wanglab/gogpt-training-data huggingface dataset:
Protein: Enhancer of mRNA-decapping protein 4 (Q3UJB9)
Organism: Mus musculus (Mouse)
Function: In the process of mRNA degradation, seems to play a role in mRNA decapping. Component of a complex containing DCP2 and DCP1A which functions in decapping of ARE-containing mRNAs. Promotes complex formation between DCP1A and DCP2. Enhances the catalytic activity of DCP2 (in vitro).
Subcellular location: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q6P2E9}. Nucleus {ECO:0000250|UniProtKB:Q6P2E9}.
Interaction partners:
- mRNA-decapping enzyme 1A
- m7GpppN-mRNA hydrolase
- Protein PAT1 homolog 1
- Enhancer of mRNA-decapping protein 3
- Probable ATP-dependent RNA helicase DDX6
- mRNA-decapping enzyme 1B
- 5'-3' exoribonuclease 1
- Protein PAT1 homolog 2
- Protein LSM14 homolog A
- Nonsense-mediated mRNA decay factor SMG5
Sequence:
MASCASIDIEDATQHLRDILKLDRPAGGSNAESQRPSSAYNGDLNGLLVPDPLSSGDGNSTNKPGIRTMPPINLQEKQVICLSGDDSSTCIGILAKEVEIVASSDSSISSKARGSNKVKIQPVAKYDWEQKYYYGNLIAVSNSFLAYAIRAANNGSAMVRVISVSTSERTLLKGFTGSVADLAFAHLNSPQLACLDEAGNLFVWRLALVKGKIQEEILVHIRQPEGTALNHFRRIIWCPFIPEESEDCCEESSPTVALLHEDRAEVWDLDMLRSSHNTWPVDVSQIKQGFIVVKGHSTCLSEGALSPDGTVLATASHDGFVKFWQIYIEGQDEPRCLHEWKPHDGRPLSCLLFCDNHKKQDPEVPFWRFLITGADQNRELKMWCTVSWTCLQTIRFSPDIFSSVSVPPSLKVCLDLSAEYLILSDVQRKVLYVMELLQNQDEGRACFSSISEFLLTHPVLSFGIQVVSRCRLRHTEVLPAEEENDSLGTESSHGAGALESAAGVLIKLFCVHTKALQDVQIRFQPQLNPDVVAPLSTHTAHEDFTFGESRPELGSEGLASAAHGSQPDLRRIVELPAPADFLSLSSETKPELMTPDAFMTPTASLQQISASPSSSSSSSSSSSSSSSSSSSSLTAVSAVSSSSAMDPSLPRPPEELTLSPKLQLDGSLTLNSSSSSLQASPRSLLPGLLPGPADKLISKGPGQVSTAASALSLDLQEVEPLGLPQASPSRTRSPDVISSASTALSQDIPEIASEALSRGFGSSVPEGLIEPNSMASAASALHLLSPRPRQGPELGSQLGLDGGPGDGDRHSTPSLLEAALTQEVATPDSQVWPTAPDITRETCSTLTESPRNGLQEKHKSLAFHRPPYHLLQQRDSQDTSAEQSDHDDEVASLASASGGFGSKIPTPRLPSKDWKTKGSPRTSPKLKRKSKKDDGDSAVGSRLTEHQVAEPPEDWPALIWQQQRELAELWHNQEELLQRLCAQLEGLQSTVTDHVERALETRHEQEQRRLERALAEGQQRGGQLQEQLTQQLSQALSSAVAGRLERSVRDEIKKTVPPCVSRSLEPVAGQLSNSVATKLTAVEGSMKENISKLLKSKNLTDAIARAAADTLQGPMQAAYREAFQSVVLPAFEKSCQAMFQQINDSFRLGTQEYLQQLESHMKSRKAREQEAREPVLAQLRGLVSTLQSATEQMAATVSSSVRAEVQHQLHVAVGSLQESILAQVQRIVKGEVSVALKEQQATVTSSIMQAMRSAAGTPVPSAHLDCQAQQAHILQLLQQGHLNQAFQQALTAADLNLVLYVCETVDPAQVFGQPPCPLSQPVLLSLIQQLASDLGTRSDLKLSYLEEAVMHLDHSDPITRDHMGSVMAQVRQKLFQFLQADPHNSLSKAARRLSLMLHGLVTPSLP
Protein: CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase (EC 2.4.3.6) (Beta-galactoside alpha-2,3-sialyltransferase 3) (Alpha 2,3-ST 3) (Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase) (N-acetyllactosaminide alpha-2,3-sialyltransferase) (ST3Gal III) (ST3GalIII) (ST3N) (Sialyltransferase 6) (Q11203)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc.
Subcellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Interaction partners:
- mRNA turnover protein 4 homolog
Sequence:
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRLGFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARIREFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDDYDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLKYIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIPTLGSVAVTMALHGCDEVAVAGFGYDMSTPNAPLHYYETVRMAAIKESWTHNIQREKEFLRKLVKARVITDLSSGI
Protein: MIP04751p (Q9VKP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MTNMKQRLRNLFRRNKMRARPTTVASDANKEQPEPPKQEPSKQKKTKQDASKQEPPKQEEPEKPPKEVEVEIIPSPTSEGEMPTYFHVGALAKDCLINGFKIGAWQMHCSTRTDNDFYLNTFGEGYPTMKNVFGGMEVFKEVGNYSTSLGWFTNNDLLSEIAVRGMNFGSRLYGLLKSTIGTKDEVSFQTKLKCGLERDPVKVELVVPLYNEPLFLGYVLVAPVENWVLGYRTEYNFDEKGFDKHALCLGYNNGRTEVGLKLENFEDLRGSIFQRIGEAWAFAIKTNLYSSENVKQFAIGVQYDFQNGTMVKAKLREDSRMGFVYQSKIGENIDVGYHLAFDGVDPIGGAHRIGVSWGFHC
Protein: Protein COLD-REGULATED 15A, chloroplastic (AtCOR15A) (Q42512)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits cryoprotective activity toward stromal substrates (e.g. LDH and rubisco) in chloroplasts and in protoplasts and confers freezing tolerance to plants in a CBF-dependent manner. Protectant against various stresses (e.g. cold, drought and heat stress) by preventing protein aggregation (e.g. LDH) and attenuating enzyme inactivation. Influences the intrinsic curvature of the inner membrane of the chloroplast envelope, and modulates the freeze-induced lamellar-to-hexagonal II phase transitions that occur in regions where the plasma membrane is brought into close apposition with the chloroplast envelope during freeze-induced osmotic contraction. Mediates a shift in the melting curves of phospholipids-containing membranes to lower temperatures. Involved in the regulation of leaf senescence by abscisic acid (ABA) in a VNI2-dependent manner.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16668917, ECO:0000269|PubMed:17384167, ECO:0000269|PubMed:8685269}.
Interaction partners:
- Low-temperature-induced 78 kDa protein
- Stress-induced protein KIN2
- Dehydrin COR47
- Low-temperature-induced 65 kDa protein
- Dehydration-responsive element-binding protein 1B
- Dehydration-responsive element-binding protein 1A
- Dehydrin ERD10
- Kinesin-like protein KIN-1
- Dehydration-responsive element-binding protein 1C
- BURP domain protein RD22
Sequence:
MAMSFSGAVLTGMASSFHSGAKQSSFGAVRVGQKTQFVVVSQRKKSLIYAAKGDGNILDDLNEATKKASDFVTDKTKEALADGEKAKDYVVEKNSETADTLGKEAEKAAAYVEEKGKEAANKAAEFAEGKAGEAKDATK
Protein: Cysteine desulfurase, mitochondrial (EC 2.8.1.7) (tRNA-splicing protein SPL1) (P25374)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10406803, ECO:0000269|PubMed:10551871}.
