wanglab/gogpt-training-data huggingface dataset:
Protein: Fibroblast growth factor 23 (FGF-23) (Q8VI82)
Organism: Rattus norvegicus (Rat)
Function: Regulator of phosphate homeostasis (By similarity). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (By similarity). Regulator of vitamin-D metabolism (By similarity). Negatively regulates osteoblasts differentiation and matrix mineralization (By similarity). Acts directly on the parathyroid to decrease PTH secretion. Up-regulates EGR1 expression in the presence of KL.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9GZV9}. Note=Secretion is dependent on O-glycosylation. {ECO:0000250|UniProtKB:Q9GZV9}.
Interaction partners:
- Fibroblast growth factor receptor 1
- Klotho
- Fibroblast growth factor receptor 4
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Polypeptide N-acetylgalactosaminyltransferase.
- Parathyroid hormone
- Klotho beta
- Phosphate regulating endopeptidase X-linked
- Fibroblast growth factor
Sequence:
MLGACLRLLVGALCTVCSLGTARAYSDTSPLLGSNWGSLTHLYTATARNSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVIIGAMTRRFLCMDLRGNIFGSYHFSPENCRFRQWTLENGYDVYLSPKHHYLVSLGRSKRIFQPGTNPPPFSQFLARRNEVPLLHFYTARPRRHTRSAEDPPERDPLNVLKPRPRATPIPVSCSRELPSAEEGGPAASDPLGVLRRGRGDARRGAGGTDRCRPFPRFV
Protein: Anaphase-promoting complex subunit 2 (Q3B7T7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
SFLREFHKWIERVVGWLGKVFLQDNPSRPTSPEAGNTLRRWRCHVQRFFYRIYASLRIEELFSIIRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKVALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPACLETGQDSEDDSGEPEDWVPDPVDADPAKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPVEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALDVYCKKYEKLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVVLLYFQDQASWTLEELSKVVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWTYIQAMLTNLESLSLERIYSMLRMFVMTGPALAEIDLQELQGYLQKKVRDQQLIYSAGVYRLPKNCN
Protein: Gnptg protein (Q4G066)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
AGRLTGFLMLLGLAAQGPAPTHAGKMKVVEEPNTFGLNNPFLPQASRLQPKREPSAVSGPPHLFRLAGKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIVNNTFKGMWMTDGDSCHSRSRQSKVELTCGKTNRLAHVSEPSTCVYALTFETPLVCHPHSLLVYPTLSEALQQRWDQVEQDLADELITPQGYEKLLRALFEDAGYLKVPGETHPTQLAGDSKGLGLETLDICRKAHAELSREVQRLTSLLEQHGIPHTQPTETTHSQLLGQQLPVGEISEQLRGDPGLRGNIL
Protein: Coatomer subunit delta (Delta-coat protein) (Delta-COP) (O74496)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Probable coatomer subunit gamma
- Probable coatomer subunit beta'
- Probable coatomer subunit zeta
- Coatomer subunit beta
- Probable coatomer subunit epsilon
- Putative coatomer subunit alpha
- ADP-ribosylation factor GTPase-activating protein glo3
- ADP-ribosylation factor 1
- Terminal uridylyltransferase cid1
- Protein transport protein sec31
Sequence:
MVVLAVSIVNRGGKAIISRQFREMSRVRVESLLSSFPALVSEKSQNTTVESDNVRFVYQPLDELYIVLITNLQSNILQDIDTLHLLSQVVTSICSSLEEREILEYAFEIFTAFDEATSLGYRDNVSLTQIKTYLEMESHEEKIQEIVSRNKEIEATEERKRRIKQLELQKKEAARRAAQNLPSADAYESIGYQTVNTTFATSNVEDESAMESYHAAAKASSAPKAKGMQLGKKKNTSLLY
Protein: Cytochrome bd-II ubiquinol oxidase subunit 1 (EC 7.1.1.3) (Cytochrome bd-II oxidase subunit I) (P26459)
Organism: Escherichia coli (strain K12)
Function: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Putative cytochrome bd-II ubiquinol oxidase subunit AppX
- Cytochrome bd-I ubiquinol oxidase subunit 2
