wanglab/gogpt-training-data huggingface dataset:
Protein: Spermatogenesis-associated protein 16 (Q8C636)
Organism: Mus musculus (Mouse)
Function: Essential for spermiogenesis and male fertility. Involved in the formation of acrosome during spermatogenesis.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:12529416, ECO:0000269|PubMed:16372119}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:16372119}. Note=Shift from Golgi to sperm acrosome. {ECO:0000269|PubMed:16372119}.
Interaction partners:
- Probable C-mannosyltransferase DPY19L2
- Zona pellucida-binding protein 1
- PRKCA-binding protein
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase zeta-1
- Sperm acrosome membrane-associated protein 1
- Golgi-associated PDZ and coiled-coil motif-containing protein
Sequence:
MDSGKSRSLETTVKRVYRDLLLPKINTSKKMSTLTNSPSSLEGTPGIKKNSGEMQAEASAERVKLTKSIKEKQNNELEKVALKRKADSEEKLVGKKEAKIMELDNQLVTTVPLPHIPLKNIMDVEMKLVYVDEEDVSYEFAQPNMCLGLQATGQTATTMPPASPRDLTTLPQIDKWLQVALKDASSCYRQKKYAVAAGQFRTALELCSKGAALGKPFEAHAEDIASIASFIETKLVTCYLRMRKPDLALNHAHRSIVLNPAYFRNHLRQAAVFRCLERYSEAARSAMIADYMFWLCGGSEHSVSKLIKLYWQAMIEEAITRAEAFSVMYTPFATRIKPENIEKVKEVFMRTHPTYVDCIYTDTQGLHVLPQTADWSCFPPQQYLLTLGFKNKEDGKFLEKVSSRKLPTYTEHKTPFSPLTREDTVRHMETVGKRILPILDFIRSTQLNGNFHACSGVMEKLHYASLLSRLQRVKEQAQVINQAMAELATVPYLQDISQQEAELLQSLMADAMDTLEGKKSDKERVWNTIQKVGRIEDFLYQLEDSFLKTKKLRTARRQKTKMKRLQTVQQN
Protein: Fc gamma receptor 1A (A0A0B4J2J0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MWLLTTLLLWVPVGGQVVNATKAVVTLQPPWLSIFQEENVTLLCEGPHLGDSSTKWFINSTAIQISTPTYSILKASFKDSGEYKCQTGLSMPSDPVQLEIYRDWLLLQTSHRVLTEGEPLALRCHPWQNKKVYNVAFYRNGESLDFSQGSEVTILKTNLSHSGIYHCSAMGKKLFKSAGVSVTVKELFATPVLRVSLSSPFPEGSLVILNCETRLFLQSPGLRLYFSFYVGSKILEDRSTSSEYHIPRAEREDDGSYWCEVATEDGRVLKRSTKLELFGPQSSDPVWFHILFYLSVGIMFLVNTVLYVKIHRLQREKKYNLEVPLVSEKGKKATSFQQVRSDDVYEEVTATVR
Protein: SD09295p (Q7YU87)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDDKRFNAAGFVKCTRNRTIEYLYQDHTPPNLWKHAPIVDPHNPYDQDEKKQYKMFTYHVEHRYNTLLPDIPFERLNLIKEYVHTNQVNTTEILNEHMTTKEYLDEYIALENQMLAARYGAIVTRRRRLVDSARFMEDNLDEGLAKKMCMDKNLPMDTNETVLIDQSLVDENSRSLTTAESTMGISQAENSTLKSSEVEATLSVSHIENSLSDSQEENPPLSSTLAINESSVLDSTRVDPIKDLTLDELLLIDSGISMEELSDIQMHTAGQSFDDEGVVLSDLEDQRQLSPMLQMVSPSMEAKTLNIIEMDADLIMNVPREVSYPILLNVMGLPIKRLRRKCIFKLPPEFDLFRQARLPIKREGQQKSPTTPRTVLQIGREAPQNEREPGSPCSLEFDEDLNFLGFRQRRPTFDSGFDIEEPRVSSCVSTIGEVKTELEDEIEANTNNLTDASASDALNENVNDTKESGLGDSLAQELNASTEPNAENNTANSSQLEVTATESSGTLSGLETTVDLGMESALVSSVLDLSTEPSAMDSNIINVTQPDNSDLEISTVQDQDTLHDEADANDLSAETPNPIADSAVDDCSLIRDWHRRLAPALEAAHERQNFNIKDLGTEILDICKAGNRTATLADVMADKDPSIMCRYMLASLVLTNHGNVSLDFENRDKSKPIDMSQFRMHLKSMKRMEINPEDDVGNINAAQSKSTPRSKQLNNSAHKPRTSTTASAPTKRKSAENSLSEVFAKTVRLIQPIPKMWPTPSDADSGISSMGSSLASTARLK
