wanglab/gogpt-training-data huggingface dataset:
Protein: Protein mss51 (Q9UTB4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a dual role in the assembly of cytochrome oxidase subunit 1 (cox1). It has a regulative function on cox1 synthesis, acting as a translational activator specific for the cox1 mRNA, and it also binds to newly synthesized cox1 protein (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase assembly factor 1
- Oxysterol-binding protein homolog C2F12.05c
- Mitochondrial cox1 translation regulator ppr4
- Uncharacterized membrane protein C757.15
- Cytochrome c oxidase subunit 2
- Pentatricopeptide repeat-containing protein 5
- Pentatricopeptide repeat-containing protein 6
- CBP3-like protein
- Cytochrome B pre-mRNA-processing protein 6
Sequence:
MSFLKNLFKKKSPTHELFHPLSRSPLTALRRRSEHIKQVYRCPISGKSVEYECPESGFPTHCNRTHWEQDKIHQSLIPKLRQINEDYHDLARPNPLPELLKLPGPMEEDEVVSLLSWDSFFYTRDFPKFQSSRTARHITSLLTYPMSIGAILHKNSPYNLKNGLTPQGLQSLTALRYMLHRPLSAQSTDPRPTRIFVLGATKECSLPPSIWLQGLNFLFPGRLFQLHFIGPEVVVPSKQPNLPSPLSLHFHQDYYHNLHRVGAFEPFDPYYDTFFLPMPLISHPLYSSSWIPTLHDLVSTRCSVWLTSPSSQRTTKDLEVLNNVLKDSIEPLLLPTVNKFASLGWSVDDSNLHEVYHANQEVFGFRALYYNVQNVSKE
Protein: Iron regulatory protein 1A (Q9NFX3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361275}.
Interaction partners:
Sequence:
MSGSGANPFAQFQESFTQDGNVYKYFDLPSIDSKYESLPFSIRVLLESAVRNCDNFHVLEKDVQSILGWTPSLKQETSDVEVSFKPARVILQDFTGVPAVVDFAAMRDAVRELGGNPEKINPICPADLVIDHSVQVDFVRSSDALTKNESLEFQRNKERFTFLKWGARAFDNMLIVPPGSGIVHQVNLEYLARVVFESDSSADGSKILYPDSVVGTDSHTTMINGLGVLGWGVGGIEAEAVMLGQSISMLLPEVIGYRLEGKLGPLATSTDLVLTITKHLRQLGVVGKFVEFYGPGVAELSIADRATISNMCPEYGATVGYFPIDENTLSYMRQTNRSEKKIDIIRKYLKATRQLRDYSLVDQDPQYTESVTLDLSTVVTSVSGPKRPHDRVSVSSMCEDFKSCLISPVGFKGFAIPPSALAASGEFQWDDGKSYKIGHGSVVIAAITSCTNTSNPSVMLGAGLLAKNAVQKGLSILPYIKTSLSPGSGVVTYYLRESGVIPYLEQLGFDIVGYGCMTCIGNSGPLDENVVNTIEKNGLVCCGVLSGNRNFEGRIHPNTRANYLASPLLVIAYAIAGRVDIDFEIEPLGVDANGKEVFLRDIWPTRSEIQEVEHKHVIPAMFQEVYSKIQLGSRDWQTLEVSDSKLYPWSEISTYIKLPPFFEGMTRALPKLKGIEKARCLLLLGDSVTTDHISPAGSIARKSPAARYLSERGLTPRDFNSYGSRRGNDAVMARGTFANIRLVNKLASKTGPSTLHVPSGEEMDIFDAAERYASEGTPLVLVVGKDYGSGSSRDWAAKGPFLLGIKAVIAESYERIHRSNLVGMGIIPLQFLPGQSADTLKLSGREVYNIVLPEGELKPGQRIQVDADGNVFETTLRFDTEVDITYYKNGGILNYMIRKMLD
Protein: Berberine bridge enzyme-like 24 (AtBBE-like 24) (EC 1.1.1.-) (Q9FKV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:O64743}.
Interaction partners:
- At5g60530/muf9_180
- FAD-dependent oxidoreductase domain-containing protein 1
- Late embryogenesis abundant
- Late embryogenesis abundant protein-related / LEA protein-like protein
- At5g54370 protein-like protein)
- NAD
- Peptide methionine sulfoxide reductase B9
- Peptide methionine sulfoxide reductase B8
Sequence:
MGNSKPLPTISCIIVSVLYFSFYCITPTSSSASIQDQFINCVKRNTHVSFPLEKTLFTPAKNVSLFNQVLESTAQNLQFLAKSMPKPGFIFRPIHQSQVQASIICSKKLGIHFRVRSGGHDFEALSYVSRIEKPFILLDLSKLKQINVDIESNSAWVQPGATLGELYYRIAEKSKIHGFPAGLCTSVGIGGYMTGGGYGTLMRKYGLAGDNVLDVKMVDANGKLLDRAAMGEDLFWAIRGGGGASFGIVLAWKIKLVPVPKTVTVFTVTKTLEQDARLKTISKWQQISSKIIEEIHIRVVLRAAGNDGNKTVTMTYLGQFLGEKGTLLKVMEKAFPELGLTQKDCTEMSWIEAALFHGGFPTGSPIEILLQLKSPLGKDYFKATSDFVKEPIPVIGLKGIFKRLIEGNTTFLNWTPYGGMMSKIPESAIPFPHRNGTLFKILYYANWLENDKTSSRKINWIKEIYNYMAPYVSSNPRQAYVNYRDLDFGQNKNNAKVNFIEAKIWGPKYFKGNFDRLVKIKTKVDPENFFRHEQSIPPMPY
Protein: RING/U-box superfamily protein (Q9FFT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKNSYKHELISTSTNETDRVINRCFLRKKTTKEVIHLKASQVESDSYSFIVTYQPNLRIRHENLDGHQLKTTLERHPDRVFKLEDNIPKQFLVSQETCLEHVMIILSAMYLPQTIQERLVRYISTESVKFRNRRCGTGGGLKVEVDVKVDVEQWVRIDCCCKQKGTCLVPALDCPICLTELSSGVSRMKLPCSHVFHRDCIMTWLKKNPSCPICRTKAHGKTVSIY
Protein: Isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS) (P00956)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
Subcellular location: Cytoplasm.
Interaction partners:
- Proline--tRNA ligase
- Arginine--tRNA ligase
- Lysine--tRNA ligase, heat inducible
- Lysine--tRNA ligase
- Leucine--tRNA ligase
- Glutamine--tRNA ligase
- Glutamate--tRNA ligase
- Asparagine--tRNA ligase
- Lipoprotein signal peptidase
- Serine--tRNA ligase
Sequence:
MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA
Protein: Contactin-4 (Brain-derived immunoglobulin superfamily protein 2) (BIG-2) (Q62845)
Organism: Rattus norvegicus (Rat)
Function: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity. May be involved in synaptogenesis.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Secreted {ECO:0000269|PubMed:16806532}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase gamma
- Amyloid-beta precursor protein
- Neuroligin-1
- Receptor-type tyrosine-protein phosphatase zeta
- Neurexin-3
Sequence:
MRLPWELLVLQSFMLCLADDYTLHGPVFVQEPSHVMFPLDSEEKKVKLSCEVKGNPKPHIRWKLNGTDVDIGMDFRYSVVEGSLLINNPNKTQDSGTYQCIATNSFGTIVSREAKLQFAYLENFKTRTRSTVSVRRGQGMVLLCGPPPHSGELSYAWIFNEHPSYQDNRRFVSQETGNLYIAKVEKADVGNYTCVVTNTVTSHQVLGPPTPLILRNDGVMGEYEPKIEVQFPETVPAEKGSTVKLECFALGNPVPTILWRRADGKPIARKARRHKSSGILEIPNFQQEDAGSYECVAENSRGKNIAKGQVTFYAQPNWVQIINDIHVAMEESVFWECKANGRPKPTYRWLKNGDPLLTRERIQIEQGTLNITIVNLSDAGMYQCVAENKHGVIYASAELSVIAESPDFSRTLLKRVTLVKVGGEVVIECKPKASPRPVYTWRKGREILRENERITISEDGNLRIINVTKSDAGSYTCIATNHFGTASSTGNVVVKDPTKVMVPPSSMDVTVGESIVLPCQVTHDHSLDIVFTWTFNGHLIDFDKDGDHFERVGGQDSAGDLMIRNIQLKHAGKYVCMVQTSVDKLSAAADLIVRGPPGPPEAVTIDEITDTTAQLSWRPGPDNHSPITMYVIQARTPFSVGWQAVSTVPELVDGKTFTATVVGLNPWVEYEFRTVAANVIGIGEPSRPSEKRRTEEALPEVTPANVSGGGGSKSELVITWETVPEELQNGRGFGYVVAFRPHGKMIWMLTVLASADASRYVFRNESVRPFSPFEVKVGVFNNKGEGPFSPTTLVYSAEEEPTKPPASIFARSLSATDIEVFWASPIGKNRGRIQGYEVKYWRHDDKEENARKIRTVGNQTSTKITNLKGNALYHLSVKAYNSAGTGPSSAAVNVTTRKPPPSQPPGNIIWNSSDSKIILNWDQVKALDNESEVKGYKVLYRWNRQSSTSVIETNKTSVELSLPFDEDYIIEIKPFSDGGDGSSSEQIRIPKISNSYARGSGASTSNACTLSAISTIMISLTARSSL
Protein: Loechrig isoform II (Loechrig isoform V) (Loechrig isoform VII) (Q8I0B2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHGITHLYRQHAVEKQLSGGESWSRQIYPSYGSSADASSQGSRLYSVDSSSSSSSNSNNSGGGGSGTAGVENLGGVTGSAYAQWQSDRHSLPQAVPDAPRSLANHHYRNSPTHQAHYQQPTSGSLKRTPSSKRSFLERSHSPAIYGSMRRSAGPDFGSPPPTAPVGGGGYFPHDLDDIYESQTDHQYFTHTGASGPQQQRPTAISIFHRVSAAHTSLDDYTLPGDASRQSMNSTDSGVSSGPFNRQRFDNSSFAKSLSIDEQDPQHSPHKEGHSKHGKHHHHHSHHHHSIHELVKHFGKKMHLWPRKHHDAQSVCTSPQNDPQENFRTRSKSLDVNTLSRPNRILDDCGATYKIYDRIVKESAHMRRASADLEKRRASVGAAGRGLRGDGTLDPHHAAILFRDSRGLPVADPFLEKVNLSDLEEDDSQIFVKFFRFHKCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDTWRDVLHNQVMPLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGVGGSESSLRASDPVLLRKVAEVEIPATAAAATTTTPPRSPSAGSGNRSLIEDIPEEETAPARSDDADSDNNKSASEDKANNNQHDQTTTAATANGDSNNSPVEVSFADEAQEEEAADQVERSNCDDDDQPALAEIERKNASMDDDEDDGMSSAVSAASALGQSLTPAAQEMALVSE
Protein: DNA-directed RNA polymerase III subunit RPC9 (Q7K1S9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQILQKIKSTKKKFGMRNLATVTYEALQYLEESPCKTQTRENIMNYVKDLSSYRLKSQEILQMINDPPTSALHTQLLIDDNKAPLTDEENEKIIQLSYKHFHGGETKGAAKETPAEKPAESTAKAGKQSGVKRNAQAKSNPAEQIAPADKTTPGDGVTPANVATPSSEATTTTPAEEASPVETSSSENNATPANEATTAPATDAPTSMETKSNPTPDGENLG
Protein: Pollen receptor-like kinase 5 (AtPRK5) (EC 2.7.11.1) (Q9LPT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth. The extracellular domain serves as a sensor for peptides derived from GRI. May act as a downstream element for ROS-dependent cell death induced by GRI.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25398910}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Protein GRIM REAPER
- Rho guanine nucleotide exchange factor 8
- Rop guanine nucleotide exchange factor 12
- Protein LURE 1.4
- Protein LURE 1.3
- Protein NETWORKED 2A
- Metacaspase-9
- Protein LURE 1.1
Sequence:
MRNWEDPFTLACNTALKKNLPSCIFIIIFISVLCPVAMSQVVVPDSDADCLLRFKDTLANGSEFRSWDPLSSPCQGNTANWFGVLCSNYVWGLQLEGMGLTGKLNLDPLVPMKNLRTISFMNNNFNGPMPQVKRFTSLKSLYLSNNRFSGEIPADAFLGMPLLKKILLANNAFRGTIPSSLASLPMLLELRLNGNQFQGQIPSFQQKDLKLASFENNDLDGPIPESLRNMDPGSFAGNKGLCDAPLSPCSSSSPGVPVVPVSPVDPKSTSPPTGKKAGSFYTLAIILIVIGIILVIIALVFCFVQSRRRNFLSAYPSSAGKERIESYNYHQSTNKNNKPAESVNHTRRGSMPDPGGRLLFVRDDIQRFDLQDLLRASAEVLGSGTFGASYKAAISSGQTLVVKRYKHMNNVGRDEFHEHMRRLGRLNHPNILPLVAYYYRREEKLLVTEFMPNSSLASHLHANNSAGLDWITRLKIIKGVAKGLSYLFDELPTLTIPHGHMKSSNIVLDDSFEPLLTDYALRPMMSSEHAHNFMTAYKSPEYRPSKGQIITKKTDVWCFGVLILEVLTGRFPENYLTQGYDSNMSLVTWVNDMVKEKKTGDVFDKEMKGKKNCKAEMINLLKIGLRCCEEEEERRMDMREVVEMVEMLREGESEDDFGSMDHRGTHNNVYSSMLLDDDDFGFSMNR
Protein: Interferon regulatory factor 3 (M0QYX3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSEN
Protein: Cadherin-22 (Pituitary and brain cadherin) (PB-cadherin) (Q63315)
Organism: Rattus norvegicus (Rat)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. PB-cadherins may have a role in the morphological organization of pituitary gland and brain tissues.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
Sequence:
MRPRPAGALRAGAALSPVLLLLLLLQLLGHLWAASTPAPSSLSPGTQQDNQLGAGRVKRGWVWNQFFVVEEYTGTEPLYVGKIHSDSDEGDGTIKYTISGEGAGTIFLIDELTGDIHATERLDREQKTFYTLRAQARDRATNRLLEPESEFIIKVQDINDSEPRFLHGPYIGSVAELSPTGTSVMQVMASDADDPTYGSSARLVYSVLDGEHHFTVDPKTGVIRTAVPDLDRESQERYEVVIQATDMAGQLGGLSGSTTVTIVVTDVNDNPPRFPQKMYQFSIQESAPIGTAVGRVKAEDSDVGENTDMTYHLREESGSGGDAFKVTTDSDTQEAIIVVQKHLDFESQQVHTVVLEALNKFVDPRFADLGTFRDQAIVRVAVTDVDEPPEFRPPSGLLEVQEDAQVGSLVGVVTARDPDAANRPVRYAIDRDSDLEQIFDIDADTGAIVTGKGLDRETAGWHNITVLAMEADNHAQLSRASLRIRILDVNDNPPELATPYEAAVCEDAKPGQLIQTISVVDRDEPQGGHRFYFRLVPEEPSNPHFSLLDIEDNTAAVHTQHVGFNRQEQDVFLLPILVVDSGPPTLSSTGTLTIRICGCDSSGTIQSCNTTAFVMAASLSPGALIALLVCVLILVVLALLILTLRRHHKSHLSSDVDEDMRDNVIKYNDEGGGEQDTEAYDMSALRSLYDFGELKGGDPGGGAASPPQAASSSERHSLPRGPSSPEPDFSVFRDFISRKVALADADLSVPPYDAFQTYAFEGAGSPAASLSSLHSGSTGSEQDFAFLRAWGPRFRPLAALYAGHRGDDEAPAS
Protein: Vesicular inhibitory amino acid transporter (GABA and glycine transporter) (Solute carrier family 32 member 1) (Vesicular GABA transporter) (rGVAT) (rat UNC-47 homolog) (RUNC-47) (O35458)
Organism: Rattus norvegicus (Rat)
Function: Antiporter that exchanges vesicular protons for cytosolic 4-aminobutanoate or to a lesser extend glycine, thus allowing their secretion from nerve terminals (By similarity). The transport is equally dependent on the chemical and electrical components of the proton gradient. May also transport beta-alanine. Acidification of GABAergic synaptic vesicles is a prerequisite for 4-aminobutanoate uptake (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10036231, ECO:0000269|PubMed:9822734}; Multi-pass membrane protein {ECO:0000255}. Presynapse {ECO:0000269|PubMed:10036231}. Note=Presents in glycine-, GABA- or GABA- and glycine-containing boutons. {ECO:0000269|PubMed:10036231}.
Interaction partners:
- Vesicular glutamate transporter 1
- Vesicular glutamate transporter 2
- Vesicular acetylcholine transporter
- Vesicular glutamate transporter 3
- Glutamate decarboxylase 2
- Synaptic vesicular amine transporter
- Chromaffin granule amine transporter
- Glutamate decarboxylase 1
- Gephyrin
- Synaptotagmin-1
Sequence:
MATLLRSKLTNVATSVSNKSQAKVSGMFARMGFQAATDEEAVGFAHCDDLDFEHRQGLQMDILKSEGEPCGDEGAEPPVEGDIHYQRGGAPLPPSGSKDQAVGAGGEFGGHDKPKITAWEAGWNVTNAIQGMFVLGLPYAILHGGYLGLFLIIFAAVVCCYTGKILIACLYEENEDGEVVRVRDSYVAIANACCAPRFPTLGGRVVNVAQIIELVMTCILYVVVSGNLMYNSFPGLPVSQKSWSIIATAVLLPCAFLKNLKAVSKFSLLCTLAHFVINILVIAYCLSRARDWAWEKVKFYIDVKKFPISIGIIVFSYTSQIFLPSLEGNMQQPSEFHCMMNWTHIAACVLKGLFALVAYLTWADETKEVITDNLPGSIRAVVNIFLVAKALLSYPLPFFAAVEVLEKSLFQEGSRAFFPACYGGDGRLKSWGLTLRCALVVFTLLMAIYVPHFALLMGLTGSLTGAGLCFLLPSLFHLRLLWRKLLWHQVFFDVAIFVIGGICSVSGFVHSLEGLIEAYRTNAED
Protein: ATP synthase subunit alpha, mitochondrial (Protein bellwether) (P35381)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- Protein stunted
- ATP synthase-coupling factor 6, mitochondrial
- ATPase protein 9
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit g
- ATP synthase subunit O, mitochondrial
- ATP synthase F
- ATP synthase subunit a
- Putative ATP synthase subunit f
- ATP synthase subunit d, mitochondrial
Sequence:
MSIFSARLASSVARNLPKAANQVACKAAYPAASLAARKLHVASTQRSAEISNILEERILGVAPKADLEETGRVLSIGDGIARVYGLNNIQADEMVEFSSGLKGMALNLEPDNVGVVVFGNDKLIKQGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGAINTKDRFRVGIKAPGIIPRVSVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTALAIDTIINQKRFNEAQDESKKLYCIYVAIGQKRSTVAQIVKRLTDSGAMGYSVIVSATASDAAPLQYLAPYSGCAMGEYFRDKGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSPAMGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTKAMKQVAGSMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYVPMAIEDQVAVIYCGVRGHLDKMDPAKITKFEKEFLQHIKTSEQALLDTIAKDGAISEASDAKLKDIVAKFMSTFQG
Protein: V-type proton ATPase subunit C 2 (V-ATPase subunit C 2) (Vacuolar proton pump subunit C 2) (Q99L60)
Organism: Mus musculus (Mouse)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity (By similarity).
Interaction partners:
- V-type proton ATPase subunit H
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E 2
- V-type proton ATPase subunit F
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit d 2
- V-type proton ATPase 116 kDa subunit a 4
Sequence:
MSEFWLISAPGDKENLQALERMNNVTSKSNLSHNTKFAIPDFKVGTLDSLVGLSDELGKLDTFAESLIKRMAQSVVEVMEDSKGKAHETLLANGVDLTSFVTHFEWDMAKYPAKQPLVSVVDTLAKQLAQIETDLKSRTAAYSVLKANLENLEKRSTGNLFTRTLSDIVSKEDFVLDSEYLITLLVIVPKSSFAQWQKTYESLSDMVVPRSTKLIAEDNEGGLFTVTLFRKVIEDFKVKAKENKFIVREFYYDEKEIKREREEMTRLLSDKKQQYPTSCVALKKGSATYRDHKVKVAPLGNPARPAAGQTDRDRESEGEGEGPLLRWLKVNFSEAFIAWIHIKALRVFVESVLRYGLPVNFQAVLLQPHKKSATKRLREVLNSVFRHLDEVAAASILDASVEIPGLQLSNQDYFPYVYFHIDLSLLD
Protein: Prolyl hydroxylase EGLN3 (EC 1.14.11.-) (Egl nine homolog 3) (EC 1.14.11.29) (HPH-1) (Hypoxia-inducible factor prolyl hydroxylase 3) (HIF-PH3) (HIF-prolyl hydroxylase 3) (HPH-3) (Prolyl hydroxylase domain-containing protein 3) (PHD3) (Q9H6Z9)
Organism: Homo sapiens (Human)
Function: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A. Target proteins are preferentially recognized via a LXXLAP motif. Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia. Also hydroxylates PKM in hypoxia, limiting glycolysis. Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis. In cardiomyocytes, inhibits the anti-apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex. In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity. Also essential for hypoxic regulation of neutrophilic inflammation. Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway. Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (Probable).
Subcellular location: Nucleus {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:12615973}. Cytoplasm {ECO:0000269|PubMed:12615973}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250|UniProtKB:Q62630}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- E3 ubiquitin-protein ligase SIAH2
- Prolyl hydroxylase EGLN2
- Egl nine homolog 1
- WD repeat domain-containing protein 83
- von Hippel-Lindau disease tumor suppressor
- Hypoxia-inducible factor 3-alpha
- Aryl hydrocarbon receptor nuclear translocator
- Protein kinase C beta type
Sequence:
MPLGHIMRLDLEKIALEYIVPCLHEVGFCYLDNFLGEVVGDCVLERVKQLHCTGALRDGQLAGPRAGVSKRHLRGDQITWIGGNEEGCEAISFLLSLIDRLVLYCGSRLGKYYVKERSKAMVACYPGNGTGYVRHVDNPNGDGRCITCIYYLNKNWDAKLHGGILRIFPEGKSFIADVEPIFDRLLFFWSDRRNPHEVQPSYATRYAMTVWYFDAEERAEAKKKFRNLTRKTESALTED
Protein: Peptidase A22B family protein (Q54CN9)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MEAVIESFKNLKMDLTIPDNGLLIAYISIWIMAIVPIYIGSFLSLKETKSESMSMSDAYTFPIIGSVFLFGLYLCFKYFDKDLINLILSYYFLLIGAIAMTNVLSSLFKYMFVGSSGSGKNKKQNEVKPLISFKIPAIKFITDAKDVKIDIYDIVSFIFAIGFSLWYIKTKHWIANNIFGLTFSIQGISFISLTEYSVGVMLLVGLFFYDIFWVFGTDVMVTVAKSFDAPIKLLFPKDIFADVYQFSMLGLGDIVLPGIFIALLLRFDRHIHQESRSKGPMKKTYFNSTLIAYALGLFTTIFVMHTFKAAQPALLYLVPFCVGSSMIVSAIKGQFKKLLWSNLDTAKDNTKKTN
Protein: Nucleolar pre-ribosomal-associated protein 1 C-terminal domain-containing protein (Q385P3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALVEPLVGHLLSKHNDTVIEGLSKIKKNATDNEGFSTEFLLHPQGFAALQNALYKQELAAPVLQAMAELVKSCNNAGVRSFVLREMCRGPCFSVLRHALSVLSDATLPTTIAALQFASVAAVYTPKVLLSRFGNVVPFHFACFRPQLPYSQRRIRLARAKFLIDLVISSRADVAESVLCMHGFLTHLLEDAGELLQEGTETGVEVAQTALQVFGKRFIDSRIPPAKKRSVLLAQKHTLRLLVKALGHSLVSESVLHILYRTVTELMESPMDFQLMHVDEEDKGMPNRLLFFILKRLRPRNTPAAARLLIFILHQAPGLIRPYFTRASSHLEEESGNGRVSASIGTISTMNVITRAMLAPIPYHLAAGKAKLEPVEARATTFFTMSPAHVAEEVCPPWVAEYVHRMINGSTDLLMLSFALQMTYAILTRAKTVLGLVVKLQEKQGRIEDEESVESENEDNECDWDAYNAKVQSALLKTVPSWEEFWHRMTQQLHHMMLPPGRSPQEENNGWKPDGKVMFLSQRMFLLMELYSEVFHLRIPWLSALPTRLPVFRPCDQPIVDALRRGEVVVSRWPAPGIAALCSLLVSSLSRGVSMTKMHHITMSSPTGGVQEWPLLLNVVAWAIKHRDEPSEEIQFALAWVARLLQWTVHSVTVRFVCELEEAYLWLSVLNEATLPCFLHMINNLLQRSLSKTADRVTQELAHGEHGVLVNAARTFAAKFDAKTSGKDDGGGENDIKFLKSDDSGGVKREKNKRDGKKFVKDLWVLDMQENMALFKLVIDRVERKWCNRVDLMREHLHSVFTVCHEEHGKRRIALTVLQAEREQRALQPLHDQVIGFCRTLTPPTLVVDTEEAEVQLLSFIRDCDVREGRQRAKLIRRLSKHSSPTLWCRYPTVCWELSALFLVRIKTRSGERDNDAMSETTEVSDLEDLSQALLQLVGGEIGDITKVLLENSSNEGNAVAFLFLLLVTVWTLLKEHSSVSHYRSSTRTTIDVNLFAPLSVLLLRTYSGTLSMVDRIRYCTLLSMNYFLRAQSQSNPLVPDGNDPMDLESTPEESDKSEEADDEGCCGDSRCYDNSAVFSGIDVLQFLTEHRFLIMDHQRAPQVTPEVDMLSLLVDAWTHEEVATAALQCPVRLHNNILLSRRGDVGWELLRTVFPEFNTPKDVELASFDTVVSANVMDPRYLVPLLHTVLAMPAEQLPRRNVGTKCIPVLLRSLSFTDSHLRRMGAAALGSVWTPSGPTRIVVGYTRLKLTQLAAKRERQSGSGSRLERQQQTETSAEWNCPLLPTPISAFLVMAMAVLGDARHPMYHDVMHFLLATKAAFSDPVPLHRFLLSFPLACITTPIMIKRHEDMRNKADKSSMVAASAEGLLDQLRSEGPIHLEFVTRLVAHGCQTCSDMKAILHSESLYSLTMLISMLAAADDIRLMMLRSVHAICTTSTTVGIMAVSDGHILQWLLGFIQQLTAEYGKDVHSYGGVLFMEALCFLQKLASLAFMLPLYGQHVRQQVCIIRRALTVNGVTTKAVLDAVDTVAGQLDGEAELTASGASMLQGRRRKVPFRGPTNGHNNSRTSRGGYGSRSGNRRRR