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Phytase AppA
- Hydrogenase-1 operon protein HyaF
- Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit
- Glutathione/L-cysteine transport system ATP-binding/permease protein CydD
- Hydrogenase-1 operon protein HyaE
- Hydrogenase-1 small chain
Sequence:
MWDVIDLSRWQFALTALYHFLFVPLTLGLIFLLAIMETIYVVTGKTIYRDMTRFWGKLFGINFALGVATGLTMEFQFGTNWSFYSNYVGDIFGAPLAMEALMAFFLESTFVGLFFFGWQRLNKYQHLLVTWLVAFGSNLSALWILNANGWMQYPTGAHFDIDTLRMEMTSFSELVFNPVSQVKFVHTVMAGYVTGAMFIMAISAWYLLRGRERNVALRSFAIGSVFGTLAIIGTLQLGDSSAYEVAQVQPVKLAAMEGEWQTEPAPAPFHVVAWPEQDQERNAFALKIPALLGILATHSLDKPVPGLKNLMAETYPRLQRGRMAWLLMQEISQGNREPHVLQAFRGLEGDLGYGMLLSRYAPDMNHVTAAQYQAAMRGAIPQVAPVFWSFRIMVGCGSLLLLVMLIALVQTLRGKIDQHRWVLKMALWSLPLPWIAIEAGWFMTEFGRQPWAIQDILPTYSAHSALTTGQLAFSLIMIVGLYTLFLIAEVYLMQKYARLGPSAMQSEQPTQQQG
Protein: Rifin (Q8I2C5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILIYNQRNHKSTTHHTLKIPITRLLCECDIYTSIYDNDPQMKEVMDNFNRQTQQRFHEYDERMQGKRQKCKDKCDKEIQKIILKDKLEKELMDKFATLHTDMQSDSIPTCVCEKSVADKVEKNYMKCTQNLGGIVAPSSGVLAGIAELGLSAWKTTALKTAIAAAEQAGAAKGLAAGAAKGATRLIELIQSTFKIQNIAGKSLGTFIDATNYNNGPFIYQAIYTKFEMSLCLPVFPGVDPVPGAVRDPTFCNLFEKFVPTNGSSNRDSIINAIETYVQPFVSDAKFTAAATAETATEEATAVLITKKTGEVTTTYASYQTAIIASIVAILVIVLVMIIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Loner ISO2 (Schizo, isoform A) (Q7KTX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSRCDNHKSRRQQLPVPAPLSSSHSNSSSSRSQGHHHHHHHQLHSSNSDLGGSESFLQYCSDSEKRPPPIVVVVGDGRSRVRRVVRTATRHVTVVSLSTRHKETQTHTSHHVTAVSFPQKSLERSGSTQYELAGAQQPGSANASTCTDSGSVGGYVYLQNHYAPGAHSSSAAINYPAQQHPQMVYQIQQYPTCHQQQQQQHLQQQQHLHQTGAGHYMQVTATGGGQYHHHHMLHGHGHHAHHHGGAVVIAGSGVGTGLGSGATSVIMQHQQQQQQQQNMHKKNSIRNGGDVLKRTRAQSAYELSQDLLEKQIELLERKYGGVRARNAAVTIQRAFRHYMMVKKFASITAMAKAEKRLSRRMVVTASSLGLAEEGASSSSAYGSATESQLTEQQQQQQAQQQQQPRVTIMAGPAGAASPGLSRTPPTRSLSMRERRQLDCSPIPRSQSGASPASISSSTVSTSALASHPHVNLLHAAEPHYYNAQALPQGAAYYTSYHGSPHDLSYASSADTSLNASWVNTSGHSPHTPYYSAAQIYMRPKGGSTTPTPSCSGSTGSGSGGSGSGSSKKVPPEVPKRTSSITAQQQTQLLLLQRQTPPPPSLLRTNGLCKTAENGSLTSVQSSGSDSSVTSAERNLNSDLGSDRSNSPHTWKRGTALNSSQQFSTHSADSAGAVSGGGVGVAGGAGVYAAQMQAAVAAATAAGGMPPADDHAISSHTSAAQYEQHEQQQHEQQQLQAAAAAAGVAQNYKMSETIRKRQYRVGLNLFNKKPEKGITYLIRRGFLENTPQGVARFLITRKGLSRQMIGEYLGNLQNQFNMAVLSCFAMELDLSGRQVDVALRKFQAYFRMPGEAQKIERLMEIFSQRYCECNADIVGRLRSSDTIFVLAFAIIMLNTDLHTPNLKPERRMRVEDFIKNLRGIDDCHDIDKDMLMGIYDRVKSDEFKPGSDHVTQVMKVQATIVGKKPNLALPHRRLVCYCRLYEIPDVNKKERPGVHQREVFLFNDLLVITKIFSKKKTSVTYTFRNSFPLCGTVVTLLDMPNYPFCIQLSQKVDGKILITFNARNEHDRCKFAEDLKESISEMDEMESLRIEAELERQKSARNRAPGNAENRDSGVADVEVCPCPYQQGSQASGEQAPNSADNSQQLKRSALSNSLLDMHEQFGNEKPQRRGSVGSLDSGMSISFQSTTTSSASRENAAAIAAAANAAAAAKMRFNMPPTAAIATPSNVYAAPGMQAYTHANFVQQSQAAYMLQQQQMLQQQAQMQAQAQAQAQAQAQAQAQAQAQAQAQPLTGRIPGRERKASRTDENGRSTEV
Protein: Potassium voltage-gated channel subfamily Q member 5 (A0A8I5ZXW9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPRHHAGGEEGGAAGLWVRSGAAAAAGGGRPGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAAALGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFVYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEAASSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKTVIDADTALGIDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALTLTSFQIPPFECEQTSDYQSPVESKDLSSSAQNSGCLSRSASANISRGLQFILTPNEFSAQTFYALSPTMHSQTTQVPMSQNDGSSVVATNNLANQISAAPKPAAPTTLQIPPPLSAIKHLSRPEPLLSNPPGVHESISDVTTCLVASKENVQFAQSNLTKDRSLRKSFDMGGETLLSVRPMVPKDLGKSLSVQNLIRSTEELNLQFSGSESSGSRGSQDFYPKWRESKLFITDEEVGAEETETDTFDGTPPPAGEAAFSSDSLRTGRSRSSQNICKTGDSTDALSLPHVKLN
