wanglab/gogpt-training-data huggingface dataset:
Protein: Terpene synthase 3 (EC 4.2.3.-) (EC 4.2.3.106) (EC 4.2.3.15) (Q86II4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into an unidentified sesquiterpene as a major product, as well as beta-maaliene, aristolene, calarene and 2 additional unidentified sesquiterpene as minor products. Is also able to convert geranyl diphosphate (GPP) into a mixture of monoterpenes including (Z)-beta-ocimene, (E)-beta-ocimene, allo-ocimene, linalool and beta-myrcene.
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase B
- Uncharacterized protein
Sequence:
METINLEKPLYSLKKFYFPSEWSYPINKNYKHIKDTYNEGVSCGIFEASNEKHFAYANGVLNCVTWFYPKYDYEQCMVAASIMLWIFVLDDFLERDHMTDEKQQYCVKKYEDILIFGKDSSYISNIEYNDLTPLDKYSLILRKRLLNPTIHRIESFNIFIHYLREWFFSIIPLKKSKGNNHDSVPIEVYQFIRTINIGLFFVVGVNSVAVRTNVHGSFWLNPIWNRMVRSASRQIIIFNDCVSYAKELNHDCAGENCLYILQKKLNLPFEKVYSELIAEAKQCIFDIQNDEKLLIKSLSHISEEEMNGVIYLVEQLHEIICGNRDWALMTPRYIHKDSPFIETNGIDSLFVPYETILDPNLY
Protein: Protein FAM81A (D4A7T8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Postsynaptic density {ECO:0000269|PubMed:30735723}. Cytoplasm {ECO:0000250|UniProtKB:Q8TBF8}.
Interaction partners:
Sequence:
MHLRRVRTMPRHSQSLTMAPYSSVSLVEQLEDRILCHEKTTAALVEHAFRIKDDIVSSLQKMQNKGGGDRLARLFLEEHIRNITAIVKQLNRDIEVLQEQIRARDNISYGTNSALKTLEMRQLSGLGDLRGRVARCDASIARLSAEHKTTYEGLQHLNKEQQAAKLILETKIKDAEGQISQLLNRVDLSISEQSTKLKMSHRDSNHQLQLLDTKFKGTVEELSNQILSARSWLQQEQERIEKELLQKIDHLSLIVKENSGASERDMEKKLTQMSARLDKIEESQRRNAEGQRKPEEEKVHGRISKLELQMTEDMKEMKAEVNAGFTAIYESIGSLRQVLEAKMKLDRDQLQKQIQQMQKPESSM
Protein: Transcription factor 4 (TCF-4) (Class A helix-loop-helix transcription factor ME2) (Immunoglobulin transcription factor 2) (ITF-2) (MITF-2) (SL3-3 enhancer factor 2) (SEF-2) (Q60722)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Isoform 2 inhibits MYOD1 activation of the cardiac alpha-actin promoter. Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription. May have a regulatory function in developmental processes as well as during neuronal plasticity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Catenin beta-1
- Myoblast determination protein 1
- Transcription factor 7-like 2
- Lymphoid enhancer-binding factor 1
- LIM domain-binding protein 1
- POU domain, class 5, transcription factor 1
- DNA-binding protein inhibitor ID-2
- Neurogenic differentiation factor 1
- Transcription factor Atoh1
- Junction plakoglobin
Sequence:
MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGTGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRENVQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNARRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPAASTFPSSFFMQDGHHSSDPWSSSSGMNQPGYGGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGTGAAGSSQTGDALGKALASIYSPDHTNNSFSSNPSTPVGSPPSLSAGTAVWSRNGGQASSSPNYEGPLHSLQSRIEDRLERLDDAIHVLRNHAVGPSTAVPGGHGDMHGIMGPSHNGAMGSLGSGYGTSLLSANRHSLMVGAHREDGVALRGSHSLLPNQVPVPQLPVQSATSPDLNPPQDPYRGMPPGLQGQSVSSGSSEIKSDDEGDENLQDTKSSEDKKLDDDKKDIKSITRSRSSNNDDEDLTPEQKAEREKERRMANNARERLRVRDINEAFKELGRMVQLHLKSDKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSSEPPPLSLAGPHPGMGDAANHMGQM
Protein: Neuronal acetylcholine receptor subunit eat-2 (Abnormal pharyngeal pumping eat-2) (Q9U298)
Organism: Caenorhabditis elegans
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane (By similarity). Nicotinic acetylcholine receptor in the MC pharyngeal motor neuron involved in pharyngeal pumping. Has a role in the determination of life span possibly via calorific restriction which affects growth rate, although this is independent of metabolic activity. Plays a role in the defense against the accumulation of ingested live pathogenic bacteria in the intestine.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:15020415}; Multi-pass membrane protein {ECO:0000269|PubMed:15020415}. Cell membrane {ECO:0000269|PubMed:15020415}; Multi-pass membrane protein {ECO:0000269|PubMed:15020415}. Note=MC motor neuron. {ECO:0000269|PubMed:15020415}.
Interaction partners:
- Insulin-like receptor
- Forkhead box protein O
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Defective pharyngeal development protein 4
- NAD-dependent protein deacetylase sir-2.1
- Protein skinhead-1
- Protein glp-1
- Uncharacterized protein
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
Sequence:
MTLKIAFFTLILLVSIERVYSSDEEYRLLKDLREGYDPVERPVADHRKPVNVKLRLILQQLVDVDERNQVITLVVWNQYTWNDYKLRWSPEEYGNITTLQIPHGTLWKPDILLFNSANEHFDASFPVHMVVSSNGDVLFAPPGIVSFSCSLSMTWFPYDQQVCYLKFGSWTYGKKLDLQIDDSDLPDGHKMDLQYYIPNGEFDLLATPAFRKSTTFLDETYVELYFHMHLKRRTMYYGLNWIVPSILISLSNILGFTMPPECGEKITLQITNFLSVMVFLAMVSEVAPPTSESIPIIAAFFSLSIVILGLSICASLIIVNIFFRHPKTHRMGDWTRYVFLEWLPWFLLMSRPEHTFCRPRREEEKNDEEAGGDGTKLLENQQHQPRPRLLVNSQLVMDSTVPYLEEIIGYLKVFKAKLDDDEEEEEEILNWRFMAMVIDRLSLFLFTGLIFGTTALIFAFCPNLFTDSPIVDIE
Protein: Vicilin Jug r 2.0101 (7S globulin) (7S seed storage protein) (Allergen Jug r 2) (Vicilin Jug r 2) (Vicilin-like Jug r 2) (allergen Jug r 2.0101) (Q9SEW4)
Organism: Juglans regia (English walnut)
Function: Seed storage protein.
Interaction partners:
Sequence:
RGRDDDDEENPRDPREQYRQCQEYCRRQGQGQRQQQQCQIRCEERLEEDQRSQEERERRRGRDVDDQNPRDPEQRYEQCQQQCERQRRGQEQTLCRRRCEQRRQQEERERQRGRDRQDPQQQYHRCQRRCQIQEQSPERQRQCQQRCERQYKEQQGRERGPEASPRRESRGREEEQQRHNPYYFHSQSIRSRHESEEGEVKYLERFTERTELLRGIENYRVVILDANPNTSMLPHHKDAESVAVVTRGRATLTLVSQETRESFNLECGDVIRVPAGATVYVINQDSNERLEMVKLLQPVNNPGQFREYYAAGAKSPDQSYLRVFSNDILVAALNTPRDRLERFFDQQEQREGVIIRASQEKLRALSQHAMSAGQRPWGRRSSGGPISLKSESPSYSNQFGQFFEACPEEHRQLQEMDVLVNYAEIKRGAMMVPHYNSKATVVVYVVEGTGRYEMACPHVSSQSYEGQGRREQEEEESTGRFQKVTARLARGDIFVIPAGHPIAITASQNENLRLLGFDINGENNQRDFLAGQNNIINQLEREAKELSFNMPREEIEEIFESQMESYFVPTERQSRRGQGRDHPLASILDFAFF
Protein: Ankyrin repeat and MYND domain containing 1 isoform 2 (A0A0S2Z596)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGAHASLSLEDEVSGAGSRQRPLEGKGGETPAAEEPGSLKNYAVFATRDVSAAPEKEEEEAEGPLRAQDLRESYIQLVQGVQEWQDGCMYQGEFGLNMKLGYGKFSWPTGESYHGQFYRDHCHGLGTYMWPDGSSFTGTFYLSHREGYGTMYMKTRLFQAEEALADHQAAAAPGRGPQPVLRAHAGPVPCCEGRGRGWGEAAAGARGEDRHLLSAAA
Protein: Split discs, isoform A (Split discs, isoform E) (Q9W5E8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSLAAVPQASATGSSSNSNINNNNALAALQDGGAAAAAAADFYQQLAAAATATATATSANGSNTSADSPVSSFPAAAAAVAVAAVAASSYQQQQQQQQLLNNEQQQQQLLEANNKMQELHKQMERFRSEQMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADESESHYSSTSSLNSGTPDLGTTPIIFPPSSDWHESIRLPVLQSTNLHVNVGNEVGAGQGTNTSSGSGGDLASTTKATLPLRDQQQLAITSTQSQVQNVSQPSTPATPSSAGSSSSGGLPFGNVSKSFISGERKDPLNMLAKNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNINDMCQIERPDWMQVMSYVTAVYKYFET
Protein: Ran-binding protein 3-like (Q6PDH4)
Organism: Mus musculus (Mouse)
Function: Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner.
Subcellular location: Nucleus {ECO:0000305|PubMed:25755279}. Cytoplasm {ECO:0000305|PubMed:25755279}.
Interaction partners:
Sequence:
MSTTQRKDDSHLFTSSCTRQLQVQEDRQQQEKYVIAQPIFVFEKGEHNFKRPAEDSLEETAEPEFTGFLRKRVRSSSVTLHTTDPQSQGVATLSQTRLRSSSFTDVPTFPPCRPVRKNNVFMTSRLLQRSDDMNNVEQGPPMRSSEQVLRPAVLQPSQTQSCQKAGTTFGPGALKSYKTKEKAEHEISEVGSSSSLLSENLPNARSSIQLSTDPCISEAPSGCQPKEDKCSFTSCSSDFVFGENMVERVLGTQKLTQPPLQNLSYAKEKTFKSVLKFPNAVSNSDSIENISLVESAAAFSSKPSQKCLLEKIDVITGEETEHNVLKINCKIFVFNKATESWSERGQGILRLNDTAGRECGTLQSRLIMRNQGSLRLVLNSRLWAQMKIQRASQKNLRITATDLEDDGIKIFLIQASAKDTGFLYAAIHHRLVALRSLAKQGDGGPAESQSDTALPQLNGESCDEDEDEIAQVTKNGSDPSRWSHRQSIVCS
Protein: NK1 transcription factor-related protein 2 (Homeobox protein SAX-1) (NKX-1.1) (P42580)
Organism: Mus musculus (Mouse)
Function: May function in cell specification, particularly in the CNS.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeodomain-interacting protein kinase 2
Sequence:
MLAWQDVGAKAAPSHHKISFSVLDILDPQKFTRAALPPVRLAALEAKKSLEEVEAGQDACSGNPIGSQETPDAVGRGIDPGSPVEGSEAEEEEEAEDAGRAHQPERWQGVHEGSPEARAVAVGTEESGAEGLPASPGSPGSPRPRRRRAESSCAKPRRARTAFTYEQLVALENKFRATRYLSVCERLNLALSLSLTETQVKIWFQNRRTKWKKQNPGADGAVQAGGGAPQPGTPGAVAGGGGSATGSSPGPPVPGALPYQTFPTYPATNVLFPAASFPLTTAANGSPFTPFLGPSYLTPFYAPHL
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (B2LYR8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MAAHIFTTTPSHLALSFPSSTNPSNPPVLLSSFRGVSLKLPRQSLSLAATIPKKPFSVFAVTKKAVAVLKGNSEVEGVVTLTQETDGPTTVNVRITGLTPGPHGFHLHEYGDTTNGCMSTGAHFNPNNMTHGAPEDEVRHAGDLGNIIANADGVAEATIVDNQIPLSGPNAVVGRASVVHELEDDLGKGGHELSLTTGNAGGRLACGVVGLTPV
Protein: ESAT-6-like protein EsxV (Antigen Mtb9.9B) (P0DOA7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probable virulence factor. In mice, elicits increased levels of IFN-gamma, IL-12 and IgG(2a), indicating a dominant Th1 host immune response.
Subcellular location: Secreted {ECO:0000305|PubMed:19876390}. Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS) (Probable). May bind to lipid membranes after dissociation of the complex (Probable). {ECO:0000305|PubMed:19876390, ECO:0000305|PubMed:21134129}.
Interaction partners:
Sequence:
MTINYQFGDVDAHGAMIRAQAGSLEAEHQAIISDVLTASDFWGGAGSAACQGFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA
Protein: PX domain-containing protein kinase-like protein (Modulator of Na,K-ATPase) (MONaKA) (Q7Z7A4)
Organism: Homo sapiens (Human)
Function: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16142408}. Cell membrane {ECO:0000269|PubMed:16142408}; Peripheral membrane protein {ECO:0000269|PubMed:16142408}. Note=Also associates with the plasma membrane. Isoform 3 is present throughout the cell.
Interaction partners:
- PHD and RING finger domain-containing protein 1
- B-cell scaffold protein with ankyrin repeats
- Calcium-activated potassium channel subunit alpha-1
- Tumor necrosis factor ligand superfamily member 4
Sequence:
MAFMEKPPAGKVLLDDTVPLTAAIEASQSLQSHTEYIIRVQRGISVENSWQIVRRYSDFDLLNNSLQIAGLSLPLPPKKLIGNMDREFIAERQKGLQNYLNVITTNHILSNCELVKKFLDPNNYSANYTEIALQQVSMFFRSEPKWEVVEPLKDIGWRIRKKYFLMKIKNQPKERLVLSWADLGPDKYLSDKDFQCLIKLLPSCLHPYIYRVTFATANESSALLIRMFNEKGTLKDLIYKAKPKDPFLKKYCNPKKIQGLELQQIKTYGRQILEVLKFLHDKGFPYGHLHASNVMLDGDTCRLLDLENSLLGLPSFYRSYFSQFRKINTLESVDVHCFGHLLYEMTYGRPPDSVPVDSFPPAPSMAVVAVLESTLSCEACKNGMPTISRLLQMPLFSDVLLTTSEKPQFKIPTKLKEALRIAKECIEKRLIEEQKQIHQHRRLTRAQSHHGSEEERKKRKILARKKSKRSALENSEEHSAKYSNSNNSAGSGASSPLTSPSSPTPPSTSGISALPPPPPPPPPPAAPLPPASTEAPAQLSSQAVNGMSRGALLSSIQNFQKGTLRKAKTCDHSAPKIG
Protein: Keratin, type II cuticular Hb4 (65 kDa type II keratin) (Keratin-84) (K84) (Type II hair keratin Hb4) (Type-II keratin Kb24) (Q99M73)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSCRSYRVSSGRRVGSFSSCSAMAPQHLNRFRSSSVSCRSGPGFRGLGGFGSRSVINFGSSSPRIAVGCSRPVRCGVGFGAGSGMAFGSGDGLGFRASSGVGLGFGAGGCPSYGFGGPGFGGPGFGGPGFGYRIGGIGGPSAPAITAVTVNQSLLTPLNLEIDPNAQRVKRDEKEQIKTLNNKFASFIDKVRFLEQQNKLLETKWSFLQEQKCARSNLEPLFDNYITNLRRQLDVLSSDQARLQAERNHLQDILEGFKKKYEEEVVFRANAENEFVALKKDVDAAFLNKSDLEANVDTLIQETEFLKALYHEEIEMLQSHISETSVIVKMDNSRDLNLDGIIAEVKAQYEEVARRSRADVESWYQTKYEEMRVTAGQHCDNLRSTRDEINELTRLIQRLKAEIEHTKAQCAKLEAAVAEAEQQGEAALNDAKCKLADLEGALQQAKQDMARQLREYQELMNVKLALDIEIVTYRRLLEGEEIRICEGVGPVNISVSSSRGGVLCGPELVSGSSLSHNGGVTFSTSSSIRATGGVLASSSLRAGGDLLSSGSRGGSVLVGDACAPSIPCALPTEGGFSSCSGGRGNRSSSVRFSSTTTSRRTRY
Protein: Radixin (Q5PQK5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cell projection {ECO:0000256|ARBA:ARBA00004316}.
Interaction partners:
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTMKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMCAPPPPPPPAVVPPTENEHDEQDEHSAEASAELSSEGVTNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM
Protein: BHLH transcription factor Mesp-b (Mesoderm posterior ba) (Q9IB69)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQTSSKNRWSSSSSESEFSSISSPETTSPDQSFSPPHQTKPPCSKLVKSSNIMRKKRRLRLKNPSERRQNASEKEKLRMRDLTKALHHLRSFLPASVAPVGQTLTKIETLRLTIQYISFLSSQLGLSEEELSYRRQENSSGCSLSSFECSSVNGGFVGTEQGYALCDGQYEDCSGYGGQYRERYGGLTQQHSTEQNGLVSIDGFIQSQQCGQMTQTPYQVYGKNFGYHLVPQTYWR
Protein: Peroxidase stcC (EC 1.11.1.-) (Sterigmatocystin biosynthesis cluster protein C) (Q00668)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Peroxidase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
Sequence:
MLLKSIQNIVCGLVPTFFLFGSAAAELDFEQWHPAGLGDLRCGCPAMNSLANHGFINHNGSNITVNEVIPLMQEVFHLSEELATIVTGLAVLSADDPASGIFNLDMLNRHNIFEHDASLTRKDFYLGGDGHTIDQPTLDEFLSYFDGKEWIDLNDAAAARYARVLDSREKNPSFLYQDQQLITSYGETIKYFRTMVDPRSNKTSAEFVRILFTEERLPVREGWQRPREEISGFSLASDVVQLALRTPEKFIGMPFDQRPFAEQAFDPLPWQRPPIWTPPNYPGFSKRHFSELVGRFAKKALPFRA
Protein: Transcription initiation factor TFIID subunit 7 (RNA polymerase II TBP-associated factor subunit F) (Transcription initiation factor TFIID 55 kDa subunit) (TAF(II)55) (TAFII-55) (TAFII55) (Q15545)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF7 forms a promoter DNA binding subcomplex of TFIID, together with TAF1 and TAF2. Part of a TFIID complex containing TAF10 (TFIID alpha) and a TFIID complex lacking TAF10 (TFIID beta).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9R1C0}.
Interaction partners:
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 4B
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 9B
- Transcription initiation factor TFIID subunit 4
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
Sequence:
MSKSKDDAPHELESQFILRLPPEYASTVRRAVQSGHVNLKDRLTIELHPDGRHGIVRVDRVPLASKLVDLPCVMESLKTIDKKTFYKTADICQMLVSTVDGDLYPPVEEPVASTDPKASKKKDKDKEKKFIWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKEAENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEDETQHQDEEDINIIDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQAVLDELKQKEDREKEQLSSLQEELESLLEK
Protein: Protein SRL3 (RAD53 lethality suppressor protein 3) (P36167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Weakly suppresses a RAD53 null mutation when overexpressed.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11914276}.
Interaction partners:
- Cyclin-dependent kinase 1
- Regulatory protein SWI4
- G1/S-specific cyclin CLN2
- Regulatory protein SWI6
- G1/S-specific cyclin CLN3
- Cyclin-dependent kinases regulatory subunit
- Probable S-adenosylmethionine-dependent methyltransferase CRG1
- Protein STB1
- Transcription factor MBP1
- G1-specific transcriptional repressor WHI5
Sequence:
MFLKTPNWETVNETPKSRVLTINELISPNLDTESNSLLATPARKYFKTSISEAQDSPTSAPSPDGNEDPTYQYNVQFHFPGPITPTTPRSKNAEMFPSPTPPLVSPTAVIEEENDDSVREFSRTLKSRLNCAMVKLSKEHEQVALIPPPPTEKIRKGSYSNKFAAKHRRCHSLDESKKFLSSLEDSSAHAAFLKAISSKHAKSNRVDNVNVSPLRWSSHRRTQSTQENSLQEVVAIDTLLKMSSSD
Protein: Serine/arginine-rich splicing factor 10 isoform 1 (A0A0S2Z504)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
Protein: ADAM metallopeptidase with thrombospondin type 1 motif B, isoform B (EC 3.4.24.-) (Q9W493)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MTCSRMWIRSRWLGLLLHYWLVVVTQGGGVRPLYGLHSDELVAGEGQLVVPRRVHPDGAFMTHQLEYAHELDHRRHRQRRSLNSEHDTQAADLHLLLPLANETLHLELMAHSYFLAPNLVVERHRRDLRTRSPLTTRHLNCHFHGKVRGQPATNVAISTCAGLVGHIRTAGNEYFIEPSKEHEPHPVNGHPHVVFQRSSVKPKHSLRKRNKRKRGGKSGSGAEVSNCGTREPRRRMETRLEWQARGKVKVQGGRQIRRHHHHHHHHHHKHKYRHHQQKISRVPHTKFKYETQFQTEPDHAEIPRRRRSISSPRHVETLIVADATMSAFHRDLNGYLLTIMNMVSALYKDPSIGNSIEIVVVRIIQLDEEESQLQLNLTQNAQKNLDRFCSWQHKLNKGSEKDPHHHDVAILITRKNICANNCMTLGLANVGGMCKPKQSCSVNEDNGIMLSHTITHELGHNFGMFHDTAKIGCHPRVGPIVHIMTPTFGADTLQVCWSNCSRKYITHFLDQGLGECLDDPPTPLDEYNYTGELPGMRYNARGQCRLQFNLTTDSEVGACSAPHEFCSTLWCKVNGECVTHMRPTAPGTLCGRNKWCQNGKCVRREELAAVNGGWGDWSEWSECSRSCGGGVSTQQRECDNPVPANGGVFCIGERKRYKICRKRPCPAEEPSFRAQQCARFDNVSYQGATYKWLPFFDKNNPCKLFCSDVDDTIIANWGATVLDGTPCTLGTNNMCIDGICKKVGCDWIVDSEVQDDRCGVCGGSGDQCQPVRETYTDPFAAKDGAYVEIVTIPARARHILIRELANSPHFLAIATGDGGDRFYLNGDSLISMPGEFEIAGAESLYDRVDEQETITIPQPIQHSISLYAIVRGNESNAGIFYEFTLPALNVTAGRQFQWRLSNWTACSASCGGGVQHREPICQENGKALGDTLPCWTHAKNKRPARQSRGCGDQPCPAHWWPGPWQFCPVTCRPVGFVAPPQRRRSVVCLDEHDVVVADAECGHLQKPAEMEPCESSLPICRTK
Protein: Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A) (P17174)
Organism: Homo sapiens (Human)
Function: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. In addition, catalyzes (2S)-2-aminobutanoate, a by-product in the cysteine biosynthesis pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1974457}.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Alanine aminotransferase 2
- Aspartate aminotransferase, mitochondrial
- Alanine aminotransferase 1
- Glutamate dehydrogenase 1, mitochondrial
- L-lactate dehydrogenase A-like 6B
- L-lactate dehydrogenase A-like 6A
- Fumarate hydratase, mitochondrial
- L-lactate dehydrogenase C chain
- L-lactate dehydrogenase A chain
Sequence:
MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ
Protein: Prolyl 4-hydroxylase 13 (AtP4H13) (EC 1.14.11.2) (F4ILF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:21680836}; Single-pass type II membrane protein {ECO:0000305|PubMed:21680836}.
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Proline iminopeptidase
- Proline dehydrogenase 2, mitochondrial
- Proline dehydrogenase 1, mitochondrial
- Arabinosyltransferase XEG113
- Hydroxyproline O-arabinosyltransferase 1
- Arabinosyltransferase RRA3
- Arabinosyltransferase RRA1
- Hydroxyproline O-arabinosyltransferase 3
- Prolyl 4-hydroxylase 5
Sequence:
MRSYGKEKKLVFPYVFIACCFFLAIFGFCFFNLFSQGISFSEIPTTRRSVNDETDSLDHGSSVSNIPFHGLSWNPRVFYLPNFATKQQCEAVIDMAKPKLKPSTLALRKGETAETTQNYRSLHQHTDEDESGVLAAIEEKIALATRFPKDYYESFNILRYQLGQKYDSHYDAFHSAEYGPLISQRVVTFLLFLSSVEEGGETMFPFENGRNMNGRYDYEKCVGLKVKPRQGDAIFFYNLFPNGTIDQTSLHGSCPVIKGEKWVATKWIRDQTYD