wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD) (F8W5E2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MSSTLWSQEKPGGSFRDDWRFYIVVKECTVERPGQKTLRIPRGSLGQACQERNSLGRTIPASKGKRSLRILDQTNVVVSVDERDVMELEEKLAELLFPITNCEERYSLLCNRSRLDRARDINCGSKVRVQLRSGDEPLPGVVRFKGALLPDRALSGIWFGVELLEEGRGQGFTEGSYQGQQLFRCEDECGVFVALDKLELWEDEELEVDRVTLEDNDPEEEGEAPPLEINSRVLVQTREGPERGTVIFCDLLPGNESLGYYVGVDMDNPIGDWDGIIDGKQLCNFASLEHTRLVPICDVMPEYSMQDQRLPKVFACRGGNDKPVSQSKPKSKVGEDPAKSLTDMPPDFNPSSSPSRAPPTTTSLSNDNKFHSLPFSLSRKVGPNGSMSHGPLSLSAGSVMGEQPELLPAATPLQRASSPPQGQPGLEVGSMVEVKENPPLCGVIRWVGLPPGLQESLAGLELEEECVGCTDGTFKGIRYFTCPPKKALFVKLKCCRPDSRFPSLHHSPNPIERCNSIAFGGYLSEVVNENTPPRTENDGLEVMVGKKKGIQGHYNSCYLDSTLFCLFSFSSVLDTVLLRPRSKTDVEYYKETQELLRTEIVNPLRIHGYVCATKIMKLRRILEKVEAASGFTSEEKDPEEFLNILFHHILRVDPLLRLRSAGQKVQDCYFYQIFMDKKDKVMVPTSQQLLEWSFINSDLKFAEAPSCLIIQMPRFGKDFKMFNKIFPSLELDITDLLDDTPRECRICGGLALYECRECYEDYDITPGKIKQFCEKCNTQVHLHPRRKIHRYVKLSVPKELHESVWRQGSYPHQQMELFAVLCIETSHYVAFVKYGSADSAWLFFDSMADRDGGQNGFNIPQVSRCPEVGEYLKMTPEELHALDPKNIQGYARRLLCDAYMCMYQSPTMSLYK
Protein: Toxic protein HokB (P77494)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration. Expression leads to membrane depolarization; when protein levels are high enough depolarization probably leads to lowered metabolic activity which in turn induces some cells to enter the persistent state in which they transiently survive antibiotic exposure. Its toxic effect is probably neutralized by antisense antitoxin RNA SokB, which is encoded in trans on the opposite DNA strand.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P0ACG4, ECO:0000305|PubMed:26051177}; Single-pass membrane protein {ECO:0000250|UniProtKB:P0ACG4}.
Interaction partners:
- Regulatory protein MokB
- Small toxic protein TisB
- Toxic protein HokE
- Toxic protein HokD
- Protein HokA
- Toxin GhoT
- Uncharacterized protein DinQ
- tRNA-specific adenosine deaminase
Sequence:
MKHNPLVVCLLIICITILTFTLLTRQTLYELRFRDGDKEVAALMACTSR
Protein: Ras-related protein Rab-7a (EC 3.6.5.2) (P36411)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (By similarity). Involved in lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}.
Interaction partners:
- Ras-related protein RabO
- Ras-related protein Rab-7B
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin beta chain
- Dynein heavy chain, cytoplasmic
- Cytoplasmic dynein 1 intermediate chain
- Cytoplasmic dynein 1 light intermediate chain 1
- RabGAP/TBC domain-containing protein
- Rab-GAP TBC domain-containing protein
Sequence:
MATKKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKELMVDDRVVTMQIWDTAGQERFQSLGVAFYRGADCCVLCYDVNVAKTFENLDSWRDEFLIQAGPRDPDNFPFVVLGNKIDLENQRVVSQKRAASWCQSKGNIPYFETSAKEAINVEQAFQTIARNAIKLEDGLVFPIPTNIQVIPEPQPAKSGCC
Protein: Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating RapGAP domain-like 1) (Tuberin-like protein 1) (p240) (Q6GYP7)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB (By similarity). May interact with the HLH region of TCF3/isoform E12.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12200424}. Nucleus {ECO:0000269|PubMed:12200424}. Note=Translocated to the nucleus, when associated with TCF3/E12.
