wanglab/gogpt-training-data huggingface dataset:
Protein: Liver carboxylesterase 1F (EC 3.1.1.1) (Carboxyesterase ES-4) (Kidney microsomal carboxylesterase) (Microsomal palmitoyl-CoA hydrolase) (Q64573)
Organism: Rattus norvegicus (Rat)
Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters. Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis (By similarity).
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:Q91WU0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91WU0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WU0}. Microsome {ECO:0000269|PubMed:12230550}.
Interaction partners:
Sequence:
MCLSFLFLVSLATCVVYGNPSSPPVVDTTKGKVLGKYVSLEGVTQSVAVFLGVPFAKPPLGSLRFAPPQPAEPWSFVKNTTTYPPMCSQDAAKGQRMNDLLTNRKEKIHLEFSEDCLYLNIYTPADFTKNSRLPVMVWIHGGGMTLGGASTYDGRVLSAYENVVVVAIQYRLGIWGFFSTGDEHSRGNWGHLDQVAALHWVQDNIANFGGDPGSVTIFGESAGGFSVSVLVLSPLTKNLFHRAISESGVVFLPGLLTKDVRPAAKQIADMAGCETTTSAIIVHCLRQKTEEELLEIMKKMNLIKLSSQRDNKESYHFLSTVVDNVVLPKDPKEILAEKNFNTVPYIVGINKQECGWLLPTMMGFVPADVELDKKMAITLLEKFASLYGIPEDIIPVAIEKYRKGSDDSIKIRDGILAFIGDVSFSIPSVMVSRDHRDAGAPTYMYEYQYYPSFSSPQRPKHVVGDHADDLYSVFGAPILRDGASEEEIKLSKMVMKFWANFARNGNPNGRGLPHWPQYDQKEEYLQIGATTQQSQRLKAEEVAFWTQLLAKRQPQPHHNEL
Protein: Hatching enzyme 1.2 (EC 3.4.24.67) (Choriolysin H homolog 1) (High choriolytic enzyme 1 homolog) (zHCE-1) (Q1LW01)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Metalloendopeptidase which participates in the breakdown of the egg envelope at the time of hatching. Cleaves the N-terminal regions of the zona pellucia glycoproteins ZP2 and ZP3, where it specifically recognizes the peptide sequences TVQQS-|-DYLIK (major site) and KLMLK-|-APEPF (minor site).
Subcellular location: Secreted {ECO:0000269|PubMed:19021768}.
Interaction partners:
- Cathepsin Lb
- G protein-coupled receptor 176.
Sequence:
MDIRASLSILLLLFGLSQASPLREFEAIFVSEPETVDITTQILETNKGSSEVLFEGDVVLPKNRNALICEDKSCFWKKNANNIVEVPYVVSGEFSINDKSVIANAISIFHAQTCIRFVPRSIQADYLSIENKDGCYSAIGRTGGKQVVSLNRKGCVYSGIAQHELNHALGFYHEQSRSDRDQYVRINWNNISPGMAYNFLKQKTNNQNTPYDYGSLMHYGKTAFAIQPGLETITPIPDENVQIGQRQGLSKIDILRINKLYGC
Protein: Expression site-associated gene (ESAG) protein, putative (Q57X44)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHRLATVPFLTLILLVVCGGSKASVQISSASPGCDGYWTYTGVKKTCWTQNMGTTKRSGVSPNPPSVSRHRSQQPSSGAGVGDQQQETQGSVSSSSTTSRGTNQLGSDGEDTFPKEDVKQVYGSAGTLSMNPIAQPSGSPREPTDATPVVDRKEEGQVDQRGLESGSAKQQNTTNGNGEEENGGKGRGSGDHATGHDRGGMAQGVVSMSGQGSAQRVETVAEQPVKNKEDDIPGENVKGPGSSHVVSTPERRNTLETVTDNGDQQKSGESNAQGENSGSCKGRAVILPVILILMYS
Protein: Protein Fe65 homolog (Q9BKZ9)
Organism: Caenorhabditis elegans
Function: Modulates pharyngeal pumping activity, at least in part by regulating expression of the acetylcholinesterase genes ace-1 and ace-2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11896189}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11896189}.
