wanglab/gogpt-training-data huggingface dataset:
Protein: Oxygen-evolving enhancer protein 2-1, chloroplastic (OEE2) (23 kDa subunit of oxygen evolving system of photosystem II) (23 kDa thylakoid membrane protein) (OEC 23 kDa subunit) (OEC23) (Q42029)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of photosystem II.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}. Note=Associated with the photosystem II complex.
Interaction partners:
- Oxygen-evolving enhancer protein 3-2, chloroplastic
- Oxygen-evolving enhancer protein 3-1, chloroplastic
- Oxygen-evolving enhancer protein 1-1, chloroplastic
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Chlorophyll a-b binding protein CP26, chloroplastic
- Photosystem II 10 kDa polypeptide
- Photosystem II reaction center W protein, chloroplastic
- Expressed protein
- Photosystem II protein D1
- PsbP-like protein 1, chloroplastic
Sequence:
MAYSACFLHQSALASSAARSSSSSSSQRHVSLSKPVQIICKAQQSHEDDNSAVSRRLALTLLVGAAAVGSKVSPADAAYGEAANVFGKPKTNTDFLPYNGDGFKVQVPAKWNPSKEIEYPGQVLRFEDNFDATSNLNVMVTPTDKKSITDYGSPEEFLSQVNYLLGKQAYFGETASEGGFDNNAVATANILESSSQEVGGKPYYYLSVLTRTADGDEGGKHQLITATVNGGKLYICKAQAGDKRWFKGARKFVESAATSFSVA
Protein: Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10) (P25972)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Interaction partners:
- Carbamoyl phosphate synthase pyrimidine-specific small chain
- Aspartate carbamoyltransferase catalytic subunit
- Dihydroorotate dehydrogenase B
- Orotidine 5'-phosphate decarboxylase
- Dihydroorotate dehydrogenase B
- Dihydroorotase
- Carbamoyl phosphate synthase pyrimidine-specific large chain
- Uracil permease
- Bifunctional protein PyrR
- Carbamoyl phosphate synthase arginine-specific large chain
Sequence:
MGGNQILKQIIAKHLLDIQAVFLRPNEPFTWASGILSPIYCDNRLTLSFPEVRNDVASGISKLVKEHFPEAEMIAGTATAGIPHAALAADHLNLPMCYVRSKPKAHGKGNQIEGAVQEGQKTVVIEDLISTGGSVLEACAALQAAGCEVLGVVSIFTYGLPKAEEAFAKAELPYYSLTDYDTLTEVALENGNIHSDDLKKLQTWKRNPESKDWFKK
Protein: Glycerol-3-phosphate phosphatase (G3PP) (EC 3.1.3.21) (Aspartate-based ubiquitous Mg(2+)-dependent phosphatase) (AUM) (EC 3.1.3.48) (Phosphoglycolate phosphatase) (PGP) (A6NDG6)
Organism: Homo sapiens (Human)
Function: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-phosphate into glycerol. Thereby, regulates the cellular levels of glycerol-3-phosphate a metabolic intermediate of glucose, lipid and energy metabolism. Was also shown to have a 2-phosphoglycolate phosphatase activity and a tyrosine-protein phosphatase activity. However, their physiological relevance is unclear. In vitro, has also a phosphatase activity toward ADP, ATP, GDP and GTP (By similarity).