Protein: Signal peptide, CUB and EGF-like domain-containing protein 3 (Q66PY1)
Organism: Mus musculus (Mouse)
Function: Is a positive regulator of the BMP signaling pathway, required for proper chondrogenesis, osteogenesis and skeletal development. It acts as coreceptor for BMP ligands, particularly BMP2 and BMP4, facilitating their interactions with BMP type I receptors (By similarity). It is required for ligand-induced recruitment of BMP receptors to lipid rafts. Binds to TGFBR2 and activates TGFB signaling (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8IX30}. Cell surface {ECO:0000250|UniProtKB:Q8IX30}.
Interaction partners:
- TGF-beta receptor type-2
- 72 kDa type IV collagenase
- Matrix metalloproteinase-9
- Signal peptide, CUB and EGF-like domain-containing protein 1
Sequence:
MGSGRVPGLCLLLLLVHARAAQHGKAAQDVDECVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHCKDVDECEREDNAGCVHDCVNIPGNYRCTCYDGFHLAHDGHNCLDVDECAEGNGGCQQSCVNMMGSYECHCRDGFFLSDNQHTCIQRPEEGMNCMNKNHGCAHICRETPKGGIACECRPGFELTKNQRDCKLTCNYGNGGCQHTCDDTEQGPRCGCHVKFVLHTDGKTCIETCAVNNGGCDSKCHDAATGVHCSCPVGFMLQPDRKTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERSCQDIDECSFDRTCDHMCVNTPGSFQCLCHRGYLLYGVTHCGDVDECSINKGGCRFGCINTPGSYQCTCPAGQGRLHWNGKDCTEPVKCQSSLGASKAMLSCNRSGKKDTCALTCPSRARFLPESENGFTVSCGTPSPKAAPARVIHSGNSTVSSSCHEAAVLPVKQRASFKIKDAKCRLHLRNKGKAEEASRILGPGSVPCSDCLVTFIHLKCDSSRKGKGRRARTPPGKEVTRLTLELEAEVRAEETTAGCGLPCLRQRMERRLKGSLKMLRKSINQDRFLLRLAGLDYELAHKPGLGAGDRAELVEVCRPGQHRAGTKCVSCPQGTYYHGQTEQCVPCPAGTFQEREGQLSCDLCPGSDAHGPLGATNVTTCAGQCPPGHHSGDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAVSFQDCDTKVQCSPGHYYNTSIHRCIRCAVGSYQPDFRQNFCTRCPGNTSTDFDGSTSVAQCKNRQCGGELGEFTGYIESPNYPGNYPAGVECVWNINPPPKRKILIVVPEIFLPSEDECGDVLVMRKNSSPSSITTYETCQTYERPIAFTARSRKLWINFKTSEANSARGFQIPYVTYDEDYEQLVEDIVRDGRLYASENHQEILKDKKLIKAFFEVLAHPQNYFKYTEKHKEMLPKSFIKLLRSKVSSFLRPYK
Protein: RING-type E3 ubiquitin transferase (Q19818)
Organism: Caenorhabditis elegans
Interaction partners:
- ATP-dependent RNA helicase cgh-1
- ALG-1 INteracting protein
- Protein argonaute-1
- ALG-1
- RRM domain-containing protein