Interaction partners:
- C2H2-type domain-containing protein
- Amyloid-beta-like protein
- Nuclear receptor domain-containing protein
- Nucleoside diphosphate kinase
Sequence:
MREGTPRVRIEVNKGSNRPSQFVSESEEQRLQRVQSRDSDTATMNFVTDDRMMEEHDEYSAFKEAYEEEESREYVIENGVKRLVNQHYDSRGYSSAGRGQKGRREEERRRNMAVDYSSQDFRQSLAAIDQASRDGAISRGEDGVRVRQIGDTTIMTEHRDPYSFYWQLDQARREAESPPRRPPPTDYVIDEEEEVLETVYSPEADDVMFENQYRRPVRHPLPPPPPIMEEEPKDLPPGWEKHEDPQGYSYYWHVDSGTIQRQPPPPVNRETQADAPPPQIIQLPPQQPVIEEHAFKQTTTKRRIEQDEMSEREIEDVAMIENGDTYHKPVRFAVRSLGWTDISEDELTAEKSSRAVNRAIVDLTTRSDIDSIPKWGDGRELIMELDDNELALLDPDSMNVIHSERIQAIRVWGVGRDNGRDFAYVSRDRGTRRFMCHVFRCDTSAKTIANTLRDICKRLMLHRRPSSLHAIESGEKRIVRSEGLTAPIDEPRKVIRCHFLGVTQVPKATGIEILNEAVDRLVSQVRSERWILADVSIAPSTIAIVEVNGQQIAECRVRYLSFLGIGRDVKHCAFIMQTSSESFMCYVFHVEPNAAAMAKMVEAACKLRYQKVLDAHSSSRHHSGMSIHGQHPPSTYHGKGWTETFRDAFGSVTSRMVPSRSAQRL
Protein: Dynamin-type G domain-containing protein (Q9N5B7)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004159}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004159}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004159}.
Interaction partners:
Sequence:
MESVNSEEHKINEAPAPPVIVINSSTKEEQEATQTDRIEGQMKKIDSVFDEQNVASLEGVNSKNEISGSVSSSSFEELNAETEDLSERSEVEKDEDLGRVVEEHKEPAQVPVESETPETSKKEIHQEEEISELEKVPETVEEEIEVVNTSVEITEVKKEVIEEVKISGLKEEETPVPKMRAQQQVPVAADRPIRRLSIARASMMTPKASPKLAKYMEPVREEGQKKKKTRSMFSWLGGDSSKKKNKEVLETVSEGLRKIYKQKLLPLEEFHKFHDFHSPALDDPDFDAKPMILLVGQYSTGKTTFIRYLLESDFPGIRIGPEPTTDRFIAVMHGDEEGSIPGNALVVDAKKQFRALSGFGNAFLNRFQCSTLPNQVLESVTIVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFKRCIEALAGNEDKIRIVLNKSDMVDHQQLMRVYGALMWSLGKVFKTPEVSRVYLGSFWDHPLHYDLNRRLFQDEQHDLFQDLQALPRNAALRKLNDLIKRARLAKVHAYIIAELRKQMPSMIGKDKKKKDLIQNLDKIYEQLQREHNISPGDFPDVNKMREKLQTQDFSKFNPLKPKLLEVVDGMLATDIARLMAQIPKEEAAAPAGSNGSADPTVRGGAFSQTTEAETPFGFGRGEGFDKGADEAEWVVSRERTTADSTFESLGPVNGYLSGRAAKEHMVKSKLPNSVLGKVWKLADIDKDGQLDADEFALANYLINLKLEGHEIPSELPKHLIPPSKRGEQDPVYPSLNDNDE
Protein: Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 1 (A0A8I5ZXF9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, ruffle {ECO:0000256|ARBA:ARBA00004466}. Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVAIQYTCRHTLNMIQHGSHTVHVWTYFHMRFPLGGDDEVMSSTLQQFSKVIDELSSCHAVLSTQLADAMMFPISQFKERDLKEILTLKEVFQIASNDHDAAINRYSRLSKKRENDKVKYEVTEDVYTSRKKQHQTMMHYFCALNTLQYKKKIALLEPLLGYMQAQISFFKMGSENLNGQLEEFLANIGTSVQNVRREMDGDVETMQQTIEDLEVASDPLYLPDPDPTKFPVNRNLTRKAGYLNARNKTGLVSSTWDRQFYFTQGGNLMSQARGDVAGGLAMDIDNCSVMAVDCEDRRYCFQITSFDGKKSSILQAESKKDHEEWICTINNISKQIYLSENPEETAARVNQSALEAVTPSPSFQQRHESLRPGGQSRPPTARTSSSGSLGSESTNLAALSLDSLVAPDTPIQFDIISPVCEDQPGQAKAFGQGGRRTNPFGESGGSTKSETEDSILHQLFIVRFLGSMEVKSDDHPDVVYETMRQILAARAIHNIFRMTESHLLVTCDCLKLIDPQTQVTRLTFPLPYVVLYATHQENKRLFGFVLRTSGGRSESNLSSVCYIFESNNEGEKVPVTIYHILKEKQQKELSKQKEIEKDLEEQSRLIAASSRPSQSGSEGQLVLSSSQSEESDLGEEGKKRESEA
Protein: External alternative NAD(P)H-ubiquinone oxidoreductase B3, mitochondrial (EC 1.6.5.9) (External alternative NADH dehydrogenase NDB3) (NADH:ubiquinone reductase (non-electrogenic) NDB3) (F4JJJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. Peroxisome {ECO:0000305|PubMed:12972666, ECO:0000305|PubMed:14701923}.
Interaction partners:
- Ubiquinol oxidase 1c, mitochondrial
- Ubiquinol oxidase 1b, mitochondrial
- Ubiquinol oxidase 1a, mitochondrial
- Ubiquinol oxidase 3, mitochondrial
- Acyl-CoA N-acyltransferases
- Small ribosomal subunit protein uS3c
Sequence:
MRPFAYFERLSQAFHDYPSLSKILVVSTISGGGLIVYSEANPSYSNNGVETKTRKRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKQNVEMSFLEAECFKIDPGSKKVYCRSKQGVNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKASLPGLNEQERKRMLHFVVVGGGPTGVEFASELHDFVNEDLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRRALATDEWLRVEGCDNIYALGDCATINQRKVMEDIAAIFKKADKENSGTLTMKEFHEVMSDICDRYPQVELYLKSKGMHGITDLLKQAQAENGSNKSVELDIEELKSALCQVDSQVKLLPATGQVAAQQGTYLAKCFDRMEVCEKNPEGPIRIRGEGRHRFRPFRYRHLGQFAPLGGEQTAAQLPGDWVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSRI
Protein: Ferredoxin-2, chloroplastic (AtFd2) (P16972)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit psaK, chloroplastic
- Plastocyanin minor isoform
- Photosystem I reaction center subunit XI, chloroplastic
- Ferredoxin-thioredoxin reductase catalytic chain, chloroplastic
- Cytochrome b6-f complex iron-sulfur subunit, chloroplastic
- Assimilatory sulfite reductase
Sequence:
MASTALSSAIVGTSFIRRSPAPISLRSLPSANTQSLFGLKSGTARGGRVTAMATYKVKFITPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQIGEGFVLTCAAYPTSDVTIETHKEEDIV
Protein: Putative alanyl-tRNA editing protein alaX (AlaX) (AlaXp) (AlaXp-II) (Alanyl-tRNA deacylase alaX) (P53960)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala).
