wanglab/gogpt-training-data huggingface dataset:
Protein: Glycine receptor subunit alphaZ1 (O93430)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q64018}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000250|UniProtKB:Q64018}. Perikaryon {ECO:0000250|UniProtKB:Q64018}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q64018}. Cell membrane {ECO:0000269|PubMed:10188956, ECO:0000269|PubMed:26344198}; Multi-pass membrane protein {ECO:0000269|PubMed:26344198}.
Interaction partners:
- Gephyrin
- Gephyrin
- Transporter
- Glycine receptor subunit beta
Sequence:
MFALGIYLWETIVFFSLAASQQAAARKAASPMPPSEFLDKLMGKVSGYDARIRPNFKGPPVNVTCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYSEYPDDSLDLDPSMLDSIWKPDLFFANEKGANFHEVTTDNKLLRISKNGNVLYSIRITLVLACPMDLKNFPMDVQTCIMQLESFGYTMNDLIFEWDEKGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEARFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVGLGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFIARQHKELLRFQRRRRHLKEDEAGDGRFSFAAYGMGPACLQAKDGMAIKGNNNNAPTSTNPPEKTVEEMRKLFISRAKRIDTVSRVAFPLVFLIFNIFYWITYKIIRSEDIHKQ
Protein: Cerebral cavernous malformations 2 protein-like (CCM2-like) (Q9NUG4)
Organism: Homo sapiens (Human)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 3
- Programmed cell death protein 10
Sequence:
MEYEVKKGKKGFVSPIRRLVFPKAGRRAACRSSVSRRPLHSMPLYPPDYLIDPQILLCDYLEKEVKFLGHLTWVTSSLNPSSRDELLQLLDTARQLKELPLKTTAEQDSILSLSARCLLLTWRDNEELILRIPTHEIAAASYLQDDALHLLVLKTGLGVDPVPAGVDASPGGAGRDPGPPGGAPEKRRVGTAERRHTICSLDWRMGWGGGAAEARAGGGGGGSLERQRAGARASGSWERRQTFSGSWERRHGGGGGGGGAGKPGGSWERRQAGSGGGGSWERRHPGPNPLDPQDPSPDAYCNLVILAVANRDAAEESCALICQVFQIIYGDQSIECVDRAGYHYTSTPERPWLCSRSESCHTDGTYAYDADFSCCSSFNGSQDTFEACYSGTSTPSFHGSHCSGSDHSSLGLEQLQDYMVTLRSKLGPLEIQQFAMLLREYRLGLPIQDYCTGLLKLYGDRRKFLLLGMRPFIPDQDIGYFEGFLEGVGIREGGILTDSFGRIKRSMSSTSASAVRSYDGAAQRPEAQAFHRLLADITHDIEALAPDDDDDDEDEPRGSRGGSDAAEDNYL
Protein: Tumor protein 63 (p63) (Chronic ulcerative stomatitis protein) (CUSP) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) (p40) (p51) (Q9H3D4)
Organism: Homo sapiens (Human)
Function: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:12446779, ECO:0000269|PubMed:20123734}.
Interaction partners:
- Tumor protein p73
- Cellular tumor antigen p53
- Transcription factor SOX-2
- p53 apoptosis effector related to PMP-22
- E3 ubiquitin-protein ligase Mdm2
- Casein kinase I isoform delta
- GA-binding protein subunit beta-1
- E3 ubiquitin-protein ligase Itchy homolog
- Keratin, type II cytoskeletal 5
- Histone acetyltransferase p300
Sequence:
MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRPILIIVTLETRDGQVLGRRCFEARICACPGRDRKADEDSIRKQQVSDSTKNGDGTKRPFRQNTHGIQMTSIKKRRSPDDELLYLPVRGRETYEMLLKIKESLELMQYLPQHTIETYRQQQQQQHQHLLQKQTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEEGE
Protein: DNA fragmentation factor subunit alpha (Q498U6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELSRGASAPDPDDVGPLKPCLLRRNHSREQHGVAASSLEELRSKACELLAIDKSLTPVTLVLAEDGTIVDDEDYFLCLPSNTKFVALACNEKWAYNDSDGGTAWLSQESFDTDQTDSGAGVKWKNVARQLKEDLSSIILLSEEELQALIDIPCAELAQELCQSCATVQGLQSTLQQVLDQREEARQSKQLLELYLQALEKEGSILSNQNESKAALGEELDAVDTGVGGEVASEVMLRSQILAALKEKPAPELSLSSQDLEVGKN
Protein: Exopolyphosphatase (ExopolyPase) (EC 3.6.1.11) (Metaphosphatase) (P0AFL6)
Organism: Escherichia coli (strain K12)
Function: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues.