Interaction partners:
Sequence:
MFSKKPHGDVKKSTQKVLDTKKDALTRLKHLRIVIENAESIDLKQFFDQHFSHIYYVFFENFVTIEASLKQKGHKSQREELDAILFIFEKILQLLPERIHQRWQFHSIGLILKKLLHTGNSLKIRREGVRLFLLWLQALQDNCSKEQLWMFSCLIPGFSAPQSEYGPRTLDNLINPPLSLQETQVTIEEVTPLVPPQSGDKGQEDLTSYFLEALLKYIVIQVKSLEWKNKENQERGFSFLFSHFKKFYLPYIFPNICKENSLYHPVLDIPQIRPKPHYVMIKKDAETNETIYCTKEPFIQARVIVIRWLVSFWLEPKPHSGPNIPGMEGEVLPKNIQRAAASLVSREESKNDTVDKVDKSAEPEQSHSNTSTLTEREPSSSSLCSIDEEHLTDIEIVRRVFSSKRSNVNFVTEIFRQAFLLPICEAAAMRKVVKVYQEWIQQEEKPLFMQEPEDTAITCSDIPCSETVADHDSAIEDGEKREEENGTSTSEHVRNSSWTKNGSYQEAFHVCEEATEQNIQAGTQAVLQVFIINSSNIFLLEPANEIKNLLDEHTDMCKRILNIYRYMVVQVSMDKKTWEQMLLVLLRVTESVLKMSSQAFLQFQGKKSMTLAGRLAGPLFQTLIVAWIKANLNVYISRELWDDLLSVLSSLTYWEELATEWSLTMETLTKVLARNLYSLDLSDLPLDKLSEQKQKKHKGKGVGHEFQKVSVDKSFSRGWSRDQPGQAPMRQRSATTTGSPGTEKARSIVRQKTVDIDDAQILPRSTRVRHFSQSEDTGNEVFGALHEEQPLPRSSSTSDILEPFTVERAKVNKEDTSPKLPPLNSETGGNSANVPDLMDEFIAERLRSGNASTMTRRGSSPGSLEIPKDLPDILNKQNQMRPVDDPGVPSEWTSPASAGSSDLMSSDSHSDSFSAFQCEGRKFDNFGFGTDIGIPSSADVDLGSGHHQSTEEQEVASLTTLHLDSETSSLNQQAFSAEVATVTGSESASPVHSALGSRSQTPSPSTLSRAHIEQKDLQLDEKLHHSVLQTPDDLEISEFPSECCSVMAGGTLTGWHADVATVMWRRMLGILGDVNAIMDPEIHAQVFDYLCELWQNLAKIRDNLGISADNLTSPSPPVLIPPLRILTPWLFKATMLTDKYKQGKLHAYKLICNTMKRRQDVSPNRDFLTHFYNIMHCGLLHIDQDIVNTIIKHCSPQFFSLGLPGATMLIMDFIIAAGRVASSAFLNAPRVEAQVLLGSLVCFPNLYCELPALHPNIPDIAVSQFTDVKELIIKTVLSSARDEPSGPARCVALCSLGIWICEELVHESHHPQIKEALNVICVSLKFTNKTVAHVACNMLHMLVHYVPRLQIHQPQSPLKIIQILIATITHLLPSTEASSYEMDKRLVVSLLLCLLDWIMALPLKTLLQPVHATGAENDKTEKSVLNCIYKVLHGCVYGAQSFSNPKYFPISLSDLASVDYDPFMHLESLKEPEPLHSPDSERSSKLQPVTEVKTQMQQGLISIAARTVITHLVNHLGHYPMSGGPAMLTSQVCENHDNHYSESTELSPELFESPNIQFFVLNNTTLVSCIQIRSEESMPGGGLAAGLVSANSNVRIIVRDLSGKYSWDSAILYGPPIVSGLPEPTSFILSMSDQEKPEEPPTSNECLEDIAVKDGLSLQLRRFRETVPTWSTIREEEDVLDELLQYLGTTSPECLQRTGISLNVPAPQPLCISEKQENDVINAILKQYTEEKEFVEKHFNDLNMKASEQDEPTPQKPQSAFYYCRLLLSILGMNSWDKRRSFHLLKKNEKLLRELRNLDSRQCRETHKIAVFYVAEGQEDKYSILTNIGGSQAYEDFVAGLGWEVNLTNHCGFMGGLQKNRSTGLTTPYFATSTVEVIFHVSTRMPSDSDDSLTKKLRHLGNDEVHIVWSEHTRDYRRGIIPTEFGDVLIVIYPMKNHMFSIQIMKKPEVPFFGPLFDGAIVNGKVLPIMVRSTAINASRALKSLIPLYQNFYEERARYLQTIVQHHLEPTTFEDFAAQVFSPAPYHHFPADADH
Protein: Ino2p (A0A1D8PRK8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mlc1p
- Calmodulin
- Ino4p
- VASt domain-containing protein
- VASt domain-containing protein
Sequence:
MSSTVTQTMNNNPTEKVTFTASNSQADFDLLDIFSNDMDFEQAYDMYNNLQEKNAMGSFEQLQKVQALNQQYVSNLQPPSSAQFPDQFAYERAQILNGEYNKQSGLMNDATNKNYSFNDDTFDQFFTNTESNALEKFLDNLANPVASVNPLQFYNNTRTSVPDEDVDLSFELHTMKVPQQFKPRSQSLEHNPPLQQKVRFTEEEHAALKQELTEAFAHPCTQLPSPSTTEYKPKPTTPKVVKQFVTPPNSGDESRKRNSDIESDESEEETTPTTKKRKRTSSKPLLSVEQKRLNHSHSEQKRRQLCKFAYQRCLELIIDLDAFNKLPELNESERKSKRARVNKDGLPNLSKHNALIRISNEMILIKSMNDSLKKLIENR