Interaction partners:
- Valine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, mitochondrial
- Serine--tRNA ligase, mitochondrial
- Glutamate--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
Sequence:
MPTPMTPVKVGALACQRNSFLFDGFKTLVVSCEPTKNKKGEIEGYEIELQDTILFPEGGGQPSDSGFLKIVEGNRNSSKIEKILVSHVSRFGLHAKHHVNDYIEPGTTVEVAVDEQKRMDYMQQHTGQHLLSAILERNYKVDTVSWSMGGIITKKKPVLEPSDYFNYIELNRKLTLDEITNVSDEINQLIINFPQEIIVEERIGEETVDEVSTSKIPDDYDLSKGVLRTIHIGDIDSNPCCGTHLKCTSQIGSILILSNQSAVRGSNSRLYFMCGKRVSLYAKSVNKILLDSKNLLSCSETQISEKITRQTKQIQQLNKREQYWIKRLARTASEELMNTLKASGKKRAYFMEEEYGTLELLLQIHKEVSNFLKDDTEGYEIILCGYERQTNTGSLLILSESGEKIANLAANLGSILQNLKGGGGKKGGKWQGKITSISNAEFAALSDYLSHDFASC
Protein: (R)-2-hydroxyisocaproyl-CoA dehydratase beta subunit (EC 4.2.1.157) (Q5U923)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Function: Involved in the reductive branch of L-leucine fermentation. Catalyzes the irreversible beta/alpha-elimination of water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. This beta/alpha-dehydration depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. The enzyme is specific for the R-isomer.
Interaction partners:
Sequence:
MEAILSKMKEVVENPNAAVKKYKSETGKKAIGCFPVYCPEEIIHAAGMLPVGIWGGQTELDLAKQYFPAFACSIMQSCLEYGLKGAYDELSGVIIPGMCDTLICLGQNWKSAVPHIKYISLVHPQNRKLEAGVKYLISEYKGVKRELEEICGYEIEEAKIHESIEVYNEHRKTMRDFVEVAYKHSNTIKPSIRSLVIKSGFFMRKEEHTELVKDLIAKLNAMPEEVCSGKKVLLTGILADSKDILDILEDNNISVVADDLAQETRQFRTDVPAGDDALERLARQWSNIEGCSLAYDPKKKRGSLIVDEVKKKDIDGVIFCMMKFCDPEEYDYPLVRKDIEDSGIPTLYVEIDQQTQNNEQARTRIQTFAEMMSLA
Protein: Procollagen C-endopeptidase enhancer 2 (Procollagen COOH-terminal proteinase enhancer 2) (PCPE-2) (Procollagen C-proteinase enhancer 2) (Q8R4W6)
Organism: Mus musculus (Mouse)
Function: Binds to the C-terminal propeptide of types I and II procollagens and may enhance the cleavage of that propeptide by BMP1.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MGGASACIPLCLLLATARMARPQTPERPVFTCGGILTGESGFIGSEGFPGMYPPNSKCTWKITVPEGKVVVLNFRFIDLENDNLCRYDFVDVYNGHANGQRIGRFCGTFRPGSLVASGNKMTVQMISDANTAGSGFMATYSAAAPDGKGDRYCGGRLEKPSGTFKTPNWPDRDYPVGVTCVWHIIAPKNQLIELKFEKFDVERDNYCRYDYVAVFNGGEVNDAKRIGKYCGDSPPVPIVSERNELLIQFLSDLSLTADGFIGHYKFRPKKFPTTTTTPVTTTLPVTTGLKPTVALCQQKCRRMGTLESNYCSSNFVLAGTVITTVTRGGSLHATVSIISIYREGNLAIQQAGKNMSVKLTVVCRQCPLLRRGLNYIIMGQVGEDGRGKIMPNSFVKMFKNKNQKPMNALKNKQC
Protein: Secreted chorismate mutase (EC 5.4.99.5) (A0A0D1DWQ2)
Organism: Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis)
Function: Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway. Interfers with the activity of host cytosolic chorismate mutase CM2 through heterodimerization.
Subcellular location: Secreted {ECO:0000269|PubMed:21976020}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:21976020}. Note=Is translocated to host plant cells and spreads to neighboring tissue. The spreading is likely to occur through plasmodesmata. {ECO:0000269|PubMed:21976020}.
