wanglab/gogpt-training-data huggingface dataset:
Protein: Centriole and centriolar satellite protein ofd1 (Oral-facial-digital syndrome 1 protein homolog) (Q7SZK7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the centrioles controlling mother and daughter centrioles length. Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis. Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12782125}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:12782125}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:12782125}. Nucleus {ECO:0000250|UniProtKB:O75665}. Note=Localizes to centriole distal ends. {ECO:0000250|UniProtKB:O75665}.
Interaction partners:
- Pericentriolar material 1.
- Centrosomal protein of 290 kDa
- Transmembrane protein 216
- Nephronophthisis 1.
- Kinesin-like protein
- Abelson helper integration site 1.
- NudE neurodevelopment protein 1.
- Meckelin isoform X1
- Intraflagellar transport 88 homolog.
- Protein moonraker isoform X1
Sequence:
MSASKEESLSPDEMRQKLYQTFKSRGLLDTLKTQLRNQLIQELQAPVRRGESASRRSADHTDSVLVSACNSVVVDHLRSAGYEYTLSVFQPECGLSKDKVLSSRDVLQIMKISPHMPLYKSLVSNIQSGQSGFLKSLLMELTDHSVYRDCSDNSTQTTSIAAHKESLVEKMQLIDEEYEVLRHRGDRWASVEAKLAEYRKEIQEQAQIELNAKLQHFMDVEIAKVKQEEKERSRKEILELRRDMEKTYELKSEALISREKNAIERLQKHQEIEEKDIYAQRQAVLREIESVRSREMELRQRMEAFDKSCALHEEKVKTMEDLLRRRELSVKTMEDSFEQKLKSELLKYQLELKEENMKRPEKLTENEERIRAEAARLQKEAAVVDAKTEDYERKSSEVKQLLMELESSRSQASLLKQQKELLREQLENMRDYPELKKHTLELQTRISLLKQQLEEKQQHNQRLTQELSAPSHEHLMLQAELRRLEAEHKLEKEELETQKNVLHTQLQHEVQQCALLKTQLMECEERTKWMNTHTEELKLQLQQTQQGPALRGPKSRTVAPEHDSDMVISALSRIRELEQEAERLEEAYRSHQQRALSAEDPTLHRGSQNYSRATAAQQHRVISRSPIFAGRPIEEEHEEFSRTPSPAERLASPPARRLSSTPQSASRSKRRADEEHDEHSLNPECVKGSSNTDRPALMFPERLISPIPAEELSSSISPNSPVMKSTTRHTQSPAKLQEILLSSSSQESSPQPEKITLHDLTEPIQMVSADQPCLLKDCEPELQQDHPDVQISSSSSSSSSSQREEEQQRETHTLQQQPHEEQTQEQRDDAGGHVTSAASPTGGAEEANPLQRYMQMLMQDKQQEQSPNKESSGSHEENLQSESHEHSAGVISHDEADDDFW
Protein: Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) (Q13705)
Organism: Homo sapiens (Human)
Function: Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:31665064}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Activin receptor type-1B
- Inhibin beta A chain
- Growth/differentiation factor 11
- TGF-beta receptor type-1
- Bone morphogenetic protein 2
- Bone morphogenetic protein 7
- Activin receptor type-2A
- Activin receptor type-1C
- Growth/differentiation factor 2
Sequence:
MTAPWVALALLWGSLCAGSGRGEAETRECIYYNANWELERTNQSGLERCEGEQDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPIGGLSLIVLLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSNLEVELWLITAFHDKGSLTDYLKGNIITWNELCHVAETMSRGLSYLHEDVPWCRGEGHKPSIAHRDFKSKNVLLKSDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCKAADGPVDEYMLPFEEEIGQHPSLEELQEVVVHKKMRPTIKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERVSLIRRSVNGTTSDCLVSLVTSVTNVDLPPKESSI
Protein: Sorting nexin-27 (MAP-responsive gene protein) (Methamphetamine-responsive transcript 1 protein) (PDZ-protein Mrt1) (Q8K4V4)
Organism: Rattus norvegicus (Rat)
Function: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes.
Subcellular location: Early endosome membrane; Peripheral membrane protein. Cytoplasm, cytosol. Note=Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products (By similarity). {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 35
- ubiquitinyl hydrolase 1
- VPS26 retromer complex component B
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-2
- Sorting nexin-3
- Sorting nexin-1
- Sorting nexin-5
- Diacylglycerol kinase zeta
Sequence:
MADEDGEGIHPSTPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGATVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVINHSFVRKLAPNEFPHKLYVQNYTSAVPGTCLTIRKWLFTTEEEVLLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLYEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT
Protein: Ribulose bisphosphate carboxylase large chain (EC 4.1.1.39) (Q5K3B1)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229, ECO:0000256|RuleBase:RU000302}.
Interaction partners:
Sequence:
MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVVGEDNQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRARGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIRSACKWSPELAAACEIWKAIKFEFEPVDKLD
Protein: Signal peptide peptidase-like 3 (SPP-like 3) (EC 3.4.23.-) (Intramembrane protease 2) (IMP-2) (Presenilin homologous protein 1) (PSH1) (Presenilin-like protein 4) (Q8TCT6)
Organism: Homo sapiens (Human)
Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries. Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1. Catalyzes the intramembrane cleavage of the envelope glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy virus independent of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis. May also have the ability to serve as a shedding protease for subsequent intramembrane proteolysis by SPPL2A and SPPL2B of the envelope glycoprotein gp130. Plays a role in the regulation of cellular glycosylation processes. Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus {ECO:0000269|PubMed:16829952}. Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}.
Interaction partners:
Sequence:
MAEQTYSWAYSLVDSSQVSTFLISILLIVYGSFRSLNMDFENQDKEKDSNSSSGSFNGNSTNNSIQTIDSTQALFLPIGASVSLLVMFFFFDSVQVVFTICTAVLATIAFAFLLLPMCQYLTRPCSPQNKISFGCCGRFTAAELLSFSLSVMLVLIWVLTGHWLLMDALAMGLCVAMIAFVRLPSLKVSCLLLSGLLIYDVFWVFFSAYIFNSNVMVKVATQPADNPLDVLSRKLHLGPNVGRDVPRLSLPGKLVFPSSTGSHFSMLGIGDIVMPGLLLCFVLRYDNYKKQASGDSCGAPGPANISGRMQKVSYFHCTLIGYFVGLLTATVASRIHRAAQPALLYLVPFTLLPLLTMAYLKGDLRRMWSEPFHSKSSSSRFLEV
Protein: Very long chain fatty acid elongase 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Elongation of very long chain fatty acids protein 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4) (Q9GZR5)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03204, ECO:0000269|PubMed:16036915, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03204}.
Interaction partners:
- Interphotoreceptor matrix proteoglycan 1
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 1
- Very-long-chain
- Very-long-chain
- Very-long-chain
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Terminal nucleotidyltransferase 5A
- Retinal-specific phospholipid-transporting ATPase ABCA4
Sequence:
MGLLDSEPGSVLNVVSTALNDTVEFYRWTWSIADKRVENWPLMQSPWPTLSISTLYLLFVWLGPKWMKDREPFQMRLVLIIYNFGMVLLNLFIFRELFMGSYNAGYSYICQSVDYSNNVHEVRIAAALWWYFVSKGVEYLDTVFFILRKKNNQVSFLHVYHHCTMFTLWWIGIKWVAGGQAFFGAQLNSFIHVIMYSYYGLTAFGPWIQKYLWWKRYLTMLQLIQFHVTIGHTALSLYTDCPFPKWMHWALIAYAISFIFLFLNFYIRTYKEPKKPKAGKTAMNGISANGVSKSEKQLMIENGKKQKNGKAKGD
Protein: GOLD domain-containing protein (Q385L4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLQCLTYARTFYPCHLLLLTILVAQGAKGFRFTVNPGRKCFTEEVPEAGRYYLQYKMTRSLTPFVAVAVTTSGGASLVVHNVAKTDAREIFELNQDRKIAICFKVSPKAVHSATSMNITLELMDAEEAELTRQKRQSYSTTNPTALGIGKASGALRQMHYIRDTTTRIRFDFLSLLAVDEDVRYSLNEMNAVAWNYVYVFAFVSSIICCATYLRLRHFFTTKKYI
Protein: T-complex protein 1 subunit beta (TCP-1-beta) (CCT-beta) (Chaperonin CCT2) (Q940P8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- T-complex protein 1 subunit alpha
- TCP-1/cpn60 chaperonin family protein
- T-complex protein 1 subunit zeta 1
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta 2
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- ATP binding protein
Sequence:
MPIDKIFKDDASEEKGERARMASFVGAMAISDLVKSTLGPKGMDKILQSTGRGHAVTVTNDGATILKSLHIDNPAAKVLVDISKVQDDEVGDGTTSVVVLAGELLREAEKLVASKIHPMTIIAGYRMASECARNALLKRVIDNKDNAEKFRSDLLKIAMTTLCSKILSQDKEHFAEMAVDAVFRLKGSTNLEAIQIIKKPGGSLKDSFLDEGFILDKKIGIGQPKRIENANILVANTAMDTDKVKIYGARVRVDSMTKVAEIEGAEKEKMKDKVKKIIGHGINCFVNRQLIYNFPEELFADAGILAIEHADFEGIERLGLVTGGEIASTFDNPESVKLGHCKLIEEIMIGEDKLIHFSGCEMGQACSIVLRGASHHVLDEAERSLHDALCVLSQTVNDTRVLLGGGWPEMVMAKEVDELARKTAGKKSHAIEAFSRALVAIPTTIADNAGLDSAELVAQLRAEHHTEGCNAGIDVITGAVGDMEERGIYEAFKVKQAVLLSATEASEMILRVDEIITCAPRRREDRM
Protein: Collagen alpha-1(XXIII) chain (Q8K4G2)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
Interaction partners:
- Collagen alpha-1
- Furin
Sequence:
MGAGERAAGGGGAQDPGAGCGSRALSALCLLLSVGSAAACLLLGAQAAALHGRVAALEQERELLRHAGPSGALAAWAETHLERLLREKLDGVAKLRTVREAPSECICPPGPPGRRGKPGRRGDPGPPGQSGRDGYPGPLGLDGKPGLPGPKGEKGTPGDFGPRGAQGQDGVAGPPGPPGPPGARGPPGDTGKDGPRGAQGPAGPRGEPGQDGEMGPKGPPGPKGEPGIPGKKGDDGMANQPGLPGPPGPKGEPGDVGPRGENGVDGIPGLKGEPGHPGVDGATGPRGAPGLKGEQGDTVVIDYDGRILDALKGPPGPQGAPGPPGIPGAKGELGLPGAPGIDGEKGPKGPKGDPGEPGPAGPKGETGEMGLSGLPGADGPKGEKGESASDHLQESLAQIIVEPGPPGPPGPPGPMGLQGIQGPKGLDGAKGEKGTSGERGPHGLPGPVGPPGLIGLPGTKGEKGRPGEPGLDGFPGPRGEKGDRSERGEKGERGVPGRKGVKGQKGEPGPPGLDQPCPVGPDGLPVPGCWHK
Protein: Wdr36 protein (Q505Q0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAEMESAVEGRTASVLFAGFRALGLFSNEVPHVVRYSALKRRFYVTTCVGKSFHTYDVQKLSLVAVSNSVPQDICCMAADGRLVFAAYGNVFSAFARNKEIVHTFKGHKAEIHLLQPFGDHVISVDTDSVLIIWHIYSEEEYLQLTFDKSVFKISTILHPSTYLNKVLLGSEQGSLQLWNIKSNKLLYTFPGWKVGVTALQQAPAVDVVAIGLVSGQVVIHNIKYDETLMKFHQDWGPITSISFRTDGHPIMAAGSPCGHIGLWDLEDKKLINQMRNAHSTAISGLTFLHREPLLVTNGADNALRIWIFDGPAGEGRLLRFRMGHSASLTKIRYYGQNGQQILSASQDGTLQSFSTVHEKFNKSLGHGLVNKKIVKRKGLQNTMSVRLPPITQFAAEEARQSDWDGIIACHQGKRSCSTWNYQRSTIGAYFLKPRGVKTNSNLTATAVDITSCGNFAIIGLSSGAVDVYNMQSGIHRGNFGDDKAHTGSVRGVAVDGLNQLVVTAGSERLLKFWNFKSKVLIHSLGLDSSPNMMLLHRDSGILGLAMDDFSIAVLDIETRKIVREFSGHHGQINDMTFSPDGRWLISAAMDCSVRTWDLPSGCLIDCFLLDSAPLNVTMSPTGDFLATSHVDHLGIYLWSNISLYSVVSLRPLPPDYVPSIVMLPGTCQTQGMEDLEEKTEPSDEMIEYESPEQLSEQLVTLSLLPESRWKNLLNLDVIKKKNKPKEPPKVPQSAPFFIPTVPGLVPRFAVPEPSSDPQQSKVVNLGILAQKSNFYLKLEEGLLNNQYEAALNLLKELGPSGIETELRNLSPDDGGSVEVMRSFLNMIGVMLDRKRDFELAQAYLALFLKLHLRTLPSEPVLLEELVKLSSQVEKDWTHLQSLFNQSMCVLNYIKSAFL
Protein: Vitamin D3 receptor (VDR) (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1) (O42392)
Organism: Gallus gallus (Chicken)
Function: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P11473, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus. Translocated into the nucleus via both ligand-dependent and ligand-independent pathways; ligand-independent nuclear translocation is mediated by IPO4. {ECO:0000250|UniProtKB:P11473}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 1
Sequence:
MSELRGSWDEQQQSMAYLPDADMDTVAASTSLPDPAGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKAMFTCPFNGDCKITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKESLKPKLSEEQQKVIDTLLEAHHKTFDTTYSDFNKFRPPVRSKFSSRMATHSSSVVSQDFSSEDSNDVFGSDAFAAFPEPMEPQMFSNLDLSEESDESPSMNIELPHLPMLPHLADLVSYSIQKVIGFAKMIPGFRDLTAEDQIALLKSSAIEVIMLRSNQSFTMEDMSWTCGSNDFKYKVSDVTQAGHSMDLLEPLVKFQVGLKKLNLHEEEHVLLMAICILSPDRPGVQDTSLVESIQDRLSDILQTYIRCRHPPPGSRLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPEHSMQLTPLVLEVFGNEIS
Protein: Succinyl-CoA:3-ketoacid coenzyme A transferase 2B, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 2B) (Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 2) (SCOT-t2) (Q9ESL0)
Organism: Mus musculus (Mouse)
Function: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). Probably play and important roles in the energy metabolism of spermatozoa.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Acetyl-CoA acetyltransferase, mitochondrial
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Acetyl-Coenzyme A acetyltransferase 3
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Acetoacetyl-CoA synthetase
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Dehydrogenase/reductase SDR family member 6
Sequence:
MAALRLLAWALPRGVSALRPRPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRACGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA
Protein: DNA-directed RNA polymerase I subunit rpa14 (RNA polymerase I subunit A14) (DNA-directed RNA polymerase I 17 kDa polypeptide) (Nucleolar protein ker1) (Q9P7P1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. A14 seems to play a role in the stability of Pol I subunit A43 and association of rrn3 to Pol I.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15647272}.
Interaction partners:
- DNA-directed RNA polymerase I subunit rpa43
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I and III subunit RPAC2
- Probable DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase I subunit RPA12
Sequence:
MATECPPKMILRKSEKLDKDASSKFLNRYIQTIERFQDEKSGSESVLSQLNRVLMYLKGEEIPLISLNLPVQGPPTEELIIPPEEMLETKEEESLKHAREENDDLHLDKETKKRLKKEKKKAARREKEEARKAKADTTQGVGEKEQS
Protein: Tumor protein p73 (A0A8I6APF4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.
Interaction partners:
Sequence:
MLYVGDPMRHLATAQFNLLSSAMDQMGSRAAPASPYTPEHAASAPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDIVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILVIITLETRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESTTKNGAASKRAFKQSPPAIPALGTNVKKRRHGDEDMFYMHVRGRENFEILMKVKESLELMELVPQPLVDSYRQQQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGVNKLPSVNQLVGQPPPHSSAAGPNLGSMGSGILNSHSHSMPANGEMNGGHSSQTMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIECFTSQGLQSIYHLQNLTIEDLGALKIPDQYRMTIWRGLQDLKQSHDCGQQLLRSSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGAGGVTGPDEWADFGFDLPDCKSRKQPIKEEFTETESH
Protein: Na(+)-translocating NADH-quinone reductase subunit C (Na(+)-NQR subunit C) (Na(+)-translocating NQR subunit C) (EC 7.2.1.1) (NQR complex subunit C) (NQR-1 subunit C) (A5F5Y7)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00427}.
Interaction partners:
Sequence:
MASNNDSIKKTLFVVIALSLVCSIIVSAAAVGLRDKQKENAALDKQSKILQVAGIEAKGSKQIVELFNKSIEPRLVDFNTGDFVEGDAANYDQRKAAKEASESIKLTAEQDKAKIQRRANVGVVYLVKDGDKTSKVILPVHGNGLWSMMYAFVAVETDGNTVSGLTYYEQGETPGLGGEVENPAWRAQWVGKKLFDENHKPAIKIVKGGAPQGSEHGVDGLSGATLTSNGVQNTFDFWLGDMGFGPFLTKVRDGGLN
Protein: Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (Q6FTK4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm {ECO:0000250|UniProtKB:P0C0W9}.
Interaction partners:
- Large ribosomal subunit protein uL1
- Ribosomal protein L15
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS12
- 60S ribosomal protein L20
- Candida glabrata strain CBS138 chromosome M complete sequence
- 40S ribosomal protein S27
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS28
Sequence:
MSAKTQNVMRELKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRNRNFSTTGNFGFGIQEHIDLGIKYDPSIGIFGMDFYIVMGRPGNRIARRKRCRATVGNSHKTSKEDTIAWFKQRYDADVLDK