Interaction partners:
- Frataxin homolog, mitochondrial
- Thiosulfate sulfurtransferase TUM1
- Iron sulfur cluster assembly protein 1, mitochondrial
- Protein ISD11
- Iron sulfur cluster assembly protein 2, mitochondrial
- Adrenodoxin homolog, mitochondrial
- Adenylyltransferase and sulfurtransferase UBA4
- NifU-like protein
- Acyl carrier protein, mitochondrial
- J-type co-chaperone JAC1, mitochondrial
Sequence:
MLKSTATRSITRLSQVYNVPAATYRACLVSRRFYSPPAAGVKLDDNFSLETHTDIQAAAKAQASARASASGTTPDAVVASGSTAMSHAYQENTGFGTRPIYLDMQATTPTDPRVLDTMLKFYTGLYGNPHSNTHSYGWETNTAVENARAHVAKMINADPKEIIFTSGATESNNMVLKGVPRFYKKTKKHIITTRTEHKCVLEAARAMMKEGFEVTFLNVDDQGLIDLKELEDAIRPDTCLVSVMAVNNEIGVIQPIKEIGAICRKNKIYFHTDAAQAYGKIHIDVNEMNIDLLSISSHKIYGPKGIGAIYVRRRPRVRLEPLLSGGGQERGLRSGTLAPPLVAGFGEAARLMKKEFDNDQAHIKRLSDKLVKGLLSAEHTTLNGSPDHRYPGCVNVSFAYVEGESLLMALRDIALSSGSACTSASLEPSYVLHALGKDDALAHSSIRFGIGRFSTEEEVDYVVKAVSDRVKFLRELSPLWEMVQEGIDLNSIKWSGH
Protein: Ephrin type-A receptor 3 (EC 2.7.10.1) (EPH-like kinase 4) (EK4) (rEK4) (Tyrosine-protein kinase TYRO4) (O08680)
Organism: Rattus norvegicus (Rat)
Function: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ephrin-A5
- Ephrin A2
- Ephrin-A1
- Ephrin-A3
- Tyrosine-protein kinase
- Ephrin-A4
- Ephrin B2
- Ephexin-1
- Ras GTPase-activating protein 1
- Tyrosine-protein kinase.
Sequence:
MDCHLSILILFGCCVLSCSRELSPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFLEHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCTCNAGYEERGFICQACRPGFYKALDGVAKCTKCPPHSSTQEDGSMNCRCENNYFRAEKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDITFNIICKKCGWNVRQCEPCSPNVRFLPRQLGLTNTTVTVTDLLAHTNYTFEIDAINGVSELSSPPRQFAAVSITTNQAAPSPVMTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTTYVFQIRARTAAGYGTNSRKFEFENSPDSFSISGENSHVVMIAISAAVAIIVLTVVTYVLVGRFCGYHKSKHSSDEKRLHFGNGHLRLPGLRTYVDPHTYEDPTQAVHEFAKELDATNIAIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPVRWTSPEATAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPLPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDIATFHTTGDWLNGMRTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV
Protein: RecBCD enzyme subunit RecD (EC 5.6.2.3) (DNA 5'-3' helicase subunit RecB) (Exodeoxyribonuclease V 67 kDa polypeptide) (Exodeoxyribonuclease V alpha chain) (Exonuclease V subunit RecD) (ExoV subunit RecD) (Helicase/nuclease RecBCD subunit RecD) (P04993)
Organism: Escherichia coli (strain K12)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. In the holoenzyme this subunit contributes ssDNA-dependent ATPase and fast 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD.
Interaction partners:
- RecBCD enzyme subunit RecC
- RecBCD enzyme subunit RecB
- Protease 3
- ATP-dependent DNA helicase RecQ
- Protein RecA
- Single-stranded-DNA-specific exonuclease RecJ
- DNA replication and repair protein RecF
- DNA helicase II
- ATP-dependent DNA helicase RecG
- Recombination protein RecR
Sequence:
MKLQKQLLEAVEHKQLRPLDVQFALTVAGDEHPAVTLAAALLSHDAGEGHVCLPLSRLENNEASHPLLATCVSEIGELQNWEECLLASQAVSRGDEPTPMILCGDRLYLNRMWCNERTVARFFNEVNHAIEVDEALLAQTLDKLFPVSDEINWQKVAAAVALTRRISVISGGPGTGKTTTVAKLLAALIQMADGERCRIRLAAPTGKAAARLTESLGKALRQLPLTDEQKKRIPEDASTLHRLLGAQPGSQRLRHHAGNPLHLDVLVVDEASMIDLPMMSRLIDALPDHARVIFLGDRDQLASVEAGAVLGDICAYANAGFTAERARQLSRLTGTHVPAGTGTEAASLRDSLCLLQKSYRFGSDSGIGQLAAAINRGDKTAVKTVFQQDFTDIEKRLLQSGEDYIAMLEEALAGYGRYLDLLQARAEPDLIIQAFNEYQLLCALREGPFGVAGLNERIEQFMQQKRKIHRHPHSRWYEGRPVMIARNDSALGLFNGDIGIALDRGQGTRVWFAMPDGNIKSVQPSRLPEHETTWAMTVHKSQGSEFDHAALILPSQRTPVVTRELVYTAVTRARRRLSLYADERILSAAIATRTERRSGLAALFSSRE
Protein: 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5) (Q9WVJ2)
Organism: Mus musculus (Mouse)
Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.