- Hunchback-like protein
- RING-type domain-containing protein
- Protein argonaute-1
Sequence:
MKKAADRPTSAVNGRHESPATSTNNTQNSGTPSLNGQDPLRSTSSSPLFGTEPLPEDDHASCPYCQQDFRKPRVLDCLHSMCEDCIIAQLDGHLQAKSAAIEEKKRATAAMLDCELETPKVKERPTPPGVIRCPICSQESHVGNDVRYVHAMLLDFVRLAEMKEVEVEKMVAHHRKPCTACKSEQEAIAFCDQCSSDLCENCTTAHTVMNLFQGHTVTTFADLRQPGAHPELRQVMCSTHNQHMRYLCAACETAACKQCLEVDHLNHKIIDINELVINAIREDVTSTVDRVEKKYNNSVADMNSLPDKSQQLNEQYEIAKYRVDKHYEELRNSIEEAYQKSVNDLEEARIRQESNIDEMYRKSQVNEARVHDAINFTRRLLTKGNGLELVVSRKKVIQQFGNLSHAIPSHGHQVELEFYTPSKKQIDHFVHQLTGTVIGRVIQPTVKDVGNATAASTDRSERGGSQPGGGRSSSAANPSQQDEWGRPVYSQNPQLGAIGGERKKNTQNGTNGTRGDSNAFGGWPPSSHPPESTTPPPVTGPQTMITGAPTQTAAPIVSQQQLSNLPNAAAMAAAAAGMRPDLVALAANHMDLAALTNGSTNGSQTPLPESIFPAMWNARQGLPAVATPTTTGLSTNASAAYMQQKLAAAQLQALASHRLNPQIMSMNNLRTNQTIQEFLAMNAMGNLSLNPQLTSAAAAALAATAAANSAVTTTASDVGQSQNSANAQRVSDLKVHSVFGTSQQGSTIRELHCPSGFCLSDTDDILIADTNNHRVVVCGPPHPWKIGRPGTDDGQLCFPRKVIALRGEAVRYVVLDKGGDGKTRAQIFEARGEFVKRLNMMALVPRGGIEVSAAAATPNGQLLLVDTAGFVYSIDVDAPRVTFWFDASTQLGEASDVAMFDNLIYITDFKHHCVQVYTSEGKFIRKMGEPSQTPYPIGIDVSKAGEVLVADTHGNHLHVVVFSPEGQHIHSFTHNEFRLSRCVGLRIAKSGHIVTLCKHNHTLFVFKPLILPNGLPVPTPVPHATSLISKFQ
Protein: Exo-1,4-beta-xylosidase xlnD (EC 3.2.1.37) (1,4-beta-D-xylan xylohydrolase xlnD) (Beta-xylosidase A) (Beta-xylosidase xlnD) (Xylobiase xlnD) (O00089)
Organism: Aspergillus niger
Function: Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAHSMSRPVAATAAALLALALPQALAQANTSYVDYNIEANPDLYPLCIETIPLSFPDCQNGPLRSHLICDETATPYDRAASLISLFTLDELIANTGNTGLGVSRLGLPAYQVWSEALHGLDRANFSDSGAYNWATSFPQPILTTAALNRTLIHQIASIISTQGRAFNNAGRYGLDVYAPNINTFRHPVWGRGQETPGEDVSLAAVYAYEYITGIQGPDPESNLKLAATAKHYAGYDIENWHNHSRLGNDMNITQQDLSEYYTPQFHVAARDAKVQSVMCAYNAVNGVPACADSYFLQTLLRDTFGFVDHGYVSSDCDAAYNIYNPHGYASSQAAAAAEAILAGTDIDCGTTYQWHLNESIAAGDLSRDDIEQGVIRLYTTLVQAGYFDSNTTKANNPYRDLSWSDVLETDAWNISYQAATQGIVLLKNSNNVLPLTEKAYPPSNTTVALIGPWANATTQLLGNYYGNAPYMISPRAAFEEAGYKVNFAEGTGISSTSTSGFAAALSAAQSADVIIYAGGIDNTLEAEALDRESIAWPGNQLDLIQKLASAAGKKPLIVLQMGGGQVDSSSLKNNTNVSALLWGGYPGQSGGFALRDIITGKKNPAGRLVTTQYPASYAEEFPATDMNLRPEGDNPGQTYKWYTGEAVYEFGHGLFYTTFAESSSNTTTKEVKLNIQDILSQTHEDLASITQLPVLNFTANIRNTGKLESDYTAMVFANTSDAGPAPYPKKWLVGWDRLGEVKVGETRELRVPVEVGSFARVNEDGDWVVFPGTFELALNLERKVRVKVVLEGEEEVVLKWPGKE
Protein: Reticulon-like protein B13 (AtRTNLB13) (O64837)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17980018}; Multi-pass membrane protein {ECO:0000269|PubMed:17980018}.
