wanglab/gogpt-training-data huggingface dataset:
Protein: Glycosaminoglycan xylosylkinase (EC 2.7.1.-) (Xylose kinase) (O75063)
Organism: Homo sapiens (Human)
Function: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O-phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT-I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19473117}; Single-pass type II membrane protein {ECO:0000269|PubMed:19473117}.
Interaction partners:
- Xylosyltransferase 1
- Golgi-associated kinase 1A
- Exostosin-like 2
- Beta-1,3-galactosyltransferase 6
Sequence:
MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELAPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAVMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDHVVEGEPYAGYDRHNAEVAAFHLDRILGFHRAPLVVGRFVNLRTEIKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDIMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLDERSILAPLYQCCIIRVSTWNRLNYLKNGVLKSALKSAMAHDPISPVLSDPHLDAVDQRLLSVLATVKQCTDQFGMDTVLVEDRMPLSHL
Protein: 3-oxosteroid 1-dehydrogenase (EC 1.3.99.4) (3-keto-Delta(4)-steroid Delta(1)-dehydrogenase) (KSDD) (3-oxo-Delta(4)-steroid 1-dehydrogenase) (KSTD) (Q7D5C1)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Function: Involved in the degradation of cholesterol. Catalyzes the elimination of the C-1 and C-2 hydrogen atoms of the A-ring from the polycyclic ring structure of 3-ketosteroids (By similarity). Is also involved in the formation of 3-keto-1,4-diene-steroid from 3-keto-4-ene-steroid (By similarity).
Interaction partners:
Sequence:
MFYMTVQEFDVVVVGSGAAGMVAALVAAHRGLSTVVVEKAPHYGGSTARSGGGVWIPNNEVLKRRGVRDTPEAARTYLHGIVGEIVEPERIDAYLDRGPEMLSFVLKHTPLKMCWVPGYSDYYPEAPGGRPGGRSIEPKPFNARKLGADMAGLEPAYGKVPLNVVVMQQDYVRLNQLKRHPRGVLRSMKVGARTMWAKATGKNLVGMGRALIGPLRIGLQRAGVPVELNTAFTDLFVENGVVSGVYVRDSHEAESAEPQLIRARRGVILACGGFEHNEQMRIKYQRAPITTEWTVGASANTGDGILAAEKLGAALDLMDDAWWGPTVPLVGKPWFALSERNSPGSIIVNMSGKRFMNESMPYVEACHHMYGGEHGQGPGPGENIPAWLVFDQRYRDRYIFAGLQPGQRIPSRWLDSGVIVQADTLAELAGKAGLPADELTATVQRFNAFARSGVDEDYHRGESAYDRYYGDPSNKPNPNLGEVGHPPYYGAKMVPGDLGTKGGIRTDVNGRALRDDGSIIDGLYAAGNVSAPVMGHTYPGPGGTIGPAMTFGYLAALHIADQAGKR
Protein: GMP reductase (EC 1.7.1.7) (Guanosine 5'-monophosphate reductase) (GMPR) (P9WKI3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the purine-salvage pathway. Catalyzes the NADPH-dependent conversion of GMP to IMP. Has no inosine-5'-monophosphate dehydrogenase (IMPDH) activity.
Interaction partners:
- GMP synthase
- Uncharacterized oxidoreductase Rv3410c
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase
- Bifunctional purine biosynthesis protein PurH
- Hypoxanthine-guanine phosphoribosyltransferase
- dITP/XTP pyrophosphatase
- Nucleoside triphosphate pyrophosphohydrolase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Transcriptional regulator BlaI
Sequence:
MMRFLDGHPPGYDLTYNDVFIVPNRSEVASRFDVDLSTADGSGTTIPVVVANMTAVAGRRMAETVARRGGIVILPQDLPIPAVKQTVAFVKSRDLVLDTPVTLAPDDSVSDAMALIHKRAHGVAVVILEGRPIGLVRESSCLGVDRFTRVRDIAVTDYVTAPAGTEPRKIFDLLEHAPVDVAVLTDADGTLAGVLSRTGAIRAGIYTPATDSAGRLRIGAAVGINGDVGAKARALAEAGVDVLVIDTAHGHQVKTLDAIKAVSALDLGLPLAAGNVVSAEGTRDLLKAGANVVKVGVGPGAMCTTRMMTGVGRPQFSAVLECASAARQLGGHIWADGGIRHPRDVALALAAGASNVMIGSWFAGTYESPGDLMRDRDDQPYKESYGMASKRAVVARTGADNPFDRARKALFEEGISTSRMGLDPDRGGVEDLIDHITSGVRSTCTYVGASNLAELHERAVVGVQSGAGFAEGHPLPAGW
Protein: dTDP-glucose 4,6-dehydratase 1 (EC 4.2.1.46) (P37759)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction.