Interaction partners:
- 2-Hydroxyacid oxidase 1
- 2-Hydroxyacid oxidase 2
- Glyoxylate reductase/hydroxypyruvate reductase
- Hydroxyacylglutathione hydrolase, mitochondrial
Sequence:
MAAAEAGGDDARCVRLSAERAQALLADVDTLLFDCDGVLWRGETAVPGAPEALRALRARGKRLGFITNNSSKTRAAYAEKLRRLGFGGPAGPGASLEVFGTAYCTALYLRQRLAGAPAPKAYVLGSPALAAELEAVGVASVGVGPEPLQGEGPGDWLHAPLEPDVRAVVVGFDPHFSYMKLTKALRYLQQPGCLLVGTNMDNRLPLENGRFIAGTGCLVRAVEMAAQRQADIIGKPSRFIFDCVSQEYGINPERTVMVGDRLDTDILLGATCGLKTILTLTGVSTLGDVKNNQESDCVSKKKMVPDFYVDSIADLLPALQG
Protein: Core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein (Glycosyltransferase) (T12J13.3 protein) (Q9SS69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Probable xyloglucan galactosyltransferase GT14
- Arabinogalactan O-methyltransferase 2
- Arabinogalactan O-methyltransferase 1
Sequence:
MAIKKLLMISFSLTSLLFSLLYIIPTTKTLFTSSKIPSLPLESNQNSNSTLPCFAYLISASKGDAGKLKRLLRSLYHRRNHYLIHLDLEAPEEEHLEMIRFVAGEPLFQPEGNVMIVGKPNLVTYRGPTMLATTLHAMALLLRCCRWDWFINLSASDYPLVTQDDLIYAFSELPRDLNFIQHTSRLGWKMNKRGKPIIIDPGLYSLNKSEIWWVSNQRSLPTSFKLFTGSAWTFLSRPFAEYCIIGYDNLPRTLLLYYTNFVSSPEGYFQTLICNSDEFKNTTVNHDLHYIAWDNPPKQHPKILGTRDYRKMVMSNRPFARKFKSNDPVLNRIDREILRRKRKLGSKPDLGPGPGARRLKSLLMRLLLRRNFVNRQCR
Protein: Calcium-transporting ATPase PAT1 (PAT1) (EC 7.2.2.10) (P54678)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Calcium ATPase involved in Ca(2+) homeostasis as a component of the contractile vacuole complex.
Subcellular location: Contractile vacuole membrane {ECO:0000269|PubMed:9885293}; Multi-pass membrane protein {ECO:0000269|PubMed:9885293}. Cell membrane {ECO:0000269|PubMed:7499325}; Multi-pass membrane protein {ECO:0000269|PubMed:7499325}. Note=Contractile vacuole complex. Localizes to the contractile vacuole membrane in unstimulated cells (PubMed:9885293). Localizes to the cell membrane and the contractile vacuole membrane in cells stimulated by calcium (PubMed:9885293). {ECO:0000269|PubMed:9885293}.
Interaction partners:
- Magnesium-transporting ATPase, P-type 1
Sequence:
MTGSHEMESIMLDSMEEEFPVSVETLGKLVDVPKGFDTYAELGGLSGLSTKLKSNIKTGLPLEKSSTEENRVLKYSKNILPDPPHQPLWSIVLDALSDHILILLIVAAVVSIVLGSIDYTSDHPETGWIDGVAILVAVILVVGITSLNDFKNQARFRELNDKSNDKEVKGIRGGEQCQISIFDVKVGDIISLDTGDIICADGVFIEGHALKCDESSITGESDPIKKGQPQDNMDPFLISGSMVIEGFGTMLVTAVGVNSFNGKTMMGLRVASEDTPLQMKLSVLASRIGYFGMGAAILMLLIAIPKYFIQRKVHDIEITREDAQPIVQLVISAITIVVVAVPEGLPLAVTMALAYGMMKMFKENNLVRNLASCETMGSATTICSDKTGTLTQNVMSVVTGTICGVFPTLDGIAQKIPKHVQSILTDGMAINSNAYEGVSSKGKLEFIGSKTECALLNFGKLFGCDYNEVRKRLEVVELYPFSSARKRMSVLVKHDQNLRLFTKGASEIILGQCGSYLDEAGNIRPISEAKAYFEEQINNFASDALRTIGLAYRDFQYGECDFKEPPENNLVFIGIVGIKDPLRPEVPEAVEICKRAGIVVRMVTGDNLVTAQNIARNCGILTEGGLCMEGPKFRELSQSEMDAILPKLQVLARSSPTDKQLLVGRLKDLGEVVAVTGDGTNDGPALKLANVGFSMGISGTEVAIAASDVVLLDDNFASIVRAVLWGRNIYDAICKFLQFQLTVNVVAVTVAFIGTLTSDVVEDKDNSSSSGSADKVTEEEPRQGSPLTAVQLLWVNLIMDTLAALALATEPPTPELLERPPNGKNAPLITRSMWKNIIGQAALQLAILFTILYQGHNIFQHFVPQAHGPIIKNGLHHYTLVFNCFVFLQLFNEINARVLGSRTNPFKNFFNNPIFIAVMIFTLGVQIIFVTFGGSATSTDSLYIVEWICCVVVGAISLPVGLLLRKIPIREPVVKNEIPVHSEAVYTSPSPNPSSSNLLGSGGAKPISKDYPTSGESTPPINDEGSPLVTRKTSVGASANDNINTPIPSSSSNLVNLNKPTQVGRGWQIVRQTHKKLVVINALKEFSQNKEPGLVDVVRGTNRGSLHLPVNQINN
Protein: Glutamate dehydrogenase 3, mitochondrial (OsGDH3) (EC 1.4.1.3) (Q6H3Y7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Ferredoxin-dependent glutamate synthase, chloroplastic
- Glutamate synthase 1, chloroplastic
- glutamate synthase
- Glutamate synthase 2, chloroplastic
- Delta-1-pyrroline-5-carboxylate synthase 1
- Delta-1-pyrroline-5-carboxylate synthase 2
- 3-methyl-2-oxobutanoate dehydrogenase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Aspartate aminotransferase
- Aspartate aminotransferase, cytoplasmic
Sequence:
MNALAATSRNFRQAARLLGLDSKLQKSLLIPLREIKVECTIPKDDGTLATFVGFRVQHDNSRGPMKGGIRYHPEVDPDEVNALAQLMTWKTAVAAVPYGGAKGGIGCTPGELSRSELERLTRVFTQKIHDLIGINTDVPAPDMGTNAQTMAWILDEYSKFHGHSPAVVTGKPIDLGGSLGRDAATGRGVMYATEALLTEYSESISGSTFVIQGLGNVGSWAAKLIHQKGGKIVAVGDVTGAIRNKSGIDIPALLKHRSEGGSLEDFYGAEVMDAAELLVHECDVLVPCALGGVLNRENAAEVKARFIIEGANHPTDTEADEILAKKGVIVLPDIYANSGGVVVSYFEWVQNIQGFMWDEEKVNRELQKYMKNAFQNIKDMCKSQNCNLRMGAFTLGVNRVAKATLLRGWEA
Protein: Kinesin-like protein KIN-14E (Kinesin-like calmodulin-binding protein) (Protein ZWICHEL) (Q9FHN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Minus-end microtubule-dependent motor protein involved in the regulation of cell division and trichome morphogenesis through microtubules bundling. Possesses basal and microtubule-stimulated ATPase activities. Acts as a hub that brings together microtubules and actin filaments to modulate the cytoskeleton during trichome formation and morphogenesis. Could be involved in the negative regulation of root growth.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:25908862}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:9450347}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:9450347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26287478}. Note=Colocalizes with microtubules during preprophase and cytokinesis. In M-phase, locates to the preprophase band then remained in the cotical division site throughout mitotis and cytokinesis. Also detected towards the poles of the anaphase spindle and on the phragmoplast but absent from the metaphase spindle (PubMed:25908862, PubMed:9450347). Colocalizes with microtubules along the trichome branch and colocalizes with F-actin at the branch apex (PubMed:26287478). {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:9450347}.
Interaction partners:
- Calcium-binding protein KIC
- Calmodulin-2
- Ankyrin repeat family protein
- Calmodulin-6
- Calmodulin-1
- Calmodulin-7
- Calcium-binding protein CP1
- Calmodulin-like protein 10
- Serine/threonine-protein kinase KIPK1
- 187-kDa microtubule-associated protein AIR9
Sequence:
MEGQRGSNSSLSSGNGTEVATDVSSCFYVPNPSGTDFDAESSSLPPLSPAPQVALSIPAELAAAIPLIDRFQVEAFLRLMQKQIQSAGKRGFFYSKKSSGSNVRERFTFEDMLCFQKDPIPTSLLKINSDLVSRATKLFHLILKYMGVDSSDRSTPPSLDERIDLVGKLFKKTLKRVELRDELFAQISKQTRHNPDRQYLIKAWELMYLCASSMPPSKDIGGYLSEYIHNVAHDATIEPDAQVLAVNTLKALKRSIKAGPRHTTPGREEIEALLTGRKLTTIVFFLDETFEEISYDMATTVSDAVEELAGTIKLSAFSSFSLFECRKVVSSSKSSDPGNEEYIGLDDNKYIGDLLAEFKAIKDRNKGEILHCKLVFKKKLFRESDEAVTDLMFVQLSYVQLQHDYLLGNYPVGRDDAAQLCALQILVGIGFVNSPESCIDWTSLLERFLPRQIAITRAKREWELDILARYRSMENVTKDDARQQFLRILKALPYGNSVFFSVRKIDDPIGLLPGRIILGINKRGVHFFRPVPKEYLHSAELRDIMQFGSSNTAVFFKMRVAGVLHIFQFETKQGEEICVALQTHINDVMLRRYSKARSAANSLVNGDISCSSKPQNFEVYEKRLQDLSKAYEESQKKIEKLMDEQQEKNQQEVTLREELEAIHNGLELERRKLLEVTLDRDKLRSLCDEKGTTIQSLMSELRGMEARLAKSGNTKSSKETKSELAEMNNQILYKIQKELEVRNKELHVAVDNSKRLLSENKILEQNLNIEKKKKEEVEIHQKRYEQEKKVLKLRVSELENKLEVLAQDLDSAESTIESKNSDMLLLQNNLKELEELREMKEDIDRKNEQTAAILKMQGAQLAELEILYKEEQVLRKRYYNTIEDMKGKIRVYCRIRPLNEKESSEREKQMLTTVDEFTVEHPWKDDKRKQHIYDRVFDMRASQDDIFEDTKYLVQSAVDGYNVCIFAYGQTGSGKTFTIYGHESNPGLTPRATKELFNILKRDSKRFSFSLKAYMVELYQDTLVDLLLPKSARRLKLEIKKDSKGMVFVENVTTIPISTLEELRMILERGSERRHVSGTNMNEESSRSHLILSVVIESIDLQTQSAARGKLSFVDLAGSERVKKSGSAGCQLKEAQSINKSLSALGDVIGALSSGNQHIPYRNHKLTMLMSDSLGGNAKTLMFVNVSPAESNLDETYNSLLYASRVRTIVNDPSKHISSKEMVRLKKLVAYWKEQAGKKGEEEDLVDIEEDRTRKDEADS
Protein: Acidic fibroblast growth factor intracellular-binding protein B (aFGF intracellular-binding protein B) (FGF-1 intracellular-binding protein B) (Q6T938)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Mediates with IER2 FGF-signaling in Kupffer's vesicle ciliogenesis and in the establishment of laterality in the embryo. May be involved in mitogenic function of FGF1 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:19164561}. Endomembrane system {ECO:0000250|UniProtKB:O43427}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43427}.