Interaction partners:
- Chorismate synthase
- Prephenate dehydrogenase [NADP
- Multifunctional tryptophan biosynthesis protein
- histidinol-phosphate transaminase
- Prephenate dehydratase domain-containing protein
Sequence:
MKLSVSIFVLLAVSAFGGGSAAAVSGKSEAAEIEAGDRLDALRDQLQRYETPIIQTILARSALGGRAPSEQDEVRAALSRNAFEPSEVISEWLQTESGARFRSTRPLPPAVEFITPVVLSRDTVLDKPVVGKGIFPIGRRPQDPTNMDEFLDTSLLSLNQSSTVDLASAVSLDVSLLHLVSARVLLGYPIALAKFDWLHDNFCHILTNTTLSKSQKLANIIQQLTDHKQEVNVLSRVEQKSKSLSHLFRNDIPYPPHTQDRILRLFQAYLIPITTQIEAAAILDHANKCT
Protein: GEO06356p1 (LD28904p) (Ubiquitin-conjugating enzyme variant 1A, isoform A) (Ubiquitin-conjugating enzyme variant 1A, isoform C) (Q9VRL1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- AT16033p
- Ubiquitin-conjugating enzyme E2 N
- E3 ubiquitin-protein ligase sina
- Ubiquitin-conjugating enzyme E2-17 kDa
- LD40663p
- Ubiquitin-conjugating enzyme E2 S
- Ubiquitin-ribosomal protein eS31 fusion protein
- GH01161p
- Death-associated inhibitor of apoptosis 2
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MANTSSTGVVVPRNFRLLEELDQGQKGVGDGTISWGLENDDDMTLTYWIGMIIGPPRTPFENRMYSLKIECGERYPDEPPTLRFITKVNINCINQNNGVVDHRSVQMLARWSREYNIKTMLQEIRRIMTMKENLKLAQPPEGSCF
Protein: Nudix hydrolase 20, chloroplastic (AtNUDT20) (EC 3.6.1.-) (Q8VXZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Bifunctional TH2 protein, mitochondrial
- Thiamine biosynthetic bifunctional enzyme TH1
- mRNA-decapping enzyme-like protein
- Nudix hydrolase
- Mitochondrial thiamine diphosphate carrier 1
- 5-formyltetrahydrofolate cyclo-ligase-like protein COG0212
- Nudix hydrolase 9
- Hydroxyethylthiazole kinase
- Mitochondrial thiamine diphosphate carrier 2
Sequence:
MASGFCSLALTVTTSLFSSHAITRRVLPILRWRSSSMSLSPLRHSRALSAATTVPISSSFTWDDVIETGRAEYNSSDLTGFFEKINRCNRGSEKLGEFIPFVIEEQIVGYIHKRFTEYLREFHDIFTFSQNGSCPDRVDGYVTLNLMLQKPEDRTRAVADVIKILGDKGIIPGIRNELYPVKPSFNAPVFFSLERAAAPYFGIKGYGVHMNGYVERDGQKLLWIGKRSLSKSTYPGMLDHLVAGGLPHGISCGGNLVKECEEEAGISRAIADRAIAVGAVSYLDIDQYCFKRDVLFCYDLELPEDFVPKNQDGEVESFKLIPVAQVASVIKKTSFFKANCSLVIIDFLFRHGFIRPESSGYLDLYQRLRNRDCS
Protein: 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNP) (CNPase) (EC 3.1.4.37) (P13233)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-anchor {ECO:0000250|UniProtKB:P16330}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter. {ECO:0000250|UniProtKB:P16330}.