Interaction partners:
- Glucose-1-phosphate thymidylyltransferase 1
- dTDP-4-dehydrorhamnose reductase
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase 2
- Putative O-antigen transporter
- UDP-galactopyranose mutase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- Lipopolysaccharide biosynthesis protein WzxC
- Lipid III flippase
- UDP-glucose 6-dehydrogenase
Sequence:
MKILVTGGAGFIGSAVVRHIINNTQDSVVNVDKLTYAGNRESLADVSDSERYVFEHADICDAPAMARIFAQHQPDAVMHLAAESHVDRSITGPAAFIETNIVGTYVLLEAARNYWSALDSDKKNSFRFHHISTDEVYGDLPHPDEVNNTEELPLFTETTAYAPSSPYSASKASSDHLVRAWKRTYGLPTIVTNCSNNYGPYHFPEKLIPLVILNALEGKALPIYGKGDQIRDWLYVEDHARALYTVVTEGKAGETYNIGGHNEKKNIDVVLTICDLLDEIVPKEKSYREQITYVADRPGHDRRYAIDAEKIGRALGWKPQETFESGIRKTVEWYLSNTKWVDNVKSGAYQSWIEQNYEGRQ
Protein: G9a, isoform A (EC 2.1.1.355, EC 2.1.1.356, EC 2.1.1.367, EC 2.1.1.368, EC 2.1.1.369, EC 2.1.1.371) (LD10743p) (Q95RU8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MTDFVELMNSMSSTFNSDCATSTAEGGTLLNLNLAEDKTLKWRNLANNQFASKEKKHKDKEEEERKEARNQEEIEDIKALLADVVDAAAVKLEEEEAQNAEKVEPHTKCEIEEEGRKEMEYDQDVAKQDSEMEKKQNGKATSITVKMESNERAEKHATEIATTSTERWENESFKTEQQNKKAAEKEEEPILAATQKLEANAEPLTTTRIEVAVASPLVVSSASVKLAADATNQMRAATSAGAATLADKNVQVSPGGTRRSRRTPRPIDTPTSVTDEHVQVENKKFGKSEQYTDCSSHLERFTLDDNTAIVRLQLKSEPDKPSLTALSPEENSAPAPKRGRGRARKIRPDAEVETSEVILPCEDSLGEKKPGRKRKLPDEPIDQQQLSDLVVVKTEQEELGDAPLGDVKRMRRSVRLGNRLHADGSPWEEVKTEALHPQPSAELSFAEVTSEILPLAVLDEKTPPKKRGRKAKTPCVKLESETSCGLPFANGNKKTNSSGGCELQLPKRSKRRIKPTPKILENDELRCEFETKHIERMTQWESAAAVDGDFETPTTGGNGSNSSTSRQKSDKSDGSNFEGGPGHPAGTSAIKKRLFSKSQRDIENYGAAMLAKSKLPPCPDVEQFLNDIKASRINANRSPEERKLNKKQQRKLAKQKEKHLKHLGLQKNHRDEPSDNDSSNTDNEFFPTTRVQVGKPSVTLRVRNSVTKELPTTATLKSRRNPVVQAAKLTRRIGARAAGEVTEAARASVPISTPDAEQLHSLDTSIQADVTPIRDLDMRPSTSRVSKFICLCQKPSQYYARNAPDSSYCCAIDHIDDQKIGCCNELSSEVHNLLRPSQRVSYMILCDEHKKRLQSHNCCAGCGIFCTQGKFVLCKQQHFFHPDCAQRFILSTSYEKELGDEEDQGVKFSSPVLVLKCPHCGLDTPERTSTVTMKCQSLPVFLRTQKYKIKPARLTTSSHLTQFGTVENANTPGATARNKGGLSTAVTLSAASSPASKTNGAQRGRAGTSNSNSRHALNSINFAQLIPESVMNVVLRGHVVSASGRVTAEFTPRDMYYAVQNDDLERVAEILAADFNVLTPIREYLNGTCLHLVAHSGTLQMAYLLLCKGASSPDFVNIVDYELRTALMCAVMNEKCDMLNLFLQCGADVAIKGPDGKTSLHIAAQLGNLEATQLIVDSYRTSRNITSFLSFIDAQDEGGWTAMVWAAELGHTDIVSFLLNQDADPNICDNDNNTVLHWSTLHNDGLDTITVLLQSGADCNVQNVEGDTPLHIACRHSVTRMCIALIANGADLMIKNKAEQLPFDCIPNEESECGRTVGFNMQMRSFRPLGLRTFVVCADASNGREARPIQVVRNELAMSENEDEADSLMWPDFRYVTQCIIQQNSVQIDRRVSQMRICSCLDSCSSDRCQCNGASSQNWYTAESRLNADFNYEDPAVIFECNDVCGCNQLSCKNRVVQNGTRTPLQIVECEDQAKGWGVRALANVPKGTFVGSYTGEILTAMEADRRTDDSYYFDLDNGHCIDANYYGNVTRFFNHSCEPNVLPVRVFYEHQDYRFPKIAFFSCRDIDAGEEICFDYGEKFWRVEHRSCVGCRCLTTTCKYASQSSSTNASPTNATTAPENETGTLSSTNTEKIGHA
Protein: HTH-type transcriptional regulator DicA (Repressor protein of division inhibition gene dicA) (P06966)
Organism: Escherichia coli (strain K12)
Function: This protein is a repressor of division inhibition gene dicB.
Interaction partners:
- Repressor protein of division inhibition gene dicB
- Division inhibition protein DicB
- DNA-binding transcriptional repressor RacR
- Uncharacterized protein YdfA
Sequence:
METKNLTIGERIRYRRKNLKHTQRSLAKALKISHVSVSQWERGDSEPTGKNLFALSKVLQCSPTWILFGDEDKQPTPPVEKPVALSPKELELLELFNALPESEQDTQLAEMRARVKNFNKLFEELLKARQRTNKR
Protein: Phosphatidylglycerophosphatase A (EC 3.1.3.27) (Phosphatidylglycerolphosphate phosphatase A) (PGP phosphatase A) (P18200)
Organism: Escherichia coli (strain K12)
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:21148555}; Multi-pass membrane protein {ECO:0000269|PubMed:21148555}.
Interaction partners:
- Phosphatidylglycerophosphatase C
- Phosphatidylglycerophosphatase B
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Cardiolipin synthase C
- Cardiolipin synthase A
- Cardiolipin synthase B
- Phosphatidylserine decarboxylase proenzyme
- Thiamine-monophosphate kinase
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
Sequence:
MTILPRHKDVAKSRLKMSNPWHLLAVGFGSGLSPIVPGTMGSLAAIPFWYLMTFLPWQLYSLVVMLGICIGVYLCHQTAKDMGVHDHGSIVWDEFIGMWITLMALPTNDWQWVAAGFVIFRILDMWKPWPIRWFDRNVHGGMGIMIDDIVAGVISAGILYFIGHHWPLGILS
Protein: Pre-mRNA-processing factor 31 (O42904)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for spliceosome assembly where it is needed to link the U4/U6XU5 tri-snRNP to the prespliceosome complexes.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 13 kDa ribonucleoprotein-associated protein
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor brr2
- Uncharacterized WD repeat-containing protein C227.12
- Pre-mRNA-splicing factor spp42
- U4/U6.U5 tri-snRNP-associated protein snu66
- U4/U5/U6 small nuclear ribonucleoprotein prp3
- Pre-mRNA-splicing factor cwf10
- Uncharacterized protein C1782.03
- LSM2-LSM8 complex subunit lsm8
Sequence:
MSLADELLADLDDIEETTESTITDELGPDAKKRRLELQLEEGNGISAELENDLDITKISDSAQKLPSEVANKFNDNNENIYQLLNSTRLRDIIEGTEKYKGTEKQAITGNIEDDLEYHLIVDSNSIAMEIDDEILRLHRLVKEWYHDRFPELSSLVLNAFDYCKTVSSLLNDLDNSKTKLSFLPSATVMVIATTATTTVGKPLPDEMIKNVKNCCEAIQQLGEEKQKIIEYVQSRISVVAPNLSAVVGSTTAANLIGIAGGLTRLGKFPACNLPALGKRRLTTIGINNPAVSGDYGFLYMSEIVQKTPPDVRKQAIRMTAAKVALAARIDSIHEYPDGSFGISARKEVERKIEKLLEPPSQKPTVALPVPDDRPKRRRGGRRIRKMKEQYAVTELRRLQNRVAFGKEEAEVFNFDETEGLGMLGQEGEGKIRAVSIDSRTKLRLPKARKAQLQSMAQKNPLAASGLQSSLSFTPIQGIELVNPLLQRQQKVEEANKWFRDGVFTQIKKDSNEPKNKFS
Protein: Ubiquinol oxidase 1, mitochondrial (EC 1.10.3.11) (Alternative oxidase 1) (Q07185)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane.
Interaction partners:
- Cytochrome P450 77A3
- Cytochrome P450 77A3
- 18 kDa Sin3-associated polypeptide
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
- Malate dehydrogenase, chloroplastic
- Uncharacterized protein
Sequence:
MMMMMSRSGANRVANTAMFVAKGLSGEVGGLRALYGGGVRSESTLALSEKEKIEKKVGLSSAGGNKEEKVIVSYWGIQPSKITKKDGTEWKWNCFSPWGTYKADLSIDLEKHMPPTTFLDKMAFWTVKVLRYPTDVFFQRRYGCRAMMLETVAAVPGMVAGMLLHCKSLRRFEHSGGWFKALLEEAENERMHLMTFMEVAKPKWYERALVITVQGVFFNAYFLGYLLSPKFAHRMFGYLEEEAIHSYTEFLKELDKGNIENVPAPAIAIDYWQLPPGSTLRDVVMVVRADEAHHRDVNHFASDIHYQGRELREAAAPIGYH
Protein: Dynein light chain (Q57Z05)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU365010}.
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain, putative
- Dynein light chain, putative
- Uncharacterized protein
- Dynein light chain roadblock
- Dynein light chain 2B, cytoplasmic, putative
- Dynein light chain 2B, cytoplasmic, putative
- Dynein light chain roadblock
- Dynein light chain roadblock
- Dynein heavy chain, cytosolic, putative
Sequence:
MSKHHEFNINADMTKEMQEEARNLVIQAFETESLENGVASFVKREFQKKYKGIWHCVVGKNFGSFVTHEMKGYIYMTWGPLSILLWKTVT
Protein: Beta-glucuronidase (EC 3.2.1.31) (P12265)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the degradation of dermatan and keratan sulfates.
Subcellular location: Lysosome {ECO:0000269|PubMed:2394691}. Endoplasmic reticulum {ECO:0000269|PubMed:2394691}. Note=A small proportion is found in the endoplasmic reticulum.
Interaction partners:
- N-acetylglucosamine-6-sulfatase
- Klotho
- UDP-glucuronosyltransferase 2A3
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase
Sequence:
MSLKWSACWVALGQLLCSCALALKGGMLFPKESPSRELKALDGLWHFRADLSNNRLQGFEQQWYRQPLRESGPVLDMPVPSSFNDITQEAALRDFIGWVWYEREAILPRRWTQDTDMRVVLRINSAHYYAVVWVNGIHVVEHEGGHLPFEADISKLVQSGPLTTCRITIAINNTLTPHTLPPGTIVYKTDTSMYPKGYFVQDTSFDFFNYAGLHRSVVLYTTPTTYIDDITVITNVEQDIGLVTYWISVQGSEHFQLEVQLLDEGGKVVAHGTGNQGQLQVPSANLWWPYLMHEHPAYMYSLEVKVTTTESVTDYYTLPIGIRTVAVTKSKFLINGKPFYFQGVNKHEDSDIRGKGFDWPLLVKDFNLLRWLGANSFRTSHYPYSEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNESLRHHLEVMEELVRRDKNHPAVVMWSVANEPSSALKPAAYYFKTLITHTKALDLTRPVTFVSNAKYDADLGAPYVDVICVNSYFSWYHDYGHLEVIQPQLNSQFENWYKTHQKPIIQSEYGADAIPGIHEDPPRMFSEEYQKAVLENYHSVLDQKRKEYVVGELIWNFADFMTNQSPLRVIGNKKGIFTRQRQPKTSAFILRERYWRIANETGGHGSGPRTQCFGSRPFTF
Protein: Four and a half LIM domains 1 (Q5JXI2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASHRHSGPSSYKVGTMAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKGLVKAPVWWPMKDNPGTTTASTAKNAP
Protein: Transcriptional repressor scratch 2 (Scratch homolog 2 zinc finger protein) (Q8BTH6)
Organism: Mus musculus (Mouse)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPRSFLVKKIKADGFQCSGVSAPTYHPLETAYVLPGTRGPPGDNGYVAHCLPPSGYDGEQKPGLELAPAEPAYPAAASEEYSDPESPQSSLSARYFRGEAAVTDSYSMDAFFISDGRSRRRRAGAGGDAAGAGDAGGGGGGGGGGERAGRSGATAGGGHRHACAECGKTYATSSNLSRHKQTHRSLDSQLARKCPTCGKAYVSMPALAMHVLTHNLRHKCGVCGKAFSRPWLLQGHMRSHTGEKPFGCAHCGKAFADRSNLRAHMQTHSAFKHYRCRQCDKSFALKSYLHKHCEAACVKAAEPPPSAGPAS
Protein: Protein SLM4 (EGO complex subunit 3) (GSE complex subunit 1) (P38247)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Component of the EGO complex, a complex involved in the regulation of microautophagy.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15989961, ECO:0000269|PubMed:29698392}; Single-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15989961}.
Interaction partners:
- Protein EGO2
- GTP-binding protein GTR1
- Protein MEH1
- GTP-binding protein GTR2
- Protein LTV1
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit delta
- Guanine nucleotide exchange factor subunit RIC1
Sequence:
MVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYATSNNDVPKNSINEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTYEMEDLHTCVAQIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLG
Protein: DNA (cytosine-5)-methyltransferase 3-like (Q9CWR8)
Organism: Mus musculus (Mouse)
Function: Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context. Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain. Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3 (By similarity). Plays a key role in embryonic stem cells and germ cells. In germ cells, required for the methylation of imprinted loci together with DNMT3A. In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization. Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation. While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes. Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes. Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA
- DNA
- Histone H3.3
- Histone H3.2
- Histone H3.1
- Histone deacetylase 1
- Transcriptional regulator ATRX
- DNA
- Methylcytosine dioxygenase TET2
- tRNA
Sequence:
MGSRETPSSCSKTLETLDLETSDSSSPDADSPLEEQWLKSSPALKEDSVDVVLEDCKEPLSPSSPPTGREMIRYEVKVNRRSIEDICLCCGTLQVYTRHPLFEGGLCAPCKDKFLESLFLYDDDGHQSYCTICCSGGTLFICESPDCTRCYCFECVDILVGPGTSERINAMACWVCFLCLPFSRSGLLQRRKRWRHQLKAFHDQEGAGPMEIYKTVSAWKRQPVRVLSLFRNIDKVLKSLGFLESGSGSGGGTLKYVEDVTNVVRRDVEKWGPFDLVYGSTQPLGSSCDRCPGWYMFQFHRILQYALPRQESQRPFFWIFMDNLLLTEDDQETTTRFLQTEAVTLQDVRGRDYQNAMRVWSNIPGLKSKHAPLTPKEEEYLQAQVRSRSKLDAPKVDLLVKNCLLPLREYFKYFSQNSLPL
Protein: Ferric uptake regulation protein (Q8KLU1)
Organism: Rhizobium leguminosarum bv. viciae
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364037}.
Interaction partners:
Sequence:
MTGALPIAIEVRLRGAGLRPTRQRVALGDLLFAKGDRHLTVEELHEEAVAAGVPVSLATVYNTLHQFTEAGLIRVLAVESAKTYFDTNVSDHHHFFVEGENEVLDIPVSNLTIANLPEPPEGMEIAHVDVVIRLRAKQG
Protein: Zinc finger and BTB domain-containing protein 20 (Dendritic-derived BTB/POZ zinc finger protein) (Zinc finger protein 288) (Q9HC78)
Organism: Homo sapiens (Human)
Function: May be a transcription factor that may be involved in hematopoiesis, oncogenesis, and immune responses. Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8K0L9}.
Interaction partners:
- Zinc fingers and homeoboxes protein 2
- Alpha-fetoprotein
Sequence:
MLERKKPKTAENQKASEENEITQPGGSSAKPGLPCLNFEAVLSPDPALIHSTHSLTNSHAHTGSSDCDISCKGMTERIHSINLHNFSNSVLETLNEQRNRGHFCDVTVRIHGSMLRAHRCVLAAGSPFFQDKLLLGYSDIEIPSVVSVQSVQKLIDFMYSGVLRVSQSEALQILTAASILQIKTVIDECTRIVSQNVGDVFPGIQDSGQDTPRGTPESGTSGQSSDTESGYLQSHPQHSVDRIYSALYACSMQNGSGERSFYSGAVVSHHETALGLPRDHHMEDPSWITRIHERSQQMERYLSTTPETTHCRKQPRPVRIQTLVGNIHIKQEMEDDYDYYGQQRVQILERNESEECTEDTDQAEGTESEPKGESFDSGVSSSIGTEPDSVEQQFGPGAARDSQAEPTQPEQAAEAPAEGGPQTNQLETGASSPERSNEVEMDSTVITVSNSSDKSVLQQPSVNTSIGQPLPSTQLYLRQTETLTSNLRMPLTLTSNTQVIGTAGNTYLPALFTTQPAGSGPKPFLFSLPQPLAGQQTQFVTVSQPGLSTFTAQLPAPQPLASSAGHSTASGQGEKKPYECTLCNKTFTAKQNYVKHMFVHTGEKPHQCSICWRSFSLKDYLIKHMVTHTGVRAYQCSICNKRFTQKSSLNVHMRLHRGEKSYECYICKKKFSHKTLLERHVALHSASNGTPPAGTPPGARAGPPGVVACTEGTTYVCSVCPAKFDQIEQFNDHMRMHVSDG
Protein: Melanopsin 1 isoform L (A9QM68)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MDLNMGTQPHSVTKSEIPDHVLYTVGTCVLVIGSIGIIGNLLVLYAFYSNKKLRTPQNFFIMNLAVSDFLMSASQAPICFINSLHREWILGDIGCDLYAFCGALFGITSMMTLLAISVDRYLVITKPLRSIQWTSKKRTIQIIAAVWLYSLGWSVAPLLGWSSYVPEGLMISCTWDYVTYSPANRSYTMILCCCVFFIPLIIILHCYLFMFLAIRSTGRDVQKLGSCSRKSFLSQSMKNEWKLAKIAFVVIIVYVLSWSPYACVTLIAWAGRGNTLTPYSKSVPAVIAKASAIYNPIIYAIIHPRYRKTIHNAVPCLRFLIRISKNDLLRGSINESSFRTSLSSHQSLAGRTKNTCVSSVSTGEANWSDVELDTVEPAHEKLQPRRSHSFSSSLRQKRDLLPDSYSCSEETEEKVSLSSSYLEKVLGRSAFPSSPVALVTSSLRAASLPVGLNSSSASRGAGSDISQMKTEESHNNGGLDSIVSNTVPQIIIIPTSETNLFQEEPEEEETELFHFHDKKNNLLDLEGLSSSTEFLEAVEKFLS
Protein: NADPH oxidase activator 1 (NOX activator 1) (Antigen NY-CO-31) (NCF2-like protein) (P67phox-like factor) (p51-nox) (Q86UR1)
Organism: Homo sapiens (Human)
Function: Functions as an activator of NOX1, a superoxide-producing NADPH oxidase. Functions in the production of reactive oxygen species (ROS) which participate in a variety of biological processes including host defense, hormone biosynthesis, oxygen sensing and signal transduction. May also activate CYBB/gp91phox and NOX3.
Subcellular location: Cytoplasm. Cell membrane. Note=Translocation to membranes depends on NOXO1 or NCF1 and maybe RAC1.
Interaction partners:
- NADPH oxidase 1
- Cytochrome b-245 light chain
- NADPH oxidase organizer 1
- Neutrophil cytosol factor 1
- Neutrophil cytosol factor 4
- Neutrophil cytosol factor 2
- NADPH oxidase 2
- NADPH oxidase 3
- Ras-related C3 botulinum toxin substrate 2
- NADPH oxidase 4
Sequence:
MASLGDLVRAWHLGAQAVDRGDWARALHLFSGVPAPPARLCFNAGCVHLLAGDPEAALRAFDQAVTKDTCMAVGFFQRGVANFQLARFQEALSDFWLALEQLRGHAAIDYTQLGLRFKLQAWEVLHNVASAQCQLGLWTEAASSLREAMSKWPEGSLNGLDSALDQVQRRGSLPPRQVPRGEVFRPHRWHLKHLEPVDFLGKAKVVASAIPDDQGWGVRPQQPQGPGANHDARSLIMDSPRAGTHQGPLDAETEVGADRCTSTAYQEQRPQVEQVGKQAPLSPGLPAMGGPGPGPCEDPAGAGGAGAGGSEPLVTVTVQCAFTVALRARRGADLSSLRALLGQALPHQAQLGQLSYLAPGEDGHWVPIPEEESLQRAWQDAAACPRGLQLQCRGAGGRPVLYQVVAQHSYSAQGPEDLGFRQGDTVDVLCEVDQAWLEGHCDGRIGIFPKCFVVPAGPRMSGAPGRLPRSQQGDQP
Protein: Translocon EspD (B7UM93)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Interaction partners:
Sequence:
MLNVNNDIQSVRSGASAATATSGINQSEVTSALDLQLVKSTAPSASWTESTALPTPPAGHSLVTPSAAEDVLSKLFGGISGEVTSRTEGTEPQRSTQNASSGYPYLSQVNNVDPQAMMMMATLLSLDASAQRVASMKNSNEIYADGQNKALDNKTLEFKKQLEEQQKAEEKAQKSKIVGQVFGWLGVAATAIAAIFNPALWAVVAISATAMALQTAVDVMGDDAPQALKTAAQAFGGLSLAAGILTAGIGGVSSLISKVGDVANKVGSNIVKVVTTLADTFVDNVASKISAVANGLTTSSRSIGTTVLNNDAAYYNVLSQVSAFAVENLTRQSEYLSQSAKAELEKATLELQNQANYIQSASQLMSDSARVNIRIVSGRV
Protein: Proctolin (Proctolin, isoform B) (RH15319p) (Q9VLV9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGVPRSHGTGIGCGSGHRWLLVWMTVLLLVVPPHLVDGRYLPTRSHGDDLDKLRELMLQILELSNEDPQQQQQQQQQQQHPQLRLHNEATGGSSSSSNINNPRVSNGNSNAAWLQKLSAMGALDELGGDGARFGPNYGRY
Protein: Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein] (P03407)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1)
Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.
Subcellular location: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
Interaction partners:
Sequence:
MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC