNIEKKRTPKVIQSLYHPNSLHILTVHEDNSLVFWDVNSGKLIHARSIFETHVNFPNPALKDCSFTETPAIFKVSWLCQRNPEYTSLLIATKATENPCLPQEITMIDLGGTPMYSVTSFDAMSKYYAKPVQQKLFSLIGKAPLINFLPLPKASPYFGGCHDTNLILLLLEDGELETLIYPAGSFSSKASIFPRSLAWVRPTVTTCIAQSVQKNLWLGMMTIAQSESFLKGGIPATRNIRRHETRSALLTGHSNGSVRIWDASHSEVTDNAVFEVNTAKVLNRATNLAIKNISFASETLELAVSSEVGDVILFKFETNKFYGQLPKSDALQLKFSRFSLDDSKTILVDVSDRGPTNVKQGFIPSTVIHAKKGAVSAIMNSNIGFVAVGFIEGTLIILDRRGPAIIFNENIRVISKAGSSYVSTVHFCVMEYGDDGFSSILMLCGTDIGELMTFKILPATNGRFEVKFTDATKTNNQGKILGINSFAKDTGYSCSATISKMQGLSKGIAIPGFVTISGANDIRLVSPGKSKDTHALFKYPIATSGLSFIPIIDGKGERKLSTIMIVLLINGDIKVLTVPELKEVKNLRCPVPLSAQYVENSSILENGDIVIRTGKFQASLISVLNESATGTNHTADISQHTPIDTLYNPDLKIGYRPQVNSLQWARGTIYCTPYQLDELLGGIERPESKYEESAIARGCISSSSSNAARKLPPGTEDHRYARPVRSSGRSNGYGVLKSVSRAIETRLDTVETTINDYATTMGQTMNDAMEETGRDMMKSAVGF | [
8491,
8496,
24978,
25079,
25112,
28816,
30815,
32405,
37341,
47631,
49061,
64085,
87448,
88008,
88009,
88252
] | The following text describes a protein:
Function:
Acts as an allosteric regulator of polarized exocytosis by promoting the targeted fusion of vesicles with the plasma membrane. Involved in maintenance of ion homeostasis in cells exposed to NaCl stress. May be involved in the targeting of the myosin proteins to their intrinsic pathways. Multicopy suppressor of RHO3. May also participate in the maintenance of cell polarity and bud growth. | 0 |
MLQEACIVSVSGESSKSSGNHGEVTGHSCSGVIVDRQRGLVLSHGVAFSPYLPDEFTSHQVRRQGWYKPQDTDRFNIEVIVRPRSEKGQPEASDRFLQPIQQPIPAATTAGGKLASELDSPPEKKCSAELLLLWRCIDFDDAVRKLMPKYDNWHFDEPPNNPADSRRDPSHQIEAVQSCVKTDWMAEVSLSWFALLKLKESEKGAESSAVVGVEQAQIGSPVMAVGTPFGVLCPSVFMNSLAKGIVCNTAGKGGALILTDARCLPGTEGGPLLTVDRDGKWMLLGLVAAPLCWKANEWIGLSLVCSFHAVLDSLAHLVPWPLIPAAAVIHSIQEPPHPALSQVEKSIVMIEAGEIWGSGVVVHVDESKVYLLTCRHVIGSSSKVKVVMCHAQKVRVTGNVVYATPSESVYDLAVVEFPNPRVKLVPVRETRRYDQGEQCFAVGYALFGQNQHMKPTVTAGVLSNVVSWQGNPIMLQSTCAVHAGVSGGALFNQQGQLMGIVVSNAKDVQLKACYPHLNFIIPSTTFAKAMDRFVQTKDAGCLSEFDSNNHYLQDVWKLQEPKPLLQSKI | [
4571,
10733,
12149,
25004,
28227,
43583,
66617,
69992,
87601,
87894,
87965,
88008,
88049
] | The following text describes a protein:
Function:
Peroxisomal protease that mediates both the removal of the leader peptide from proteins containing a PTS2 target sequence and processes several PTS1-containing proteins. Catalyzes the processing of PTS1-proteins involved in the peroxisomal beta-oxidation of fatty acids.