Interaction partners:
- Myelin basic protein
- Oligodendrocyte transcription factor 2
- Myelin-oligodendrocyte glycoprotein
- Myelin-associated glycoprotein
- Glial fibrillary acidic protein
- Myelin proteolipid protein
- Platelet-derived growth factor receptor alpha
- Oligodendrocyte transcription factor 1
- Galactocerebrosidase
- Transcription factor SOX-10
Sequence:
MSTSFARKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLIVEKYHNGTKMVSADAYKIIPGSRADFSEEYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSLDDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLDLVSYFGKRPPGVLHCTTKFCDYGKATGAEEYAQQDVVRRSYGKAFKLSISALFVTPKTAGAQVVLNEQELQLWPSDLDKPSSSESLPPGSRAHVTLGCAADVQPVQTGLDLLEILQQVKGGSQGEEVGELPRGKLYSLGKGRWMLSLAKKMEVKAIFTGYYGKGKPVPVHGSRKGGAMQICTII
Protein: Cytoplasmic polyadenylation element-binding protein 1 (CPE-BP1) (CPE-binding protein 1) (CPEB-1) (Orb/CPEB-related RNA-binding protein) (Protein Zorba) (ZOR-1) (Zebrafish orb-type a) (Q9YGX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation and early development. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9784598}. Note=Microtubule-associated.
Interaction partners:
- Symplekin
- Cyclin B2
- Aurora kinase A
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK
- V-mos Moloney murine sarcoma viral oncogene homolog
- polynucleotide adenylyltransferase
- Poly
- polynucleotide adenylyltransferase
- B-cell translocation gene 4
Sequence:
MAFSLRENPRLLNCLDSDIPALSTCSNADAFCRMNTMLGNSLDLSGVCTTPTAKCKRDPFNDRPDSDLSAVRSRMLFPSGGQDSSRGLPDVNNWGLGLQSLSLSDWERPWSSHDTDPSVKTNTASLQGILGTPSQLTNKLSNYSDSSIGATDFLEKFPGMARLNSQSFLDSHSISPVDSETSGFSSGSDHLSDLLSSLRISPSVPFLMSSMQRDPLKLALDSRMDHSSSPLTPPPSASPSGSLSHRWPGASIWPSWDLMKTPESPFSIEREAWLHRQAASINEATFTWSGQLPPRHYQNPVYSCKVFLGGVPWDITEAGLINTFKCYGPLSVEWPGKDGKHPRCPPKGNMPKGYVYLVFESDKSVRALLQDCTEDLLHPEGYSEYYFKMSSRRMRCKDAQVIPWVISDSNYVSCPSQRLDPRNTVFVGALHGMLNAEALASIMNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTPKFTKKVQIDPYLEDAICQSCSREPGPFFCRDKTCFKYYCRSCWHRQHSMDILSNHRPLMRNQKKRDAN
Protein: Calcium-independent mitochondrial carrier protein SCaMC-3L (Mitochondrial ATP-Mg/Pi carrier protein SLC25A41) (Small calcium-binding mitochondrial carrier protein 3-like) (SCaMC-3-like) (SCaMC-3L) (Solute carrier family 25 member 41) (Q8BVN7)
Organism: Mus musculus (Mouse)
Function: Calcium-independent ATP-Mg/Pi exchanger that catalyzes the electroneutral exchange of Mg-ATP or free ADP against an hydrogenphosphate and participates in the net transport of adenine nucleotides across the mitochondria inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18928449}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O94502}.
Interaction partners:
- Uncharacterized protein C1orf141 homolog
- NADH-ubiquinone oxidoreductase chain 3
- Transmembrane protein 210
- Cortexin domain containing 2
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
MGVHLEVLDTGEQLMVPVDVLEEENKGTLWKFLLSGAMAGAVSRTGTAPLDRARVYMQVYSSKSNFRNLLSGLRSLVQEGGVRSLWRGNGINVLKIAPEYAIKFSVCEQSKNFFYGVHSSQLFQERVVAGSLAVAVSQTLINPMEVLKTRLTLRFTGQYKGLLDCARQILERDGTRALYRGYLPNMLGIIPYACTDLAVYELLQCLWQKLGRDMKDPSGLVSLSSVTLSTTCGQMASYPLTLVRTRMQAQDTVEGSNPTMQGVFKRILSQQGWPGLYRGMTPTLLKVLPAGGISYLVYEAMKKTLGVQVLSR
Protein: dCTP deaminase (EC 3.5.4.13) (Deoxycytidine triphosphate deaminase) (Q9PN07)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Catalyzes the deamination of dCTP to dUTP.
