wanglab/gogpt-training-data huggingface dataset:
Protein: Prominin, isoform E (A0A0B4LGM0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDQRNLTLPTPAATTIMSSSSAAMSAGFASLGGPTTSALTGSTIALATTTTTAPPTTTPATFFTYSIPGMDIAPGPFIFTYVSEFLSLITPEELPLDSIRDVLHKNTSLLDFASNAIKIESGFIALMSVFAILALVPLIATCAWCCGRRSTQEEVDHIRNAPCHIRDESLEESLRCRKSAGLVTLWVVFILLTLSDFSIFYANSRLSAGIEMTPEMVKSAVHDVEVFLKDTHLQIKQKLDNGFHVSVERVVKDLEDVDVLLGEPIQAEISAHTGLELAYDSLTTLSLANAELIYRVLMLQETVGRALKLSQEAAARMEELQIQLSVLQRQCTYRDRPLCDTLRIRSFEENGVVDALKTLQEDQSIFRMRYLGEIEFGATVKNLTSEVGVSRSIFSNFPQQVKHDTAYERNYTLEQLASIRHRTTANAQQLTSTVNGLLRRLEDTWSSLQPAYNELKEWADAYWSVGWIAGTVIVWVMLFMLMSYCCFLCESNAKSGVVFFIAVMLICLASICLTIFGVFSLAVGGNAEVFVCRSLYDEDYNMLGKLLDKPGYAYAREPQTGIIGELLRPVGVNRSVVNVGLGQALRGCEQNQASYNVFQLDAFVNTSKIADLRQFPKVSTAIDAISVSGRTLLSLTQSVQNILDNMLQTSSFNLTTYRSSVGAPTPEKDLATFIDQMQRVALQIQDVATSSRMTTLGSRSKRLQASILQPLENLQNEILYHLTALELQRDPWAKQVNQTLNHLKSIQSYLENKAGEICHNMTRDYRDRLKAYLTTSKATMESQLGDTTTKCRPFYDTFDASRTFLCRNMVDFINGLTFFIFLTLLLWAIGTPVGLNLITVQTRLNVMQAAQARSKGRHRRSDRSPEHEQRSGSRGRKKQRTSSSATSGRSGKRDQSRERSTSSTARPKPPLRRTATEETLDLADEESTPSRQQQQQPPPQRRQESDRERVRERDQRSRERELSRGRDASAMNTPVRSRSRQQLRHDPEDDNWGSSSGPSRANSRERDRESSQTRKILNIWQSRNKAKTPLRRQGTEEFDFEDAHDDRGWQAQTQNQVQNQSRAHNQSSVSPEQRPDPRSHRSNLRTKPKFQRTGTDEFDLDDSDAYGAGGHLDADVAAARRTPPRGAPPPPPPPAAGLNSDRTVRWNEDETEDFDFEEVDAPKSPMYLSHNLQ
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (LONHs) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) (P36776)
Organism: Homo sapiens (Human)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein, helicase Twinkle (TWNK) and the large ribosomal subunit protein bL32m. bL32m is protected from degradation by LONP1 when it is bound to a nucleic acid (RNA), but TWNK is not.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03120, ECO:0000269|PubMed:7961901}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- ATP-dependent clpX-like chaperone, mitochondrial
- Mitochondrial disaggregase
- 60 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Aconitate hydratase, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- ATP-dependent zinc metalloprotease YME1L1
- Protein cereblon
- 10 kDa heat shock protein, mitochondrial
Sequence:
MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER
Protein: Zinc finger CCCH domain-containing protein 3 (AtC3H3) (EC 3.1.-.-) (Zinc finger CCCH domain-containing protein ZFN-like 4) (Q94AD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses RNA-binding and ribonuclease activities in vitro.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Zinc finger CCCH domain-containing protein 15