Interaction partners:
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-1
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit alpha type-2
Sequence:
MKDVPAFLQQSQSSGPGQAAVWHRLEELYTKKLWHQLTLEVLDFVQDPCFAQGDGLIKLYENFISEFEHRVNPLSLVEIILHVVRQMTDPNVALTFLEKTREKVKSSDEAVILCKTAIGALKLNIGDLQATKETIEDVEEMLNNLPGVTSVHSRFYDLSSKYYQTIGNHASYYKDALRFLGCVDIKDLPVSEQQERAFTLGLAGLLGEGVFNFGELLMHPVLESLRDTDRQWLIDTLYAFNSGAVDRFQTLKCAWGQQPDLAANEAQLLRKIQLLCLMEMTFTRPANHRQLTFEEIAKSAKITVNKVELLVMKALSVGLVRGSIDEVDKRVHMTWVQPRVLDLQQIKGMKDRLELWCTDVKSMEMLVEHQAQDILT
Protein: Protein INVOLVED IN DE NOVO 2 (Protein RNA-DIRECTED DNA METHYLATION 12) (Q8VZ79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a complex with FDM1/IDNL1 and FDM2/IDNL2 that is required for RNA-directed DNA methylation (RdDM) and that functions at a downstream step of the RdDM pathway and downstream of small interfering RNA (siRNA) formation. Required for de novo DNA methylation, siRNA accumulation and siRNA-mediated maintenance methylation. Required for several post-transcriptional gene silencing pathways. Binds double-stranded RNAs (dsRNAs) with 5'-overhangs through its XS domain. Binds long non-coding RNA (lncRNA) in an AGO4-dependent manner and associates with DRM2, resulting in DNA methylation of RdDM target loci. Mediates the silencing of a subset of MORC6 target loci.
Interaction partners:
- Protein RNA-directed DNA methylation 3
- SWI/SNF complex subunit SWI3B
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- DNA-directed RNA polymerase V subunit 1
- Protein RDM1
- DNA
- Protein CHROMATIN REMODELING 35
- Histone-lysine N-methyltransferase family member SUVH9
- Protein MICRORCHIDIA 6
- Histone-lysine N-methyltransferase family member SUVH2
Sequence:
MGSTVILSSDDEDSDISESEMDEYGDKMYLNLKGGKLKVRLSPQAFICPYCPNKKKTSFQYKDLLQHASGVGNSNSDKRSAKEKASHLALVKYLQQDLADSASEAEPSSKRQKNGNPIQDCDHDEKLVYPWKGIVVNIPTTKAQDGRSAGESGSKLRDEYILRGFNPTRVRPLWNYLGHSGTAIVEFNKDWNGLHNGLLFDKAYTVDGHGKKDWLKKDGPKLGLYGWIARADDYNGNNIIGENLRKTGDLKTIAELTEEEARKQELLVQNLRQLVEEKKKDMKEIEELCSVKSEELNQLMEEKEKNQQKHYRELNAIQERTMSHIQKIVDDHEKLKRLLESERKKLEIKCNELAKREVHNGTERMKLSEDLEQNASKNSSLELAAMEQQKADEEVKKLAEDQRRQKEELHEKIIRLERQRDQKQAIELEVEQLKGQLNVMKHMASDGDAEVVKEVDIIFKDLGEKEAQLADLDKFNQTLILRERRTNDELQEAHKELVNIMKEWNTNIGVKRMGELVTKPFVDAMQQKYCQQDVEDRAVEVLQLWEHYLKDSDWHPFKRVKLENEDREVEVIDDRDEKLRELKADLGDGPYNAVTKALLEINEYNPSGRYITTELWNFKADKKATLEEGVTCLLDQWEKAKRKRGMA
Protein: G-box-binding factor (GBF) (P36417)
Organism: Dictyostelium discoideum (Social amoeba)
Function: cAMP-responsive transcriptional activator regulating late gene expression. Essential component of the developmental switch between early and late development. Binds to a number of CA/GT-rich gene regulatory elements.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Tiger protein C1
- UTP--glucose-1-phosphate uridylyltransferase 2
Sequence:
MLSTHHHQGNSSSSSSSSSPSQTIGGSDLSNISALPLPLPSIFTTAQNQMNPPILFPPTSSLLGGSSNTPSFLLPPSSIMSSNVFPSHDGQYPDMPNMVDQYQIHPNQNPHYNYQYQLMFMQQQAQQNQPPQQNQQQQHHQQQQQQPQHHQQMQQQQHHQQMQQQQQHHQQMQQQQHHQQMQHHQLQQHQHQHQQQQQQQQHQQQHHQQQQQQQQQHHQQQQHHQHSQPQQQHQHNQQQQHQHNQQQHQQQQNQIQMVPQQPQSLSNSGNNNNNNNNNNNSNNNNNNNNNNNSHQLNNLTLSQNNTSGSNTPSPSTKGKRKHHETSNSEKKDSSGQTIPKCTRCNEAASWKHDKRRWWCKECKKAFTPGITKMQQVPQQAQLQPLQNHNQIIPQLWDSQQNNSSQNTPPTQPQNNMNQINHQLLQQQHQQAQLQAHLNLTASNQQVPPQLQQQINGGLPNNNNSLITQNTLNSLSTSVSCPPCPLCRGISSWKHDKKRYFCKECKKPFTPVGAGLSPSSSPSSPKKKSNITPITTSSTSSSSSTPSIINNNNNNNANSSKNNTPKKQLSPPPSVLQSPSSSSISQSPLQLNYQTPTYSPNPSLPSIGGNLNSLANSIKPDGGILISGLSPPKSSSSLNNLNSFSNTGALLSSNGINLANLGNPLSQLNKKQKKRSDKDINDGGVQVLVSCVDTNVNNCSSIIPDGDSW
Protein: Peroxisomal acyl-coenzyme A oxidase 1 (AOX) (EC 1.3.3.6) (Palmitoyl-CoA oxidase) (Peroxisomal fatty acyl-CoA oxidase) (Straight-chain acyl-CoA oxidase) (SCOX) [Cleaved into: Peroxisomal acyl-CoA oxidase 1, A chain; Peroxisomal acyl-CoA oxidase 1, B chain; Peroxisomal acyl-CoA oxidase 1, C chain] (Q15067)
Organism: Homo sapiens (Human)
Function: Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids. Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)).
Subcellular location: Peroxisome {ECO:0000269|PubMed:32169171}.
Interaction partners:
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal bifunctional enzyme
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Sterol carrier protein 2
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MNPDLRRERDSASFNPELLTHILDGSPEKTRRRREIENMILNDPDFQHEDLNFLTRSQRYEVAVRKSAIMVKKMREFGIADPDEIMWFKKLHLVNFVEPVGLNYSMFIPTLLNQGTTAQKEKWLLSSKGLQIIGTYAQTEMGHGTHLRGLETTATYDPETQEFILNSPTVTSIKWWPGGLGKTSNHAIVLAQLITKGKCYGLHAFIVPIREIGTHKPLPGITVGDIGPKFGYDEIDNGYLKMDNHRIPRENMLMKYAQVKPDGTYVKPLSNKLTYGTMVFVRSFLVGEAARALSKACTIAIRYSAVRHQSEIKPGEPEPQILDFQTQQYKLFPLLATAYAFQFVGAYMKETYHRINEGIGQGDLSELPELHALTAGLKAFTSWTANTGIEACRMACGGHGYSHCSGLPNIYVNFTPSCTFEGENTVMMLQTARFLMKSYDQVHSGKLVCGMVSYLNDLPSQRIQPQQVAVWPTMVDINSPESLTEAYKLRAARLVEIAAKNLQKEVIHRKSKEVAWNLTSVDLVRASEAHCHYVVVKLFSEKLLKIQDKAIQAVLRSLCLLYSLYGISQNAGDFLQGSIMTEPQITQVNQRVKELLTLIRSDAVALVDAFDFQDVTLGSVLGRYDGNVYENLFEWAKNSPLNKAEVHESYKHLKSLQSKL
Protein: Chloride channel accessory 3A2 (A0A0G2JFW5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XGPSAARELETLSDMTGGLRFYANKHVSSLIDAFSRISSTSGSVSQQALQLESKAFNVRAGAWINSTVPVDSTVGNDTFFVITWTVQKPEIILQDPKGKKYITSDFQDDELNIRSARLQIPGTAETGTWTYSITGTKSQLITMTVTTRARSPTMEPLLATAHMSQSTAQYPSRMIVYVRVSQGFLPVLGANVTAIIEAEHGHQVTLELWDNGAGKIVLNPPRPDVQEEAIEATVEDFNRVTSGGSFTVSGAPPD
Protein: Magnesium transporter MgtE (Q5SMG8)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Highly selective magnesium channel that plays an important role in Mg(2+) homeostasis. Functions as a Mg(2+)-dependent gating channel. Exhibits low activity with cobalt, suggesting that it might also be involved in the uptake of Co(2+) as a micronutrient. Also exhibits low activity with Ca(2+), but it shows almost no activity with Mn(2+).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:25367295}; Multi-pass membrane protein {ECO:0000269|PubMed:17700703, ECO:0000269|PubMed:19798051, ECO:0000269|PubMed:25367295}.
Interaction partners:
Sequence:
MEEKLAVSLQEALQEGDTRALREVLEEIHPQDLLALWDELKGEHRYVVLTLLPKAKAAEVLSHLSPEEQAEYLKTLPPWRLREILEELSLDDLADALQAVRKEDPAYFQRLKDLLDPRTRAEVEALARYEEDEAGGLMTPEYVAVREGMTVEEVLRFLRRAAPDAETIYYIYVVDEKGRLKGVLSLRDLIVADPRTRVAEIMNPKVVYVRTDTDQEEVARLMADYDFTVLPVVDEEGRLVGIVTVDDVLDVLEAEATEDIHKLGAVDVPDLVYSEAGPVALWLARVRWLVILILTGMVTSSILQGFESVLEAVTALAFYVPVLLGTGGNTGNQSATLIIRALATRDLDLRDWRRVFLKEMGVGLLLGLTLSFLLVGKVYWDGHPLLLPVVGVSLVLIVFFANLVGAMLPFLLRRLGVDPALVSNPLVATLSDVTGLLIYLSVARLLLEAV
Protein: BZIP domain-containing protein (A7RFN4)
Organism: Nematostella vectensis (Starlet sea anemone)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
AYGRDKDQKYIEKRMKNNLAAKRSREAKRQREIEAMQKTLTLEKENSDLNKEVNKLKKMIARLENKLR
Protein: At4g13790 (SAUR-AC-like protein (Small auxin up RNA)) (SAUR-like auxin-responsive protein family) (Q9SVN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Auxin-responsive family protein
- At5g50760
Sequence:
MAFLRSFFATKHIIRRSFTTESLSTPKGFFAVYVGENLKKKRYLVPVCYLNKPSFQALLRKAEEEFGFNHPTGGLSLPCDEAFFFTVTSQIR
Protein: Formate transporter FocA (Q9KRE7)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- Carbonic anhydrase
Sequence:
MEHNQFDSLLPPQMAERAAITGEGKAKKAAYKSFLLAISAGIQIGIAFVFYTVVTTGAHDMPYGVTKLLGGLAFSLGLILVVITGGELFTSSVLILVAKASGKISWKELVRNWTVVYFGNLCGSIILVFIMLATRQFMEDGGQLGLNAMAISQHKLHHTFLQAFALGLMCNILVCLAVWMTFSARSLTDKVMVLILPVAMFVSSGFEHCIANMFQVPMAIGIKYFAPESFWAMTGANIAQYADLNFVNFIVNNLIPVTLGNIVGGGVFVGMWYWLIYLKD
Protein: Protein-L-isoaspartate O-methyltransferase domain-containing protein 2 (Q9NV79)
Organism: Homo sapiens (Human)
Function: May act as a substrate recognition component of an ECS (Elongin BC-CUL5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. May bind to the methyltransferase cofactor S-adenosylmethionine (AdoMet) via the N-terminal AdoMet binding motif, but probably does not display methyltransferase activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P22061}.
Interaction partners:
- Cullin-5
Sequence:
MGGAVSAGEDNDELIDNLKEAQYIRTELVEQAFRAIDRADYYLEEFKENAYKDLAWKHGNIHLSAPCIYSEVMEALDLQPGLSFLNLGSGTGYLSSMVGLILGPFGVNHGVELHSDVIEYAKQKLDFFIRTSDSFDKFDFCEPSFVTGNCLEISPDCSQYDRVYCGAGVQKEHEEYMKNLLKVGGILVMPLEEKLTKITRTGPSAWETKKILAVSFAPLIQPCHSESGKSRLVQLPPVAVRSLQDLARIAIRGTIKKIIHQETVSKNGNGLKNTPRFKRRRVRRRRMETIVFLDKEVFASRISNPSDDNSCEDLEEERREEEEKTPPETKPDPPVNFLRQKVLSLPLPDPLKYYLLYYREK
Protein: Prosaposin receptor GPR37 (Endothelin B receptor-like protein 1) (ETBR-LP-1) (G-protein coupled receptor 37) (Parkin-associated endothelin receptor-like receptor) (PAELR) (O15354)
Organism: Homo sapiens (Human)
Function: Receptor for the neuroprotective and glioprotective factor prosaposin. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade.
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:25977097}. Synapse {ECO:0000269|PubMed:25977097}. Cell membrane {ECO:0000269|PubMed:17059562, ECO:0000269|PubMed:25977097, ECO:0000269|PubMed:26869225}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17059562}; Multi-pass membrane protein {ECO:0000269|PubMed:17059562}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Prosaposin
- Alpha-synuclein
- Synphilin-1
- Sodium-dependent dopamine transporter
- E3 ubiquitin-protein ligase CHIP
- Interleukin-8
- Somatostatin receptor type 1
- G-protein coupled receptor 37-like 1
Sequence:
MRAPGALLARMSRLLLLLLLKVSASSALGVAPASRNETCLGESCAPTVIQRRGRDAWGPGNSARDVLRARAPREEQGAAFLAGPSWDLPAAPGRDPAAGRGAEASAAGPPGPPTRPPGPWRWKGARGQEPSETLGRGNPTALQLFLQISEEEEKGPRGAGISGRSQEQSVKTVPGASDLFYWPRRAGKLQGSHHKPLSKTANGLAGHEGWTIALPGRALAQNGSLGEGIHEPGGPRRGNSTNRRVRLKNPFYPLTQESYGAYAVMCLSVVIFGTGIIGNLAVMCIVCHNYYMRSISNSLLANLAFWDFLIIFFCLPLVIFHELTKKWLLEDFSCKIVPYIEVASLGVTTFTLCALCIDRFRAATNVQMYYEMIENCSSTTAKLAVIWVGALLLALPEVVLRQLSKEDLGFSGRAPAERCIIKISPDLPDTIYVLALTYDSARLWWYFGCYFCLPTLFTITCSLVTARKIRKAEKACTRGNKRQIQLESQMNCTVVALTILYGFCIIPENICNIVTAYMATGVSQQTMDLLNIISQFLLFFKSCVTPVLLFCLCKPFSRAFMECCCCCCEECIQKSSTVTSDDNDNEYTTELELSPFSTIRREMSTFASVGTHC