Subcellular Localization:
Peroxisome. | 0 |
MMQALTMRSWLATLVTALLAVAIWPDPGQSLPQGAPETVCDTMLPFHSGGSVLPQNSVSPFSVETSSSTLGQGQTLRVDLTGVPAGLSFGGYMIQARNRNPPHQIIGQFGPARDGTIKLMNCENSVNNSATHSNAGPKQQVILEWQSPVDFLGQVVFNATIAQSYNEFWVGVPSQPVQIVRRDLSAAPPLPTQSPSAPAGTTRAPYVPPSYVAPNNVVAVSSDPIYNGCGQSKNCFGFPDGCVATKSCTSITVVTVRGDVFEFEIQSGKGTNAAYVAVGLSDDAKMGDDLTTECVPENGRVNLYSSLTSASPYSAVRSNVNQNSARLLDASIVDGVIYCRVQRDAVTNVQGRTFDLRNGKYHLLVASGSSLKENSVGYHDIGRLPSAQPINLAEVQDLSGSSRLLIQLHGAFMIAAWIGTTSLGIIFARYFKQTWVGSQSCGTDQWFAWHRLLMVTTWSLTVAAYVLIWVELKQAVWHAHSIIGLITVILCFIQPIGALFRPGPNDKKRPYFNWGHWLGGNLAHILGIVTIFFSVKLPKAELPEWMDWILVSFVVVHVLVHLIFSIGGMASERHLSQRANTFQMGDMSHHQQHAMRNGMSMERKMDAPYAGMRKGLLGVYGVVLILFVTVLILLVVLAPIEQFLGKS | [
0,
8483,
25325,
30291,
32536,
35425,
38297,
40123,
41546,
69274,
76891,
87080,
87425,
87522,
87678,
87760,
87767,
87873,
88008,
88159,
88161,
88162
] | The following text describes a protein:
Function:
Putative ferric-chelate reductases reduce Fe(3+) to Fe(2+) before its transport from the endosome to the cytoplasm.
Subcellular Localization:
Membrane; Multi-pass membrane protein. | 0 |
MEDLEETLFEEFENYSYALEYYSPGTDLEEKAHLGVVHWVSLVLYCLAFVLGIPGNAIVIWFTGFKWKKTVTTLWFLNLAIADFIFLLFLPLYISYVAMSFHWPFGICLCKANAFIAQLNMFASVFFLTVISLDRYIYLIHPVLSHRYRTLRNSLVIVIVVWLLASLMGGPALFFRETLESNNRTVCYNNFHEQDPDLVLMRHHVLTWVKVIVGYLFPLLTMSICYLSLIFKVKKRSILASSKHFWTILAVVLAFLICWTPYHLFSIWELTIHHNSYFHQVLQAGIPLSTGLAFLNSCLNPILYVLISKKFQVRFRASVAEILKYTLWEVSCSGTVSEPLRNSETKNLCLLETAQ | [
8705,
14280,
24926,
25079,
26195,
28715,
32092,
34627,
34628,
36171,
36627,
37835,
50338,
87276,
87413,
87484,
87522,
87760,
88006,
88008,
88152,
88159,
88161
] | The following text describes a protein:
Function:
Receptor for the chemoattractant adipokine chemerin/RARRES2 and for the omega-3 fatty acid derived molecule resolvin E1. Interaction with RARRES2 initiates activation of G proteins G(i)/G(o) and beta-arrestin pathways inducing cellular responses via second messenger pathways such as intracellular calcium mobilization, phosphorylation of MAP kinases MAPK1/MAPK3 (ERK1/2), TYRO3, MAPK14/P38MAPK and PI3K leading to multifunctional effects, like, reduction of immune responses, enhancing of adipogenesis and angionesis. Resolvin E1 down-regulates cytokine production in macrophages by reducing the activation of MAPK1/3 (ERK1/2) and NF-kappa-B. Positively regulates adipogenesis and adipocyte metabolism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. | 0 |
MDRYWEQDPMRPMVYRDFLGEMEYPGYSMPMQMEIDEDDFGPMDMQFEVGGISPFQMKPEDSDFFNKFEDDFDDSDIN | [
9425,
9426,
87196,
88008
] | The following text describes a protein:
Function:
Mediates responses to the synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D). Not involved in the response to indole-3-acetic acid (IAA). May interact with RUB modification-related components and may regulate the culling-ring ubiquitin E3 ligase complex (CRL) activity. | 0 |
MARKKTLDFEQSLTELQTLVERLESGELSLEESLGAFEQGIRLTRECQTSLSQAEQKVQILLERDGELSEAPFDAEGDEA | [
4023,
8082,
25040,
25173,
29482,
39007,
64722,
87367,
87449,
87601,
87850,
88008
] | The following text describes a protein:
Function:
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Subcellular Localization:
Cytoplasm. | 0 |
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