- Zinc finger CCCH domain-containing protein 14
- Zinc finger CCCH domain-containing protein 17
- Zinc finger CCCH domain-containing protein 59
- PPPDE putative thiol peptidase family protein
- PPPDE thiol peptidase family protein
- Zinc finger CCCH domain-containing protein 62
- Protein JINGUBANG
- Zinc finger CCCH domain-containing protein 36
- 30-kDa cleavage and polyadenylation specificity factor 30
Sequence:
MRTPMSDTQHVQSSLVSIRSSDKIEDAFRKMKVNETGVEELNPYPDRPGERDCQFYLRTGLCGYGSSCRYNHPTHLPQDVAYYKEELPERIGQPDCEYFLKTGACKYGPTCKYHHPKDRNGAQPVMFNVIGLPMRLGEKPCPYYLRTGTCRFGVACKFHHPQPDNGHSTAYGMSSFPAADLRYASGLTMMSTYGTLPRPQVPQSYVPILVSPSQGFLPPQGWAPYMAASNSMYNVKNQPYYSGSSASMAMAVALNRGLSESSDQPECRFFMNTGTCKYGDDCKYSHPGVRISQPPPSLINPFVLPARPGQPACGNFRSYGFCKFGPNCKFDHPMLPYPGLTMATSLPTPFASPVTTHQRISPTPNRSDSKSLSNGKPDVKKESSETEKPDNGEVQDLSEDASSP
Protein: Type II alpha-keratin IIA (Q6PVZ5)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Keratin, type I cytoskeletal 14
- Tumor protein 63
- Fork-head domain-containing protein.
- Cadherin-1
- BRICHOS domain-containing protein.
Sequence:
MSRISYRSSTGGGMRGFSSGSAIVGGSGGGTRSSFSSVSVSRVGGGRAGGGGGFGAGGGFGSRSLYNLGGSKRISLGGLRSGAGVGYGFGGGAGFGLGYGGGAGAALGLGGAGGGGGYGLGGFGMGGPGFGGRGGPGFPVCPPGGIHEVTVNQSLLAPLKLDIDPEIQKVRTQEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGHTVTRKSLEPLFETYINNLRRQLDSLMGERGRLDSELRSMQDMVEDFKNKYEDEINRRTGAENEFVVLKKDVDGAYMNKVELQAKADGLADEINFLRALYEAELSQMQQQVSDTSVVLSMDNNRSLDLNSIIAEVKAQYEDIANRSRAEAEAWYQNKYEELQVSAGRHGDDLRNTKMEISEINRMVQRLRNEIESVKKQCANLQAAIAEAEERGEMALKDAKSKLAELEDALQKAKADLARQLREYQELMNVKLALDIEIATYRKLLEGEESRLAGEGVGAVSVSVVSSSSGMGYGGGMGGGLSTGGGLCMGGGLSMGSGLGMGGGGGSYTMSSSVGGGGFGGGSGSYSYGGGSNFSSSSSRGVSSSTGGSVRIVSKTTTSKKTIR
Protein: Naphthalene 1,2-dioxygenase/salicylate 5-hydroxylase systems, ferredoxin--NAD(P)(+), reductase component (NDO/S5H systems, ferredoxin--NAD(P)(+), reductase component) (EC 1.18.1.7) (Ferredoxin reductase NagAa) (Ferredoxin--NAD(P)(+) reductase (naphthalene dioxygenase/salicylate 5-hydroxylase ferredoxin-specific)) (O52378)
Organism: Ralstonia sp
Function: Component of two multicomponent enzyme systems which are involved in the catabolism of naphthalene. Plays a role as an electron transfer component for both salicylate 5-hydroxylase (S5H) and naphthalene 1,2-dioxygenase (NDO) systems, by transferring electrons from NAD(P)H to the oxygenase component via the ferredoxin NagAb. The electron transport chain from the two systems can use both NADH and NADPH as electron donors at approximately similar rates.
Interaction partners:
Sequence:
MELVVEPLNLHLNAETGSTLLDVLRSNEVPISYSCMSGRCGTCRCRVIAGHLRDNGPETGRPQAGKGTYVLACQAVLTEDCTIEIPESDEIVVHPARIVKGTVTAIDEATHDIRRLRIKLAKPLEFSPGQYATVQFTPECVRPYSMAGLPSDAEMEFQIRAVPGGHVSNYVFNELSVGASVRISGPLGTAYLRRTHTGPMLCVGGGTGLAPVLSIVRGALESGMSNPIHLYFGVRSEQDIYDEERLHALAARFPNLKVNVVVATGPAGPGRRSGLVTDLIGRDLPNLAGWRAYLCGAPAMVEALNLLVARLGIVPGHIHADAFYPSGV
Protein: F-box domain-containing protein (G5EDF8)
Organism: Caenorhabditis elegans
Interaction partners:
- J domain-containing protein
- Phospholipid-transporting ATPase
- Large ribosomal subunit protein eL33
Sequence:
MALQELPEKVLNEILSKLEPKHRLVVRKVCRILRRLVSFEVIDFKITSEAKVELKFDEFCIKWPRKIKGNDCIGMALNDLQSWLKMPLKMLCIDTGEQTEHFEELIDRLKSMKPVQADILGLWMSVDQCIKLFPYFEAGKLERIAMHYEEEELDKFHELTLLEQWKKAKRLLFEPQVGVDTNETPIEAFFHREFFTLNVLQISDQDARKIKEILLKKPNFKGCVFECWTETDVSRLFQPIIEFPREHPDTAKFEYSTNGSKFSIVVHCRWSVYISRM
Protein: Mitochondrial import inner membrane translocase subunit Tim22 (Q9CQ85)
Organism: Mus musculus (Mouse)
Function: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9Y584}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim29
- Acylglycerol kinase, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit Tim13
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Mitochondrial import inner membrane translocase subunit TIM50
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MAATAPKAGGSAPEAAGSAEAPLQYSLLLQYLVGDKRQPRLLEPGSLGGIPSPAKSEEQKMIERAMESCAFKAVLACVGGFVLGGAFGIFTAGIDTNVGFDPKDPYRTPTAKEVLKDMGQRGMSYAKNFAIVGAMFSCTECLVESYRGKSDWKNSVISGCITGGAIGFRAGVKAGAIGCGGFAAFSAAIDYYLR
Protein: Polyubiquitin-C [Cleaved into: Ubiquitin] (P0CG48)
Organism: Homo sapiens (Human)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion outer membrane {ECO:0000269|PubMed:24751536}; Peripheral membrane protein {ECO:0000305|PubMed:24751536}.
Interaction partners:
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Ubiquitin carboxyl-terminal hydrolase isozyme L3
- Ubiquitin carboxyl-terminal hydrolase 5
- Ubiquitin-conjugating enzyme E2 K
- NF-kappa-B essential modulator
- E3 ubiquitin-protein ligase RNF31
- Ubiquitin carboxyl-terminal hydrolase isozyme L1
- Ubiquitin-like modifier-activating enzyme 1
- E3 ubiquitin-protein ligase parkin
- Sequestosome-1
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGV
Protein: Probable mannosyltransferase YUR1 (EC 2.4.1.-) (P26725)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possible glycosyltransferase involved in N-linked glycosylation. Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- Glucosidase 2 subunit alpha
- Alpha-1,2-mannosyltransferase MNN2
- Protein KRE1
Sequence:
MAKGGSLYIVGIFLPIWTFMIYIFGKELFLIRKYQKIDSTYTALSQRVKEQYDTSRRRNYFPKVKLSRNSYDDYTLNYTRQNDSDSFHLRENATILMLVRNSELEGALDSMRSLEDRFNNKYHYDWTFLNDVPFDQDFIEATTSMASGKTQYALIPPEDWNRPQWINDTLFEERLRVMEDEGVLYGGSKSYRNMCRFNSGFFFRQSILDNYDYYFRVEPNVKYYCDFPYDPFRVMRLKGKKYGFVISLYEYEETIPTLWDAVEEYLVASEETILRKEDSAYAFLTDSGLVGKHYPVVEANSDYNLCHFWSNFEIGDLNFFRSDEYKHFFETLDAKGGFYYERWGDAPVHSIGVSLLLRPDEIIHFDELGYFHSPFGTCPASYAVRLDQRCRCKSDDESVIDITPHSCLMRWWKNGSGKYFLKEEQDEI
Protein: Coilin (Sphere organelles protein SPH-1) (Sphere protein 1) (Q09003)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000269|PubMed:8349728}. Note=Sphere organelles.