Interaction partners:
- Reticulon-like protein B14
- Protein ROOT HAIR DEFECTIVE 3
- AT1G27990 protein
- Late embryogenesis abundant protein
- Reticulon-like protein B21
- Late embryogenesis abundant protein
- SNF1-related protein kinase regulatory subunit gamma-like PV42b
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- Protein DMP1
Sequence:
MANDVTKDPTPKSDIVEDIYLWRRKKLAFSTLLVSTSTWILLSFYGFTTITIVSWIGIAVVSMIFLWGSLLRLLSKVEPELSGLEVSEEFVVETVRSCRMLMEEMVRWMFRVGAESEWFVFARTVLGFWILSRIGNLLDFHTCLFIGLVMGLTVPKLWEEYGDQIQKHLGSLKDKSKGAYNTTHEKILEMKNKLHHGTEEKVKKSE
Protein: MIP17260p (Prip, isoform C) (D3DMU9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin
Sequence:
MGKFEYSLGLNELKSKELRLWQALIGEFLGNLILNFFACGACTQIEDGTFKALAFGLAIFMAITIVGHLSGGHVNPAVTAGMLVAGRISLIRAFFYVVFQCLGAIAGTAAVKILIDQDYYNGLGHTSLAPNITELQGLGIEFFLGLLLVLVVFGACDPHKPDSRYTAPLAIGMAVTLGHLGTIRYTGASMNPARTVGTAFATDIWASHWVYWVGPVLGGVAAALLYTQVLEAKPVPKVNEASEKYRTHADEREGCKPNHNPNHLAYTYLA
Protein: Adenylate kinase isoenzyme 1 (AK 1) (EC 2.7.4.3) (EC 2.7.4.4) (EC 2.7.4.6) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (Myokinase) (P39069)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP (By similarity). Exhibits nucleoside diphosphate kinase activity, catalyzing the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate substrates with either ATP or GTP as phosphate donor (By similarity). Also catalyzes at a very low rate the synthesis of thiamine triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P00568, ECO:0000255|HAMAP-Rule:MF_03171}.
Interaction partners:
- Adenylate kinase 7
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MEDKLKKAKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRAEVSSGSSRGKMLSSIMEKGELVPLETVLDMLRDAMLAKVDSSNGFLIDGYPREVKQGEEFERKIAQPTLLLYVDAGPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVISFYDKRGIVRKVNAEGSVDTVFSQVCTYLDSLK
Protein: Vacuolar protein sorting-associated protein 18 homolog (B5DFJ4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004492}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004492}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004492}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004630}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004630}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004630}.