Protein: Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (Rotamase B) (Q8X166)
Organism: Aspergillus niger
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MNFKNIFLSFFFVLAVGLALVHAEDAQPRGPKITSKVFFDIEHGDKPLGRVVLGLYGKTVPKTAENFRALATGEKGFGYEGSTFHRVIKDFMIQGGDFTRGDGTGGKSIYGEKFADENFKLRHTRKGLLSMANAGKDTNGSQFFITTVPTPWLDGRHVVFGEVLEGYEIVAQIENVPKGRSDRPVETVKIVKSGELESEDKAGEKGSSHEEL
Protein: Nitric oxide synthase 3 (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (NOS type III) (NOSIII) (Nitric oxide synthase, endothelial) (Endothelial NOS) (eNOS) (Q28969)
Organism: Sus scrofa (Pig)
Function: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets (By similarity).
Subcellular location: Membrane, caveola {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity. {ECO:0000250}.
Interaction partners:
- Calmodulin like 5
- Uncharacterized protein.
- Calmodulin 3
- Heat shock protein HSP 90-alpha
- Arginase
- Argininosuccinate synthase
- Arginase-1
- Uncharacterized protein
- Argininosuccinate lyase
- non-specific serine/threonine protein kinase
Sequence:
MGNLKSVGQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPAPATPHAPEHSPAPNSPTLTRPPEGPKFPRVKNWEVGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQSRPSPGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVATTGTYHLGESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAITVFPQRTPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPPELFALPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYVLSPAFRYQPDPWKGSAAKGTGIARKKTFKEVANAVKISASLMATVMPKRVKASILYASETVRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNGSPRPEQHRSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQASCETFCVGEDAKAAARDIFSPKRSWKRQRYRLSAQVEGLQLLPGLVHVHRRKMFQATVLSVENLQSSKSTRATILVRLDTEGQEGLQYQPGDHIGICPPNRTGLVEALLSRVEDPTPPTESVGVEQLEKGSPGGPPPSWVRDPRLPPYTLRQALTFFLDITSPPSPRLLRVLSTLAEEPSEQQELETLSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPTPLLLTQLALLQPRYYSVSSAPSTYPGEIHPTVAVLAYRTQDGLGPLHYGVCSTWLGQLKPGDPVPCFIRAAPSFRLPPDPSLPCILVGPGTGIAPFRGFWQERLHDIESKGLQPAPMTLVFGCRCSQLDHLYRDEVQDAQQRGVFGRVLTAFSREPDSPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATSVLQTVQRILATEGNMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERHLRGAVPWTFDPPGPDTPGP
Protein: Reduced folate transporter (Intestinal folate carrier 1) (IFC-1) (Plasma membrane folate antiporter SLC19A1) (Reduced folate carrier 1) (RFC-1) (RFC1) (Solute carrier family 19 member 1) (P41438)
Organism: Mus musculus (Mouse)
Function: Antiporter that mediates the import of reduced folates. Mechanistically, acts as a secondary active transporter, which exports intracellular organic anions down their concentration gradients to facilitate the uptake of its substrates (By similarity). Has high affinity for N5-methyltetrahydrofolate, the predominant circulating form of folate. Also able to mediate the import of antifolate drug methotrexate. 5-amino-4-imidazolecarboxamide riboside (AICAR), when phosphorylated to AICAR monophosphate, can serve as an organic anion for antiporter activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10787414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}. Apical cell membrane {ECO:0000269|PubMed:10787414}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}. Basolateral cell membrane {ECO:0000250|UniProtKB:P41440}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41440}.
Interaction partners:
- Proton-coupled folate transporter
- Folate receptor alpha
- Folate receptor beta
- Methylenetetrahydrofolate reductase
- Methionine synthase reductase
- Folylpolyglutamate synthase, mitochondrial
- Gamma-glutamyl hydrolase
- Dihydrofolate reductase
Sequence:
MVPTGQVAEKQAYEEPRQDHELKSWRCLVFYLCFFGFMAQLRPGESFITPFLLERKFTKEQVTNEIIPMLPYSHLAVLVPVFLLTDYLRYKPVLVLQCLSFVCVWLLLLLGTSVVHMQLMEVFYSVTMAARIAYSSYIFSLVHPSRYQRMASYSRAAVLLGVFISSVLGQALVTVGHISTYTLNCVSLGFILFSLVLSLFLKRPKRSLFFNRSTLARGALPCELDQMHPGPDRPETRKLDRMLGTCRDSFLVRMLSELVENARQPQLRLWCLWWVFNSSGYYLITYYVHVLWRSTDSSLSYNGAVDAASTLLSAITSFSAGFLSIRWTLWSKLVIAGVIAIQASLVFCMFQIRDIWVCYVTFVLFRGAYQFLVPIATFQIASSLSKELCALVFGINTFLATALKTCITLVVSDKRGLGLQVRDQFRIYFIYFLMLSITCFAWAGLDGLRYCQRGRHQPLAQAQELRSPLETSVQAISLQDGDLRGPQPSAPQLLSEDGMEDDRGDLRVEAKA
Protein: Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Q9VC92)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Elongation of very long chain fatty acids protein
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
MEPGPSAVNYEGSESVCGMPVEAHDPLYLKAYRQSVQNPAAFWEEQGNLLDWDRPWEKVLDNSNPPFTKWYVGGYLNACYNSIDRHILAGRGSNVALIHDSPLTGTLRRVTYQELYDQIVLLAGGLAKLGVVKGDRVVIYMPLIPETIIAMLAIVRLGAIHSVVFGGFAARELCSRIEHVEPKLVIASNVGVEPGKVVPYLDILHSAISMSRWRPPQRNIIFRRDNVSPDTTKLDPLTDVLWSDILKMAEGERPIACVPIEANDPLYILYTSGTTDKPKGVLRTIGGHLVALVYTLRTLYGINPGHTWWAASDMGWVVGHSYICYGPLCLGATSVMYEGKPDRTPDPGQYFRIIDQYQVRSIFSVPTSFRVIRRADPDISYGRQYSMKSLRAIFIAGEHCDYETKSWIEKTFKVPVLNHWWQTETGSAVTATCLGFQQNLSPPTYSTGLPLMGYDVKILKADGSEAQTSELGRIALKLPLPPGNMATLYKNEELFRTLYFQKFPGYYDTMDAGYKDERGYIFVTARDDDVINVAGHRLSTSSLEDAVLRHPDVVDVAVFGVPEATKGQVPLCLYIPVENCKKTDAKLSTEIIKLIRDVVGPIAAFRLVTSVNNLPRTRSGKTMRKAMADFARNERVVLPATIDDASVFIEIRRALNQLGYAMTAPDPIVAKLLD
Protein: Small VCP/p97-interacting protein (P0C0A9)
Organism: Rattus norvegicus (Rat)
Function: Overexpression causes the formation of large vacuoles that seemed to be derived from the endoplasmic reticulum.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q8NHG7}; Lipid-anchor {ECO:0000250|UniProtKB:Q8NHG7}. Smooth endoplasmic reticulum membrane {ECO:0000269|PubMed:12529442}; Peripheral membrane protein {ECO:0000269|PubMed:12529442}. Golgi apparatus membrane {ECO:0000269|PubMed:12529442}; Peripheral membrane protein {ECO:0000269|PubMed:12529442}. Cell membrane {ECO:0000269|PubMed:12529442}; Peripheral membrane protein {ECO:0000269|PubMed:12529442}. Lysosome membrane {ECO:0000250|UniProtKB:Q8NHG7}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 2A
- Nuclear protein localization protein 4 homolog
- NSFL1 cofactor p47
- UBX domain protein 8
- UBX domain-containing protein 4
Sequence:
MGLCFPCPAESAPPSPSPEEKRAKLAEAAERRQKEAASRGILDIQSVEAKKKKKEQLEKQMETSGPPAGGLRWTVS
Protein: Casein kinase I isoform alpha-like (CKI-alpha-like) (EC 2.7.11.1) (CK1) (Q8N752)
Organism: Homo sapiens (Human)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Axin-2
- Glycogen synthase kinase-3 beta
- Axin-1
- Catenin beta-1
- Adenomatous polyposis coli protein 2
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Beta-adrenergic receptor kinase 1
- Protein smoothened
Sequence:
MTNNSGSKAELVVGGKYKLVRKIGSGSFGDVYLGITTTNGEDVAVKLESQKVKHPQLLYESKLYTILQGGVGIPHMHWYGQEKDNNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFLHRDIKPDNFLMGTGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKHLIGTVRYASINAHLGIEQSRRDDMESLGYVFMYFNRTSLPWQGLRAMTKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEVPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTQTGKQTEKNKNNVKDN
Protein: Probable mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (PEP) (Q9P7X1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P10507}.
Interaction partners:
- Cytochrome b-c1 complex subunit 9
- Probable mitochondrial-processing peptidase subunit alpha
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b
Sequence:
MLRLQNLPKLVRRFATTALPKTETTTLKNGLTVATEHHPYAQTATVLVGVDAGSRAETAKNNGAAHFLEHLAFKGTKNRSQKALELEFENTGAHLNAYTSREQTVYYAHAFKNAVPNAVAVLADILTNSSISASAVERERQVILREQEEVDKMADEVVFDHLHATAYQGHPLGRTILGPKENIESLTREDLLQYIKDNYRSDRMIISSAGSISHEELVKLAEKYFGHLEPSAEQLSLGAPRGLKPRFVGSEIRARDDDSPTANIAIAVEGMSWKHPDYFTALVMQAIIGNWDRAMGASPHLSSRLSTIVQQHQLANSFMSFSTSYSDTGLWGIYLVTENLGRIDDLVHFTLQNWARLTVATRAEVERAKAQLRASLLLSLDSTTAIAEDIGRQLLTTGRRMSPQEVDLRIGQITEKDVARVASEMIWDKDIAVSAVGSIEGLLDYNRIRSSISMNRW
Protein: Cytochrome P450 11B2, mitochondrial (Aldosterone synthase) (ALDOS) (Aldosterone-synthesizing enzyme) (CYPXIB2) (Corticosterone 18-monooxygenase, CYP11B2) (EC 1.14.15.5) (Cytochrome P-450Aldo) (Cytochrome P-450C18) (Cytochrome P450(11beta,aldo)) (P450(11beta,aldo)) (Cytochrome P450-Aldo-1) (Steroid 11-beta-hydroxylase, CYP11B2) (EC 1.14.15.4) (Steroid 18-hydroxylase) (P30099)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase that catalyzes the biosynthesis of adrenal mineralocorticoid aldosterone. Catalyzes three sequential oxidative reactions of 11-deoxycorticosterone/21-hydroxyprogesterone, namely 11-beta hydroxylation followed with two successive oxidations at C18 to yield 18-hydroxy and then 18-aldehyde derivatives, resulting in the formation of aldosterone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
Sequence:
MGACDNDFIELHSRVTADVWLARPWQCLHRTRALGTTATLAPKTLKPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQAFQELGPIFRHSAGGAQIVSVMLPEDAEKLHQVESILPRRMHLEPWVAHRELRGLRRGVFLLNGAEWRFNRLKLNPNVLSPKAVQNFVPMVDEVARDFLEALKKKVRQNARGSLTMDVQQSLFNYTIEASNFALFGERLGLLGHDLNPGSLKFIHALHSMFKSTTQLLFLPRSLTRWTSTQVWKEHFDAWDVISEYANRCIWKVHQELRLGSSQTYSGIVAALITQGALPLDAIKANSMELTAGSVDTTAIPLVMTLFELARNPDVQQALRQETLAAEASIAANPQKAMSDLPLLRAALKETLRLYPVGGFLERILNSDLVLQNYHVPAGTLVLLYLYSMGRNPAVFPRPERYMPQRWLERKRSFQHLAFGFGVRQCLGRRLAEVEMLLLLHHMLKTFQVETLRQEDVQMAYRFVLMPSSSPVLTFRPIS
Protein: Conserved protein (O05899)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- mannose-6-phosphate isomerase
- Acetyltransferase
- Probable phosphomannomutase PmmA
- Glutathione S-transferase domain-containing protein
- Secreted protein
- Glutamine--fructose-6-phosphate aminotransferase
- UDP-N-acetylmuramate--L-alanine ligase
- Cell envelope integrity protein Cei
- Probable nucleoside hydrolase IunH
- Probable conserved transmembrane protein
Sequence:
MNVARAIDLEDTEGLIAADRGALLRAASMAGAQVRAIAAAADEGELDLLRGSDRPRSVIWVTGRGTAETAGTILASTLGAGAAEPIVLASAAPPWVGPLDVLIVAGDDPGDPALVGAAAIGVRRGARVVVVAPYEGPLRDSTAGRVAVLEPRLRVPDEFGLSRYLAAGLAALQTVDPKLRIDLASLADELDAEALRNSAGREVFTNPAKALAARVSGCQLALAGDNAATLALARHGSSVMLRIANQVVAATRLSDAVVALRAGTPPDALFHDEEIDGPAPQRLRVLALALAGERTVVAARVAGLDDAYLVAAEDVPELLDAPVGSGGAVLAVRLEMAAVYLRLVRG
Protein: Catechol O-methyltransferase (EC 2.1.1.6) (A0A140VJG8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004228}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004228}; Extracellular side {ECO:0000256|ARBA:ARBA00004228}.
Interaction partners:
Sequence:
MPEAPPLLLAAVLLGLVLLVVLLLLLRHWGWGLCLIGWNEFILQPIHNLLMGDTKEQRILNHVLQHAEPGNAQSVLEAIDTYCEQKEWAMNVGDKKGKIVDAVIQEHQPSVLLELGAYCGYSAVRMARLLSPGARLITIEINPDCAAITQRMVDFAGVKDKVTLVVGASQDIIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVICPGAPDFLAHVRGSSCFECTHYQSFLEYREVVDGLEKAIYKGPGSEAGP
Protein: Homeobox protein aristaless-like 4 (Q9H161)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in skull and limb development. Plays an essential role in craniofacial development, skin and hair follicle development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:19692347}.
Interaction partners:
- Exostosin-2
- Transcriptional activator GLI3
- Zona pellucida sperm-binding protein 2
Sequence:
MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRAFPGGDKFGTTFLSAAAKAQGFGDAKSRARYGAGQQDLATPLESGAGARGSFNKFQPQPSTPQPQPPPQPQPQQQQPQPQPPAQPHLYLQRGACKTPPDGSLKLQEGSSGHSAALQVPCYAKESSLGEPELPPDSDTVGMDSSYLSVKEAGVKGPQDRASSDLPSPLEKADSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWLGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVTDFLSVSGAGSHVGQTHMGSLFGAASLSPGLNGYELNGEPDRKTSSIAALRMKAKEHSAAISWAT
Protein: E3 ubiquitin-protein ligase TRIM63 (EC 2.3.2.27) (Iris RING finger protein) (Muscle-specific RING finger protein 1) (MuRF-1) (MuRF1) (RING finger protein 28) (RING-type E3 ubiquitin transferase TRIM63) (Striated muscle RING zinc finger protein) (Tripartite motif-containing protein 63) (Q969Q1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, M line. Cytoplasm, myofibril, sarcomere, Z line. Note=Colocalizes with TNNI3 in myocytes (By similarity). Localizes to the M- and Z-lines in skeletal muscle. {ECO:0000250}.
Interaction partners:
- Titin
- F-box only protein 32
- Telethonin
- Nebulin
- Next to BRCA1 gene 1 protein
- Forkhead box protein O1
- Protein YIPF1
- Myosin-binding protein C, cardiac-type
- Sequestosome-1
- E2 ubiquitin-conjugating enzyme
Sequence:
MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