Interaction partners:
Sequence:
MAAPSPVRVKLLFDYPPPAIPESCMFWLLLDAKRCRVVTDLASIIRHKYMDGQGGGISLYVEDCLLPPGESILVIRDNDSIRVKWDGAAIERNQEAETCNDGAQNKSKKRHWKKSEDECDSGHKRKKQKSSSTQVDLKSGKDGGIRDKRKPSPPMECNASDPEELRESGRKTHKGKRTKKKSEAPIENPPDKHSRKCPPQASNKALKLSWKRQTSSSDSSDTSSCSDQPTPTTQQKPQSSAKRQNQAATRESVTHSVSPKAVNGISSTKNKKADAPISSSDMDTAVGGNETLICPVPPEDLSTHIQQHSQSPTSDSAESIELVIKKSNASLSSLTDNRVAGVSDKLSPNVSGRGRGRGEDFSWRGQRGRWFRGQGNNSNRGRGRGDSSNVFYKYNTEKEKQQQLEESATNVSIIIQNPQETMKRDYSSLPLLAAAPQVGKLIAFKLLEVSENYTPEVSEYKEGKILSFDPVTKQIEMEIISQQTMRKPGKFDVVYQSEDGEDIVEYAVPQESKVMLNWNTLIEPRLLMEKESQVQC
Protein: Protein MEMO1 (Q38B52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- AMMECR1 domain-containing protein
Sequence:
MTYSRRATHAGSWYEGSPNALKALVDTLFSTASKSPLKESEKMIGVISPHAGISYSGNTASHVYVHLRDYIYGHKGRSITRIFLLGPSHHKGFDGVEVCAAQRYETPFGPLVVNAKVGQEVEKELRAAGVPVGTMHRMTDEDEHSIEMQLPFISHLLHYPPNGYKPAMDRVELVPLLIGGTNRKMENLIGSVLSKYLKDNQNFFVISSDFCHWGARFQYMYHYEKAEYPDIGDAIISMDHEGMRLLEARDMDGWYKYLSTTNNTICGRRPISVLMAALDSKKEAVVRFLHYSQSNRCKNMSDSSVSYAGAIVTLDESGDKSAP
Protein: Cyclin-O (P0C242)
Organism: Mus musculus (Mouse)
Function: Specifically required for generation of multiciliated cells, possibly by promoting a cell cycle state compatible with centriole amplification and maturation. Acts downstream of MCIDAS to promote mother centriole amplification and maturation in preparation for apical docking (By similarity). May be involved in apoptosis in lymphoid cells; however, this result requires additional evidences in vivo. May be involved in oocyte meiotic resumption in oocytes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24747639, ECO:0000269|PubMed:26777464}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P22674}. Note=Localizes to the apical part of cytoplasm. {ECO:0000269|PubMed:24747639}.
Interaction partners:
- Cyclin-dependent kinase 2
- Multicilin
- Cell division cycle protein 20 homolog B
- Cyclin-A1
- Cyclin-A2
- Geminin coiled-coil domain-containing protein 1
Sequence:
MVTPCPASPGSPAAGAGRRDSHQNLRAPVKKSRRPCLRRKKPLRPLNACSLPGDSGVCDLFESPSSSSDGADSPAVSAARDCSSLLNPAQPLTALDLQTFREYGQSCYDFRKAQENLFHPRESLARQPQVTAESRCKLLSWLLQVHRQFGLSFESLCLTVNTLDRFLLTTPVAADCFQLLGVTCLLIACKQVEVHPPRLKQLLALCGGAFSRQQLCNLECIVLHKLHFSLGAPTINFFLEHFTQWRMEAGQAEVTEALEAQTLARGVAELSLTDYAFTTYTPSLMAICCLALADGLLQHQHEMDLRLGEHPEATLQDCLGKLQTLVSINSSSLPRILPPQIWERCSLPQSWQ
Protein: ADP-ribosylation factor guanine nucleotide-exchange factor sec72 (ARF-GEP sec72) (Q9P7V5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May play a role in protein transport.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11075}. Golgi apparatus {ECO:0000250|UniProtKB:P11075}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P11075}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:P11075}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P11075}.
Interaction partners:
- Uncharacterized protein C211.03
- ADP-ribosylation factor guanine nucleotide-exchange factor sec71
Sequence:
MQDASEPVINMPALPMNSVNEQHDRHEDLPEVGTTSVTKIINDSDNEDDENGMDLGRVASESLEGDAVVSIDINTEDSSLSPAKQENEKSPEGIEQKYQEEDLKDDKKSNETIATPVPDAASRASLEKQKSGLTNLEKSTHVVLIKCIEQLIQIKVCMKNEKMKNLMEQLKPLLQTECQFDKFLIVELFQYCFESSQDEVMNISLDTISKLASFAYFSSKDKTPASFGPPKSLLQCMVDMVCDSINDEVVDGNLQLNVVKALSAFILCSEQDSMLHGAILLNSVRKLFNVFLLGDSDTIQSVAQASLTQAVTVVYERLRASHTQSNSTSALPEEDASVTENWVHDEDEPDKKITLHSMASAGTSSLDHVKVDADDPAVTSVENSSIQDAFLVFRSMCRLAVRQTSPDKVSNIRSQAMRAKLISLHLIYRILEKNSDLFMDPTLQFRGIPALKGMTLVHASRQYICLVLSRNAVSPVPQVFEVCCDIFYLMVFSLRAHFKQEIEVFFREVYFPMLDLKNTSYNQKLHTLLIIQRICLNPRALVELYINYDCDRSSTTNVFEQLLFSISKVTTNGPSETISEDIEEILPSLESSERSSTPFLNTNSASLKSEVVQLTTFSDFQLKLKTLQCVLDILQSLSNWAESGLYLSRRGVSTDEQGFVGDYDALSRSDTPVTNPYYNGKQSFEANSHSSSSIALADPSQFESNKQRKKLLRTCINKFNYKPTRGLKMLSENEYVDINDPKAIAEFLFRADGIDKTTLGDYLGEGDEKSISVMHEFIDCLSFINLKFVDALRRLLQCFRLPGEAQKIDRIMLKFSERYMKENPSAFANADTAYILAYSIILLNTDLHSPRIKNKMTKEDFIKNNRGINDGADLDEDYLGFVYDDILKNEIAMKDDQELAAIAPLMNNFSTSSGFTTFTSNGRDLQRVACIQASEEMANKATSVLKKLLYQQKHGSQKTNVYYNATHFEHIGPMLEATWMPILAALSNPLQNSDYVNELNMCLDGFQLVVRIACLFDLDLIRDAFIKTLTNFTNLHSTSEIKLRNTMVIKTLLRIASTEGNNLKDSWKDILTIISQLERVQLIGVGVDETEVPDVINARVRRKNVNIGSSNSIRHVSGSTSRSTRTRSLSKPLSPEAVSELMSTEVVLSIDRIFTQTSSLSGSAIVSFFKALCEVSWDEITSSSDLEQPRLYSLQKLVEISYYNMQRIRVEWSSIWNVLGRFFNMVGSDENRHVAVFALDSLRQLSMHFLEIEELSLFSFQKEFLKPFEYVMASDTVVEVKELVLQCVKQMIQAKISKIKSGWKTLFGVFTFAAKARSEILISMTFDTLVNLFSEHYDTLMQQNCLIDMLISFTELCKNGTNQKISLQSLEIIREVYSSLSTMIKEGLSSKPSVNETFSKYVFPVLFAYYDIIMSAEDLEVRSRALQNLFYIFLEESDDFTEETWEVVSRKFIFPIFSIFGPEADEATVMLRDEEIRTWQSTTLVEALRSLVTLLTRRFDKLHNLLKGYLWLFSNCICRDNITLSRIGTNCMQQLLSGNAYRFEVKDWNLVADMFIELFKETTPHQLLLLETFSNGQGAPVYSENENTQLSHKRGGSLPETSRSISTSSISPEKQMEFRSMIRKCILQLLLISIVAELLDNEEVFNHIPHEHVLKITVAIYDSWQFARKFNEDKSLRITLLNVGFMKQLPNLLRQETASALLYITLLFRLLKTRDPLGKTETDQKIHKLLFPVCAEMLDMYASLVVEKHTRNHAAWQPVIATILDSILNLPLELFSENIHTLYFSCCSMIAKENLDDQLRELLKNYFNRVGHILLNLNAQQE
Protein: Protein associated with UVRAG as autophagy enhancer (Pacer) (Protein Rubicon-like) (Q9H714)
Organism: Homo sapiens (Human)
Function: Regulator of autophagy that promotes autophagosome maturation by facilitating the biogenesis of phosphatidylinositol 3-phosphate (PtdIns(3)P) in late steps of autophagy. Acts by antagonizing RUBCN, thereby stimulating phosphatidylinositol 3-kinase activity of the PI3K/PI3KC3 complex. Following anchorage to the autophagosomal SNARE STX17, promotes the recruitment of PI3K/PI3KC3 and HOPS complexes to the autophagosome to regulate the fusion specificity of autophagosomes with late endosomes/lysosomes. Binds phosphoinositides phosphatidylinositol 3-phosphate (PtdIns(3)P), 4-phosphate (PtdIns(4)P) and 5-phosphate (PtdIns(5)P). In addition to its role in autophagy, acts as a regulator of lipid and glycogen homeostasis (By similarity). May act as a tumor suppressor (Probable).
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:28306502}; Peripheral membrane protein {ECO:0000269|PubMed:28306502}. Note=Associates with late autophagic structure (PubMed:28306502). Recruitment to autophagosome membrane is promoted by autophagic stimuli (PubMed:28306502). {ECO:0000269|PubMed:28306502}.
Interaction partners:
- Phosphopentomutase
- Solute carrier organic anion transporter family member 1A2
- AFG2-interacting ribosome maturation factor
- Pre-mRNA-splicing factor CWC25 homolog
- Protein limb expression 1 homolog
- UV radiation resistance-associated gene protein
- Syntaxin-17
- Beclin-1
Sequence:
MVSQSTVRQDSPVEPWEGISDHSGIIDGSPRLLNTDHPPCQLDIRLMRHKAVWINPQDVQQQPQDLQSQVPAAGNSGTHFVTDAASPSGPSPSCLGDSLAETTLSEDTTDSVGSASPHGSSEKSSSFSLSSTEVHMVRPGYSHRVSLPTSPGILATSPYPETDSAFFEPSHLTSAADEGAVQVSRRTISSNSFSPEVFVLPVDVEKENAHFYVADMIISAMEKMKCNILSQQQTESWSKEVSGLLGSDQPDSEMTFDTNIKQESGSSTSSYSGYEGCAVLQVSPVTETRTYHDVKEICKCDVDEFVILELGDFNDITETCSCSCSSSKSVTYEPDFNSAELLAKELYRVFQKCWILSVVNSQLAGSLSAAGSIVVNEECVRKDFESSMNVVQEIKFKSRIRGTEDWAPPRFQIIFNIHPPLKRDLVVAAQNFFCAGCGTPVEPKFVKRLRYCEYLGKYFCDCCHSYAESCIPARILMMWDFKKYYVSNFSKQLLDSIWHQPIFNLLSIGQSLYAKAKELDRVKEIQEQLFHIKKLLKTCRFANSALKEFEQVPGHLTDELHLFSLEDLVRIKKGLLAPLLKDILKASLAHVAGCELCQGKGFICEFCQNTTVIFPFQTATCRRCSACRACFHKQCFQSSECPRCARITARRKLLESVASAAT
Protein: Vacuolar zinc transporter COT1 (Cobalt toxicity protein 1) (P32798)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar transporter that regulates zinc homeostasis by mediating zinc transport and storage into the vacuole. Plays a role in resistance to zinc shock resulting from sudden influx of zinc into cytoplasm. May also participate in the regulation of cobalt levels under normal physiological conditions and may be important in the supply of metal that is required for metalloenzyme or cofactor synthesis. Involved in the resistance to cobalt and rhodium ions.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:35175277, ECO:0000269|PubMed:9712830}; Multi-pass membrane protein {ECO:0000255}. Note=Targeted to vacuole membrane via the AP-3 pathway. {ECO:0000269|PubMed:35175277}.
Interaction partners:
- Vacuolar zinc transporter ZRC1
- Protein ZRG17
- Zinc-regulated transporter 3
- Zinc-regulated transporter 2
- Zinc-regulated transporter 1
- Zinc transporter YKE4
- Zinc-responsive transcriptional regulator ZAP1
- Copper-transporting ATPase
- Protein CCC1
- Iron transporter FTH1
Sequence:
MKLGSKQVKIISLLLLDTVFFGIEITTGYLSHSLALIADSFHMLNDIISLVVALWAVNVAKNRNPDSTYTYGWKRAEILGALINAVFLIALCVSILIEALQRIIAPPVIENPKFVLYVGVAGLISNTVGLFLFHDNDQEHGHGHGHSHGGIFADHEMHMPSSHTHTHAHVDGIENTTPMDSTDNISEIMPNAIVDSFMNENTRLLTPENASKTPSYSTSSHTIASGGNYTEHNKRKRSLNMHGVFLHVLGDALGNIGVMLSAFFIWKTDYSWKYYTDPLVSLIITGIIFSSALPLSCKASKILLQATPSTLSGDQVEGDLLKIPGIIAIHDFHIWNLTESIFIASLHIQLDISPEQFTDLAKIVRSKLHRYGIHSATLQPEFITREVTSTERAGDSQGDHLQNDPLSLRPKTYGTGISGSTCLIDDAANCNTADCLEDH
Protein: Uncharacterized protein YbhJ (P75764)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Isocitrate dehydrogenase
- Citrate synthase
- Aconitate hydratase B
- Isocitrate lyase
- Aconitate hydratase A
- Inner membrane protein YbhI
- Putative isomerase YbhH
- Large ribosomal subunit protein bL36B
- 2-methylcitrate synthase
- Large ribosomal subunit protein uL15
Sequence:
MIKLSEKGVFLASNNEIIAEEHFTGEIKKEEAKKGTIAWSILSSHNTSGNMDKLKIKFDSLASHDITFVGIVQTAKASGMERFPLPYVLTNCHNSLCAVGGTINGDDHVFGLSAAQRYGGIFVPPHIAVIHQYMREMMAGGGKMILGSDSHTRYGALGTMAVGEGGGELVKQLLNDTWDIDYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVKNKVMEFVGPGVSALSTDFRNSVDVMTTETTCLSSVWQTDEEVHNWLALHGRGQDYCQLNPQPMAYYDGCISVDLSAIKPMIALPFHPSNVYEIDTLNQNLTDILREIEIESERVAHGKAKLSLLDKVENGRLKVQQGIIAGCSGGNYENVIAAANALRGQSCGNDTFSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAFCGPCFGAGDTPINNGLSIRHTTRNFPNREGSKPANGQMSAVALMDARSIAATAANGGYLTSASELDCWDNVPEYAFDVTPYKNRVYQGFVKGATQQPLIYGPNIKDWPELGALTDNIVLKVCSKILDEVTTTDELIPSGETSSYRSNPIGLAEFTLSRRDPGYVSRSKATAELENQRLAGNVSELTEVFARIKQIAGQEHIDPLQTEIGSMVYAVKPGDGSAREQAASCQRVIGGLANIAEEYATKRYRSNVINWGMLPLQMAEVPTFEVGDYIYIPGIKAALDNPGTTFKGYVIHEDAPVTEITLYMESLTAEEREIIKAGSLINFNKNRQM