wanglab/gogpt-training-data huggingface dataset:
Protein: Fringe glycosyltransferase (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (Q24342)
Organism: Drosophila melanogaster (Fruit fly)
Function: Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity; extends the O-linked fucose on the Notch EGF repeats. Boundary-specific cell-signaling molecule that is responsible for dorsal-ventral cell interactions during wing development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10899003}; Single-pass type II membrane protein {ECO:0000269|PubMed:10899003}.
Interaction partners:
- Neurogenic locus Notch protein
- Beadex, isoform D
- GDP-fucose protein O-fucosyltransferase 1
- Protein serrate
- Protein apterous
Sequence:
MMSLTVLSPPQRFKRILQAMMLAVAVVYMTLLLYQSAYGYPGIQVPHSQVDALASEAVTTHRDQLLQDYVQSSTPTQPGAGAPAASPTTVIIRKDIRSFNFSDIEVSERPTATLLTELARRSRNGELLRDLSQRAVTATPQPPVTELDDIFISVKTTKNYHDTRLALIIKTWFQLARDQTWFFTDTDDHYYQEKTKGHLINTKCSQGHFRKALCCKMSAELDVFLESGKKWFCHFDDDNYVNVPRLVKLLDEYSPSVDWYLGKPSISSPLEIHLDSKNTTTNKKITFWFATGGAGFCLSRALTLKMLPIAGGGKFISIGDKIRFPDDVTMGFIIEHLLKVPLTVVDNFHSHLEPMEFIRQDTFQDQVSFSYAHMKNQWNVIKVDGFDMKTDPKRFYSLHCQLFPYFSFCPPR
Protein: Major facilitator superfamily domain-containing protein 6 (Macrophage MHC class I receptor 2 homolog) (Q6ZSS7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Major facilitator superfamily domain-containing protein 9
Sequence:
MADDKVAILTDDEEEQKRKYVLADPFNGISREPEPPSNETPSSTETSAIPEEEIDWIEKHCVKINNDLLISKVFYFFFYSAYGSLYPLLPVYYKQLGMSPSQSGLLVGIRYFIEFCSAPFWGVVADRFKKGKIVLLFSLLCWVLFNLGIGFVKPATLRCVPKIRPTTHPTNASHQLTILPTNSSFTSFLTISPKMREKRNLLETRLNVSDTVTLPTAPNMNSEPTLQPQTGEITNRMMDLTLNSSTATPVSPGSVTKETTTVIVTTTKSLPSDQVMLVYDQQEVEAIFLVILVVVIIGEFFSASSVTIVDTVTLQYLGKHRDRYGLQRMWGSLGWGLAMLSVGIGIDYTHIEVLIDGKGCKPPEYRNYQIVFIVFGVLMTMALIVATQFRFRYNHFKNDDSKGKEVEIPQVERNNSTESSEETPTTTSHSQAFNFWDLIKLLCSVQYGSVLFVAWFMGFGYGFVFTFLYWHLEDLNGTTTLFGVCSVLSHVSELTAYFFSHKLIELIGHIRVLYIGLACNTARYIYISYLENAWTVLPMEVLQGVTHAAIWAACISYLSAAVPPELRTSAQGILQGLHLGLGRGCGAMIGGVLVNYFGAAATFRGIGMACLVILLLFALIQWLAVPDEEEDKTMLAERIPVPSSPVPIATIDLVQQQTEDVMPRIEPRLPPKKTKHQEEQEDVNKPAWGVSSSPWVTFVYALYQIKEMMQLTRDNRASEIQPLQGTNENRENSPAGRAQPVPCETHSDPSRNQPSPDAAASQTQTSPAHPSVDPCTEESEEQQAQLAAGGH
Protein: Elongation factor 2 (C0H9N2)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Elongation factor 1-gamma
- Ubiquitin-like protein FUBI isoform X1
- 40S ribosomal protein S30
- 40S ribosomal protein S15
- 60S acidic ribosomal protein P0
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L18
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL11
Sequence:
