wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor TCP18 (Protein BRANCHED 1) (Protein TEOSINTE BRANCHED 1-LIKE 1) (A1YKT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that prevents axillary bud outgrowth and delays early axillary bud development. Indirectly required for the auxin-induced control of apical dominance.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00701, ECO:0000269|PubMed:17307924}.
Interaction partners:
- Homeobox-leucine zipper protein ATHB-53
- Transcription factor TCP19
- Protein SPEAR4
- Transcription factor TCP20
- Protein TWIN SISTER of FT
- Protein SPEAR2
- Putative high mobility group B protein 11
- Zinc finger AN1 and C2H2 domain-containing stress-associated protein 11
- Tubulin-tyrosine ligase
- Transcription factor TCP22
Sequence:
MNNNIFSTTTTINDDYMLFPYNDHYSSQPLLPFSPSSSINDILIHSTSNTSNNHLDHHHQFQQPSPFSHFEFAPDCALLTSFHPENNGHDDNQTIPNDNHHPSLHFPLNNTIVEQPTEPSETINLIEDSQRISTSQDPKMKKAKKPSRTDRHSKIKTAKGTRDRRMRLSLDVAKELFGLQDMLGFDKASKTVEWLLTQAKPEIIKIATTLSHHGCFSSGDESHIRPVLGSMDTSSDLCELASMWTVDDRGSNTNTTETRGNKVDGRSMRGKRKRPEPRTPILKKLSKEERAKARERAKGRTMEKMMMKMKGRSQLVKVVEEDAHDHGEIIKNNNRSQVNRSSFEMTHCEDKIEELCKNDRFAVCNEFIMNKKDHISNESYDLVNYKPNSSFPVINHHRSQGAANSIEQHQFTDLHYSFGAKPRDLMHNYQNMY
Protein: Lymphoid enhancer-binding factor 1 (LEF-1) (P27782)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds DNA in a sequence-specific manner (By similarity). Participates in the Wnt signaling pathway. Activates transcription of target genes in the presence of CTNNB1 and EP300. PIASG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1. TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 (By similarity). Regulates T-cell receptor alpha enhancer function (By similarity). Required for IL17A expressing gamma-delta T-cell maturation and development, via binding to regulator loci of BLK to modulate expression. May play a role in hair cell differentiation and follicle morphogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10498690}. Note=Found in nuclear bodies upon PIASG binding.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Catenin beta-1
- Four and a half LIM domains protein 2
- Serine/threonine-protein kinase NLK
- Junction plakoglobin
- Transcription factor SOX-17
- Mothers against decapentaplegic homolog 2
- Histone lysine acetyltransferase CREBBP
- Axin-2
- C-terminal-binding protein 1
Sequence:
MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVRQAPSSQEPYHDKAREHPDEGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSDVNSKQGMSRHPPAPEIPTFYPLSPGGVGQITPPIGWQGQPVYPITGGFRQPYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI
Protein: Gastrotropin (GT) (Fatty acid-binding protein 6) (Ileal lipid-binding protein) (ILBP) (P51162)
Organism: Mus musculus (Mouse)
Function: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes. Stimulates gastric acid and pepsinogen secretion (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P80020}. Membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P50119}; Cytoplasmic side {ECO:0000250|UniProtKB:P50119}.
Interaction partners:
- Bile acid receptor
- Fatty acid-binding protein, intestinal
- Ileal sodium/bile acid cotransporter
- Organic solute transporter subunit alpha
- Organic solute transporter subunit beta
- Fatty acid-binding protein, heart
- Bile salt export pump
- Fatty acid-binding protein 9
- Fibroblast growth factor 15
Sequence:
MAFSGKYEFESEKNYDEFMKRLGLPGDVIERGRNFKIITEVQQDGQDFTWSQSYSGGNIMSNKFTIGKECEMQTMGGKKFKATVKMEGGKVVAEFPNYHQTSEVVGDKLVEISTIGDVTYERVSKRLA
Protein: Aluminum-activated malate transporter 9 (AtALMT9) (Q9LS46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar malate channel. Has a higher selectivity for malate than for fumarate. Exhibits also a weak chloride conductance.
Subcellular location: Vacuole membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tonoplast dicarboxylate transporter
- Chloride channel protein CLC-c
- S-type anion channel SLAH1
- Sodium/hydrogen exchanger 1
- Chloride channel protein CLC-a
- GDSL esterase/lipase At1g33811
- Guard cell S-type anion channel SLAC1
- GDSL esterase/lipase At5g18430
- S-type anion channel SLAH3
Sequence:
MAAKQGSFRHGILEKRERLLSNNGFSDFRFTDIESNDLLENENCGRRTRLCCCCSCGNLSEKISGVYDDAKDVARKAWEMGVSDPRKIVFSAKIGLALTIVALLIFYQEPNPDLSRYSVWAILTVVVVFEFTIGATLSKGFNRALGTLSAGGLALGMAELSTLFGDWEEIFCTLSIFCIGFLATFMKLYPSMKAYEYGFRVFLLTYCYILISGFRTGQFIEVAISRFLLIALGAGVSLGVNMFIYPIWAGEDLHNLVVKNFMNVATSLEGCVNGYLRCLEYERIPSKILTYQASEDPVYKGYRSAVESTSQEESLMSFAIWEPPHGPYKSFNYPWKNYVKLSGALKHCAFTVMALHGCILSEIQAPEERRQVFRQELQRVGVEGAKLLRELGEKVKKMEKLGPVDLLFEVHLAAEELQHKIDKKSYLLVNSECWEIGNRATKESEPQELLSLEDSDPPENHAPPIYAFKSLSEAVLEIPPSWGEKNHREALNHRPTFSKQVSWPARLVLPPHLETTNGASPLVETTKTYESASALSLATFASLLIEFVARLQNVVDAFKELSQKANFKEPEIVTTGTDVEFSGERVGLGQKIRRCFGM
Protein: Uncharacterized transporter C323.07c (Q9UT92)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKRFFSKLFSKSPTSGRVPSPDSDYSEEEQRLLAEENGYFQDSNEYVEPNIPAVYGSMIPVAQQLQQHHVHTPGESFADNASGYPVIKHELSELLRLGSPTVIAYLLQSSEQFSTVFTLGHLGKEYLAASSLSTMTAAISAFSIFQGVISSLDTLATQAFGANKPYNVAIYLQRCLLILAVLHIPVALIWLNLEHILIFLHQDPMVAHLCGRYMRVFILAAPGYAVFEALKRYLQAQGIFTPITYVLCFAAPLNILLNYLLVWHPTIGFGFLGAPVAVATTFWFQSICLILYICFSSTPIPWPGFSRQALKNLSPMLHFSFHGMLMIVTEWAAYEMTSLGAGYLGTAPLASQSILLTSTSLLFQIPFAFAVASSTRVGHLIGSGRANLARLCSRVAYSLALCISIFDGSLIFCFRDVWGSLFTSDPEVLAVVKDIFPILSLFIVTDGLNAVGGGLLRGTGKQYIGGLISIGSSYLFALPVTVFVVVYFNTGLKGIWCGMILSSVTAITCQFTVLFNTDWHRVLQEARHRLTHV
Protein: Periodic tryptophan protein 1 homolog (PWP1) (Protein no child left behind) (A1Z8D0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chromatin-associated factor that regulates transcription. Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription. Regulates the localization to the nucleolus of Cdk7, a regulator of the Pol I-elongation factor TFIIH. Acts as regulator of cell proliferation and tissue growth as part of the TORC1 and Myc signaling pathway in response to nutrients. Required in males for both germline stem cell (GSC) maintenance and early stages of germ cell differentiation of germ cell cysts. Not required for female germline stem cell (GSC) maintenance, but necessary to regulate germ cell differentiation and egg chamber development. In female somatic cells, required for follicle stem cell survival and maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:21752937}. Nucleus, nucleolus {ECO:0000269|PubMed:29065309}. Chromosome {ECO:0000269|PubMed:21752937}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29065309}. Note=Co-localizes with active forms of RNA polymerase II (PubMed:21752937). Associates with open chromatin and chromosomal puffs of polytene chromosomes in larval salivary glands (PubMed:21752937). Nucleolar localization is controlled by mTORC1 signaling (PubMed:29065309). {ECO:0000269|PubMed:21752937, ECO:0000269|PubMed:29065309}.
Interaction partners:
- Ribosome biogenesis protein BRX1 homolog
- Probable rRNA-processing protein EBP2 homolog
- Glutamate-rich WD repeat-containing protein 1
- RRM domain-containing protein
- LD47550p
- Ribosome production factor 2 homolog
- Ribosomal L1 domain-containing protein CG13096
- RRM domain-containing protein
- Nucleolar GTP-binding protein 2
- GH01043p
Sequence:
MAEEGPPEPSIDFVPALCFVPRGVAKDRPDKIVLTQAELARIIGDTQQELDEESDDDAEEGENAEEDQNDMDVDDHADANSENRDPQDEFQFQEYDNEANANVTSLANIVDAGEQIPDEDEDSEAEDEVIKPSDNLILVGHVQDDAASMEVWVFNQEEEALYTHHDFLLPSFPLCIEWMNHDAGSEKAGNMCAIGCMDPIITVWDLDIQDAIEPTFKLGSKGSRKQNKEQYGHKDAVLDLSWNTNFEHILASGSVDQTVILWDMDEGQPHTTITAFGKQIQSLEFHPQEAQSILTGCADGYVRLFDCRDAEGVNSSSIEWKVDGEVEKVLWHPTQTDYFIVGTNDGTLHYADKRSPGQLLWSVKAHNEEISGVCFNNQKPNLLTSTSTEGTLKVWNFDGTEAKHVYEHEFNMGRLQCMRQCPEDPYTLAFGGEKPPRCAIFNIKNSIAVRRTFGIPDAE
Protein: Stac-like, isoform S (A0A0B4LFG4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGISAHAAPASFWNHPRRIRRTPTSDRDGVDQCRPWICRRKDRRPAHPAANRPPESRVCGPSSTFRWDDWAAPAPRTRERATDCARMCMCTSRIPYSVARICARTTSMHSSRPASRSSSFIRRPLTRRQRMAVGGVTRRLWRTMRVYTIHQGRGVRRARAAQAVAAYLRDRRARIGKGWPAQGHGVRISATEQWADKPVVRRPGDPTRRVAAGAVPVLAERLPKVTGSSVKSSSGRRSRRRRIFGWRGPRGGSLSPQGGSMASYNGVLKDYSHSSLNEAFKSQNNVNFKLIKTVSDFSETLSRLYEEHATALQVAVSNYRKKNAELRKERPACHLAIFQAWETFLQEVETDSQACNDVASVLSRQVSRPMLDKSFHRKVQSRKIFTHRESFETIIAKTEEKLSKCRVDYKQCHLAHRQNPSQHSLTEYIDAHNAYVQQLHATNGMLEAYHTDTLPQQMQELEEIHNDLVAIVSDSLMQGAEVIAGKANDQAKRYNSLSNQCAAVSPQQDLVNFVRLLAQPSQAQKIPRRLFASPQAEVGEEAGDHNEMTPCLRNELVFDRHSTLSQRSALESLKREAIELELQIRQLQDSIEALNRTQTRGIEGQLYNKVNELQEDLSMKKFDLRAKQIHLAAIRAQKDLFVSKVEPTSPRNERKFSAATAPSMKTKWLKAFKSLKPAGSGSAQQADRRNGASSTASEPLRPNLDGSHHLQEYTYKKITACDVCSQILRGHTRQGLRCRICKLNAHGDCAPNLPRCQPKQKLLRRQKSTSELENRVDIEEETGADKSVQAKQMDGSVAGGSALPVPVLSERELGRAPPPDIPIVSVSELALQEQQQQQQQQQQQHQQQQRSLASVAQAAAVRAGRGVRPPPVAMPILGVQLQQQELQQQRGGLPVPSQDISSSSASANPKSETTRPFGEPLMLLKSTESNPDESKGNRRVR
Protein: E3 ubiquitin-protein ligase makorin-2 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase makorin-2) (B0F0H3)
Organism: Xenopus laevis (African clawed frog)
Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (By similarity). Inhibits neurogenesis and axis formation during embryonic development by modulating the phosphatidylinositol 3-kinase (PI3K) pathway. Acts downstream of PI3K and akt1 to up-regulate gsk3b mRNA expression.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9ERV1}. Nucleus {ECO:0000250|UniProtKB:Q9ERV1}.
Interaction partners:
Sequence:
MSPKQVTCRYFLHGVCREGSRCLFSHDLATSKPSTVCRFFLRGQCAYGTRCRYDHVKPCNGTVFIPPQEMSPVLSPPPLFPAQEAAVPPTIPAPQRREKKTLVLRDRDLCGASVDPALQPGCITESQGSEGEAKPHSYLEAICTGLDESQDPASYPGAPQQLCPFAQAGECHCGDSCPYLHGDACEICGLQVLHPHDQEQRRDHEKLCMENFELDMERAFAVQASEGRVCSICMERVYEKQSPAQRRFRILSDCNHTYCLTCIRQWRCARQFDNPVIKSCPECRVISEFVIPSAYWVEDQSKKDELIEAFKQGMGKKLCKYFDQGRGTCPFGGKCLYLHSYPDGTRAQPEKPRKQLGSEGSVRFLNSLRLWDFIEDREQRGVPNAEVGKLGELFMHLSGADEELPAPFN
Protein: Delta-TIP homolog (O48875)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
LPLGGQITILTGIFYWIAQLLGSIVACFLLKAVTGGLTVPIHGLGAGVGAIQGVVMEIIITFALVYTVYATAADPKKGSLGTIAPIAIGFIVGANILAAGPFSGG
Protein: GATA zinc finger domain containing 2A (C9JGN4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTEEACRTRSQKRALERDPTEDDVESKKIKMERGLLASDLNTDGDMRVTPEPGAGPTQGLLRATEATAMAMGRGEGLVGDGPVDMRTSHSDMKSERRPPSPDVIVLSDNEQPSSPRVNGLTTVALKETSTEALMKSSPE
Protein: Forkhead box protein F1 (A1L1S5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTAEVQQPSVQTPAHSSPMTEKPVQTPVMETSSSSSSTKAKKTNAGIRRPEKPPYSYIALIVMAIQSSPTKRLTLSEIYQFLQSRFPFFRGSYQGWKNSVRHNLSLNECFIKLPKGLGRPGKGHYWTIDPASEFMFEEGSFRRRPRGFRRKCQALKPSMYSMMNGLGFNHIPESYNFQGGGGGLSCPPNSLSLESGIGMMNGHLASNMEGMGLAGHSMPHLSTNSGHSYMGSCTGSSGTEYPHHDSSASPLLTSGGVMDPHAVYSSTASAWPSAPPTSLNNGTSYIKQQPLSPCNPGASSLQPSLPTHSLEQSYLHQNGHGTTDLQGIPRYHTQSPSMCDRKEFVFSFNAMTSSSMHSPGSSSYYHHQQVSYQDIKPCVM
Protein: Matrix protein 2 (BM2) (Q5V9A4)
Organism: Influenza B virus (B/Maryland/1/2001)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004224}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004224}. Virion membrane {ECO:0000256|ARBA:ARBA00004462}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004462}.
Interaction partners:
Sequence:
MLEPFQILSICSFILSALHFMAWTIGHLNQIKRGVNMKIRIKGPNKETINREVSILRHSYQKEIQAKETMKEVLSDNMEVLSDHIVIEGLSAEEIIKMGETVLEIEELH
Protein: Tubulin alpha-1C chain (EC 3.6.5.-) (Alpha-tubulin 6) (Tubulin alpha-6 chain) [Cleaved into: Detyrosinated tubulin alpha-1C chain] (Q9BQE3)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta chain
- Tubulin beta-3 chain
- Tubulin beta-2A chain
- Tubulin beta-4B chain
- Tubulin alpha-1B chain
- Tubulin beta-6 chain
- Tubulin beta-8 chain
- Tubulin beta-4A chain
- Tubulin beta-2B chain
- Tubulin beta-1 chain
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSADGEDEGEEY
Protein: Acyl-coenzyme A thioesterase 4, mitochondrial (Acyl-CoA thioesterase 4) (HlTE4) (EC 3.1.2.-) (2-methylbutanoyl-CoA hydrolase TE4) (EC 3.1.2.-) (2-methylpropanoyl-CoA hydrolase TE4) (EC 3.1.2.-) (3-methylbutanoyl-CoA hydrolase TE4) (EC 3.1.2.-) (Acyl-CoA thioester hydrolase 4) (Butanoyl-CoA hydrolase TE4) (EC 3.1.2.-) (Propanoyl-CoA hydrolase TE4) (EC 3.1.2.-) (S4TF94)
Organism: Humulus lupulus (European hop)
Function: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on acyl CoAs with short chains (propanoyl-CoA and butanoyl-CoA), branched short chains (2-methylpropanoyl-CoA, 2-methylbutanoyl-CoA and 3-methylbutanoyl-CoA) and medium chains (octanoyl-CoA).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23300257}.
Interaction partners:
Sequence:
MMTPIGIRIRKQIPLSYHYSSIQALLSRFTPTPYNPISNSSSSTQTIPTQFHESQCTNPISRPTVFLFDPPPIRFTHTKSFSTDPSSLDFPSNQPPVVSTISSHHNISQPIDAGSSIRKPISLWPGMFNSPVTNALWEARSNMFEKYGEPTADPPSQSELVTKSPAQSRTSILYNLSSDYALREHYRNPWNMIRIGKLLEDLDALAGTIAFKHCTNEDGMSRPLLLVTASVDKMVLKKPISIDTDLSIVGAVTWVGRSSMEIQLQVLQTTHESSDPSDSVSLVANFTFVARDSKTGKSAVINQISPETGEEKLLWREADERNKMRKMKRKIQKDLELEKQYIERLNALLAEGRVFCDLPALADRNSILMKDTCLENSFICQPQQRNIYGRIFGGFLMRRAVELAFSTTYSFAGVVTHFLEVDHVDFLRPVDVGDFLRLKSCVLYTELQNPTEPLINVEVVAHVTRPELRSSEVSNKFYFTFSVGPEAVKDGLLVRNVVPATEEEARRVLERMDAETPHPHSQYENEI
Protein: Xylosyl- and glucuronyltransferase LARGE2 (EC 2.4.-.-) (Glycosyltransferase-like 1B) (LARGE xylosyl- and glucuronyltransferase 2) [Includes: Alpha-1,3-xylosyltransferase LARGE2 (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE2 (EC 2.4.1.-)] (Q8N3Y3)
Organism: Homo sapiens (Human)
Function: Bifunctional glycosyltransferase with both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain-containing extracellular proteins with high affinity and in a phosphorylated-O-mannosyl trisaccharide dependent manner. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By similarity). Supports the maturation of DAG1 more effectively than LARGE1. In addition, can modify both heparan sulfate (HS)- and chondroitin/dermatan sulfate (CS/DS)-proteoglycans (PGs), namely GPC4, with a glycosaminoglycan (GAG)-like polysaccharide composed of xylose and glucuronic acid to confer laminin binding (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15661757}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-glucuronyltransferase 1
- Dystroglycan 1
- Xylosyl- and glucuronyltransferase LARGE1
- Ribitol-5-phosphate transferase FKTN
- Protein O-mannosyl-transferase 1
- Protein O-mannosyl-transferase 2
- Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1
- Ribitol 5-phosphate transferase FKRP
Sequence:
MLPRGRPRALGAAALLLLLLLLGFLLFGGDLGCERREPGGRAGAPGCFPGPLMPRVPPDGRLRRAAALDGDPGAGPGDHNRSDCGPQPPPPPKCELLHVAIVCAGHNSSRDVITLVKSMLFYRKNPLHLHLVTDAVARNILETLFHTWMVPAVRVSFYHADQLKPQVSWIPNKHYSGLYGLMKLVLPSALPAELARVIVLDTDVTFASDISELWALFAHFSDTQAIGLVENQSDWYLGNLWKNHRPWPALGRGFNTGVILLRLDRLRQAGWEQMWRLTARRELLSLPATSLADQDIFNAVIKEHPGLVQRLPCVWNVQLSDHTLAERCYSEASDLKVIHWNSPKKLRVKNKHVEFFRNFYLTFLEYDGNLLRRELFVCPSQPPPGAEQLQQALAQLDEEDPCFEFRQQQLTVHRVHVTFLPHEPPPPRPHDVTLVAQLSMDRLQMLEALCRHWPGPMSLALYLTDAEAQQFLHFVEASPVLAARQDVAYHVVYREGPLYPVNQLRNVALAQALTPYVFLSDIDFLPAYSLYDYLRASIEQLGLGSRRKAALVVPAFETLRYRFSFPHSKVELLALLDAGTLYTFRYHEWPRGHAPTDYARWREAQAPYRVQWAANYEPYVVVPRDCPRYDPRFVGFGWNKVAHIVELDAQEYELLVLPEAFTIHLPHAPSLDISRFRSSPTYRDCLQALKDEFHQDLSRHHGAAALKYLPALQQPQSPARG
Protein: Transcription factor COE3 (Early B-cell factor 3) (EBF-3) (Olf-1/EBF-like 2) (O/E-2) (OE-2) (Q9H4W6)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:28017373}.
Interaction partners:
- Zinc finger protein 423
Sequence:
MFGIQENIPRGGTTMKEEPLGSGMNPVRSWMHTAGVVDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVEKEKEPNNEKTNNGIHYKLQLLYSNGVRTEQDLYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEGTAPSYLENATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSYKSKQFCKGAPGRFVYTALNEPTIDYGFQRLQKVIPRHPGDPERLPKEVLLKRAADLVEALYGMPHNNQEIILKRAADIAEALYSVPRNHNQIPTLGNNPAHTGMMGVNSFSSQLAVNVSETSQANDQVGYSRNTSSVSPRGYVPSSTPQQSNYNTVSTSMNGYGSGAMASLGVPGSPGFLNGSSANSPYGIVPSSPTMAASSVTLPSNCSSTHGIFSFSPANVISAVKQKSAFAPVVRPQASPPPSCTSANGNGLQAMSGLVVPPM
Protein: Mediator of RNA polymerase II transcription subunit 15 (Mediator complex subunit 15) (Positive cofactor 2 glutamine/Q-rich-associated protein) (PC2 glutamine/Q-rich-associated protein) (mPcqap) (Q924H2)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 24
Sequence:
MDVSGQETDWRSAAFRQKLVSQIEDAMRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPTPGAAGIGMPPRGPGQSLGGMGGLGAMGQPLPLSGQPPPGTSGMAPHGMAVVSTATPQTQLQLQQVALQQQQQQQQQQQFQQQQAALQQQQQQQQQQQQQQQFQAQQNAMQQQFQAVVQQQQLQQQQQQQHLIKLHHQSQQQQIQQQQLQRMAQLQLQQQQQQQQQQALQAQPPMQQPSMQQPQPPPSQALPQQLSQLHHPQHHQPPPQAQQSPIAQNQPPQIPPQSQSQPLVSQAQALPGPMLYAAQQQLKFVRAPMVVQQPQVQPQVQQVQPQVQPQAAVQAAQSAQMVAPGVQMIAEALAQGGMHVRARFPPTSTMSAGPSSSISLGGQPTTQVSQSSLTMLSSPSPGQQVQTPQSMPPPPQPSPQPGSQPNSNVSSGPAPSPSSFLPSPSPQPSQSPVTARTPQNFSVPSPGPLNTPVNPSSVMSPAGSSQAEEQQYLDKLKQLSKYIEPLRRMINKIDKNEDRKKDLSKMKSLLDILTDPSKRCPLKTLQKCEIALEKLKNDMAVPTPPPPPVLPTKQQDLCQPLLDAVLANIRSPVFNHSLYRTFVPAMMAIHGPPIVSPVVCSRKRRFEEDERQSIPNVLQGEVARLDPKFLVNLDPSHCSNNGTVHLICKLDDKDLPSVPPLELSVPADYPAQSPMWIDRQWQYDANPFLQSVHRCMTSRLLQLPDKHSVTALLNTWAQSIHQACLSAA
Protein: Long-chain-fatty-acid--CoA ligase heimdall (EC 6.2.1.3) (Very long-chain-fatty-acid--CoA ligase double bubble) (Q9V3U0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Probably by regulating lipid storage and catabolism, plays a role in neuronal function.
Interaction partners:
- long-chain-fatty-acid--CoA ligase
- Very long-chain-fatty-acid--CoA ligase bubblegum
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2 homolog
- carnitine O-palmitoyltransferase
- Long-chain-fatty-acid--CoA ligase
- Fatty acid synthase
- Fatty acid synthase
- Fatty acid synthase
- Stumps, isoform E
Sequence:
MNDLKPATSYRSTSLHDAVKLRLDEPSSFSQTVPPQTIPEFFKESCEKYSDLPALVWETPGSGNDGWTTLTFGEYQERVEQAALMLLSVGVEERSSVGILAFNCPEWFFAEFGALRAGAVVAGVYPSNSAEAVHHVLATGESSVCVVDDAQQMAKLRAIKERLPRLKAVIQLHGPFEAFVDHEPGYFSWQKLQEQTFSSELKEELLARESRIRANECAMLIFTSGTVGMPKAVMLSHDNLVFDTKSAAAHMQDIQVGKESFVSYLPLSHVAAQIFDVFLGLSHAGCVTFADKDALKGTLIKTFRKARPTKMFGVPRVFEKLQERLVAAEAKARPYSRLLLARARAAVAEHQTTLMAGKSPSIYGNAKYWLACRVVKPIREMIGVDNCRVFFTGGAPTSEELKQFFLGLDIALGECYGMSETSGAITLNVDISNLYSAGQACEGVTLKIHEPDCNGQGEILMRGRLVFMGYLGLPDKTEETVKEDGWLHSGDLGYIDPKGNLIISGRLKELIITAGGENIPPVHIEELIKKELPCVSNVLLIGDHRKYLTVLLSLKTKCDAKTGIPLDALREETIEWLRDLDIHETRLSELLNIPADLQLPNDTAALAATLEITAKPKLLEAIEEGIKRANKYAISNAQKVQKFALIAHEFSVATGELGPTLKIRRNIVHAKYAKVIERLYK
Protein: Chymotrypsin inhibitor Ani s 6 (allergen Ani s 6) (A1IKL3)
Organism: Anisakis simplex (Herring worm)
Function: Inhibits alpha-chymotrypsin, but not trypsin.
Subcellular location: Secreted {ECO:0000305|PubMed:17180690}.
Interaction partners:
Sequence:
MFQSTFFLVLMVCVATARFANKDHCPPNEEYNECGNPCQEKCDNGEPVICTYQCEHRCFCKQGYVRLTEDGECVPEEFCKPIHY