Interaction partners:
Sequence:
MGLKADNWIRKMALEHKMIEPFCEANIGKGVVSYGLSSYGYDIRVGREFKIFTNVNSTVVDPKNFVEENVVDFEGDVCIVPANSFALARTIEYFKMPDNVLAICLGKSTYARCGIIVNVTPFEPGFEGHITIEISNTTPLPAKIYANEGIAQVLFLQGDEKCDTTYKDKKGKYQAQTGITLPRILK
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (P32131)
Organism: Escherichia coli (strain K12)
Function: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. It can use NAD or NADP, but NAD is preferred.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12114526}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Oxygen-dependent coproporphyrinogen-III oxidase
- Protoporphyrinogen IX dehydrogenase [quinone]
- Outer membrane protein W
- Glutamyl-tRNA reductase
- Der GTPase-activating protein YihI
- Delta-aminolevulinic acid dehydratase
- Ferrochelatase
- Protein HemY
- Glutamate-1-semialdehyde 2,1-aminomutase
Sequence:
MSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIPFCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYLNKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAELNPDRLSVFNYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVAQREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRGIALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDVDEKGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI
Protein: Activity-dependent neuroprotector homeobox b isoform X1 (A0A8M3B615)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MRAHTHLCTSGRRMFQLPVNNLSSLRKARKNVKKVLGDIGLDFCKEHVDDYKDFVPNEFYLKNTTWDDVCMWDPSMTKSQDYRSKPFCCSGCTFSSKFFSAYKSHFRNVHSEDFENRILLNCPYCTYNGNKKTLETHIRLFHMPNVVRQNTGGLHGAGVGLKDGARLEKTRDNIEQAVYYCKKCTYRDPLYNVVRKHIYREHFQHVAAPYLVRPGEKTTTPNGTTAGSGTGSTTDGGVANSMSTAIHCKRCLFVPRTYEALVQHVIEDHERIGYQVTAMIGHTNVVVPRAKPVIMVSPKSQSEKTVGGVMPKSAVVTGVRPLSTQQLSRIVIPKGSLNSSGLLSGVHLKQGVFGLKPGATQSLSIGGQQVQLSIPQQSQTSKPQLSASLRSAVSASASTSILKIPQLNSRVQAAATTVSAVTSKKGNSVIGTSYTQKWKICTICNELFPENVYSSHFEKEHKAEKVPAVANYIMKIHNFTSKCLYCNRYLPSDTLLNHMLIHGLSCPHCRATFNDVEKMVTHMRGVHPNESVGPRTDSPLTFDLTLQQGNPKNVQLIVTTYNMRDAPEESVAFHAQNNALPPSLQGNKQVTPTIPKIPSDASGAMPVKATPQAAVPYKKDIGKTLCPLCFSILKGPISDSLAHHLRDRHQVIQTVHPVEKKLTYKCIHCLGVYTSNMTASTITLHLVHCRGVSKTQNGRPAPSARVVQAQGAGLKRAGLANFDQTEPKRKKPDDQTGQSPSPSTEKHEEPVVFALDPKGYENESYETRKAFLTQYFNKQPYPTRREVEKLASSLWLWKSDIASHFSNRRRRCLLNCETLNTRVLMGFKMEDVLNLDHPLNFDSKCYFQNHKHDHKRRTTRFRIGRSANAILLRQKATTNGDLQQKHEMLPRVSSKALLYSNGQNAIIGSNCFDSVKSTLKSGALVNSEPISVDSDSDNEGNVQDASLTALSLSHEEPATNDKVEGSDSDVRENAHSENGYGSTDLLNETSQQDDECQSGITNKLEQSETQLTEQQV