Interaction partners:
- Vacuolar protein sorting-associated protein 33A
- Vacuolar protein sorting-associated protein 11 homolog
- VPS39 subunit of HOPS complex
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- VPS8 subunit of CORVET complex
- Transforming growth factor, beta receptor associated protein 1
- Vacuolar protein sorting-associated protein 33B
- CCZ1 homolog, vacuolar protein trafficking and biogenesis associated
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MASILDEYEDSLSRSAVLQTGCPSVGIPHSGYVNAHLEKEVPIFTKQRIDFTPSERITSLVVSCSQLCMSLGKDTLLRIDLGKASEPNRVELGRKDDAKVHKMFLDHTGSHLLVALSSTEVLYMNRNGQKARPLARWKGQLVESVGWNKALGSESSTGPILVGTAQGQIFEAELSASEGGLFGPAPDLYFRPLYVLNEEGGPAPVCSLEAERGPDGRGFVIATTRQRLFQFIGRAVEDAEAQGFSGLFAAYTDHPPPFREFPGNLGYSELAFYTPKLRSAPRAFAWMMGDGVLYGSLDCGRPDSLLSEEKVWEYPAGIGPGANPPLAIVLTQFHFLLLLADRVEAVCTLTGQVVLRDHFLEKFGPLRHMVKDSSTGHLWAYTERAVFRYHVQREARDVWRTYLDMNRFDLAKEYCRERPDCLDTVLAREADFCFRQHRYLESARCYALTQSYFEEIALKFLEARQEEALAEFLQRKLAGLKPTERTQATLLTTWLTELYLSRLGALQGDPDALNLYRDTRECFRTFLSSPRHKEWLFASRASIHELLASHGDTEHMVYFAVIMQDYERVVTYHCQHEAYEEALAVLARHRDPQLFYKFSPVLIRHIPRQLVDAWIEMGSRLDARQLIPALVNYSQGGDAQQVSQAIRYMEFCVNVLGETEQAIHNYLLSLYARGQPASLLAYLEQAGASPHRVHYDLKYALRLCAEHGHHRACVHVYKVLELYEEAVDLALQVDVDLAKQCADLPEEDEELRKKLWLKIARHVVQEEEDVQTAMACLASCPLLKIEDVLPFFPDFVTIDHFKEAICSSLKAYNHHIQELQREMEEATASAQRIRRDLQELRGRYGTVEPQDKCSTCDFPLLNRPFYLFLCGHMFHADCLLQAVRPGLPTYKQARLEELQRKLGTAPPPTKGSVKAKEAEAGAAAVGPSREQLKADLDELVAAECVYCGELMIRSIDRPFIDPQHYEEEHLSWL
Protein: Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1) (xChk1) (Q6DE87)
Organism: Xenopus laevis (African clawed frog)
Function: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome. Recognizes the substrate consensus sequence [R-X-X-S/T]. Phosphorylates wee1 at 'Ser-549' and cdc25c at 'Ser-287', which creates binding sites for 14-3-3 proteins which activate wee1 and inhibit cdc25c. Phosphorylates cdc25a at 'Ser-504' which prevents the interaction of cdc25a with CDK2-cyclin E1, CDC2-cyclin A1 and CDC2-cyclin B1. This inhibitory effect does not require 14-3-3 protein binding. Activation of wee1 and inhibition of CDC25 results in increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and consequent inhibition of cell cycle progression. May promote DNA repair, regulate chromatin assembly and the transcription of genes that regulate cell-cycle progression. May also play a role in replication fork maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:11133168, ECO:0000269|PubMed:14767054}. Chromosome {ECO:0000250|UniProtKB:O14757}. Cytoplasm {ECO:0000269|PubMed:11133168, ECO:0000269|PubMed:14767054}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14757}.
