wanglab/gogpt-training-data huggingface dataset:
Protein: 3-ketoacyl-CoA synthase (EC 2.3.1.-) (A9XUG6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAEESKQRRNVKPVKVQTASSSEERRSNNNLPNFLLSVRLKYVKLGYYYVISNAMYLMLVPLLGIASVHLSTLTIQDFVRLWDQLKFNLVSVTLCSGLLVFLATLYFMSRPRKVYLVNFACYKPEADRICTREIFMERSGLTGSFTGENLAFQKKILERSGLGQKTYLPEAVMRVPANPCMAEARKEAETVMFGAIDELLDKTGVKAKDIGILVVNCSLFNPTPSLSAMVVNRYKLRGNILSYNLGGMGCSAGLISIDLAKQLLRVHPHSYALVVSMENITLNWYFGNDRSMLLSNCFFRMGGVAILLSNHSSDRHRSKYQLIHTVRTHKGADDKCYNCVFQREDDTKRIGISLSKDLMAVAGEALKTNITTLGPLVLPMSEQLLFFVTLVARKVLKMKIKPYIPDFKLAFEHFCIHAGGRAVLDELEKNLDLTDWHMEPSRMTLYRFGNTSSSSLWYELAYSEAKGRIRRGDRTWQIAFGSGFKCNSAVWKALKTINPAKEKSPWIDEIDEFPVHVPGVANIASSYKS
Protein: Protein virilizer homolog (A2AIV2)
Organism: Mus musculus (Mouse)
Function: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop codon: recruits the catalytic core components METTL3 and METTL14, thereby guiding m6A methylation at specific sites. Required for mRNA polyadenylation via its role in selective m6A methylation: m6A methylation of mRNAs in the 3'-UTR near the stop codon correlating with alternative polyadenylation (APA).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q69YN4}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VIRMA, in the nucleus (PubMed:29547716). {ECO:0000269|PubMed:29547716}.
Interaction partners:
- E3 ubiquitin-protein ligase Hakai
- Zinc finger CCCH domain-containing protein 13
- N
- N
- Pre-mRNA-splicing regulator WTAP
- Putative RNA-binding protein 15B
- RNA-binding protein 15
- RNA N
- N
- Cleavage and polyadenylation specificity factor subunit 5
Sequence:
MAVDSSMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSGLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPTLKRNLKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPMSLPVSGDKEEDVPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEPQEEGEDDEDDVDVEEEEDEDEDDCHTVDSIPDDEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPNFDVEYTPEDLASVPPMTYDPYDRELAPLLYFSCPYKTTFEIEISRMKDQGPDKENSGAVEASVKLTELLDLYQEDRGAKWVTALEEIPSLIIKGLSYLQLKNTEQDSLGQLVDWTMQALNLQVAFRQPIALNVRQLKAGTKLVTSLAECGAPGVTELLQAGVINVLFDLLFADHVSSSLKLNAFKALDSVISMTEGMEAFLRSTQNEKSGYQRLLELILLDQTVRVVTAGSAILQKCHFYEILSEIKRLGDHIAEKTSAVPNHSEPDQDTDAVLERANPDYENEVEASMDMDLLESSIISEGEIEKLTNLLEEVFHVMETAPHTMTQPPVKSFPTIARITGPPERDDPYPVLFRYLHSHHFLELVTLLLSIPITSAHQGVLQATKDVLKFLAQSQKGLLFFMSEYEATNLLIRALCHLYDQDEEEGLQSDGADDAFALWLQDSTQTLQCITELFSHFQRCTASEETDHSDLLGTLHNLYLITFNPVGRSAVGHVFSLDKNLQSLITLMEYYSKEALGDSKSKKSVAYNYACVLTLVVAQSSSGVQMLEQHAASLLKLCKADENNAKLQELGKWLEPLKNLRFEINCIPNLIEYVKQNIDNLMTAEGVGLTTALRVLCNVACPPPPVEGQQKDLKWNLAVIQLFSAEGMDTFIRVLQKLNSILTQPWRLHVNMGTTLHRVTTISMARCTLTLLKTMLTELLRGGSFEFKDMRVPSALVTLHMLLCSIPLSGRLDSDEQKIQNDIIDILLTFTQGVNEKLTISEETLANNTWSLMLKEVLSSILKVPEGFFSGLILLSELLPLPLPMQTTQVIEPHDISVALNTRKLWSMHLHVQAKLLQEIVRSFSGTTCQPIQHMLRRICVQLCDLASPTALLIMRTVLDLIVEDLQSTSEDKEKQYTSQTTRLLALLDALASHKACKLAILHLINGTIKGDERYAEIFQDLLALVRSPGDSVTRQQCVEYVTSILQSLCDQDIALILPSPSEGPASELEQLSNSLPSKELMTAICDCLLATLANSESSYNCLLTCVRTMMFLAEHDYGLFHLKSSLRKNSSALHSLLKRVVSTFSKDTGELASASLDFMRQILNADAMGCCGDDSGLMEVEGAHPPRTMSLNAAELKQLLQSKEESPESLFLELEKLVLEHSKDDDSLESLLDNVIGLKQMLESSGEPLPLSDQDVEPVLSAPESLQNLFNNRTAYVLADVMDDQLKSMWFTPFQAEEIDTDLDLVKVDLIELSEKCCSDFDLHSELERSFLSEPSSPGRSKTTKGFKLGKHKHETFITSSGKSEYIEPAKRAHVVPPPRGRGRGGFGQGIRPHDIFRQRKQNTSRPPSMHVDDFVAAESKEVVPQDGIPPPKRPLKVSQKISSRGGFSGNRGGRGAFHSQNRFFTPPASKGNYSRREGTRGSSWSAQNTPRGNYNESRGGQSNFNRGPLPPLRPLSSTGYRPSPRDRASRGRGGLGPSWASTNSGSGGSRGKFVSGGSGRGRHVRSFTR
Protein: Telomere ends associated, isoform E (A1Z818)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYPVSFAAFQKLIVNLSEIASELKTANGDNRTLVEWSRWYYKEFYRNPSIRARFPVKVAPCPRRTRDNLLKVPEPGGISQNDVANVAAAGPSQVEQPEVLVEGSQLTTLAETAKSHDAVEGVAVECKPSGSESPDVIVNVERCGAFIFPVSFDVFLQCINKMLLFKKIVRSIEHCLVLLSDDERRLLTLQRFYNRFYMYPEKRSPTNIFNATTEIPLEKLLESGKPLDKKAVKTVAELTAMKSLTKNSIVSFEVFKKNMANLSDIVEQMRQLDANYASKDVQECALDYYLAFYITPRIRYKYAYKLKPCTSTFKACMLSILGKDIAEKLRKSLPQLANPSPGLDSRRPNTSYITESKGSLGSQNTSGSSQIQTSPSMEVAHEPSEGLSQLATLSPENCAAGAISTTEGLSSSHNTLETFENQANLRNDANKLSRCMPALASPERHLHSSKAPEKSSEVLSPQVKPHQSKEVAEEQSDRAPQLEIPPSGFEVPMSKTPESPASKTRASDETPAKPEEITDSTDVYETSFVTDVEVDLKKHGRFIFPVSLETFRQYINYDEIIRAILVNNHIKDEHQLSKLISDPSHPQCKKFFRQFYNKFYARNDVRQRFKYKFNCPNPKMLAKLKQKAKPLDEKALFTMNRTDNAKAVNESKSQVPFTPKTTTENCPPNPISLEMFKRHVSNLDDIVNEMQKCDEYKEKSKEEVIQDYYEGFYSGPDMREKFECRFKPCPSKKIRQLLSFPPKNKELPPKNPNCQVACTTENLSDESCLQSSRNVVRETQNITEENRPIAEHESIPSTRTPSSNDDKPGEECPPYPVSLELFKSHVSNLDDIANNMQKCVEYRGKSKDEVIRDYYKGFYSGPEMREKFACRFKPCTGHILQQLLSYPGKNVNDCLQETDCLATCTTRTPLKESCLQSKSEMSLPVRRNALEILMKSRKRTKVAKEAISSKPMTTQNTSQFQPEPFPEDALVVPEDVTTNQGTQPLELQHELEVTEPIKDYIQLNAERLYELSSKLKIGWNYTAHNFLDKLFKGINCPVTQAFLEEQYKRYSVSTGHIVANTIAAEENEPQLSSNSVDIESVCTAQTTATDTQATEMHTIPKALDQSSEPTKESSSVNLNNNLESPAKIKMIHAESSNNSRNSTNRPNTEIEAGSTKILEDGARVTTEGNSENENSSVEKKENQFLLERAKEIFFAEGSKDHNLKYLICTSEGLMRTIWRILYQLDLQEFSYYTSIHDGEDLYKSEDNLHLCFRHVVDHGNWPVNLCVLLPRLKHLLHSKGVQLDRLNLSKISPKIFSPWELGTYSDFDQIVAQEYIHRTGEEIEDVVKLCQEREKLYACCWAHNQWLPRAPQIANETLNAELGEVEPVIERILLKKICGVKDGDENKPTEIVSIPSSPSTVCSRISTQPAEDKLSQQPSQLNSLNFVDVTGVELASQVPQMVVDPLVSNQIEETSQVPETQYDAPASLQMASVKQEPISFLNNQRAFCDSEKCQWEHINPEEQTIDLDSTESDGPSLSCFAIQNQNSEDQIHFILEDSVHAENHDYVKKTEVPKSTDPAQLGTNVNTLSVRSMPACQVSVIPKKRQAASPRLNSKRMKLMNDKVPQLRHEFQPLPMGVKVVQSKALILPDSQNIRTSQTAKTKPTESPPHHQVNITPSQEFAVGNTLLECSELQGLLDSNDVNDGKVNKEDHPVSGSACTSKRLAASSPQSSVIYRDLELFSFYKSLTLEQIIKYRIEGPLPGATYQKALVKINDKLCNVRGPLISSLFPYLSSTLRSDLELVLHDLGEFFYKRSWPAHTDATVDFRKRVLFVFMNLSPRFAPFSIKFDNESREWGTCIEANVGDKSLDQRDTTFNAEELIKPNILNSIEQLKCKLVT
Protein: Thrombospondin-2 (P35442)
Organism: Homo sapiens (Human)
Function: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties.
Interaction partners:
- Platelet glycoprotein 4
- Leukocyte surface antigen CD47
- Matrix metalloproteinase-9
- Lysosome membrane protein 2
- Syndecan-4
- Scavenger receptor class B member 1
- Integrin alpha-V
- Integrin beta-3
- Integrin alpha-3
- Integrin beta-1
Sequence:
MVWRLVLLALWVWPSTQAGHQDKDTTFDLFSISNINRKTIGAKQFRGPDPGVPAYRFVRFDYIPPVNADDLSKITKIMRQKEGFFLTAQLKQDGKSRGTLLALEGPGLSQRQFEIVSNGPADTLDLTYWIDGTRHVVSLEDVGLADSQWKNVTVQVAGETYSLHVGCDLIDSFALDEPFYEHLQAEKSRMYVAKGSARESHFRGLLQNVHLVFENSVEDILSKKGCQQGQGAEINAISENTETLRLGPHVTTEYVGPSSERRPEVCERSCEELGNMVQELSGLHVLVNQLSENLKRVSNDNQFLWELIGGPPKTRNMSACWQDGRFFAENETWVVDSCTTCTCKKFKTICHQITCPPATCASPSFVEGECCPSCLHSVDGEEGWSPWAEWTQCSVTCGSGTQQRGRSCDVTSNTCLGPSIQTRACSLSKCDTRIRQDGGWSHWSPWSSCSVTCGVGNITRIRLCNSPVPQMGGKNCKGSGRETKACQGAPCPIDGRWSPWSPWSACTVTCAGGIRERTRVCNSPEPQYGGKACVGDVQERQMCNKRSCPVDGCLSNPCFPGAQCSSFPDGSWSCGSCPVGFLGNGTHCEDLDECALVPDICFSTSKVPRCVNTQPGFHCLPCPPRYRGNQPVGVGLEAAKTEKQVCEPENPCKDKTHNCHKHAECIYLGHFSDPMYKCECQTGYAGDGLICGEDSDLDGWPNLNLVCATNATYHCIKDNCPHLPNSGQEDFDKDGIGDACDDDDDNDGVTDEKDNCQLLFNPRQADYDKDEVGDRCDNCPYVHNPAQIDTDNNGEGDACSVDIDGDDVFNERDNCPYVYNTDQRDTDGDGVGDHCDNCPLVHNPDQTDVDNDLVGDQCDNNEDIDDDGHQNNQDNCPYISNANQADHDRDGQGDACDPDDDNDGVPDDRDNCRLVFNPDQEDLDGDGRGDICKDDFDNDNIPDIDDVCPENNAISETDFRNFQMVPLDPKGTTQIDPNWVIRHQGKELVQTANSDPGIAVGFDEFGSVDFSGTFYVNTDRDDDYAGFVFGYQSSSRFYVVMWKQVTQTYWEDQPTRAYGYSGVSLKVVNSTTGTGEHLRNALWHTGNTPGQVRTLWHDPRNIGWKDYTAYRWHLTHRPKTGYIRVLVHEGKQVMADSGPIYDQTYAGGRLGLFVFSQEMVYFSDLKYECRDI
Protein: Polypeptide N-acetylgalactosaminyltransferase-like 6 (EC 2.4.1.41) (Polypeptide GalNAc transferase 17) (GalNAc-T17) (pp-GaNTase 17) (Protein-UDP acetylgalactosaminyltransferase 17) (Putative polypeptide N-acetylgalactosaminyltransferase 17) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17) (Q49A17)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQQTFPLGLGDGQFYSWTDGLRRKDWHDYESIQKEAMRSGKGEHGKPYPLTEEDHDDSAYRENGFNIFVSNNIALERSLPDIRHANCKHKMYLERLPNTSIIIPFHNEGWTSLLRTIHSIINRTPGSLIAEIILVDDFSEREHLKDKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAMRGAFDWEMYYKRIPIPPELQRADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCSRVGHIYRKYVPYKVPSGTSLARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKELRKQLKCKDFKWFMAAVAWDVPKYYPPVEPPPAAWGEIRNVAANLCVDSKHGATGTELRLDICVKDGSERTWSHEQLFTFGWREDIRPGEPLHTRKFCFDAISHNSPVTLYDCHGMKGNQLWGYRKDRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIFEHINMTVLEKFNHHANS
Protein: L-lysine 4-hydroxylase (EC 1.14.11.-) (Alpha-ketoglutarate-dependent dioxygenase) (KDO5) (L-lysine hydroxylase) (J3BZS6)
Organism: Flavobacterium sp. (strain CF136)
Function: Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-lysine, leading to (4R)-4-hydroxy-L-lysine.
Interaction partners:
- Siderophore synthetase component
- Acyl-CoA synthetase
- Carrier domain-containing protein
- Siderophore synthetase component
- PLP-dependent enzyme, glutamate decarboxylase
- Lysine/ornithine N-monooxygenase
- AraC family transcriptional regulator
Sequence:
MKSQSIMSVERSAETSLTLEIPTSPLIIKITQQERNILSNVGNLLVKAFGNYENPDYIASLHLHAFQLLPERITRILSQFGSDFSAEQYGAIVFQGLIEVDQDDLGPTPPNWQGADYGKLNKYGFICSLLHGAVPSKPVQYYAQRKGGGLLHAVIPDEKMAATQTGSGSKTDLFVHTEDAFLSNQADFLSFLYLRNEERVPSTLYSIRSHGKMNPVMKKLFEPIYQCPKDANYNDEDVANSGPTASVLYGNRELPFIRFDAAEQIFNENAGQTSEALGNLMDFWDEAKTLINSDYIPNSGDLIFVNNHLCAHGRSAFIAGQRIENGEIIKCERRQMLRMMSKTSLIHIRSVTRTDDPYFIMEEHLGKIFDLD
Protein: Synaptonemal complex protein 1 (SCP-1) (Cancer/testis antigen 8) (CT8) (Q15431)
Organism: Homo sapiens (Human)
Function: Major component of the transverse filaments of synaptonemal complexes, formed between homologous chromosomes during meiotic prophase. Required for normal assembly of the central element of the synaptonemal complexes. Required for normal centromere pairing during meiosis. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q62209}. Chromosome {ECO:0000250|UniProtKB:Q62209}. Chromosome, centromere {ECO:0000250|UniProtKB:Q62209}. Note=In tripartite segments of synaptonemal complexes, between lateral elements in the nucleus. Its N-terminus is found towards the center of the synaptonemal complex while the C-terminus extends well into the lateral domain of the synaptonemal complex (By similarity). Only rarely detected at centromeres during leptotene and zygotene. Detected at centromeres during mid-diplotene, when it is no longer present along chromosome arms. No longer detected at centromeres at later stages of meiosis (By similarity). {ECO:0000250|UniProtKB:Q03410, ECO:0000250|UniProtKB:Q62209}.
Interaction partners:
- Synaptonemal complex central element protein 1
- Synaptonemal complex central element protein 2
- Synaptonemal complex protein 3
- Synaptonemal complex protein 2
- Testis-expressed protein 12
- Synaptonemal complex central element protein 3
- Meiotic recombination protein REC8 homolog
- HORMA domain-containing protein 1
- Structural maintenance of chromosomes protein 1B
- Cohesin subunit SA-3
Sequence:
MEKQKPFALFVPPRSSSSQVSAVKPQTLGGDSTFFKSFNKCTEDDFEFPFAKTNLSKNGENIDSDPALQKVNFLPVLEQVGNSDCHYQEGLKDSDLENSEGLSRVYSKLYKEAEKIKKWKVSTEAELRQKESKLQENRKIIEAQRKAIQELQFGNEKVSLKLEEGIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMITAFEELRVQAENSRLEMHFKLKEDYEKIQHLEQEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKVNQLEEKTKLQSENLKQSIEKQHHLTKELEDIKVSLQRSVSTQKALEEDLQIATKTICQLTEEKETQMEESNKARAAHSFVVTEFETTVCSLEELLRTEQQRLEKNEDQLKILTMELQKKSSELEEMTKLTNNKEVELEELKKVLGEKETLLYENKQFEKIAEELKGTEQELIGLLQAREKEVHDLEIQLTAITTSEQYYSKEVKDLKTELENEKLKNTELTSHCNKLSLENKELTQETSDMTLELKNQQEDINNNKKQEERMLKQIENLQETETQLRNELEYVREELKQKRDEVKCKLDKSEENCNNLRKQVENKNKYIEELQQENKALKKKGTAESKQLNVYEIKVNKLELELESAKQKFGEITDTYQKEIEDKKISEENLLEEVEKAKVIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKSKEQEQSSLRASLEIELSNLKAELLSVKKQLEIEREEKEKLKREAKENTATLKEKKDKKTQTFLLETPEIYWKLDSKAVPSQTVSRNFTSVDHGISKDKRDYLWTSAKNTLSTPLPKAYTVKTPTKPKLQQRENLNIPIEESKKKRKMAFEFDINSDSSETTDLLSMVSEEETLKTLYRNNNPPASHLCVKTPKKAPSSLTTPGSTLKFGAIRKMREDRWAVIAKMDRKKKLKEAEKLFV
Protein: Uncharacterized protein (Q389C1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRKGIFSHIIDRIAGVPHRSVAAIPYGQWFSLYVQCLKAHQRNTAAGRDANELKVARQNLDVSLLSSVVSQKWTEVIVPSDDKCDARQPRSSVGNVLWWHESAEGAWLSSNNKIRGLELVTTSFLLEPLLAGRSIAAWTETVQQSSAAGGPLMQNDKGQPSLSPNKSGVLVVVVPFSTLFQLRAEAYPRAHTASADGENTQQRQLSLQERRARVAVLNSLHQLMELQCNSNNRWTNVEFAIWSPVSEFDAIMHISQVRLSLPDAAKKRITLETVCECEATRSAYLAHYLTLTKKNVPLAVLAPQSRQTELQQVPITNSCVRAQSACESEVRRQGHLKRSTVHRQAVTGCSELVRRMATREENLRQIMIP
Protein: Processive diacylglycerol beta-glucosyltransferase (EC 2.4.1.315) (Beta-diglucosyldiacylglycerol synthase) (Beta-DGS) (DGlcDAG synthase) (Glc2-DAG synthase) (Beta-gentiobiosyldiacylglycerol synthase) (Beta-monoglucosyldiacylglycerol synthase) (Beta-MGS) (MGlcDAG synthase) (Diglucosyl diacylglycerol synthase (1,6-linking)) (Glucosyl-beta-1,6-glucosyldiacylglycerol synthase) (UDP glucosyltransferase) (UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase) (Q5HH69)
Organism: Staphylococcus aureus (strain COL)
Function: Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer two glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). In vitro, UgtP can also use cholesterol, cholesterolglucoside and the fluorescent substrate 6-(N-7-nitrobenz-2-oxa-1,3-diazol-4-yl)-amino-caproyl-sphingosine (NBD-ceramide) as sugar acceptors, but it can only use UDP-glucose as sugar donor.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01280}.
Interaction partners:
Sequence:
MVTQNKKILIITGSFGNGHMQVTQSIVNQLNDMNLDHLSVIEHDLFMEAHPILTSICKKWYINSFKYFRNMYKGFYYSRPDKLDKCFYKYYGLNKLINLLIKEKPDLILLTFPTPVMSVLTEQFNINIPVATVMTDYRLHKNWITPYSTRYYVATKETKQDFIDVGIDPSTVKVTGIPIDNKFETPINQKQWLIDNNLDPDKQTILMSAGAFGVSKGFDTMITDILAKSANAQVVMICGKSKELKRSLTAKFKSNENVLILGYTKHMNEWMASSQLMITKPGGITITEGFARCIPMIFLNPAPGQELENALYFEEKGFGKIADTPEEAIKIVASLTNGNEQLTNMISTMEQDKIKYATQTICRDLLDLIGHSSQPQEIYGKVPLYARFFVK
Protein: Zinc finger protein 251 (Q9BRH9)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAATFQLPGHQEMPLTFQDVAVYFSQAEGRQLGPQQRALYRDVMLENYGNVASLGFPVPKPELISQLEQGKELWVLNLLGAEEPDILKSCQKDSEVGTKKELSILNQKFSEEVKTPEFVSRRLLRDNAQAAEFREAWGREGKLKERVGNSAGQSLNKPNIHKRVLTEATVGRERSLGERTQECSAFDRNLNLDQNVVRLQRNKTGERVFKCDICSKTFKYNSDLSRHQRSHTGEKPYECGRCGRAFTHSSNLVLHHHIHTGNKPFKCDECGKTFGLNSHLRLHRRIHTGEKPFGCGECGKAFSRSSTLIQHRIIHTGEKPYKCNECGRGFSQSPQLTQHQRIHTGEKPHECSHCGKAFSRSSSLIQHERIHTGEKPHKCNQCGKAFSQSSSLFLHHRVHTGEKPYVCNECGRAFGFNSHLTEHVRIHTGEKPYVCNECGKAFRRSSTLVQHRRVHTGEKPYQCVECGKAFSQSSQLTLHQRVHTGEKPYDCGDCGKAFSRRSTLIQHQKVHSGETRKCRKHGPAFVHGSSLTADGQIPTGEKHGRAFNHGANLILRWTVHTGEKSFGCNEYGKAFSPTSRPTEDQIMHAGEKPYKCQECGNAFSGKSTLIQHQVTHTGQKPCHCSVYGKAFSQSSQLTPPQQTRVGEKPALNDGSKRYFIHIKKIFQERHF
Protein: Olfactory receptor 2C1 (Odorant receptor OR3) (Olfactory receptor 15) (Olfactory receptor 256-17) (P23275)
Organism: Mus musculus (Mouse)
Function: Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanetiol (MTMT). Also binds odorants acetophenone and benzaldehyde. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (Probable). May be involved in the molecular processes underlying fasciculation and targeting of olfactory axons.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15342743, ECO:0000305|PubMed:25901328, ECO:0000305|PubMed:29659735}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Huntingtin-interacting protein K
Sequence:
MEVDSNSSSGSFILMGVSDHPHLEIIFFAVILASYLLTLVGNLTIILLSRLDARLHTPMYFFLSNLSSLDLAFTTSSVPQMLKNLWGPDKTISYGGCVTQLYVFLWLGATECILLVVMAFDRYVAVCRPLHYMTVMNPRLCWGLAAISWLGGLGNSVIQSTFTLQLPFCGHRKVDNFLCEVPAMIKLACGDTSLNEAVLNGVCTFFTVVPVSVILVSYCFIAQAVMKIRSVEGRRKAFNTCVSHLVVVFLFYGSAIYGYLLPAKSSNQSQGKFISLFYSVVTPMVNPLIYTLRNKEVKGALGRLLGKGRGAS
Protein: Neuromedin U (Neuromedin-U precursor) (F1R3S8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRNSNQCERATAHSAMSPGNTSALMLAVLLLSFIPITTSAPMLLNPSSLEHEQLLTQITDLCSFYLSADPSFRTSDVLEDLCFLMLGSLQKSKEITARETSKRENLQGPGRIQSRGYFLYRPRNGRRSDEYV
Protein: Ornithine decarboxylase (ODC) (EC 4.1.1.17) (P78599)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P08432}.
Interaction partners:
- Spermidine synthase
- Arginase
- Agmatinase
- Afp99p
- Polyamine oxidase
- Ornithine aminotransferase
- S-adenosylmethionine decarboxylase proenzyme
- Corticosteroid-binding protein
- Spermine synthase
- Protein ARG5,6
Sequence:
MKHTIIENEPEIKLQNDLNHHIEISPNTKTTNGTTTTTTTLNVNKTLKAIDLIETSIKNHISTIDHENCLPNDEDSFFVCDLGEIINSVNQWQQILPMVQPYYAVKCNSNPQILTTLSELGVNFDCASKNEIDLVLSLGIHQAHERIIYANPCKTNSFIRHAADENVNLTTVDNVHELYKLAKFHPHCKILIRLITDDSTAQCQLSTKFGCDLNTAIGEILPKAKELGLQVHGVAFHVGSGAKDFSSIYQAIKDSRILFDEMLSMGFTPKLLDIGGGFERETFPQSSQMVKFALEKFFPIEFSQLNEIKFIAEPGRFMVANAFTLITHIIARRDLPTGGNNNNNDMTPSAMLYINDGVYGNLNCILFDHQTPKVYVLTNENQLFYKQEMMRSLSVNNNNNNNNKTDGFKFSIWGPTCDGLDCVSSLAKLSKNVQVGDWLFFENVGAYTSCASTKFNGLSSGETKTLYVNSNEE
Protein: DNA helicase II (EC 5.6.2.4) (DNA 3'-5' helicase II) (P03018)
Organism: Escherichia coli (strain K12)
Function: A helicase with DNA-dependent ATPase activity. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).
Interaction partners:
- DNA mismatch repair protein MutL
- UvrABC system protein B
- ATP-dependent DNA helicase RecG
- ATP-dependent DNA helicase RecQ
- UvrABC system protein A
- Holliday junction branch migration complex subunit RuvA
- UvrABC system protein C
- Replicative DNA helicase DnaB
- Protein RecA
- Beta sliding clamp
Sequence:
MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
Protein: Actin binding protein (Q54TU2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEQLLEAISDAVSSMVLYSVEADESNAAIPNILPGAQGVKSTVDYLVDLASKSAALWDNFNQPDMKVKMIDTCDKIKESTGFLLESATILSNMPFNKPAKKILLKGAKGIMEHMVVLLQQADLYEVTRLIRYCRRCESKLKIFIGLDPGETFFATAAQDFVTSTVEVGKIVTKRIGEIDDYALKKRFEEANSSLKVEVPVVLQHFAYYQRDANDRHSFDQGHIVAKTIFSIIDEIITVARLSAKSPFDLSMIQGLDLRDDDDLKDVNILISQEKSRLLSAIEAGDGKEASRALKAIKKGLTDQIVISKALAKSTDNPIEKKRLEDAARNAEFILDSIVAQFGQAVEELLSRPDNSILFNRLKANLDTIMEASDQMVTSSARLSSNDVSEATKNLEELIEKVRGNISKSEFEKLAVNIPLLQPTFNDILDIVDGIAMGTQDATIKQSLEFASKEGRNRGSEIIGRLEQLSKQLEKNPNNKREIELEMNQLLTQLNQIGRDLLKAVSLGTSNQIYETHKSIEENLAKLKQAVLSNDQKEVTTALRAIRKGMNDQLNIAKSIERITEDQQMKDALQAAILKADEELNDLIKNLYTSTQEAMLDSSNPKAIAKLDESIRGIDEMNQSFLGAVSRDIMTENTKQMELKLAQLVHSLKSGDQQLTVQVLKGVIEDIKKQGLVAELASNSIKDSDEHRANRIKERAVDLTNTGPNLVKSVKANLIEMNSDNLSALVQNIGQIRETNKDLNNAVFMSTEEELLENSAKIDQEMRRIQTALANGKPITEQEINSLMKKMNNQIRLAHQHAKSMKDPNSKKILLDTTDNLNKLVSLLVDACKQSIDNPSDEKAKQKVKDLLNEAIKANLDLIGNSFSTAEELVYGTPNLLKLISKLEEAMANGDLDEIKRCFKELNEELSKQLFLARIAEASITDPERKKQLLEAIADLERLQTDLYPSVMEFISNPNSKEARENLQQLLRKLKNDVERVSSISSTSPSEHLESKSYAVANELNKVERGLHSNNQAEVNDGANKAIAGIKQQIQLSKHIAEHTDNIAQKREIIDLSDRLEKQALVLQQAIKESLANPSSAAHKEKVYQASCATRTLMAQLIAASSSKVPEEQIITTAQSIKRDLDNLSIALAKGGKDAEKAIKEFKSGETKQKIELLKAYASKVQNPHQKKQINQAIAQLEENVKQSIDFVEKTIGTTTDKPSTVEQQKKLKELIDNSSVAANQVISVSTGSNEDRLLSKAVKINETLDRISKSAHGGNKADVDSNVKELREELGDTIQLIKQASENVKDPHKKVALNEIAEKLKLVSQPISNAANNTISKPSDNASKTELNNLINQTKELLGKAVVNSTNNDNPTQQLDQVLYKASNDINRLNNAVESGDQKSIGDSLTNLKDTENRLKILGNSLPSNSVESEKVKKSIQEISNQVLPSIINNATVILTQPKDSNNSKSIVNKESKKALSDLSNVISITNKSPEEKIIANGTVLHRDTDQLNTSTKQSKIDPTQVQNNVDTIYKTVAEQTLLARALANQTSNTSRKQSLQDKSDQLEKLLPELEKANKDIQSSASSGKPVDKQMVDRLDKITNDIKSINQSIVSEAINEKLEKEHKEREIREAAYREEQERLRREKEEREKAQQDEVLAAAQKIAERTKNLNKDQTPEGKLYSTAQGIAGIMRDLSIAATTNDKKGMITCSKLLAEQVALYLQQAKETASKCTDPKLKEQIITAAQAAKNFTVQLKIIAAVKAASDDDDPSSNKQQLVKCAKGLAKAIVGTINAVEIGQIRVK
Protein: NF-kappa-B inhibitor beta (NF-kappa-BIB) (I-kappa-B-beta) (IkB-B) (IkB-beta) (IkappaBbeta) (Thyroid receptor-interacting protein 9) (TR-interacting protein 9) (TRIP-9) (Q15653)
Organism: Homo sapiens (Human)
Function: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proto-oncogene c-Rel
- NF-kappa-B inhibitor alpha
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B essential modulator
- NF-kappa-B inhibitor epsilon
- Transcription factor RelB
- F-box/WD repeat-containing protein 1A
Sequence:
MAGVACLGKAADADEWCDSGLGSLGPDAAAPGGPGLGAELGPGLSWAPLVFGYVTEDGDTALHLAVIHQHEPFLDFLLGFSAGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQPRPRRPREAPDTYLAQGPDRTPDTNHTPVALYPDSDLEKEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGAPEPEGEDEKSGPCSSSSDSDSGDEGDEYDDIVVHSSRSQTRLPPTPASKPLPDDPRPV