Protein: E3 ubiquitin-protein ligase PRT1 (EC 2.3.2.27) (Proteolysis 1 protein) (RING-type E3 ubiquitin transferase PRT1) (Q8LBL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. Functions in the N-end rule pathway of protein degradation, where it specifically recognizes and ubiquitinates proteins with a N-terminal bulky aromatic amino acid (Phe). Does not act on aliphatic hydrophobic and basic N-terminal residues (Arg or Leu) containing proteins.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31x fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Cullin-like protein 3
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- Cullin-2
- Cullin-3A
Sequence:
MAETMKDITMKNDESQEEEIPDQFLCCVCLELLYKPIVLSCGHLSCFWCVHKSMNGFRESHCPICRDPYVHFPSVCQKLYFLLKKMYPLAHKKREEQVLKEEQERECFSPQIDLVLDLSVCSGDSLNVSDKQKVEECSNAANLLSSSSSRGDIPCIPKNQEPTDAKALNVHENELLKDNKVSKQISKDDLLCSACKELLVRPVVLNCGHVYCEGCVVDMAEESEKIKCQECNVCDPRGFPKVCLILEQLLEENFPEEYNSRSSKVQKTLAHNSKGNIQSYLKEGPSLSNDNNNDDPWLANPGSNVHFGAGCDSCGVYPIIGDRYRCKDCKEEIGYDLCKDCYETPSKVPGRFNQQHTPDHRLELARSPQVLINFNSIGILLGPVISNEGMDTDEGEEGPPGSSNESSSTE
Protein: Bcl-2-modifying factor (Q8K589)
Organism: Rattus norvegicus (Rat)
Function: May play a role in apoptosis.
Interaction partners:
- Bcl-2-related protein A1
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Bcl-2-like protein 2
- Dynein light chain 2, cytoplasmic
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-like protein 11
- Mitogen-activated protein kinase 8
- Dynein light chain
- Dynein light chain
Sequence:
MEPPQCVEELEDDVFQPEDGEPGTQPGSLLSADLFAQSQLDCPLSRLQLFPLTHCCGPGLRPVSQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAGSALGEQPPEGQFLQHRAEVQIARKLQCIADQFHRLHMQQHQQNRDRAWRQVFLFLQNLALNRRENREGVGPW
Protein: Nuclear prelamin A recognition factor (J3KT43)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKCEHCTRKECSKKTKTDDQENVSADAPSPAQENGEKGEFHKLADAKIFLSDCLACDSCMTAEEGVQLSQQNAKDFFRVLNLNKKCDTSKHKVLVVSVCPQSLPYFAAKFNLSVTDASRRLCGFLKSLGWVRYAERVLGRPITAHLCTAKSPQQVMGSLVKDYFARQQNLSPEKIFHVIVAPCYDKKLEALQESLPPALHGSRGADCVLTSGEIAQIMEQGDLSVRDAAVDTLFGDLKEDKVTRHDGASSDGHLAHIFRHAA
Protein: Laminin subunit gamma 1 (F1MD77)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Laminin subunit beta-1
- Integrin alpha-6
- Laminin subunit alpha-2
- Uncharacterized protein.
- Integrin beta-1
- Nidogen-1
- Laminin subunit alpha-5
- Integrin alpha-5
- Integrin alpha-3
- Laminin subunit alpha-4
Sequence:
MRGSDRAAAALRPRGRVWPVLVVLAAAAAGCARAAMDECTDEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQPHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPNSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKATRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNDPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEFDKLVCNCKHNTYGVDCEKCLPFFNDRPWRRATAESASECQPCDCNGRSQECYFDPELYRSTGHGGHCTNCQDNTDGAKCERCRENFFRLGNREACSPCHCSPVGSLSTQCDSYGRCSCKPGVMGDKCDRCQPGYHSLTEAGCRPCSCNPSGSIDECNIETGRCVCKDNVEGFNCERCKPGFFNLESSNPRGCTPCFCFGHSSVCTNAVGYSVYSITSTFETDEDGWRAEQRDGSEASFEWSSERQDIAVISDSYFPRYFIAPAKFLGKQVLSYGQNFSFSFRVDRRDTRLSAEDLVLEGAGMRVSVPLIAQGNSYPSETTVKYVFRLHEATDYPWRPTLTPFEFQKLLNNLTSIKIRGTYSERSAGYLDDVTLASAHPGPGVPATWVESCTCPVGYGGQFCEVCLSGYRRETPSLGPYSPCVLCTCNGHSETCDPESGVCNCRDNTAGPNCEKCSDGYYGDSTAGTSLDCQPCPCPGGSSCAVVPKTQEVVCTNCPTGTTGRRCELCDDGHFGDPLGSNGPVRLCRLCQCNDNIDPNAVGNCNRLTGECLKCIYNTAGFYCDRCKDGFFGNPLAPNPADKCRACDCNPYGTVKQQSSCNPVTGQCECLPHVTGRDCGACDPGFYNLQSGQGCERCDCHALGSTNGQCDVHSGQCECQPGITGQHCEHCEVNHFGFGPEGCKPCDCHPEGSLSLQCKDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQECPACYRLVKDKVADHRAKLRELENLIANLGTGDEMVTDQAFEDRLKEVEREVTDLLREAQDVKDVDQNLMDRLQRVNNTLFSQISRLQNIRNTIEETGNLAEQARSRVESTEQLIEIASRELEKAKVAIANVSVTQPESTGDPNNMTLLAEEARKLAERHKQEADDIVRVAKTANDTSAEAYNLLLRTLAGENQTASEIEELNRKYEQAKNISQDLEKQAARVHEEAKKAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAEDLDRLIDQKLKDYEDLRDDMRGKEFEVKKLLEKGKTEQQTADQLLARADAAKALAEEAAEKGRNTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINQTIIEANEKTREAQQALGNAAADATEARNKAHEAERIASAVQKNATSTKAEAERTFAEVTDLDNEVNNMLKQLQEAEKELKKKQEDADQDMMMAGMASQAAQEAEINARKAKNSVTNLLNLINDLLEQLGQLDTVDLNKLNEIEGTLNKAKEEMKVSDLDRKVSNLENEARKQEAAIMDYNRDIEEILKDIRNLEDIKKTLPSGCFNTPSIEKP
Protein: Origin recognition complex subunit 2 (xORC2) (Q91628)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MSHEAHNGTKLFKVQFTPDEEVLEHITDKQGVTPQSNTAAQRIVAVKNIIKNDDLHVDEATPESWREQNYVDVLGVDTEDTLQNGPGTGGGDVYSFYTIKRSNKMAQLATEMARTPAKTVSFSVSDNPEEAVSPPANKQTENKTPSKGRKNEFISTTPHRLRKRLSAPSQPSDSESDYSASNSDEELEEKSSAAKTPSKVSQTPGKTPSKKGKKNTASNLVEEYFEAHSSSKVLTSDRTLQRLQTPKLDQETLRKLLDQTPSAFADELHRISKKHEALFYKWMLQLHLGFNIILFGLGSKQSLIEKFRTSLLQDSLHIVINEFFPSITAKSILNSITEEALGHPGAFRSPLDQMDFILQRFKDDPSLELYLLIHNLDSQMLRGEKCQQVLGQLASIPNLHLLASVDHINAPLMWDQSKQSLYNWLWYETTTFGSYIEETSYENSLLVKRSGALALSSLTHVLRSLTPNARGIFRLLAEYQMANKDNPSYTGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGMDGVEYLLIPLDLGTLTDFLEMEDKDT
Protein: Sterile alpha motif domain-containing protein 7 (SAM domain-containing protein 7) (Q8C8Y5)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of gene expression in the retina. It functions as a negative regulator of CRX-controlled genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:23565263, ECO:0000269|PubMed:28900001}. Cytoplasm {ECO:0000269|PubMed:23565263}. Note=Co-localizes with PHC2 and RNF2 in nuclear polycomb bodies. {ECO:0000269|PubMed:28900001}.
Interaction partners:
- Short-wave-sensitive opsin 1
Sequence:
MTNPMMSVSSLLTSGQQKVPMVPSPFGPPIVDRDVLSSSIAPTDPSQFCVPSQFGSSGLPNANMPNPLSSHFYSGWGILPPEPIKAVTTRNEMFERHHAARAEMEMYSLYQQRRMERVNPKGLSGLGIPLFYGSSCLGGPTGFQGRSTLPASDVHLHRSTFRHLQGNPILLATRPHFTECWGQKYRLRRGAVYQKPPESDTESFKSQAEEKSSSQMPTLSYEEEEYIKDPDIEVDNQQKPRVADGKPTTVPANPHGELHTHQRKPSSLEANAWDDGKGKPSEQVYEGCDGKNGVFRPVSILPLSGTHEQVALRENCSLSDIQKWTVDDVYNFIRSLPGCSDYAQVFKDHAIDGETLPLLTEQHLRGTMGLKLGPALKIQSQVSQHVGNMFCKKLPSLPTHARQAFDQPADTSPLLDMSSWSDGLSIPGPQDLLSPKRTEQDVMRN
Protein: Small ribosomal subunit protein uS9m (37S ribosomal protein S9, mitochondrial) (O14006)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein bL12m
Sequence:
MFRSLAKLRCFASSLGLSSHKNIKSVPLIRNIHYIPDNPSYFTQNARFNEIYLHLENILKFAPKIIAAEEDVPKKWKTLEQYQKEFSDPKTTKVGYRKITRLLNELNEIVPEYRTEAVQKALEKFIRPDIVVKTTLKSQMLDENGMSITKGKRKSSKATVKMLPGTGKFYVNGSPFDVYFQRMVHRKHAVYPLAACNRLTNYNVWATVHGGGPTGQSGAVHAAISKSLILQEPSLKQVIKDTHCVLNDKRKVERKKTGQPKARKKYTWVKR
Protein: Plasma membrane ATPase 1 (EC 7.1.2.1) (Proton pump 1) (P05030)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Inorganic pyrophosphatase
- Inorganic pyrophosphatase, mitochondrial
- Plasma membrane ATPase 2
- Serine/threonine-protein kinase PTK2/STK2
- General amino-acid permease GAP1
- 1,3-beta-glucanosyltransferase GAS1
- Plasma membrane ATPase proteolipid 1
- Pyruvate kinase 1
- Protein STD1
- Arginine permease CAN1
Sequence:
MTDTSSSSSSSSASSVSAHQPTQEKPAKTYDDAASESSDDDDIDALIEELQSNHGVDDEDSDNDGPVAAGEARPVPEEYLQTDPSYGLTSDEVLKRRKKYGLNQMADEKESLVVKFVMFFVGPIQFVMEAAAILAAGLSDWVDFGVICGLLMLNAGVGFVQEFQAGSIVDELKKTLANTAVVIRDGQLVEIPANEVVPGDILQLEDGTVIPTDGRIVTEDCFLQIDQSAITGESLAVDKHYGDQTFSSSTVKRGEGFMVVTATGDNTFVGRAAALVNKAAGGQGHFTEVLNGIGIILLVLVIATLLLVWTACFYRTNGIVRILRYTLGITIIGVPVGLPAVVTTTMAVGAAYLAKKQAIVQKLSAIESLAGVEILCSDKTGTLTKNKLSLHEPYTVEGVSPDDLMLTACLAASRKKKGLDAIDKAFLKSLKQYPKAKDALTKYKVLEFHPFDPVSKKVTAVVESPEGERIVCVKGAPLFVLKTVEEDHPIPEDVHENYENKVAELASRGFRALGVARKRGEGHWEILGVMPCMDPPRDDTAQTVSEARHLGLRVKMLTGDAVGIAKETCRQLGLGTNIYNAERLGLGGGGDMPGSELADFVENADGFAEVFPQHKYRVVEILQNRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLEIFLGLWIAILDNSLDIDLIVFIAIFADVATLAIAYDNAPYSPKPVKWNLPRLWGMSIILGIVLAIGSWITLTTMFLPKGGIIQNFGAMNGIMFLQISLTENWLIFITRAAGPFWSSIPSWQLAGAVFAVDIIATMFTLFGWWSENWTDIVTVVRVWIWSIGIFCVLGGFYYEMSTSEAFDRLMNGKPMKEKKSTRSVEDFMAAMQRVSTQHEKET
Protein: Peroxisomal multifunctional enzyme type 2 (MFE-2) (17-beta-hydroxysteroid dehydrogenase 4) (17-beta-HSD 4) (D-bifunctional protein) (DBP) (Multifunctional protein 2) (MFP-2) [Cleaved into: (3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12); Enoyl-CoA hydratase 2 (EC 4.2.1.107) (EC 4.2.1.119) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase)] (P97852)
Organism: Rattus norvegicus (Rat)
Function: Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from straight-chain, 2-methyl-branched-chain fatty acids bile acid intermediates. With EHHADH, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity.
Subcellular location: Peroxisome {ECO:0000269|PubMed:8856068}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal acyl-coenzyme A oxidase 3
- Peroxisomal acyl-coenzyme A oxidase 2
- Alpha-methylacyl-CoA racemase
- Peroxisomal bifunctional enzyme
- Peroxisomal targeting signal 1 receptor
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA delta isomerase 2
- Peroxisomal membrane protein PEX13
Sequence:
MASPLRFDGRVVLVTGAGGGLGRAYALAFAERGALVVVNDLGGDFKGVGKGSSAADKVVEEIRRRGGKAVANYDSVEAGEKLVKTALDTFGRIDVVVNNAGILRDRSFSRISDEDWDIIQRVHLRGSFQVTRAAWDHMKKQNYGRIIMTASASGIYGNFGQANYSAAKLGLLGLANTLVIEGRKNNIHCNTIAPNAGSRMTETVMPEDLVEALKPEYVAPLVLWLCHESCEENGGLFEVGAGWIGKLRWERTLGAIVRKRNQPMTPEAVRDNWVKICDFSNASKPKSIQESTGGIIEVLHKIDSEGISQNHTGQVASADASGFAGVVGHKLPSFSSSYTELQCIMYALGVGASVKNPKDLKFVYEGSADFSCLPTFGVIVAQKSLMSGGLAEVPGLSINFAKVLHGEQYLELYKPLPRSGELKCEAVIADILDKGSGIVIVMDVYSYSGKELICYNQFSVFVVGSGGFGGKRTSEKLKAAVAVPSRPPDAVLRDTTSLNQAALYRLSGDSNPLHIDPSFASIAGFEKPILHGLCTFGFSARHVLQQFADNDVSRFKAIKVRFAKPVYPGQTLQTEMWKEGNRIHFQTKVQETGDIVISNAYVDLVPTSGVSAQTPSEGGALQSALVFGEIGRRLKDVGREVVKKVNAVFEWHITKNGNVAAKWTIDLKNGSGEVYQGPAKGSADTTITISDEDFMEVVLGKLNPQNAFFSGRLKARGNIMLSQKLQMILKDYAKL
Protein: Glycogen phosphorylase (EC 2.4.1.1) (Q9XTL9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). Required for glycogen breakdown in skeletal muscle.
Interaction partners:
- Phosphoglucomutase 1
- 1,4-alpha-glucan branching enzyme
- Glycogen debranching enzyme
- Glycogen [starch] synthase
- UTP--glucose-1-phosphate uridylyltransferase
- ATP-dependent 6-phosphofructokinase
- Enolase
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 2a
- Phosphoglucomutase 2b
Sequence:
MSKPQSDADRRKQISVRGIAEVGNVTEVKKNFNRHLHYTLVKDRNVSTLRDYYFALANTVKDNMVGRWIRTQQHYYEKDPKRVYYLSLEYYMGRSLTNTMINLGIQSECEEAMYQLGLDIENLEEMEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFAQKIKNGEQVEEPDDWLRYGNPWEKARPEFMLPVNFYGRVIDTPEGKKWVDTQRVFAMPYDNPIPGYNNNHVNTLRLWSAKSPIDFNLKFFNDGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFMCAATLQDIIRRYKASKFGSREAVRNTFDHFPDKVAIQLNDTHPSLAIPELMRILVDEEHLTWEKAWDITVRSCAYTNHTVLPEALERWPVSLLESILPRHLQIIYHINFLHMENVKKKFPDDLDRMRRMSMVEEDGEKRINMAHLSIVGSHAVNGVAAIHSQILKDSLFHDFYEMEPQKFQNKTNGITPRRWLLLCNPGLSDLIAEKIGDEWPVHLDQLVALKKWAKDPNFQRNVARVKQENKLKLAAILEKDYGVKINPSSMFDIQVKRIHEYKRQLLNCLHIITLYNRIKKDPTANFTPRTIMIGGKAAPGYYVAKQIIKLICAVGNVVNNDPIVGDKLKVIFLENYRVTLAEKIMPAADLSEQISTAGTEASGTGNMKFQLNGALTIGTLDGANVEMAEEMGLDNIFIFGMTVDEVEALKKKGYNAYDYYNANPEVKQVIDQIQGGFFSPGNPNEFKNIADILLKYDHYYLLADYDAYIKAQDLVSKTYQNQAKWLEMSINNIASSGKFSSDRTIAEYAREIWGVEPTWEKLPAPEDQPQN
Protein: Ras-related protein Rab-31 (EC 3.6.5.2) (Ras-related protein Rab-22B) (Q13636)
Organism: Homo sapiens (Human)
Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. Required for the integrity and for normal function of the Golgi apparatus and the trans-Golgi network. Plays a role in insulin-stimulated translocation of GLUT4 to the cell membrane. Plays a role in M6PR transport from the trans-Golgi network to endosomes. Plays a role in the internalization of EGFR from the cell membrane into endosomes. Plays a role in the maturation of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:17678623, ECO:0000269|PubMed:19725050, ECO:0000269|PubMed:21586568}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:17189207, ECO:0000269|PubMed:21586568}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Rapidly recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). {ECO:0000269|PubMed:21255211}.
Interaction partners:
- Ras-related protein Rab-22A
- Geranylgeranyl transferase type-2 subunit alpha
- Rab GDP dissociation inhibitor beta
- Rab GDP dissociation inhibitor alpha
- Rab proteins geranylgeranyltransferase component A 2
- Rab proteins geranylgeranyltransferase component A 1
- Ras and Rab interactor 3
- Inositol polyphosphate 5-phosphatase OCRL
- Ras GTPase-activating protein 1
- GTPase-activating protein and VPS9 domain-containing protein 1
Sequence:
MMAIRELKVCLLGDTGVGKSSIVCRFVQDHFDHNISPTIGASFMTKTVPCGNELHKFLIWDTAGQERFHSLAPMYYRGSAAAVIVYDITKQDSFYTLKKWVKELKEHGPENIVMAIAGNKCDLSDIREVPLKDAKEYAESIGAIVVETSAKNAINIEELFQGISRQIPPLDPHENGNNGTIKVEKPTMQASRRCC
Protein: Magnetosome protein MamS (Q6NE49)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: May play a role in magnetite crystal growth and size.
Subcellular location: Magnetosome membrane {ECO:0000305|PubMed:14766587}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Magnetosome protein MamR
- Magnetosome protein MamT
- Multi-heme protein MamP
- Probable membrane transporter protein MamO
- Magnetosome protein MamM
- Magnetosome protein MamN
- Magnetosome protein MamB
- Magnetosome protein MamQ
- Magnetosome formation protease MamE
- Magnetosome protein MamH
Sequence:
MDFRPDQVVARIRGAVEGALTAQSVLGIGGALVLILVVIALLPDRFTRGEGKTATAVSSGAAQALPAALPGLSPFTPAKPLQFSGRVTQVASIGNDVGWGQVHVWIDNGTGALQEISVAPQSYLNQIGCPSFDGARISGIGFLFDAGRPNAELYAKSVLVGGRTCKLRDDEGLALWMTVQ