Interaction partners:
Sequence:
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRKTEEAVAVKIVDMTRAADCPENIKKEICINRMLSHTNIVRFYGHRREGNIQYLFLEYCRGGELFDRIEPDVGMPEQDAQKFFQQLIAGVEYLHSIGITHRDIKPENLLLDERDQLKISDFGLATVFRHNGKERLLNKMCGTLPYVAPELIKSRAFHADPVDVWSCGIVLTAMLAGELPWDQPNEVCQEYCDWKEKNHYLTPWKKISATPLALLCKMLTENPQSRITIPDIKKDRWFTEIIKKGLKRSRVISGGSSDSSVLCKQIRSDIDISHFSHSEEKTALSSTQPEPRTALATWDSNSSYIDNLVQGKGISFSQPACPDNMLLNSQLIGTPGSSQNVWQRLVKRMTRFFTKVNAESSYSNLMDTCEKMGYVLKKSCANEVTLSTTDRRNNKLIFKVNLVEMEDRILLDFRLSKGDGLEFKRHFLKIKKKMDAVVAVQKVLPDT
Protein: Coagulation factor V (Activated protein C cofactor) (Proaccelerin, labile factor) [Cleaved into: Coagulation factor V heavy chain; Coagulation factor V light chain] (P12259)
Organism: Homo sapiens (Human)
Function: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Prothrombin
- Coagulation factor X
- Vitamin K-dependent protein S
- Vitamin K-dependent protein C
- Coagulation factor VIII
- Multiple coagulation factor deficiency protein 2
- Multimerin-1
- Methylenetetrahydrofolate reductase
- Antithrombin-III
- Tissue factor
Sequence:
MFPGCPRLWVLVVLGTSWVGWGSQGTEAAQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGPTLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREYTYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFDKQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFSIHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKNCPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIGKHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPHGVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSDVDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCENPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTGHSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDDDEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIRSFRNSSLNQEEEEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGSPLRHLIGKNSVLNSSTAEHSSPYSEDPIEDPLQPDVTGIRLLSLGAGEFKSQEHAKHKGPKVERDQAAKHRFSWMKLLAHKVGRHLSQDTGSPSGMRPWEDLPSQDTGSPSRMRPWKDPPSDLLLLKQSNSSKILVGRWHLASEKGSYEIIQDTDEDTAVNNWLISPQNASRAWGESTPLANKPGKQSGHPKFPRVRHKSLQVRQDGGKSRLKKSQFLIKTRKKKKEKHTHHAPLSPRTFHPLRSEAYNTFSERRLKHSLVLHKSNETSLPTDLNQTLPSMDFGWIASLPDHNQNSSNDTGQASCPPGLYQTVPPEEHYQTFPIQDPDQMHSTSDPSHRSSSPELSEMLEYDRSHKSFPTDISQMSPSSEHEVWQTVISPDLSQVTLSPELSQTNLSPDLSHTTLSPELIQRNLSPALGQMPISPDLSHTTLSPDLSHTTLSLDLSQTNLSPELSQTNLSPALGQMPLSPDLSHTTLSLDFSQTNLSPELSHMTLSPELSQTNLSPALGQMPISPDLSHTTLSLDFSQTNLSPELSQTNLSPALGQMPLSPDPSHTTLSLDLSQTNLSPELSQTNLSPDLSEMPLFADLSQIPLTPDLDQMTLSPDLGETDLSPNFGQMSLSPDLSQVTLSPDISDTTLLPDLSQISPPPDLDQIFYPSESSQSLLLQEFNESFPYPDLGQMPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPKEEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPMDMREFVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRDCRMPMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAWSVEKLAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFKGNSTRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCSTPLGMENGKIENKQITASSFKKSWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSEMYVKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWNQSIALRLELFGCDIY
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Triose-phosphate isomerase) (P00942)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Phosphoglycerate mutase 1
- Transaldolase
- Enolase 2
- Transaldolase NQM1
Sequence:
MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN
Protein: Mediator of RNA polymerase II transcription subunit 9 (Mediator complex subunit 9) (Q9NWA0)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 26
- Mediator of RNA polymerase II transcription subunit 29
Sequence:
MASAGVAAGRQAEDVLPPTSDQPLPDTKPLPPPQPPPVPAPQPQQSPAPRPQSPARAREEENYSFLPLVHNIIKCMDKDSPEVHQDLNALKSKFQEMRKLISTMPGIHLSPEQQQQQLQSLREQVRTKNELLQKYKSLCMFEIPKE
Protein: Cytochrome c oxidase subunit VII (A0A1D8PJG0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 9, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit
Sequence:
MRMKQPDDQKSEREREKKYRLIIFNSLLILVNTIYFLSSNYPSHHPIYSIMNPQRIIELQKHYQNTPKPLWLRGRQSAFLVYPFYALFAVSTVIPLYYSVRAVAGIKDE
Protein: Early growth response protein (Q8QG62)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363046}.