MVNFTVDQIRAIMDKKSNIRNMSVIAHVDHGKSTLTDSLVSKAGIIAGSRAGETRFTDTRKDEQERCITIKSTAISMYYELGENDMAFIKQSKDGLGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEDLFQTFQRIVENVNVIIATYGEDEAGPMGAIMIDPVIGTVGFGSGLHGWAFTLKQFAEMYVTKFSAGKDTQLGSAERCKKVEDMMKKLWGERFFDPATGKFSKSNLGPDGKKLPRTFSQLVLDPIFKVFDAIMNFKKDETAKLIEKLDIKLDSEDKEKEGKPLLKAVMRRWLPAGEALLQMITIHLPSPVTAQKYRCELLYEGPGDDEAAMGIKNCDPKAPLMMYISKMVPTTDKGRFYAFGRVFSGCVSTGLKVRIMGPNFTPGKKEDLYIKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQYLIKTGTITTFEQAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHAGIPLKKSDPVVSYRETVSEESEVMCLSKSPNKHNRLYMRAKPFPDGLAEDIEKGDVSPRQELKIRARFLADKYEWDVSEARKIWCFGPDGTGPNLLMDVTKGVQYLNEIKDSVVAGFQWAVKEGVLCEENMRAVRFDIHDVTLHTDAIHRGGGQIIPTARRVLYACQLTAQPRLMEPVYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVMGTPMFIVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILQGDPQDPTTKTAIVVAETRKRKGLKEGIPALDNYLDKL
Protein: Sugar transporter STL1 (P39932)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Glycerol uptake/efflux facilitator protein
- Mitogen-activated protein kinase HOG1
- High-osmolarity-induced transcription protein 1
- Glycerol-1-phosphate phosphohydrolase 2
- Catalase T
- NADPH-dependent methylglyoxal reductase GRE2
Sequence:
MKDLKLSNFKGKFISRTSHWGLTGKKLRYFITIASMTGFSLFGYDQGLMASLITGKQFNYEFPATKENGDHDRHATVVQGATTSCYELGCFAGSLFVMFCGERIGRKPLILMGSVITIIGAVISTCAFRGYWALGQFIIGRVVTGVGTGLNTSTIPVWQSEMSKAENRGLLVNLEGSTIAFGTMIAYWIDFGLSYTNSSVQWRFPVSMQIVFALFLLAFMIKLPESPRWLISQSRTEEARYLVGTLDDADPNDEEVITEVAMLHDAVNRTKHEKHSLSSLFSRGRSQNLQRALIAASTQFFQQFTGCNAAIYYSTVLFNKTIKLDYRLSMIIGGVFATIYALSTIGSFFLIEKLGRRKLFLLGATGQAVSFTITFACLVKENKENARGAAVGLFLFITFFGLSLLSLPWIYPPEIASMKVRASTNAFSTCTNWLCNFAVVMFTPIFIGQSGWGCYLFFAVMNYLYIPVIFFFYPETAGRSLEEIDIIFAKAYEDGTQPWRVANHLPKLSLQEVEDHANALGSYDDEMEKEDFGEDRVEDTYNQINGDNSSSSSNIKNEDTVNDKANFEG
Protein: Ion transport domain-containing protein (O61220)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Transient receptor potential cation channel subfamily A member 1 homolog
- Ion transport domain-containing protein
- Cyclic nucleotide-gated channel
- Cyclic nucleotide-binding domain-containing protein
- Guanine nucleotide-binding protein alpha-17 subunit
- Ion transport domain-containing protein
- Transient receptor potential channel
Sequence:
MGSSSSTQSSMNNFVGMGRLREDMKIYQLVDMHGGGELLPWLRYAIISSDTSFIDAYLETKVKDFLYNGGKGKLVTVTELVKLRNKERNERLGAFSRKKGKGKSGPNVLDDFNQEGENVGDLKKALKLLDGGGKGGRNESKYREISWKLEERGSMGETIIGCCLLHASDIHNALVLKILDYYPKLLNDIHISEDFYGLSPLHQAIINTDCKLVYKFLKLGADVNSRCYGAFFCADDQKASRTDSLEHEYVELSLKTNYTGNMYLGEYPLSFAACLNQPESFRLLLAFKANPNAQDTNGNSVLHMCVIHENMAMFKLALECGASLRTVNKQSLSPLTLAAKLAKKEMFDEILELEGDSVWAYGDASSTAYPLAKIDTINETTGELNEASALSLVVYGQTVEHLELLDGLLDTLLEAKWEAFAKRNMIVSFTAFTLYYICFVTAFTLRPIGFSTEMLTEGWINRYSEPFPGRYGKNSTLQQVKPVINATSRGLVEWSEPLSQCHLRNYWDPDIPFANSYIRLVFELFVVIGICVQVFLDFRDIKRIGRKKWWNVLTAFPAKITFKLTYFLVLAMIPTRLACDLSPVLLVVDNVLITVTMIFTTVHYLYYCRVIRFVGPFVLMVYTIIATDIFRFMLIYGIFLMGFSQSFSLIFLSCEREANVIKKLITDQSEASEGSDNKFNLTRQISAYDTAIVKNAEVFENVMQSPIEAFVRTFILTIGEFTVLYRNLALCPANTMVWIGKVVFILFELFVSIMQFNMLIAMMTRTYETIFQTQLEYKRQRAQVILMLELSLSPKERHQYLLKYSRPTGTNKKTRSLVVSKKSAFSRDSKKGQKVLEEKMKKMIEEKKAVLKRKMKDMEIKEGIRPVTGYSRTPRPHTQYMNRGAGGGANGVQNGNGAAH
Protein: SUMO ligase SizA, putative (AFU_orthologue AFUA_6G05240) (C8V0C1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- SUMO-conjugating enzyme UBC9
- Myosin-binding domain-containing protein
- Chromosomal organization and DNA repair protein Mms21, putative
- E2 ubiquitin-conjugating enzyme
- Postreplication repair E3 ubiquitin-protein ligase rad18
Sequence:
MASGQTSELQSVIALVKTLTNAQLKDILRDEGLAVSGLKAALQVRIINALEGHFQAGRLGRYDSLRKFIYATAHRSMPPSPSIPPPVPGNYYQQIPTTHSVQSHHRQSPLGMPVASHGSVPGPLIFKDSPFYRIIRQLTPTIECKAREHTRDSVELKIHLDADVASRLLAEPKLRVMIFCAADSGLNQFTKSDIAFPHQVELKANLDEVKANLRGLKNKPGTTRPADITNYIRKKAGYTNHVVMTYALTQKRFFIVANLVECTAIEELVDKLKRRKTITREQVLQEMKSKAEDADIVATSTVMSLKCPLSTRRIEVPCRSVLCTHNQCFDASSFLQLQEQAPTWSCPVCAKATSYESLNVDQYVDDILRSTPLDVEQVIIEPNGQWSTPKDEAVATGPGTFTPATDDDELVEIREPGVTPVKQENLSSLDLWRQTPATSREQSSAWSSSKRPAPVIDLTGSDDDDDSPIRPPKRQAVHLHRPLPKQDPRSSYTGGYPLPTFGSE
Protein: NT-3 growth factor receptor (EC 2.7.10.1) (GP145-TrkC) (Trk-C) (Neurotrophic tyrosine kinase receptor type 3) (TrkC tyrosine kinase) (Q03351)
Organism: Rattus norvegicus (Rat)
Function: Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation (By similarity). NTRK3 isoforms containing insertions within the kinase domain can autophosphorylate in response to NTF3/neurotrophin-3, but cannot mediate downstream phenotypic responses.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Neurotrophin-3
- Beta-nerve growth factor
- Neurotrophin-4
- Neurotrophic factor BDNF precursor form
- Receptor-type tyrosine-protein phosphatase S
- SHC-transforming protein 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Tumor necrosis factor receptor superfamily member 16
- Glial cell line-derived neurotrophic factor
- SHC-transforming protein 3
Sequence:
MDVSLCPAKCSFWRIFLLGSVWLDYVGSVLACPANCVCSKTEINCRRPDDGNLFPLLEGQDSGNSNGNASINITDISRNITSIHIENWRGLHTLNAVDMELYTGLQKLTIKNSGLRNIQPRAFAKNPHLRYINLSSNRLTTLSWQLFQTLSLRELRLEQNFFNCSCDIRWMQLWQEQGEARLDSQSLYCISADGSQLPLFRMNISQCDLPEISVSHVNLTVREGDNAVITCNGSGSPLPDVDWIVTGLQSINTHQTNLNWTNVHAINLTLVNVTSEDNGFTLTCIAENVVGMSNASVALTVYYPPRVVSLVEPEVRLEHCIEFVVRGNPTPTLHWLYNGQPLRESKIIHMDYYQEGEVSEGCLLFNKPTHYNNGNYTLIAKNALGTANQTINGHFLKEPFPESTDFFDFESDASPTPPITVTHKPEEDTFGVSIAVGLAAFACVLLVVLFIMINKYGRRSKFGMKGPVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVVIGMTRIPVIENPQYFRQGHNCHKPDTYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIASQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMSRDVYSTDYYREGPYQKGPFSVSWQQQRLAASAASTLFNPSGNDFCIWCEVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERPRVCPKEVYDVMLGCWQREPQQRLNIKEIYKILHALGKATPIYLDILG
Protein: Beta-(1-->2)glucan export ATP-binding/permease protein NdvA (EC 7.5.2.3) (Q2YQ73)
Organism: Brucella abortus (strain 2308)
Function: Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01728, ECO:0000269|PubMed:15039351}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01728, ECO:0000269|PubMed:15039351}.
Interaction partners:
- Spermidine/putrescine import ATP-binding protein PotA
- Putative ATP-binding protein BAB2_0493
- ATP/GTP-binding site motif A
- ABC transporter, transmembrane region:ATP/GTP-binding site motif A
- ATP/GTP-binding site motif A
Sequence:
MSLLKIYWRAMQYLAVERTATITMCVASVLVALVTLAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFAQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTYEFPNSGQGVYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVTQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGLKLEDKQPKQPVVEGSNVMPFPVKGAVA
Protein: Phosphoprotein (Protein P) (O55778)
Organism: Hendra virus (isolate Horse/Autralia/Hendra/1994)
Function: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity).
Interaction partners:
Sequence:
MDKLDLVNDGLDIIDFIQKNQKEIQKTYGRSSIQQPSTKDRTRAWEDFLQSTSGEHEQAEGGMPKNDGGTEGRNVEDLSSVTSSDGTIGQRVSNTRAWAEDPDDIQLDPMVTDVVYHDHGGECTGHGPSSSPERGWSYHMSGTHDGNVRAVPDTKVLPNAPKTTVPEEVREIDLIGLEDKFASAGLNPAAVPFVPKNQSTPTEEPPVIPEYYYGSGRRGDLSKSPPRGNVNLDSIKIYTSDDEDENQLEYEDEFAKSSSEVVIDTTPEDNDSINQEEVVGDPSDQGLEHPFPLGKFPEKEETPDVRRKDSLMQDSCKRGGVPKRLPMLSEEFECSGSDDPIIQELEREGSHPGGSLRLREPPQSSGNSRNQPDRQLKTGDAASPGGVQRPGTPMPKSRIMPIKKGTDAKSQYVGTEDVPGSKSGATRYVRGLPPNQESKSVTAENVQLSAPSAVTRNEGHDQEVTSNEDSLDDKYIMPSDDFANTFLPHDTDRLNYHADHLNDYDLETLCEESVLMGIVNAIKLINIDMRLNHIEEQMKEIPKIINKIDSIDRVLAKTNTALSTIEGHLVSMMIMIPGKGKGERKGKTNPELKPVIGRNILEQQELFSFDNLKNFRDGSLTDEPYGGVARIRDDLILPELNFSETNASQFVPLADDASKDVVRTMIRTHIKDRELRSELMDYLNRAETDEEVQEVANTVNDIIDGNI
Protein: Solanesyl diphosphate synthase 1, chloroplastic (AtSPS1) (EC 2.5.1.85) (All-trans-nonaprenyl-diphosphate synthase 1 (geranylgeranyl-diphosphate specific)) (Geranylgeranyl diphosphate synthase) (EC 2.5.1.29) (Q8S948)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in providing solanesyl diphosphate for plastoquinone-9 (PQ-9) formation in plastids. Catalyzes the elongation of the prenyl side chain of PQ-9 in plastids. Contributes to the biosynthesis of plastochromanol-8 (PC-8) in plastids. Does not contribute to the synthesis of tocopherol or ubiquinone. PQ-9 and PC-8 are lipophilic antioxidants that act as protectant against photooxidative stress under high light stress conditions. Prefers geranylgeranyl diphosphate to farnesyl diphosphate as substrate. No activity with geranyl diphosphate or dimethylallyl diphosphate as substrate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23913686, ECO:0000269|PubMed:26432861}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- Solanesyl diphosphate synthase 2, chloroplastic
- Homogentisate solanesyltransferase, chloroplastic
- Phytoene synthase 1, chloroplastic
- Fibrillin-5, chloroplastic
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Farnesyl pyrophosphate synthase 1, mitochondrial
- Homogentisate phytyltransferase 1, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
Sequence:
MMTSCRNIDLGTMMMACGCGRRQFPSLAKTVCKFTSSNRSYGGLVGSCKAVPTKSKEISLLNGIGQSQTVSFDLKQESKQPISLVTLFELVAVDLQTLNDNLLSIVGAENPVLISAAEQIFGAGGKRMRPGLVFLVSHATAELAGLKELTTEHRRLAEIIEMIHTASLIHDDVLDESDMRRGKETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLFDCDTKLDEYLLKSFYKTASLVAASTKGAAIFSRVEPDVTEQMYEFGKNLGLSFQIVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEREPRLREIIESEFCEAGSLEEAIEAVTKGGGIKRAQELAREKADDAIKNLQCLPRSGFRSALEDMVLYNLERID
Protein: Emb|CAB62340.1 (von willebrand factor A domain protein) (Q9FGW7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDGRGGCCIARYGGYGGRYGLSKADRIMLRFRPIAPKPASDGGSVSLTGKSGSTTTTSGGSSDLSGKSGRGKRKYQKDCSGGNSRRCNKKKRDLSGDTATTTAVTLSLLPETPEKRVFPDLNAFPVEKQKRNGPLWLSFNGGGEILTPYKTAEISRRTVVVSSCVTVERVTDAWIDGYGLGETNQERKMNLVEDTCPGFISDGVGRVTWTNEAYKKMAREDINIPMEEGVPEDISYDNFHVNVRLVMKERPMLTYPAFTCRVRLQYTCQDRERGSVTVPCDVWRMDGGGFAWRLDVKAALCL
Protein: tRNA (cytosine(48)-C(5))-methyltransferase (EC 2.1.1.-) (aTrm4) (tRNA (cytosine-5-)-methyltransferase Trm4) (Q60343)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes AdoMet-dependent formation of m5C in tRNA. Cytidine residue at either position 40 or position 48 is likely to be methylated.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- UPF0113 protein MJ1410
- Ribosomal RNA large subunit methyltransferase E
- Uncharacterized protein MJ1408
- Uncharacterized GTP-binding protein MJ1464
- Uncharacterized NOP5 family protein MJ0694
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein eS8
- Probable tRNA pseudouridine synthase B
- tRNA
- Translation initiation factor 6
Sequence:
MMIVYKGEKMQFIRVNTLKINPEVLKKRLENKGVVLEKTFLDYAFEVKKSPFSIGSTPEYLFGYYMPQSISSMIPPIVLNPREDDFILDMCAAPGGKTTHLAQLMKNKGTIVAVEISKTRTKALKSNINRMGVLNTIIINADMRKYKDYLLKNEIFFDKILLDAPCSGNIIKDKNRNVSEEDIKYCSLRQKELIDIGIDLLKKDGELVYSTCSMEVEENEEVIKYILQKRNDVELIIIKANEFKGINIKEGYIKGTLRVFPPNEPFFIAKLRKI
Protein: Ring finger protein 38 (A0A0G2K236)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGSAAAAVAVAAATSAAAAAAAHFQPRPSSPRPGPAEIGPPRRPRPPPPPPPPRPEPITAGRLSPPGHGSLRSGAQGVGACGRAPGAGSVGASFQCQSIHHDHICHDDSDKSEDSPSPKRQRLSHSVFDYTSASPAPSPPMRPWEMTSNRQPPSVRPNQHHFSGERCNTPARNRRSPPVRRQRGRRERLSRHNSISQDENYHHLPYAQQQAIEEPRAFHPPNVSPRLLHPAAHPPQQNAVMVDIHDQLHQGTVPVSYTVTTVAPHGIPLCTGQHIPACSTQQVPGCSVVFSGQHLPVCSVPPPMLQACSVQHLPVPYAAFPPLISSDPFLLHPPHLSPHHPPHLPPPGQFVPFQTQQSRSPLQRIENEVELLGEHLQVGSFTYPPSAHPPTLPPSAPLQFLTHDPLHQEVSFGVPYPPFMPRRLTGRSRYRSQQPVPPPTYHPSLLPYVLSMLPVPPTVGPTFSFELDVEDGEVENYEALLNLAERLGEAKPRGLTKADIEQLPSYRFNPSNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKGNRTCPICRADASEVHRDSE
Protein: Homeobox B8 (I3L3R1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MSSYFVNSLFSKYKTGESLRPNYYDCGFAQDLGGRPTVVYGPSSGGSFQHPSQIQEFYHGPSSLSTAPYQQNPCAVACHGDPGNFYGYDPLQRQSLFGAQDPDLVQYADCKLAAASGLGEEAEGSEQSPSPTQLFPWMRPQAAGRRRGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKFPSSKCEQEELEKQKLERAPEAADEGDAQKGDKK
Protein: TRAF1 (Q9UAC5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MIVTYLQISYFPYLQIYPGPDPKHIMGSLVFCIHHKQGCKWSDELRKLKGHLNACKHDATQCPNKCGAQIPRIMMTDHLQYTCTMRRTRCEFCQSEFSGAGLEEHNGSCGQEPVYCEAKCGQRILRGRMTLHKSKDCAKRLRRCAHCQREFSADTLPLHAAQCPRAPLACPQRCDAGPIPRGELEAHLRDECQSLAVSCSFKEAGCRFKGPRQMLEAHLESNAAAHLSLMVALSSRQGQQIQMLKSAVSKLSINYTGTLLWKITDWSAKMAEARGKDGLELVSPPFYTSQYGYKLQASMFLNGNGPGENTHVSVYIKVLPGEYDALLKWPFSHSITFTLFEQGAQSGQGGVAESFVPDPTWENFQRPSNEPDQLGFGFPRFISHELLHSRPFIKGDTVFLRVKVDPSKIVAV
Protein: Gamma-synuclein (Persyn) (Sensory neuron synuclein) (Q63544)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MDVFKKGFSIAREGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKGERGTSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEEGEEAKSGGD
Protein: Crescent (Frizzled related protein 2 L homeolog precursor) (Putative wnt inhibitor frzb2) (Q9I897)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAPQLCQSLGKPLIVLLCFLACGSQSMYLDFFGSSSRCMRIPKSMALCYDIGYSEMRIPNLLEHETMAEAIQQSSSWLPLLARECHPDARIFLCSLFAPICFDRYIFPCRSLCEAVRSSCAPIMACYGYPWPEILKCDKFPEDHGMCISTITNDTGSTRRTVPRASCRDCELEEGSTSKEILDTFCHNDFVAKVRITKKNITSANLYDFDLDSKLEILKHGSLPKTDVLPRLQQWLDLDATCVQNIMRGTRTGVYVICAEVQEGKVVVNNAYAWQKKNKNLHFAVRKWKNHKCRP
Protein: Peroxisomal targeting signal receptor (PTS1 receptor) (PTS1R) (Peroxin-5) (Peroxisomal protein PAS8) (P33292)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Function: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (By similarity). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins (By similarity). PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity). Required for PEX7 ubiquitination.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:7641682}; Peripheral membrane protein {ECO:0000269|PubMed:7641682}; Cytoplasmic side {ECO:0000269|PubMed:7641682}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35056}. Peroxisome matrix {ECO:0000250|UniProtKB:P35056}. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol. Cys-10 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix (By similarity). The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzyme UBP15, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.
Interaction partners:
Sequence:
MSLIGGGSDCAAGSNPLAQFTKHTQHDTSLQQSMRNGEFQQGNQRMMRNESTMSPMERQQMDQFMQQQNNPAFNFQPMQHELNVMQQNMNAPQQVANNSWNQEFRMKDPMVANAPSAQVQTPVQSTNWAQDFQQAGPEVQHHAQQHQHPILSVPGVRAGIYGGGRLMGGSMMNRAAQMQQQNPAQAQTSEQSQTQWEDQFKDIESMLNSKTQEPKTKQQEQNTFEQVWDDIQVSYADVELTNDQFQAQWEKDFAQYAEGRLNYGEYKYEEKNQFRNDPDAYEIGMRLMESGAKLSEAGLAFEAAVQQDPKHVDAWLKLGEVQTQNEKESDGIAALEKCLELDPTNLAALMTLAISYINDGYDNAAYATLERWIETKYPDIASRARSSNPDLDGGDRIEQNKRVTELFMKAAQLSPDVASMDADVQTGLGVLFYSMEEFDKTIDCFKAAIEVEPDKALNWNRLGAALANYNKPEEAVEAYSRALQLNPNFVRARYNLGVSFINMGRYKEAVEHLLTGISLHEVEGVDASEMSSNQGLQNNALVETLKRAFLGMNRRDLVDKVYPGMGLAQFRKMFDF
Protein: Cytochrome c oxidase assembly factor 6 homolog (Q5JTJ3)
Organism: Homo sapiens (Human)
Function: Involved in the maturation of the mitochondrial respiratory chain complex IV subunit MT-CO2/COX2. Thereby, may regulate early steps of complex IV assembly. Mitochondrial respiratory chain complex IV or cytochrome c oxidase is the component of the respiratory chain that catalyzes the transfer of electrons from intermembrane space cytochrome c to molecular oxygen in the matrix and as a consequence contributes to the proton gradient involved in mitochondrial ATP synthesis. May also be required for efficient formation of respiratory supercomplexes comprised of complexes III and IV.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:25339201, ECO:0000269|PubMed:25959673}.
Interaction partners:
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Protein SCO1 homolog
Sequence:
MGPGGPLLSPSRGFLLCKTGWHSNRLLGDCGPHTPVSTALSFIAVGMAAPSMKERQVCWGARDEYWKCLDENLEDASQCKKLRSSFESSCPQQWIKYFDKRRDYLKFKEKFEAGQFEPSETTAKS
Protein: Protein kinase superfamily protein (F4JN38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MGACISFFSSSSPSKTGLHSHAATTNNHSNGTEFSSTTGATTNSSVGQQSQFSDISTGIISDSGKLLESPNLKVYNFLDLKTATKNFKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRVKQIMDKGIKGQYTTKVATEMARITLSCIEPDPKNRPHMKEVVEVLEHIQGLNVVPNRSSTKQAVANSSRSSPHHYRYKAGALGAERKRATPGRFGSVEK
Protein: Proteasome subunit beta (A0A087X2I4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANAFFFYPQLSLWPWSGMAPVEE
Protein: CHK kinase-like domain-containing protein (Q9VBS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTAETGTAPMPTWLRANLFEELLSKRYGGNYAGIKSFKPEAGLKPGENYSTIMLRLKLEVELQDHTIENVSYMLKTPYDFEMYREILRKNNMFAVERDVFIQVIPELEQMYKDVGVEVKFGAKAYEIDAPDDYVLLQDLGPLGFRNVDRLEGLDMVHTKCVLKKMAQWHAVSATRIHLKGPYPQNYLQPTYADTMKESIEQVAETLGKYFLKCLPLYEGYEEYSAAVHKMQPKIVDLMYAMNTPDPQDFNALNHGDCWTSNIMFKYEDESPEPIETYFVDLQLPKVTSVAYDLIYFLLGSTKFEIQLSQFDYFIKYYHDHLVEHLRMLNYPEAKTPTLGFLHTQLLKYGRVGYHIAFILCPPVLLDRTEDANLTDFVTETDNGDGLKLAMYSNARYKKHVSAILKWLNNRGAFQC