Interaction partners:
Sequence:
MELDVFVGNTTVLDEDIYQLWLDGHSVSDVVRQRMDAGVLLECEASPDVLQSDTIDQFRTFQMCERLLQSPSKVANQLLFQIPSDQQAMLIERYYEFDSVFAREVLGKKLSKGTKKDLDDVSAKTGIALKSCRRQFDNFKRVFKVVEELKGPLVENIQRHFLLSDDLARDYATIVFFANSRFETGKRKLQYLSFQDFAFCAGQLISYWTVGAVDNMIEDMDVDLEKDFLHDLKDLKVLVNDKDLLDQHKSLVCGQLRGKIKVFNEMEASFKNLSRALVNIASKLTHAKDVRDLFIDLVEKFIEPCRSDKWTSGDLRLFLTHYSTSVHTLEAFRHQVIWDRYMGVIKSCILKMYHD
Protein: Nudix hydrolase 1 (AtNUDT1) (7,8-dihydro-8-oxoguanine-triphosphatase) (8-oxo-dGTP diphosphatase) (8-oxo-dGTPase) (EC 3.6.1.55) (Dihydroneopterin triphosphate diphosphatase) (EC 3.6.1.67) (Dihydroneopterin triphosphate pyrophosphohydrolase) (DHNTP pyrophosphohydrolase) (NADH pyrophosphatase) (EC 3.6.1.22) (Q9CA40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the hydrolysis of some nucleoside diphosphate derivatives. Its substrate specificity is unclear. In vitro, it can use NTP, dNTP, 8-oxo-GTP, 8-oxo-dGTP, dGTP, dATP, dTTP or dihydroneopterin triphosphate (DHNTP) as substrate. Has some NADH pyrophosphatase activity in vitro; however, such activity may not be relevant in vivo due to the high concentration of manganese used during the experiments. Plays an important role in protection against oxidative DNA and RNA damage by removing oxidatively damaged form of guanine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17804481}.
Interaction partners:
- Nudix hydrolase 11
- GTP cyclohydrolase 1
- Nudix hydrolase 10
- Nudix hydrolase 2
- Nudix hydrolase 14, chloroplastic
- Nudix hydrolase 25
- Nudix hydrolase 12, mitochondrial
- Nudix hydrolase 4
- Nudix hydrolase 13, mitochondrial
- Nudix hydrolase 19, chloroplastic
Sequence:
MSTGEAIPRVAVVVFILNGNSILLGRRRSSIGNSTFALPGGHLEFGESFEECAAREVMEETGLKIEKMKLLTVTNNVFKEAPTPSHYVSVSIRAVLVDPSQEPKNMEPEKCEGWDWYDWENLPKPLFWPLEKLFGSGFNPFTHGGGD
Protein: (S)-N-methylcoclaurine 3'-hydroxylase isozyme 1 (EC 1.14.14.102) (Cytochrome P450 80B1) (Cytochrome P450 80B3) (Q9SP06)
Organism: Papaver somniferum (Opium poppy)
Function: Involved in the biosynthesis of benzylisoquinoline alkaloids. Catalyzes the 3'-hydroxylation of (S)-N-methylcoclaurine.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:15849302}. Note=Like CYP80B3b (AC I3V6B1), the full-length CYP80B3 is probably anchored to the membrane by a signal anchor (Probable). Localized to the parietal region of the sieve element cytoplasm (PubMed:14508000). {ECO:0000269|PubMed:14508000, ECO:0000305}.
Interaction partners:
Sequence:
SLVAVVITTFLYLIFRDSSPKGLPPGPKPWPIVGNLLQLGEKPHSQFAQLAETYGDLFSLKLGSETVVVASTPLAASEILKTHDRVLSGRYVFQSFRVKEHVENSIVWSECNETWKKLRKVCRTELFTQKMIESQAEVRESKAMEMVEYLKKNVGNEVKIAEVVFGTLVNIFGNLIFSQNIFKLGDESSGSVEMKEHLWRMLELGNSTNPADYFPFLGKFDLFGQSKDVADCLQGIYSVWGAMLKERKIAKQHNNSKKNDFVEILLDSGLDDQQINALLMEIFGAGTETSASTIEWALSELTKNPQVTANMRLELLSVVGKRPVKESDIPNMPYLQAFVKETLRLHPATPLLLPRRALETCKVLNYTIPKECQIMVNAWGIGRDPKRWTDPLKFSPERFLNSSIDFKGNDFELIPFGAGRRICPGVPLATQFISLIVSSLVQNFDWGFPKGMDPSQLIMEEKFGLTLQKEPPLYIVPKTRD
Protein: Embryonic ectoderm development (B5DF02)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Histone-lysine N-methyltransferase EZH2
- SUZ12 polycomb repressive complex 2 subunit
- [histone H3]-lysine
- Protein Jumonji
- Histone-binding protein RBBP7
- Zinc finger protein AEBP2
- RB-binding protein 4, chromatin-remodeling factor.
- Metal-response element-binding transcription factor 2
- RB binding protein 4, chromatin remodeling factor like 1
- E3 ubiquitin-protein ligase RING2
Sequence:
MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR
Protein: Ent-copalyl diphosphate synthase 2, chloroplastic (Ent-CDP synthase 2) (OsCPS2) (OsCPS2ent) (EC 5.5.1.13) (Diterpene cyclase 2) (OsCyc2) (Ent-kaurene synthase A) (Q6Z5I0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to the phytoalexin precursor ent-copalyl diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- diphosphomevalonate decarboxylase
- Diphosphomevalonate decarboxylase
- Os02g0668100 protein
- Os01g0248701 protein
- Phytoene synthase 3, chloroplastic
- Phytoene synthase 2, chloroplastic
- Squalene synthase
- Squalene synthase
- Phytoene synthase 1, chloroplastic
Sequence:
MQMQVLTAASSLPRATLLRPAAAEPWRQSFLQLQARPIQRPGIMLHCKAQLQGQETRERRQLDDDEHARPPQGGDDDVAASTSELPYMIESIKSKLRAARNSLGETTVSAYDTAWIALVNRLDGGGERSPQFPEAIDWIARNQLPDGSWGDAGMFIVQDRLINTLGCVVALATWGVHEEQRARGLAYIQDNLWRLGEDDEEWMMVGFEITFPVLLEKAKNLGLDINYDDPALQDIYAKRQLKLAKIPREALHARPTTLLHSLEGMENLDWERLLQFKCPAGSLHSSPAASAYALSETGDKELLEYLETAINNFDGGAPCTYPVDNFDRLWSVDRLRRLGISRYFTSEIEEYLEYAYRHLSPDGMSYGGLCPVKDIDDTAMAFRLLRLHGYNVSSSVFNHFEKDGEYFCFAGQSSQSLTAMYNSYRASQIVFPGDDDGLEQLRAYCRAFLEERRATGNLMDKWVIANGLPSEVEYALDFPWKASLPRVETRVYLEQYGASEDAWIGKGLYRMTLVNNDLYLEAAKADFTNFQRLSRLEWLSLKRWYIRNNLQAHGVTEQSVLRAYFLAAANIFEPNRAAERLGWARTAILAEAIASHLRQYSANGAADGMTERLISGLASHDWDWRESKDSAARSLLYALDELIDLHAFGNASDSLREAWKQWLMSWTNESQGSTGGDTALLLVRTIEICSGRHGSAEQSLKNSADYARLEQIASSMCSKLATKILAQNGGSMDNVEGIDQEVDVEMKELIQRVYGSSSNDVSSVTRQTFLDVVKSFCYVAHCSPETIDGHISKVLFEDVN
Protein: IpaB/EvcA family protein (L0028) (Mitochondria associated protein) (Q9R8E4)
Organism: Escherichia coli
Interaction partners:
Sequence:
MFSPMTMAGRSLVQATAQTLKPAVTRAAMQAGTGATGMRFMPVQSNFVINHGKLTNQLLQAVAKQTRNGDTQQWFQQEQTTYISRTVNRTLDDYCRSNNSVISKETKGHIFRAVENALQQPLDMNGAQSSIGHFLQSNKYFNQKVDEQCGKRVDPITRFNTQTKMIEQVSQEIFERNFSGFKVSEIKAITQNAILEHVQDTRL
Protein: Protein FAM209A (Q5JX71)
Organism: Homo sapiens (Human)
Function: May play a role in sperm acrosome biogenesis.
Subcellular location: Nucleus inner membrane {ECO:0000250|UniProtKB:A2APA5}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane and coiled-coil domain-containing protein 5A
Sequence:
MWTLKSSLVLLLCLTCSYAFMFSSLRQKTSEPQGKVQYGEHFRIRQNLPEHTQGWLGSKWLWLLFVVVPFVILQCQRDSEKNKEQSPPGLRGGQLHSPLKKKRNASPNKDCAFNTLMELEVELMKFVSKVRNLKRAMATGSGSNLRLRKSEMPADPYHVTICEIWGEESSS
Protein: Fibroblast growth factor 1 (FGF-1) (Acidic fibroblast growth factor) (aFGF) (Heparin-binding growth factor 1) (HBGF-1) (P61149)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequential autophosphorylation on tyrosine residues which act as docking sites for interacting proteins, leading to the activation of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its binding to integrin, subsequent ternary complex formation with integrin and FGFR1, and the recruitment of PTPN11 to the complex are essential for FGF1 signaling. Induces the phosphorylation and activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1. Can induce angiogenesis.
Subcellular location: Secreted {ECO:0000269|PubMed:15627653}. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1 (By similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59 (By similarity). {ECO:0000250}.
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 4
- S100 calcium-binding protein A13
- Fibroblast growth factor-binding protein 1
- Fibroblast growth factor 2
- Synaptotagmin-1
- Vascular endothelial growth factor receptor 1
- Receptor protein-tyrosine kinase
Sequence:
MAEGEITTFAALTERFNLPLGNYKKPKLLYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESAGEVYIKGTETGQYLAMDTEGLLYGSQTPNEECLFLERLEENHYNTYTSKKHAEKNWFVGLKKNGSCKRGPRTHYGQKAILFLPLPVSSD
Protein: RNA-binding Fox protein 1, isoform J (Q9VT99)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYYPHMVQAGVAPFPGAPAGYAAAPNPGAAVVAAAAAAQQQQQQQQQQQQQQQQAQQQQQQQVAGGPPSAADSLSMAVAAAAAKQSADPVTQMKSGSEAAGSGNSNNNNTAGAGTGAPGAAGGLTTEYSSGGCGGGGASTANSVVVATSVSDVVNASLYMQQKTNLSTQTQTQYEYEYEYNGTSLAEPRVPGPIPHPLTNGHAVDQVQQPPVQQQHLQSSLPPQNVLSISTVLIANEAAESQQSSAMQNAGGGGNTGGGGGGGGGGTPSSPLSNSPSSATASQAGGCGLTLNGSATEGSMSGDTSPVASGEPLLQTPPAHQQQQQQQQPLLCSSPTSMQSSGTSVTGSSIASGTLAATSSSGVGLLPTTGLDSIANGGAPTGCAVVPASTSQVIAHLNAAAAAASGIVSPSANVATSLSSALVPAQSVAAVAAASLDAKSQPKRLHVSNIPFRFRDPDLRAMFGQFGTILDVEIIFNERGSKGFGFVTFANSNDAERARERLHGTVVEGRKIEVNNATARVQTKKVTAVPNVCVQWPEAAVAAAMRGVAIQRGHVGVVGATPYHHPHHPHHHPALLAASAAAAQQQQQRQLAAAAVATAAVAQQQQQQQQAVVQQQQQQVAAAAQQQHQQQQQQQQQAVQQQQAVQQQQQHQQQQQQQQQQQHAAVAAAAAAASHPHMHAAHAHAHAHALGPQLAQLQAVAVPTAASNAAALQQSLAAAIQNPSGNPNAAAAAAAYAARLSAATGATQSPQTAAAAAAAASMAASANAANNAAALHGFAPVYYDPFLAAAASADPNLRFQATAPLLKTPLSQAQQQAYATAATTYTAVAARAAYGAAAAAAAQPALAGYATVAGYAREYADPYLGHGIGPVPGYGATMYRGGFNRFTPY
Protein: Seed allergenic protein RAG1 (Seed allergenic protein RA17) (allergen Ory s aA_TI) (Q01883)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Seed storage protein.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MASNKVVFSVLLLVVLSVLAAAMATMADHHQVYSPGEQCRPGISYPTYSLPQCRTLVRRQCVGRGAASAADEQVWQDCCRQLAAVDDGWCRCGALDHMLSGIYRELGATEAGHPMAEVFPGCRRGDLERAAASLPAFCNVDIPNGPGGVCYWLGYPRTPRTGH
Protein: Carboxylesterase 1E (EC 3.1.1.1) (Egasyn) (Liver carboxylesterase 22) (Es-22) (Esterase-22) (Q64176)
Organism: Mus musculus (Mouse)
Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q63108}. Microsome membrane {ECO:0000250|UniProtKB:Q63108}.
Interaction partners:
- Beta-glucuronidase
- Cytochrome P450 2E1
- Myeloperoxidase
- Arylamine N-acetyltransferase 1
- Arylamine N-acetyltransferase 2
- Cytidine deaminase
- Arylamine N-acetyltransferase 3
- UDP-glucuronosyltransferase 2A3
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 2B17
Sequence:
MCLSALILVSLAAFTAGAGHPSSPPMVDTVQGKVLGKYISLEGFTQPVAVFLGVPFAKPPLGSLRFAPPQPAEPWSSVKNATSYPPMCFQDPVTGQIVNDLLTNRKEKIPLQFSEDCLYLNIYTPADLTKSDRLPVMVWIHGGGLVLGGASTYDGLVLSTHENVVVVVIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIAKFGGDPGSVTIFGESAGGESVSVLVLSPLAKNLFQRAISESGVALTAGLVKKNTRPLAEKIAVISGCKNTTSAAMVHCLRQKTEEELLGTTLKLNLFKLDLHGDSRQSHPFVPTVLDGVLLPKMPEEILAEKNFNTVPYIVGINKQEFGWILPTMMNYPPSDVKLDQMTAMSLLKKSSFLLNLPEDAIAVAIEKYLRDKDYTGRNKDQLLELIGDVVFGVPSVIVSRGHRDAGAPTYMYEFQYSPSFSSEMKPDTVVGDHGDEIYSVFGAPILRGGTSEEEINLSKMMMKFWANFARNGNPNGQGLPHWPEYDQKEGYLQIGATTQQAQKLKEKEVAFWTELLAKKQLPTEHTEL
Protein: RNA-binding protein Hfq (HF-1) (Host factor-I protein) (HF-I) (P0A6X3)
Organism: Escherichia coli (strain K12)
Function: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32. Binds with high specificity to tRNAs. Binds sRNA antitoxin RalA. In vitro, stimulates synthesis of long tails by poly(A) polymerase I. Required for RNA phage Qbeta replication. Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease E
- Poly
- tRNA dimethylallyltransferase
- Carbon storage regulator
- Transcription termination factor Rho
- RNA polymerase sigma factor RpoS
- Catalase HPII
- Modulator of FtsH protease HflK
- RNA polymerase sigma-54 factor
Sequence:
MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE
Protein: Armadillo repeat-containing protein 6 (Q8BNU0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MASKRITQETFDAAVRENIEEFEMGTEEAIREAVEQFESQGVDLSNIVKTIPKVSLDGLQEPTHSVLQALNDLQESLTGSRLQEVSAHLVRFCDQCKQQKASRYLAAQKGAYPILLAAWQLAATSNQGLLLQALNALAVLTDGQPDLLDAQGLHLLVATLAQNAANTELTCCGIRCVRHVCLKHEQNRQDLVKAGVLPLLTAAITQHGQHADVVREACWALRVMTFDDDIRVPFGHAHEHAKMIVQENKGLKVLIEAARAFSDNPGVLSELCSTLSRLAVRNEFCQEVIDLGGLGILVTLLADCNDHQDLVKQVLSALRAIAGNDDVKDAIVRAGGTESIVAAMTRHLASPQVCEQSCAALCVLALRKPDNSRVIIEGGGALAALQAMKAHPQEAGVQKQACMLIRNLVSRSQVFSKPILDLGAEELILQARAAHPDCEDVAKAALRDLGCRVELRELWTGKKGDLAL