Interaction partners:
Sequence:
MAAAKAEMQLLPSLQISDPFGVFPHSPPAMDGHYPKLEEMMLLSGGGQQFLAPSGAPESAGFGAAGEPSEQHFEHLAADTFPEISLNNEKTMPETSYPNQTTRLPPITYTGRFSLEPAPNGSNTLWPEPLFSLVSGLVSMANAPPTSTPSSSSPSSSQSTPLSCSVQASENSPIYSAAPTFPTSSSDIFPEPQTQPFPNPSGVPIQYPPPAYPTAKTNFQVPMIPDYLFPQQQSELNLISADQKPFSALETRAQQPSLTPLSTIKAFATQTGSQELKTLNTNYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKVEKAASVSATSSSVAAYSSSVATSYSSSIATTYPSSVRTVYSSPASSSYPSPAHTTFPSPSIATTYSSGTATFQTQVATSFPSPGVTNNFSSQVTSALSDMTSTFSPRTIEIC
Protein: Cytochrome c oxidase copper chaperone (Q14061)
Organism: Homo sapiens (Human)
Function: Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:19393246}. Cytoplasm {ECO:0000269|PubMed:19393246}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Protein SCO1 homolog
- Cytochrome c oxidase assembly protein COX19
- Protein SCO2 homolog
- Copper transport protein ATOX1
- Cytochrome c oxidase assembly protein COX11
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase assembly factor 6 homolog
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 7
- FAD-linked sulfhydryl oxidase ALR
Sequence:
MPGLVDSNPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI
Protein: Flagellar motor switch protein FliM (P23453)
Organism: Bacillus subtilis (strain 168)
Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation.
Subcellular location: Cell membrane; Peripheral membrane protein. Bacterial flagellum basal body.
Interaction partners:
- Flagellar basal-body rod protein FlgG
- Chemotaxis protein CheY
- Flagellar biosynthesis protein FlhA
- Flagellar biosynthetic protein FliP
- Flagellar protein FliL
- Flagellar biosynthetic protein FliQ
- Probable flagellar assembly protein FliH
- FlaA locus uncharacterized protein YlxG
- Flagellar biosynthesis protein FlhF
- Flagellar basal body rod protein FlgB
Sequence:
MSGEVLSQNEIDALLSAISTGEMDAEELKKEEKEKKVKVYDFKRALRFSKDQIRSLTRIHDNFARLLTTHFSAQLRTYIHISVSSVDQVPYEEFIRSIPNMTILNLFDVHPMEGRIMMEVNPTIAYTMMDRVMGGIGISHNKVDSLTEIETKIISNLFENALGNYKEAWQSIADIEPEMTEFEVNPQFVQMVSPNETVVVISLNTQIGEISGVINLCIPHIVLEPLIPKLSVHYWMQSDRNEPKPEETKSLEKRIMTAQIPVVAELGTSELTIEEFLSLEVGDCITLDKSVTDPLTVLVGDKPKFLGQAGRVNRKQAVQILDHDIRGEQDGE
Protein: Mitochondrial peptide methionine sulfoxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (PMSR) (Q9D6Y7)
Organism: Mus musculus (Mouse)
Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Subcellular location: [Isoform 1]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Membrane; Lipid-anchor.
Interaction partners:
- Methionine-R-sulfoxide reductase B3, mitochondrial
- Methionine-R-sulfoxide reductase B2, mitochondrial
- Thioredoxin
- Methionine-R-sulfoxide reductase B1
- Thioredoxin, mitochondrial
- Glutaredoxin-1
- Glutaredoxin-2
- Thioredoxin domain-containing protein 3
- Cystathionine gamma-lyase
Sequence:
MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVYRPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLGGTGVSCPMAIKK