wanglab/gogpt-training-data huggingface dataset:
Protein: Protein male-specific lethal-3 (P50536)
Organism: Drosophila melanogaster (Fruit fly)
Function: The MSL proteins are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). Mle, msl-1 and msl-3 are colocalized on the X chromosome. Each of the MSL proteins requires all the other MSLs for wild-type X-chromosome binding.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972, ECO:0000269|PubMed:7768187}. Chromosome {ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:19029895, ECO:0000269|PubMed:7768187}. Note=Msl-3 is associated with hundreds of discrete sites along the length of the X chromosome in males and not in females, and is also associated with 10-20 autosomal sites in males (PubMed:16543150, PubMed:18510926, PubMed:19029895). Recruited to the male X chromosome following association with roX1 and roX2 non-coding RNAs (PubMed:11014199). {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:19029895}.
Interaction partners:
- Protein male-specific lethal-1
- Histone acetyltransferase MOF
- Dosage compensation regulator mle
- E3 ubiquitin-protein ligase msl-2
- MRG/MORF4L binding protein
- Enhancer of polycomb-like protein
- Chromatin modification-related protein MEAF6
- Chromosomal serine/threonine-protein kinase JIL-1
- DNA methyltransferase 1-associated protein 1
- Protein MBD-R2
Sequence:
MTELRDETPLFHKGEIVLCYEPDKSKARVLYTSKVLNVFERRNEHGLRFYEYKIHFQGWRPSYDRCVRATVLLKDTEENRQLQRELAEAAKLQIRGDYSYKGTPDKPSAKKKRGGKAAHVEEPIVVPMDTGHLEAEHEMAPTPRAAGNRTRDNSGGKRKEKPPSGDGRLKGNRGRQTETFYNNAINDVSVYNHVPQEDRIMMRVSERLRELIEYDRNMIKVLGKQHALPARVPIVTIMENFVKQQAVELAISIKQDSSRARNTQSRNARMEREYDRVMSTVCMLKEVVDGLRIYFEFHVDDHLLYTEEKEYVHNYLTDDNMRNCSLILNKSYEYINPSGDTELIGLDGTPVVEGSGDTNGQIGVINIGGPEYEKQLQKCLLYIVTASGKNTAQAYERTSPYTAAYKLPVEMRGFLNETFKWRLLSAESPPEKSMVFGAPHLVRLMIKMPMFLNASPISNKKLEDLLPHLDAFINYLENHREWFDRENFVNSTALPQEDLQRELLDSLDGIAA
Protein: Grainyhead-like protein 2 homolog (Brother of mammalian grainyhead) (Transcription factor CP2-like 3) (Q8K5C0)
Organism: Mus musculus (Mouse)
Function: Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. During embryogenesis, plays unique and cooperative roles with GRHL3 in establishing distinct zones of primary neurulation. Essential for closure 3 (rostral end of the forebrain), functions cooperatively with GRHL3 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure. Regulates epithelial morphogenesis acting as a target gene-associated transcriptional activator of apical junctional complex components. Up-regulates of CLDN3 and CLDN4, as well as of RAB25, which increases the CLDN4 protein and its localization at tight junctions. Comprises an essential component of the transcriptional machinery that establishes appropriate expression levels of CLDN4 and CDH1 in different types of epithelia. Exhibits functional redundancy with GRHL3 in epidermal morphogenetic events such as eyelid fusion and epidermal wound repair. In lung, forms a regulatory loop with NKX2-1 that coordinates lung epithelial cell morphogenesis and differentiation. In keratinocytes, plays a role in telomerase activation during cellular proliferation, regulates TERT expression by binding to TERT promoter region and inhibiting DNA methylation at the 5'-CpG island, possibly by interfering with DNMT1 enzyme activity. In addition, impairs keratinocyte differentiation and epidermal function by inhibiting the expression of genes clustered at the epidermal differentiation complex (EDC) as well as GRHL1 and GRHL3 through epigenetic mechanisms (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:20978075, ECO:0000269|PubMed:22696678}. Membrane {ECO:0000250|UniProtKB:Q6ISB3}. Note=detected at cell-cell contact areas. {ECO:0000250|UniProtKB:Q6ISB3}.
Interaction partners:
- Epithelial splicing regulatory protein 1
- Transcription factor Ovo-like 2
Sequence:
MSQESDNNKRLVALVPMPSDPPFNTRRAYTSEDEAWKSYLENPLTAATKAMMSINGDEDSAAALGLLYDYYKVPRDKRLLSVSKASDSQEDQDKRNCLGTSEAQINLSGGENRVQVLKTVPVNLCLSQDHMENSKREQYSVSITESSAVIPVSGITVVKAEDFTPVFMAPPVHYPRADSEEQRVVIFEQTQYDLPSIASHSSYLKDDQRSTPDSTYSESFKDGASEKFRSTSVGADEYTYDQTGSGTFQYTLEATKSLRQKQGEGPMTYLNKGQFYAITLSETGDNKCFRHPISKVRSVVMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDVNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPIHRAYCQIKVFCDKGAERKIRDEERKQNRKKGKGQASQAQCNNSSDGKMAAIPLQKKSDITYFKTMPDLHSQPVLFIPDVHFANLQRTGQVYYNTDDEREGSSVLVKRMFRPMEEEFGPTPSKQIKEENVKRVLLYVRKENDDVFDALMLKSPTVKGLMEALSEKYGLPVEKITKLYKKSKKGILVNMDDNIIEHYSNEDTFILNMESMVEGFKITLMEI
Protein: Squalene monooxygenase (EC 1.14.14.17) (Squalene epoxidase) (SE) (Q14534)
Organism: Homo sapiens (Human)
Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:26434806, ECO:0000269|PubMed:28972164, ECO:0000269|PubMed:30626872}; Peripheral membrane protein {ECO:0000269|PubMed:26434806, ECO:0000269|PubMed:28972164}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:26434806}; Peripheral membrane protein {ECO:0000269|PubMed:26434806, ECO:0000269|PubMed:28972164}.
Interaction partners:
- Lanosterol synthase
- Squalene synthase
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- 7-dehydrocholesterol reductase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Sigma non-opioid intracellular receptor 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Cholesterol 25-hydroxylase
Sequence:
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSGSQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGEMPRNLREYMVEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGGMTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSATDDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPWITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
Protein: Transcriptional repressor Rhit (Repressor of heat-inducible transcription) (Zinc finger protein 13) (Zinc finger protein Krox-8) (P10754)
Organism: Mus musculus (Mouse)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSADSQSIAATENEEKSHEVPGNVQHCGDMLSGQEETVPLGTSQESTHIKAEPEEPHSEGASREDRTPGTQRWMSPCPGPKDKGPFLPGGVVPSPWTPVLSRGGRTRERKMAAALLTAWSQMPVTFEDVALYLSQEEWGRLDHTQQNFYRDVLQGKNGLALGAVEMGKVVPALAVATLEDTKSIRTRARWAPGEDPKCGQHVASGPGTKLTRDTGKAGQLKPAPSESRPLKTPEDSGPEKPSEGEEALKSGEEGLVPDGDTGKKTYKCEQCGKGFSWHSHLVTHRRTHTGEKPYTCTDCGKRFGRSSHLIQHQIIHTGEKPYTCPSCWKSFSHHSTLIQHQRIHTGEKPYVCDRCAKRFTRRSDLVTHQGTHTGAKPHKCPICSKCFTQSSALVTHQRTHTGVKPYPCPECGKCFSQRSNLIAHNRTHTGEKPYHCLDCGKSFSHSSHLTAHQRTHRGVRPYSCPLCGKSFSRRSNLHRHEKIHTTGPKALAMLMLGAAAAGALTAPPPAST
Protein: Polyamine aminopropyltransferase (Agmatine aminopropyltransferase) (EC 2.5.1.104) (N1-aminopropylagmatine synthase) (Norspermidine aminopropyltransferase) (EC 2.5.1.126) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Spermine synthase) (EC 2.5.1.22) (Thermine synthase) (Thermospermine synthase) (Triamine/agmatine aminopropyltransferase) (TAAPT) (Q5SK28)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to agmatine to yield N1-aminopropylagmatine. An efficient aminopropyltransferase activity has been also observed with norspermidine which produces thermine, and spermidine which produces spermine and thermospermine. The aminopropyl activity with homospermidine, mitsubishine, thermine, 1,3-diaminopropane, putrescine (1,4-diaminobutane), spermine and caldopentamine are very low. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
Interaction partners:
Sequence:
MDYGMYFFEHVTPYETLVRRMERVIASGKTPFQDYFLFESKGFGKVLILDKDVQSTERDEYIYHETLVHPAMLTHPEPKRVLIVGGGEGATLREVLKHPTVEKAVMVDIDGELVEVAKRHMPEWHQGAFDDPRAVLVIDDARAYLERTEERYDVVIIDLTDPVGEDNPARLLYTVEFYRLVKAHLNPGGVMGMQAGMILLTHHRVHPVVHRTVREAFRYVRSYKNHIPGFFLNFGFLLASDAFDPAAFSEGVIEARIRERNLALRHLTAPYLEAMFVLPKDLLEALEKETMVSTDQNPFYVTPEGEARQAPYKG
Protein: Polyadenylate-binding protein 1 (E5RJB9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCK
Protein: Vexin (Q8BG31)
Organism: Mus musculus (Mouse)
Function: Required for neurogenesis in the neural plate and retina. Strongly cooperates with neural bHLH factors to promote neurogenesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29518376}. Nucleus {ECO:0000269|PubMed:29518376}. Note=Nuclear localization is essential for its function in neurogenesis. {ECO:0000269|PubMed:29518376}.
Interaction partners:
Sequence:
MHQIYSCSDENIEVFTTVIPSKVSSSSRRRVKSSHHLLAKNVVIESDLYPPPRPLELLPQRCERRDTGDRRWLQTGRLQTARPPGAHPTKTPSRPVGISEPKTSNLCGNRAYGKSLIPPVARISVKAPAGAEVAAKGSEHGAVLGRGSRHLKKIAEEYPALPQGAEASLPLTGSTSCGVPGILRKMWTRHKKKSEYVGATNSAFEAD
Protein: Thiamine pyrophosphokinase (EC 2.7.6.2) (A0A1D8PNT8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Trifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase/thiaminase
- Acid phosphatase
- Phytase PHO112
- GTP:AMP phosphotransferase, mitochondrial
- Adenylate kinase
- Alkaline phosphatase
- Alkaline phosphatase
- Tyrosine protein phosphatase
Sequence:
MSEDSELIEQVIEQPDSLIISPPSDSSSSSYNHIQPFVYLESTATTQTNHNVLLILNQKITIDLISLWKKCEIIVCADGGANSLYEYFNDNNHHHHHENLQRSDYIPDYIVGDFDSISPDVKTYYESHGSKIIRQSSQYYNDFTKSIHCIQLHYQLNHTKENWFESIDEVDGLAKLWNGLNNSSDVVVDIDITIYVLNAIGGRFDQTVQSINQLYIMNEDYPKVTVFFITTNDIIFLLKKGVNYISYKNRLMFHKDNGSSPTPTCGLLPLSNKTPIILNSYGLKYDMRNWKTEMLGQVSSSNRISGETGFIVECSDDIVMNIEIDV
Protein: Small nuclear ribonucleoprotein-associated protein B (snRNP-B) (snRPB) (Sm protein B) (Sm-B) (SmB) (P27048)
Organism: Mus musculus (Mouse)
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (By similarity). Is also a component of the minor U12 spliceosome (By similarity). As part of the U7 snRNP it is involved in histone pre-mRNA 3'-end processing.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14678}. Nucleus {ECO:0000269|PubMed:19470752}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000250|UniProtKB:P14678}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein G
- U1 small nuclear ribonucleoprotein A
- U1 small nuclear ribonucleoprotein 70 kDa
- U7 snRNA-associated Sm-like protein LSm11
- U1 small nuclear ribonucleoprotein C
Sequence:
MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGLPPGRGTPMGMPPPGMRPPPPGMRGLL
Protein: Colicin-A (P04480)
Organism: Citrobacter freundii
Function: This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPGFNYGGKGDGTGWSSERGSGPEPGGGSHGNSGGHDRGDSSNVGNESVTVMKPGDSYNTPWGKVIINAAGQPTMNGTVMTADNSSMVPYGRGFTRVLNSLVNNPVSPAGQNGGKSPVQTAVENYLMVQSGNLPPGYWLSNGKVMTEVREERTSGGGGKNGNERTWTVKVPREVPQLTASYNEGMRIRQEAADRARAEANARALAEEEARAIASGKSKAEFDAGKRVEAAQAAINTAQLNVNNLSGAVSAANQVITQKQAEMTPLKNELAAANQRVQETLKFINDPIRSRIHFNMRSGLIRAQHNVDTKQNEINAAVANRDALNSQLSQANNILQNARNEKSAADAALSAATAQRLQAEAALRAAAEAAEKARQRQAEEAERQRQAMEVAEKAKDERELLEKTSELIAGMGDKIGEHLGDKYKAIAKDIADNIKNFQGKTIRSFDDAMASLNKITANPAMKINKADRDALVNAWKHVDAQDMANKLGNLSKAFKVADVVMKVEKVREKSIEGYETGNWGPLMLEVESWVLSGIASSVALGIFSATLGAYALSLGVPAIAVGIAGILLAAVVGALIDDKFADALNNEIIRPAH
Protein: Peroxisomal ATPase PEX1 (Peroxin-1) (A0A8I6ALA5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MWSHSIRHTSDVTRNFKMQEWRFQGWENLSAARSDLALCWFQELHAISLEEHLLDQIRIVFPKAIVPIWVDQQTYIFIQIVALMPTAPYGRLETNTKLLIQPKTRQAKESTFPKEGDARGQAHNYGREQKGTVKELQTKQLHKNTEAVPVSNGRNPEVPGDSVKPRWWAVLGSMFSFGPDNKQESAWGSLELGAFKNMQSQTVPLDSIFRVCQVQPPSVHNTPANSVFHKHCTVHVFPWDQEYFDVEPSFTVVYGKLVKLHSPKQQQDKSKQGVLLPEKEKQLSQSPGHKRIGSDGSEEAAETCVLKVVWNGLEELKNATEFTKSLEPLHHGKVWIPADLRKRLNIEMHAVVRITPLETTPVIPRALRLQPAENLPRDVSEEEVKAVFSSWLQESATTMFPLIISKQECIKLEIKDGLKEFSLSIVHSQEKEKEQGRTVFVLSPILLQKISVQVLLEPMIGEHSEEIDILLPSLTLSSLGGVSSLSVSAMEHITHSLLGRPLSRQLMALVAGLRNGALLITGGKGSGKSTLAKAICKEAHDALDAHVEMVDCKALRGKRLESIQKALEVAFSEAAWRQPSVILLDDLDLIAGLPSTPEHEHSPEAVQSQRLAHALNNMIKEFVSMGSLVALIATSQLQHSLHPSLVSAQGVHTFQCIQHIQPPDQEQRCEILHSVVKNKLGCDISKSPDLDLKCIAKETEAFVARDFTVLVDRAIHSSLSRQQNPTREGLTLTTADFQKALRGFLPASLRNVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVVARESGMNFISIQGPELLSKYIGASEQAVRDVFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILTVLSKSLPLADDVDLQHVASVTESFTGADLKALLYNAQLEALQGRLLPGGLHDGGSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGASCDLSSHCLSAPSSMTQDLPATPGKDPLFTQHPVFRTPSQEGSQDLTQEQRDQLRADISIIKGRYQSQSGEDESLNQPGPIKTSFAISQAHLMTALAHTRPSINEDEGKEFAELYENFQNPKKRKNQSGTVFRTGQKVTLA
Protein: GH14382p (Multiplexin, isoform N) (Q8MT89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMVISTRAKLVITALILFFLLGIVLVTGSTKGWFNPNRYNGERVAARIQATDIFDASGMQPPGQTQYTHERPYRGIKGEKGERGPKGDSIRGPPGPPGPPGPKGETAPYPPFVETTSAGAKYTGECTCNASDILEAIKDNESLRESLRGAPGTPGKDGKPGTPGHTGATGVPGARGARGSEGAQGLKGEPGVDGLPGVMGPPGPPGPPGLPENYDESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTFTTAPEYETWYPRMLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (Q9W719)
Organism: Gallus gallus (Chicken)
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Pribosyltran domain-containing protein.
- Purine nucleoside phosphorylase
- Adenylosuccinate synthetase isozyme 2
- GMP synthase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase
- AMP deaminase 1
- Adenylosuccinate synthetase isozyme 1
- Guanine deaminase
- AMP deaminase
Sequence:
MATHSPCIVIGDDEQGYDLDLFCIPKHYADDLEKVYIPHGLIMDRTERLAREIMKGMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDKSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMKTLLSLLKQYNPKMVKVASLLVKRTPRSVGYRPDFVGFEVPDKFVVGYALDYNEYFRDLNHICVISETGKQKYKA
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (Q5B224)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- DNA topoisomerase I
- Chromosome segregation protein sudA
- Ubiquitin-like domain-containing protein
- DNA repair protein Rad18, putative
- SUMO-conjugating enzyme UBC9
- Condensin complex subunit 2
- Flavoprotein, putative
- Nuclear condensin complex subunit Smc4, putative
- Myosin-binding domain-containing protein
- Ubiquitin-conjugating enzyme E2 2
Sequence:
MSDDDSLMGSVFSDDGSSDFMTDEAPKPKKAAKKAAPKKAPAKKAAVKPKKKAKADSEDEMSDPDDPLDVDSVLSQTPPKKVPAAATKKSGFKPLADVENESIPIDDVDASEEVKASSKYQKLNLREHITIRPDSYIGSVERTTQEMWVYNSEIDGMEFREVSYVPGLYKIFDEIVVNAADNKQNDDNMDEIRVTYSRETNEISVWNNGKGIPVEMHEEHGMYIPQLIFGNLLTSSNYDDAKEKITGGRNGFGAKLCNVFSTEFTVETQDSKQKKRYLQTWTDNMQTVGKPKITAAKGSDFTRVTFKADFPRFGMDGIDDDFEALIKRRVYDLAGTTGVTVKLNGTRLPVRNFKKYMEMYTKAIRRERGDDDSKSDPIITCSPHPYWEIGFAVSDGSFKQVSFVNSIATTSGGTHVNYIADQIAGKLSESLKKNKKGTGSILKPAQIRNYCFLFVNAKIVNPAFSSQTKEQLTTKQTQFGSKPILDESFLKKVANSGVLDSLKRFADHKADLMLKKSDGGRRSRMNNPKLTDANRAGTKDGYKCTLILTEGESAKGLAMAGRAVVGADLFGVYPLRGKMLNVRDASFDQISKNEEIQSIKNFMGLQHKKEYTDTKGLRYGHLMIMTDQDHDGSHIKGLLINFLEAQFPSLLKIPEFLIEFITPIVKVWKGDIKDPTKQHSFFTIQEYNAWKEKHGHERGWEHKYYKGLGTSSTEEAQEYFRDLDRHLKEFHVMQDKEHELIELAFSKKKVEERKEWLRQYNPDTFMDHSVAKISYTDFINNELIQFSMADNLRSIPSMVDGMKPGQRKVMYTVMKRNIKKDVKVLDLTGQVFSLTAYHHGDASMHQTIIGLAQDFVGSNNVNTLEPSGNFGSRLKGGADASSARYIHTRLSPFARKIFHPHDDPILKYLEDDGKEIEPWVYVPVVPMILINGADGIGTGWSTSIPNYNPEDIVDNLKRMIRGEEIKPMQPWFKGFKGEVTQLGPDKYKFSGLIKQVSDKELEVTELPIRTWTQDFINKLEEMIKADKAPSLIKDYKDYNTNSDVHLVLQLDEKNVKEPLTQEFLEEKFKLSKTIATTNLVAFNAEGQMTKYPNVEAILEEFYRLRLKFYGKRKQHQLDQLQIELEKLTNQARFVQMIIDGDLVVSKKKKSVLVKELDSLGFKRFNKTADAAKAGETEKVIEASEDEDTEAQDDTQDLAHAFDYLLGMAIWSLTQERVEKLRRQIGEKEHEIDELIKLSSEDIWLRDLDEFINEWRFQLSETDRRRRGQQKKGRRVSTKLATAARAVGGKKRKAAGDDSDDDFVVSKSKKKAAANKTEPAGGIMSFLKKTPKPEPAANDSDSDSDFGFGIEEVMPKKSRGPVKASPQLKDEDGDLDMEASEVEVAPKKSRGPPKAAPKAAAKLKDEDKDEDEPKVKPVTKRGRPAKPKPKDDDSDGLDDDEFMEIAKAEAAKTAPPRAGRKAAPKYTLDDSDSDNGDDLLGDVSKMVKGIGGAAGGSATDSRQLFSELSRPGSSTGLPTNSKTSKFDNDFDADETDYSKLIPQNSPRRSLQVKPKDVKASESIDLDDEEDKPIKPAKTKAAPKAKAAPAPKAGTGKGRGRPKKDATATASSLKQTTLSPAAKAYASKQAKGASTASKKKTLMDDSEDDIDAMANDILDSPVGIRDEAPAPPRSTASRPSRRTTTKKSYVIEDDDSEDGADNQDDSFDLSD
Protein: 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (HMG-CoA reductase 1) (EC 1.1.1.34) (P12683)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA). HMG1 and HMG2 catalyze the reduction of hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate-limiting step within the first mosule. The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2
- Hydroxymethylglutaryl-CoA synthase
- Mevalonate kinase
- Squalene synthase ERG9
- Farnesyl pyrophosphate synthase
- Squalene epoxidase ERG1
- Isopentenyl-diphosphate delta-isomerase
- Phosphomevalonate kinase
- Geranylgeranyl pyrophosphate synthase BTS1
- Lanosterol 14-alpha demethylase CYP51
Sequence:
MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQCILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCSMYAHQLKTLTNFCILSAFILIFELILTPTFYSAILALRLEMNVIHRSTIIKQTLEEDGVVPSTARIISKAEKKSVSSFLNLSVVVIIMKLSVILLFVFINFYNFGANWVNDAFNSLYFDKERVSLPDFITSNASENFKEQAIVSVTPLLYYKPIKSYQRIEDMVLLLLRNVSVAIRDRFVSKLVLSALVCSAVINVYLLNAARIHTSYTADQLVKTEVTKKSFTAPVQKASTPVLTNKTVISGSKVKSLSSAQSSSSGPSSSSEEDDSRDIESLDKKIRPLEELEALLSSGNTKQLKNKEVAALVIHGKLPLYALEKKLGDTTRAVAVRRKALSILAEAPVLASDRLPYKNYDYDRVFGACCENVIGYMPLPVGVIGPLVIDGTSYHIPMATTEGCLVASAMRGCKAINAGGGATTVLTKDGMTRGPVVRFPTLKRSGACKIWLDSEEGQNAIKKAFNSTSRFARLQHIQTCLAGDLLFMRFRTTTGDAMGMNMISKGVEYSLKQMVEEYGWEDMEVVSVSGNYCTDKKPAAINWIEGRGKSVVAEATIPGDVVRKVLKSDVSALVELNIAKNLVGSAMAGSVGGFNAHAANLVTAVFLALGQDPAQNVESSNCITLMKEVDGDLRISVSMPSIEVGTIGGGTVLEPQGAMLDLLGVRGPHATAPGTNARQLARIVACAVLAGELSLCAALAAGHLVQSHMTHNRKPAEPTKPNNLDATDINRLKDGSVTCIKS
Protein: Serine (or cysteine) peptidase inhibitor, clade A, member 3I (D3Z450)
Organism: Mus musculus (Mouse)
Interaction partners:
- Haptoglobin
Sequence:
MAGVSPAVLGCPDVTLERNTAVHEVQENITSGDSLTVASSNTDFAFSLYRKLVLKNPDENVVFSPFSIFTALALLSLGAKSNTLKEILEGLKFNLTETPEPDIHQGFRYLLDLLSQPGDQVQISTGSALFVEKHLQILAEFKEKARALYQAEAFTADFLQPCQAKKLINDYVSNQTQGKIKELISDLDKSTLMVLVNYIYFKGKWKMPFDPRDTFNSKFYLDEKRSVKVPMMKIEELTTPYFRDDELSCSVVELKYTGNASALFILPDQGKMQQVETSLHPETLRKWKNSLKPSRISELHLPKFSISNDYSLEHVLPVLGIREVFSMQADLSAITGTMDLRVSQVVHKAVLDVTETGTEAAAATGVKVNLRCGKIYSMTIYFKRPFLIIISDINTHIALFMAKVTNPK
Protein: PMS1 homolog 1, mismatch repair system component (A0A8I6AGZ9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKQLPAATVRLLSSSQTITSVVSVVKELIENSLDAGANSIDVKLENYGFDKIEIRDNGAGIKAVDVPVMAVKYYTSKISSHEDLQTLTTYGFRGEALGAICNVAEVVVTTRTAADDFSTQYVLDGSGHILSQKPSHLGQGTTVTVLKLFKNLPVRRQFYSTPKKCKDELKNVQDLLISYAVLKPDLRITFVHNKIHLRGLFPKHDADHNSTSLSTPERSFIFINSRPVHQKDILKLIRHYYNLKCLKESTRLYPIFFLKIDVPSAEVDINLTPDKSQVLLQNKESVLIALENLLMTCYGPLPTTESYENNRVDVSSANVVISETTETDVLFNKMESSGNKYPNADTLAIPFQNDESRKNTDHHLNEQINIGHCDGHFSGEYSHINKDTFQNIPRNNLSSEANQSKHSETHSAGSIEHIQGENGRSGTGENGEDGKKTLPEKALEICVDDWSKGNVFNSMGENIEPVKILVPQKSLSCKVTNSHPNPEPENLSVGPGSRTSNVIDNRPGQLTAYDLISSRAVKKPMSACALFIQDHRTQFLAENPKTGLEDVTAQIKAQWETLSEEEKHKYEEKAKKDLERYNNQMKKAIEQEAQVSLKDGRKKLRATGAWGCTQRHKVKDLSNQPKLDELFQSQNEKKSENIKITKIPFSMENLKVNFNKQKEVDLEEKDEICLIHSLKFPDAWLVTSRADVMLLNPYRVEEALLFKRLLENHKFLAEPLEKPIVLTESLFNGSDYLEVLHKMSTVEERCRGSVYLCDPRLTANGFKIRLTPGVSSAENYLEIEGMAKCLPFYGVMDLKEILNAIVNKNAKEIYECRPRKVINYLEGEAVRLSRQLPMYLPQEDVQDLIYKMKHQFGKEIKGCVHGRPFLHHLIHLPGTS