wanglab/gogpt-training-data huggingface dataset:
Protein: SP2523 (Q7KIS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQQTQLVSEPAKSLVEEVMKSAEQMVEQPKQQKSLNERQLTEDFLLMEQQTQLPSDIVKPTDKLIDGIESAAPVGDEASPFHTPKLTTSVVTQEPQQLASEYDSDTFGKQATIPLGDSKIDQGLIAPVSMEPRKSLTDAEFCKSVGETITKKMSVGVIEISDELKKIESEIPHSQTPPPTPSDNKTDKQNEEPELISLERDYLADTVTTLHTTTESTLERVSAITKIETLHERKVELSNLDTEKISHEIETGGDLPNSSETDTTPVPPSKESESKTETEPTVVTNAFTTTSHDTPTPKPRVLKASSPVSEGTDSTTIPGPVPKPEIPIDISFDANAPVPKPRAPIKHTEPFENLAALAEQSDSISLRSFELTEDISKTDEPSTELSIRSQLRDIVTTTTVSEDHTESFEPTSEISVDDADTEKSEGAEKTTSFYIGESSRNVIIKTSTRSASVTPQEEEAQGEIGIDAKDISLMKEVSVDSDEANDVFKEFITMKPEDPIAMDSKITRQGSETRNDILEFENADKDKTAEQKLSKVTTEESLTTSTGSSGRAIIEIAPSSSEDPDESSKEIPEIVNTISEKAAASDNFELPLEKSEWETSEKEIPTEGKPKVVHSPQQPQEASMKSTLDRFHVDEILAEEQVTDEHSSSDHKSFKDQTPSELGSSTVPQEYTFAVESEDISSFIGIPEASMQTSTLDSTQPPEGLFDTTIKETLNKQAAMAHYAQDVFGRGERRDDHGSLGFISTGTAEELSSMEEHMAKEEQASLGFISTETAEDFSSMEDYYSEKLAIASVVADEVATEKSLTTSTFEELSSDQSMKPIDVVVHRLKTETSPDSINRWSIPDVDTSSSSESFHRSFDKTQSRPLSSDLDNLVTTTGTGTSSDYQTAREFTTTGRTEGTEYISAVSTLGSSSLDSQSETSANLASIDVSELSETLVASSAEVDAFEAEEMSRLRDLRADDEDSDESVELPGTAGYPSIEQQSLMKRSQEMIFKPKTLDDEPLAVQVAQIEEYPKPKEAERTWGLAYPLEDSKVDSPRESEKGEDILLYHGDPRRSIDESKLASSLDEGSILSVSMSSTSNIDTVVENFDDIIGSAGSSSLTGIEGFQYGHDESIPSASVPEDATFMLEMESKEHSPQDSNASTPPGGESKRRGHKRNESISGDALKNLDKEVALLGEGKESESESDTDPYESEYARQFRSPKERKSKKKKQAAAEMDHSGELEKRPFTPSQLVAEVIVEDSITEELEAEAAMIEERRPSQNMQDYSNIPDIMVTEDIKSPILEEETDEFPEKMLYKVRTEEELHKASDTSVYQKAKAEEKEQDFQRRVQEQYRQKLEELKRAEVGAEYDDRKAPDSPDSFEMVEQPDISDEFVIIEEVAKEANEVDLGGQSIKIKPVKYEQKHDEDVEKIIIKSAPADPKLGSQLYKDDLNFEFEESPPTGASSSSEQQEESDSSETAAANKRWVEMQLTDNQLRYPYDLAGAVLEDIKEEDGEFEVGSSRISSFKDSFSSTPEYDVAARRYHSRGEHDDVSMSSLQEFESLEQAISLENRNRTHQGSTDSSNGSFTRRYVVRHSGSGTAPGDDVSVSSLKDFEGLENACIEAHLIEIKAREEAALLSRSDESNKSNGSDKGATGNVVVTKVTRTVTRTEVVPSSQVESIEALLKQKLEREEGSVQGRVTDIGTTELDTKSKIDSQDSEKDSIDSMEISKSHDMMTSSIESFDISKDATTRSDVDSLEIDKRHSRQESIESFGDEQLDLMTKFVSGGGVTLGDGLTTTTTTTTTSTDADGHEHTVTRVITTITNVGGGIQELPMDESGMSKDVSVDSLNMCVEQTTSSAGTTATYQTSAGNSQMSGSVTSCASSTLMEDSFPGVGGMSSSQMSASFWSHDESTVVEDEGRDLAKKPQQGH
Protein: Linker histone H1M (Q4V956)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU003894}.
Interaction partners:
Sequence:
MAPKKAAAEPTATITKGSENEITETKPAAPEDSNAKSAARKVSPHPSTMEMVKEALKELDSRKGVSAQAIRGYIKEKYTTVDETRLKYMVRRALNKGMDTGVFVRPANSGSTTGAQGRFRIAAKTKAKEAKAQSKENADPNEPKATKPKKEKATKAKGEGATKEKPTKKKETTDDAKPKTSEQNGTASKVAPAKKPKAKNAAGEGGAKPKPSKAKASKEGAEEPATKKGGKKNAARAEDGESGAAATEKAPGKRAKK
Protein: Ubiquitin-conjugating enzyme E2 variant 2 (DDVit 1) (Enterocyte differentiation-associated factor 1) (EDAF-1) (Enterocyte differentiation-promoting factor 1) (EDPF-1) (MMS2 homolog) (Vitamin D3-inducible protein) (Q15819)
Organism: Homo sapiens (Human)
Function: Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase RAD18
- Polyubiquitin-B
- Helicase-like transcription factor
- E3 ubiquitin-protein ligase SHPRH
- Ubiquitin-ribosomal protein eL40 fusion protein
- TNF receptor-associated factor 6
- Ubiquitin-conjugating enzyme E2 B
Sequence:
MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN
Protein: Phosphotransbutyrylase (EC 2.3.1.19) (Q72EF1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Probable butyrate kinase
- Acetate kinase
- Acetolactate synthase small subunit
- Succinate--CoA ligase subunit alpha
- Pyruvate:ferredoxin oxidoreductase
Sequence:
MSVLQAGTATETPRTSDAGRQNEGADGAVAAPRTLDDIVAAVVRRGIPVRVAVAACAEPNALAAVLEARDMGMAVPVLVGDIAATESIATERGLSLEGCEVEDEPVPVKAVQRAVDRVRTGGADVLMKGLVNTDVLLRVVLNRVSGLSAGGLLSHVAVCSLPATCGGEASASSRLVCITDAAVNISPNMERKLGIVRNAICVARSLGIPSPRVAMLAATEKVMLPAMPATLDAQIVARMADQGEFGDAMVAGPMALDVAISPDIAARKGVSHPVAGRADILCAPDIESGNILYKSLTTLAHVEMAGILTGTTAPVVVPSRGDSRRSKLLSLALAAYVAMECRL
Protein: V-type proton ATPase subunit F (V-ATPase subunit F) (V-ATPase 14 kDa subunit) (Vacuolar proton pump subunit F) (P39111)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular location: Vacuole membrane {ECO:0000305|PubMed:7929071}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase subunit d
- V-type proton ATPase catalytic subunit A
Sequence:
MAEKRTLIAVIADEDTTTGLLLAGIGQITPETQEKNFFVYQEGKTTKEEITDKFNHFTEERDDIAILLINQHIAENIRARVDSFTNAFPAILEIPSKDHPYDPEKDSVLKRVRKLFGE
Protein: Galanin receptor type 3 (GAL3-R) (GALR-3) (O88853)
Organism: Mus musculus (Mouse)
Function: Receptor for the hormone galanin and spexin-1.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Galanin receptor type 1
- Spexin
- Galanin receptor type 2
- Galanin-like peptide
Sequence:
MADIQNISLDSPGSVGAVAVPVVFALIFLLGMVGNGLVLAVLLQPGPSAWQEPGSTTDLFILNLAVADLCFILCCVPFQAAIYTLDAWLFGAFVCKTVHLLIYLTMYASSFTLAAVSVDRYLAVRHPLRSRALRTPRNARAAVGLVWLLAALFSAPYLSYYGTVRYGALELCVPAWEDARRRALDVATFAAGYLLPVTVVSLAYGRTLCFLWAAVGPAGAAAAEARRRATGRAGRAMLTVAALYALCWGPHHALILCFWYGRFAFSPATYACRLASHCLAYANSCLNPLVYSLASRHFRARFRRLWPCGHRRHRHHHHRLHRALRRVQPASSGPAGYPGDARPRGWSMEPRGDALRGGETRLTLSARGPQ
Protein: Tubulin alpha-1A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Alpha-tubulin isotype M-alpha-1) (Tubulin alpha-1 chain) [Cleaved into: Detyrosinated tubulin alpha-1A chain] (P68369)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37865089}.
Interaction partners:
- Tubulin beta-2B chain
- Tubulin beta-4A chain
- Tubulin beta-4B chain
- Tubulin beta-2A chain
- Microtubule-associated protein
- Tubulin beta-5 chain
- Tubulin alpha-1B chain
- Cell division control protein 42 homolog
- Tubulin beta-6 chain
- Tubulin beta-3 chain
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Leucine rich adaptor protein 1-like (Q8IV03)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDSPLPDLRDIELKLGRKVPESLVRSLRGEEPVPRERDRDPCGGSGGGGGGGGGCSSSSSYCSFPPSLSSSSSSSPTSGSPRGSHSSALERLETKLHLLRQEMVNLRATDVRLMRQLLVINESIESIKWMIEEKATITSRGSSLSGSLCSLLESQSTSLRGSYNSLHDGSDGLDGISVGSYLDTLADDVPGHQTPSDLDQFSDSSLIEDSQALHKRPKLDSEYYCFG
Protein: Sugar efflux transporter B (P33026)
Organism: Escherichia coli (strain K12)
Function: Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport lactose and glucose.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MHNSPAVSSAKSFDLTSTAFLIVAFLTGIAGALQTPTLSIFLTDEVHARPAMVGFFFTGSAVIGILVSQFLAGRSDKRGDRKSLIVFCCLLGVLACTLFAWNRNYFVLLFVGVFLSSFGSTANPQMFALAREHADKTGREAVMFSSFLRAQVSLAWVIGPPLAYALAMGFSFTVMYLSAAVAFIVCGVMVWLFLPSMRKELPLATGTIEAPRRNRRDTLLLFVICTLMWGSNSLYIINMPLFIINELHLPEKLAGVMMGTAAGLEIPTMLIAGYFAKRLGKRFLMRVAAVGGVCFYAGMLMAHSPVILLGLQLLNAIFIGILGGIGMLYFQDLMPGQAGSATTLYTNTSRVGWIIAGSVAGIVAEIWNYHAVFWFAMVMIIATLFCLLRIKDV
Protein: FAD assembly factor SdhE (Antitoxin CptB) (P64559)
Organism: Escherichia coli (strain K12)
Function: An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH. Required for flavinylation of the flavoprotein subunit FdrA of fumarate reductase (FDR). Binds 2 different sites on the flavoprotein target FrdA (and presumably also SdhA), possibly positioning FAD and protein to facilitate the covalent bond formation; covalent attachment of FAD is not required for SDH or FDR complex enzyme formation. Overexpression of this protein and YgfX (formerly cptA) restores production of prodigiosin antibiotic (Pig) in Serratia strains with deletions of sdhE-ygfX.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:G4V4G2}.
Interaction partners:
- Inner membrane protein YgfX
- Fumarate reductase flavoprotein subunit
- Succinate dehydrogenase flavoprotein subunit
Sequence:
MDINNKARIHWACRRGMRELDISIMPFFEHEYDSLSDDEKRIFIRLLECDDPDLFNWLMNHGKPADAELEMMVRLIQTRNRERGPVAI
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Triose-phosphate isomerase) (P07669)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glucose-6-phosphate isomerase
- Phosphoglycerate mutase
- ATP-dependent 6-phosphofructokinase
- Transaldolase
- Enolase 1-1
- Enolase 1-2
Sequence:
MARKFFVGGNFKMNGSLESMKTIIEGLNTTKLNVGDVETVIFPQNMYLITTRQQVKKDIGVGAQNVFDKKNGAYTGENSAQSLIDAGITYTLTGHSERRTIFKESDEFVADKTKFALEQGLTVVACIGETLAEREANETINVVVRQLNAIADKVQNWSKIVIAYEPVWAIGTGKTATPEQAQEVHAEIRKWATNKLGASVAEGLRVIYGGSVNGGNCKEFLKFHDIDGFLVGGASLKPEFHNIVNVHSL
Protein: very-long-chain 3-oxoacyl-CoA synthase (EC 2.3.1.199) (Q9SQV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sphinganine C4-monooxygenase 1
- Glycerophosphocholine acyltransferase 1
- Delta-9 acyl-lipid desaturase 2
- Oleosin
Sequence:
MASIYSSLTYWLVNHPYISNFTWIEGETLGSTVFFVSVVVSVYLSATFLLRSAIDSLPSLSPRILKPITAVHSLILCLLSLVMAVGCTLSITSSHASSDPMARFLHAICFPVDVKPNGPLFFWAQVFYLSKILEFGDTILIILGKSIQRLSFLHVYHHATVVVMCYLWLRTRQSMFPIALVTNSTVHVIMYGYYFLCAVGSRPKWKRLVTDCQIVQFVFSFGLSGWMLREHLFGSGCTGIWGWCFNAAFNASLLALFSNFHSKNYVKKPTREDGKKSD
Protein: Glycerol-3-phosphate dehydrogenase 1 (EC 1.1.5.3) (P9WN81)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Glycerol kinase
- Glycerol-3-phosphate dehydrogenase [NAD
- Diacylglycerol kinase
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase 2
- Glycerol-3-phosphate acyltransferase
- Uncharacterized HTH-type transcriptional regulator Rv2250c
- Putative acyltransferase plsB1
- 1-acylglycerol-3-phosphate O-acyltransferase
- Possible flavoprotein
Sequence:
MLMPHSAALNAARRSADLTALADGGALDVIVIGGGITGVGIALDAATRGLTVALVEKHDLAFGTSRWSSKLVHGGLRYLASGNVGIARRSAVERGILMTRNAPHLVHAMPQLVPLLPSMGHTKRALVRAGFLAGDALRVLAGTPAATLPRSRRIPASRVVEIAPTVRRDGLDGGLLAYDGQLIDDARLVMAVARTAAQHGARILTYVGASNVTGTSVELTDRRTRQSFALSARAVINAAGVWAGEIDPSLRLRPSRGTHLVFDAKSFANPTAALTIPIPGELNRFVFAMPEQLGRIYLGLTDEDAPGPIPDVPQPSSEEITFLLDTVNTALGTAVGTKDVIGAYAGLRPLIDTGGAGVQGRTADVSRDHAVFESPSGVISVVGGKLTEYRYMAEDVLNRAITLRHLRAAKCRTRNLPLIGAPANPGPAPGSGAGLPESLVARYGAEAANVAAAATCERPTEPVADGIDVTRAEFEYAVTHEGALDVDDILDRRTRIGLVPRDRERVVAVAKEFLSR
Protein: Thiamine transport system permease protein ThiP (P31549)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Probably responsible for the translocation of the substrate across the membrane (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Thiamine import ATP-binding protein ThiQ
- Thiamine-binding periplasmic protein
- Thiamine kinase
- Thiamine-phosphate synthase
- Ferric enterobactin transport ATP-binding protein FepC
- Vitamin B12-binding protein
- Fe
- Iron
- Iron
Sequence:
MATRRQPLIPGWLIPGVSATTLVVAVALAAFLALWWNAPQDDWVAVWQDSYLWHVVRFSFWQAFLSALLSVIPAIFLARALYRRRFPGRLALLRLCAMTLILPVLVAVFGILSVYGRQGWLATLCQSLGLEWTFSPYGLQGILLAHVFFNLPMASRLLLQALENIPGEQRQLAAQLGMRSWHFFRFVEWPWLRRQIPPVAALIFMLCFASFATVLSLGGGPQATTIELAIYQALSYDYDPARAAMLALLQMVCCLGLVLLSQRLSKAIAPGTTLLQGWRDPDDRLHSRICDTVLIVLALLLLLPPLLAVIVDGVNRQLPEVLAQPVLWQALWTSLRIALAAGVLCVVLTMMLLWSSRELRARQKMLAGQVLEMSGMLILAMPGIVLATGFFLLLNNTIGLPQSADGIVIFTNALMAIPYALKVLENPMRDITARYSMLCQSLGIEGWSRLKVVELRALKRPLAQALAFACVLSIGDFGVVALFGNDDFRTLPFYLYQQIGSYRSQDGAVTALILLLLCFLLFTVIEKLPGRNVKTD
Protein: Tetraspanin-14 (Tspan-14) (DC-TM4F2) (Transmembrane 4 superfamily member 14) (Q8NG11)
Organism: Homo sapiens (Human)
Function: Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Negatively regulates ADAM10-mediated cleavage of GP6 (By similarity). Promotes ADAM10-mediated cleavage of CDH5 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26686862}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10
- CD9 antigen
- Tetraspanin-15
Sequence:
MHYYRYSNAKVSCWYKYLLFSYNIIFWLAGVVFLGVGLWAWSEKGVLSDLTKVTRMHGIDPVVLVLMVGVVMFTLGFAGCVGALRENICLLNFFCGTIVLIFFLELAVAVLAFLFQDWVRDRFREFFESNIKSYRDDIDLQNLIDSLQKANQCCGAYGPEDWDLNVYFNCSGASYSREKCGVPFSCCVPDPAQKVVNTQCGYDVRIQLKSKWDESIFTKGCIQALESWLPRNIYIVAGVFIAISLLQIFGIFLARTLISDIEAVKAGHHF
Protein: Protein REDUCED CHLOROPLAST COVERAGE 1 (F4HS99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as the scaffold of a protein complex, which sequesters key factors that are required for the G2 to M transition in meristematic tissues (By similarity). Together with REC2, REC3 and FMT/CLU, contributes to the establishment of the cellular volume devoted to the chloroplast compartment.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26862170}. Cytoplasm, cytosol {ECO:0000269|PubMed:26862170}. Note=Excluded from the nucleus upon treatment with amitrole, which inhibits cell expansion and chloroplast function. {ECO:0000269|PubMed:26862170}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g76280
- Outer membrane OMP85 family protein
- F28J7.36 protein
- Embryo defective 2739
- Protein ARABIDILLO 1
- GPI ethanolamine phosphate transferase 1
- Beta-adaptin-like protein A
- Large ribosomal subunit protein P1y
- 65-kDa microtubule-associated protein 5
- Large ribosomal subunit protein P1z
Sequence:
MAPKNNRGKTKGDKKKKEEKVLPVIVDVIVNLPDETEAILKGISTDRIIDVRRLLSVNFDTCHVTNYSLSHEIRGSRLKDTVDVSALKPCVLTLTEEDYNEGTAVAHVRRLLDIVACTTCFGPSPEKSDSVKSAQVKGGGKNSKQSDTSPPPSPASKDTVVDEAGETSHSFPKLGSFYEFFSLAHLTPPLQYIRLATKRETEDIAKEDHLLSIDVKLCNGKLVHIEGCRKGFYSIGKQRIICHNLVDLLRQISRAFDNAYSDLLKAFSERNKFGNLPYGFRANTWLIPPTAAQSPAAFPPLPVEDERWGGDGGGQGRDGSYDLVPWSNEFAFIASMPCKTAEERQVRDRKVFLLHNLFVDVATFRAIKAVQKVMAEPVLAEEDSEVLYSETVRDLTVTVTRDTSNASSKVDTKIDGIQATGLDKKKLMERNLLKGLTADENTAAHDVATLGTISLKYCGYIAVVKLEKESEELSPPSQIVDLLEQPEGGANALNINSLRFLLHKSSPEQNKKTPQQHDDELTSSREFVSKMLEESIAKLEGEEIDRDSIMRWELGACWIQHLQDQKNTEKDKKQTGEKSKNELKVEGLGKPLKSLNSSKKKTDVSSPKTPQTALSSQVDAVSSEADTAASLQSDAEKNAQENVLILKNLLSDAAFTRLKESDTGLHHKSLQELVDLAQNYYTEVAIPKLVADFGSLELSPVDGRTLTDFMHTRGLRMRSLGYVVKLSDKLSHVQSLCVHEMIVRALKHILQAVISAVATDTDKIAIKVAAALNMMLGIPENVAATPHNPWNVHPLIFRWLEKFLKKRYDYDLNAFSYKDLRKFAILRGLCHKVGIELIPRDFDMDSPAPFRKTDVVSLVPVHKTFYFKSMQQAACSSADGRQLLESSKTALDKGKLEDAVTYGTKALAKLVAVCGPYHRMTAGAYSLLAVVLYHTGDFNQATIYQQKALDINERELGLDHPDTMKSYGDLAVFYYRLQHTELALKYVKRALYLLHLTCGPSHPNTAATYINVAMMEEGLGNVHVALRYLHKALKCNQRLLGPDHIQTAASYHAIAIALSLMEAYHLSVQHEQTTLRILRAKLGPDDLRTQDAAAWLEYFESKAFEQQEAARNGTPKPDASIASKGHLSVSDLLDYINPSHNAKGKESVAAKRKNYILKLKEKSKQSNVSEHLVEIPREKQKEMSEEDTEETGSEEGKSSEENHETILAPVEEPPSPPVIEDATMDNSNPITSSDVSTEPQHPDGSEDGWQPVQRPRSAGSYGRRMKQRRASIGKVYTYQKKNVEADIDNPLFQNATQQNDKYYILKKRTASYSSYADHHSPGLTTQGTKFGRKIVKTLAYRVKSTQPSSGNAKTAGETSEEDGLKTDASSVEPPTLSSTVQSEAYHTKNSVVSLGKSPSYKEVALAPPGSIAKYQVWVPQAEVSDKQEDDEMEKKTEQGTSMELTRDEQMITGLEEEVKKEISADPESNITQGEEEIKVELQPSEGVLGGSHINENDESGGGIQVEEQVEVELINDGVTDMIHSTREQQVIDQLAADSEDLKAKLSISTTDSGDASRGLLPNKKLSASAAPFNPSSPPSIIRPTPIGMNIGPSWPVNMTLHHGPPPPYPSPPTTPNLMQPMSFVYPPPYSQSVPTSTYPVTSGPFHPNQFPWQLNVSDFVPRTVWPGCHPVEFPPPHMITEPIAATVLEPTVILPTDIDTSGVEETKEGTQDVAVADEVMDSVNHVNNAVARSETENGNRKSEEGEKTFSILLRGRRNRKQTLRMPISLLNRPYDSQPFKLGYSRVIRDSEAPKSVA
Protein: piRNA biogenesis protein EXD1 (Exonuclease 3'-5' domain-containing protein 1) (Exonuclease 3'-5' domain-like-containing protein 1) (Inactive exonuclease EXD1) (BmExd1) (H9IUR0)
Organism: Bombyx mori (Silk moth)
Function: RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposable elements, preventing their mobilization, which is essential for the germline integrity. The PET complex is required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs. In the PET complex, EXD1 probably acts as an RNA adapter. EXD1 is an inactive exonuclease.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26669262}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000269|PubMed:26669262}.
Interaction partners:
- Putative ATP-dependent RNA helicase TDRD12
- Piwi-like protein Siwi
- RNA helicase-like protein.
- Dynein light chain.
Sequence:
MDNLYTKGELLQVHTKNYDVFEGRFYSMAQDKTKISLYDVKEIPHGDANDGVLHYYDSEIREVVKLQESTEKKVLKISQTKYEEILKISKKYIFINQVDKSFHEAVDDLNQQDFIAVSGDGANMGRKCKMPFLVLSTDHQIYIFDIQVMQYHAFESGLKKILEGDSPKKIAHDCRKLSDCLYHKHNVKLKSVFDTQVGDLIITKNKKVTLPNKVKSLGECLTNYLGLQQNTIDEKLDIVQSTERPLSVKIKDSLARNIAFLHHLSEVINEEMQLPFYRGVECYIENIRSSDDFKAWELCGKLNQIPKEFRNAIDY
Protein: E3 ubiquitin-protein ligase CBL-B (EC 2.3.2.27) (Casitas B-lineage lymphoma proto-oncogene b) (RING-type E3 ubiquitin transferase CBL-B) (SH3-binding protein CBL-B) (Signal transduction protein CBL-B) (Q8K4S7)
Organism: Rattus norvegicus (Rat)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBL, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14604964}. Note=In mast cells, translocates to lipid raft upon FCER1 engagement.
Interaction partners:
- Receptor protein-tyrosine kinase
- Tyrosine-protein kinase
- E3 ubiquitin-protein ligase NEDD4
- Tyrosine-protein kinase Fyn
- SH3 domain-containing kinase-binding protein 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Proto-oncogene tyrosine-protein kinase LCK
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- SH2B adapter protein 2
Sequence:
MANSMNGRNPGGRGGNPRKGRILGIIDAIQDAVGPPKQAAADRRTVEKTWKLMDKVVRLCQNPKLQLKNSPPYILDILPDTYQHLRLILSKYDDNQKLAQLSENEYFKIYIDSLMKKSKRAIRLFKEGKERMYEEQSQDRRNLTKLSLIFSHMLAEIKAIFPNGQFQGDNFRITKADAAEFWRKFFGDKTIVPWKVFRQCLHEVHQISSGLEAMALKSTIDLTCNDYISVFEFDIFTRLFQPWGSILRNWNFLAVTHPGYMAFLTYDEVKARLQKYSTKPGSYIFRLSCTRLGQWAIGYVTGDGNILQTIPHNKPLFQALIDGSREGFYLYPDGRSYNPDLTGLCEPTPHDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTEPIIVDPFDPRDEGSRCCSIIDPFSIPMLDLDDDDDREESLMMNRLASVRKCTDRQNSPVTSPGSSPLAQRRKPQPDPLQIPHLSLPPVPPRLDLIQKGIVRSPCGSPTGSPKSSPCMVRKQDKPLPAPPPPLRDPPPPPERPPPIPPDSRLSRHFHHGESVPSRDQPMPLEAWCPRDAFGTNQVMGCRILGDGSPKPGVTANSNLNGRHSRMGSDQVLMRKHRRHDLPSEGAKVFSNGHLAPEEYDVPPRLSPPPPVTALLPSIKCTGPIANCLSEKTRDTVEEDDDEYKIPSSHPVSLNSQPSHCHNVKPPVRSCDNGHCILNGTHGTPSEMKKSNIPDLGIYLKGEDAFDALPPSLPPPPPPARHSLIEHSKPPGSSSRPSSGQDLFLLPSDPFFDPASGQVPLPPARRAPGDGVKSNRASQDYDQLPSSSDGSQAPARPPKPRPRRTAPEIHHRKPHGPEAALENVDAKIAKLMGEGYAFEEVKRALEIAQNNLEVARSILREFAFPPPVSPRLNL
Protein: Membrane-associated kinase regulator 5 (Q9FLX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive effector of CLE45 peptide signaling. Post-transcriptionally regulated amplifier of the CLE45 peptide signal that acts downstream of BAM3 in the regulation of the transition of root protophloem cells from proliferation to differentiation; thus preventing primary root elongation but stimulating lateral roots development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27354416}. Cytoplasm, cytosol {ECO:0000269|PubMed:27354416}. Note=Recruited to the plasma membrane upon CLE45 peptide application. {ECO:0000269|PubMed:27354416}.
Interaction partners:
- CLAVATA3/ESR
- Probable membrane-associated kinase regulator 1
- Probable membrane-associated kinase regulator 6
- CLAVATA3/ESR
- CLAVATA3/ESR
- Type IV inositol polyphosphate 5-phosphatase 6
- Leucine-rich repeat receptor-like serine/threonine-protein kinase RGI4
- CLAVATA3/ESR
- Probable membrane-associated kinase regulator 4
- Protein BREVIS RADIX
Sequence:
MEALTFMKFWLTNNTTIKPRREIRISESAVDSTTGSEDPDLDLCEGEDSFFELKISLSDFKTPKEKQRLETTTTTTTYSVSNKSKVLPFVDISSKPQQSPTTLLKSGQKFRAFSFKKSEKSTTTEKKKEENNRTSLNVRFRVDDETTTTSFRKTASIARSQQTDDTMFDDSVSKRFFSLIKPLYTKSTKKQSSSTITSPTSSPATREKQRSNIPSGMRSVRRQLGKSRSASAAIGGMSPANRIDESLQVQQDGIQSAILHCKKSFHGSRESSLLSRSTSESSSQEKLSTSSSEDSYLFSRISSDSISEKSMDSLTSIKEQREKISD