Subcellular location: Cell membrane {ECO:0000305|PubMed:8380170}; Peripheral membrane protein {ECO:0000305|PubMed:8380170}.
Interaction partners:
- Polyphosphate kinase
- GTP pyrophosphokinase
- Guanosine-5'-triphosphate,3'-diphosphate pyrophosphatase
- Bifunctional
- Phosphoribosylglycinamide formyltransferase
Sequence:
MPIHDKSPRPQEFAAVDLGSNSFHMVIARVVDGAMQIIGRLKQRVHLADGLGPDNMLSEEAMTRGLNCLSLFAERLQGFSPASVCIVGTHTLRQALNATDFLKRAEKVIPYPIEIISGNEEARLIFMGVEHTQPEKGRKLVIDIGGGSTELVIGENFEPILVESRRMGCVSFAQLYFPGGVINKENFQRARMAAAQKLETLTWQFRIQGWNVAMGASGTIKAAHEVLMEMGEKDGIITPERLEKLVKEVLRHRNFASLSLPGLSEERKTVFVPGLAILCGVFDALAIRELRLSDGALREGVLYEMEGRFRHQDVRSRTASSLANQYHIDSEQARRVLDTTMQMYEQWREQQPKLAHPQLEALLRWAAMLHEVGLNINHSGLHRHSAYILQNSDLPGFNQEQQLMMATLVRYHRKAIKLDDLPRFTLFKKKQFLPLIQLLRLGVLLNNQRQATTTPPTLTLITDDSHWTLRFPHDWFSQNALVLLDLEKEQEYWEGVAGWRLKIEEESTPEIAA
Protein: Forkhead box protein P1 (Q498D1)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor. Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential. Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal cord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintenance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18. Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis. Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor. Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B. Can negatively regulate androgen receptor signaling (By similarity). Acts as a transcriptional activator of the FBXL7 promoter; this activity is regulated by AURKA (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H334}. Note=Not found in the nucleolus. {ECO:0000250|UniProtKB:Q9H334}.
Interaction partners:
- Forkhead box P4
- Nuclear factor of activated T-cells 2
Sequence:
MMQESGSEAKSNGSTIQNGSSGGNHLLECGTLRDTRSNGEAPAVDLGAADLAHVQQQQQQALQVARQLLLQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQMQQILQQQVLSPQQLQVLLQQQQALMLQQQQLQEFYKKQQEQLQLQLLQQQHAGKQPKEQQQQQVATQQLAFQQQLLQMQQLQQQHLLSLQRQGLLTIQPGQPALPLQPLAQGMIPTELQQLWKEVTSAHTAEETTGSNHSSLDLTSTCVSSSAPSKTSLIMNPHASTNGQLSVHTPKRESLSHEEHPHSHPLYGHGVCKWPGCEAVCDDFPAFLKHLNSEHALDDRSTAQCRVQMQVVQQLELQLAKDKERLQAMMTHLHVKSTEPKAAPQPLNLVSSVTLSKSASEASPQSLPHTPTTPTAPLTPVTQGPSVITTTSMHTVGPIRRRYSDKYNVPISSADIAQNQEFYKNAEVRPPFTYASLIRQAILESPEKQLTLNEIYNWFTRMFAYFRRNAATWKNAVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISGNPSLIKNMQSGHAYCTPLNAALQASMAENSIPLYTTASMGNPTLGSLASAIREELNGAMEHTNSNESDSSPGRSPMQAVHPIHVKEEPLDPEEAEGPLSLVTTANHSPDFDHDRDYEDEPVNEDME
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 4A (Mast cell surface glycoprotein Gp49B) (CD antigen CD85k) (Q64281)
Organism: Mus musculus (Mouse)
Function: Inhibitory receptor involved in the down-regulation of the immune response. Receptor for FN1. Receptor for integrin ITGAV/ITGB3. Inhibits IgE-mediated mast cell activation, at least in part through interaction with ITGAV/ITGB3. Also inhibits KITLG/SCF-mediated mast cell activation. Through interaction with ITGAV/ITGB3, inhibits antibody production by memory and marginal zone B cells, probably by suppressing their differentiation into plasma cells. Inhibits IFNG production by CD8 T cells, CD4 T cells and natural killer cells. Inhibits antigen presentation by dendritic cells to T cells, preventing T cell activation. Inhibits lipopolysaccharide-mediated neutrophil-dependent vascular injury. Suppresses the allergic inflammatory response by inhibiting infiltration of neutrophils and eosinophils and preventing mast cell degranulation. Inhibits lysis by natural killer cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10982834, ECO:0000269|PubMed:11323698, ECO:0000269|PubMed:8855262, ECO:0000269|PubMed:8977169}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 6
- Tyrosine-protein kinase SYK
- High affinity immunoglobulin gamma Fc receptor I
- Low affinity immunoglobulin gamma Fc region receptor III
- Low affinity immunoglobulin gamma Fc region receptor III-A
- Apolipoprotein E
- High affinity immunoglobulin epsilon receptor subunit gamma
- Integrin alpha-X
Sequence:
MIAMLTVLLYLGLILEPRTAVQAGHLPKPIIWAEPGSVIAAYTSVITWCQGSWEAQYYHLYKEKSVNPWDTQVPLETRNKAKFNIPSMTTSYAGIYKCYYESAAGFSEHSDAMELVMTGAYENPSLSVYPSSNVTSGVSISFSCSSSIVFGRFILIQEGKHGLSWTLDSQHQANQPSYATFVLDAVTPNHNGTFRCYGYFRNEPQVWSKPSNSLDLMISETKDQSSTPTEDGLETYQKILIGVLVSFLLLFFLLLFLILIGYQYGHKKKANASVKNTQSENNAELNSWNPQNEDPQGIVYAQVKPSRLQKDTACKETQDVTYAQLCIRTQEQNNS
Protein: Small ribosomal subunit protein eS12 (40S ribosomal protein S12) (P25398)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS26
- Small ribosomal subunit protein uS14
Sequence:
MAEEGIAAGGVMDVNTALQEVLKTALIHDGLARGIREAAKALDKRQAHLCVLASNCDEPMYVKLVEALCAEHQINLIKVDDNKKLGEWVGLCKIDREGKPRKVVGCSCVVVKDYGKESQAKDVIEEYFKCKK
Protein: Kidney mitochondrial carrier protein 1 (Solute carrier family 25 member 30) (Q9CR58)
Organism: Mus musculus (Mouse)
Function: Probable transporter.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:15809292}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSALNWKPFVYGGLASITAECGTFPIDLTKTRLQIQGQTNDANFREIRYRGMLHALMRIGREEGLKALYSGIAPAMLRQASYGTIKIGTYQSLKRLAVERPEDETLLVNVVCGILSGVISSAIANPTDVLKIRMQAQNSAVQGGMIDSFMSIYQQEGTRGLWKGVSLTAQRAAIVVGVELPVYDITKKHLILSGLMGDTVATHFLSSFTCGLVGALASNPVDVVRTRMMNQRALRDGRCAGYKGTLDCLLQTWKNEGFFALYKGFWPNWLRLGPWNIIFFLTYEQLKKLDL
Protein: Hydrogenase-2 small chain (HYD2) (EC 1.12.99.6) (Membrane-bound hydrogenase 2 small subunit) (NiFe hydrogenase) (P69741)
Organism: Escherichia coli (strain K12)
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.
Subcellular location: Cell membrane; Peripheral membrane protein; Periplasmic side. Periplasm.
Interaction partners:
- Hydrogenase-2 large chain
- Hydrogenase-1 large chain
- Probable Ni/Fe-hydrogenase 2 b-type cytochrome subunit
- Hydrogenase-2 operon protein HybA
- Hydrogenase-2 operon protein HybE
- Hydrogenase 2 maturation protease
- Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit
- Hydrogenase maturation factor HypB
- Hydrogenase-1 small chain
- Hydrogenase maturation factor HybF
Sequence:
MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECTGCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGSIPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVLPGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDAGRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGIGFHKGIHQLANVENQTPRSQKPDVNAKEGGNVSAGAIGLLGGVVGLVAGVSVMAVRELGRQQKKDNADSRGE
Protein: Uncharacterized membrane protein YMR155W (Q03795)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized membrane protein YJL163C
Sequence:
MVKKHQNSKMGNTNHFGHLKSFVGGNVVALGAGTPYLFSFYAPQLLSKCHIPVSASSKLSFSLTIGSSLMGILAGIVVDRSPKLSCLIGSMCVFIAYLILNLCYKHEWSSTFLISLSLVLIGYGSVSGFYASVKCANTNFPQHRGTAGAFPVSLYGLSGMVFSYLCSKLFGENIEHVFIFLMVACGCMILVGYFSLDIFSNAEGDDASIKEWELQKSRETDDNIVPLYENSNDYIGSPVRSSSPATYETYALSDNFQETSEFFALEDRQLSNRPLLSPSSPHTKYDFEDENTSKNTVGENSAQKSMRLHVFQSLKSSTFIGYYIVLGILQGVGLMYIYSVGFMVQAQVSTPPLNQLPINAEKIQSLQVTLLSLLSFCGRLSSGPISDFLVKKFKAQRLWNIVIASLLVFLASNKISHDFSSIEDPSLRASKSFKNISVCSAIFGYSFGVLFGTFPSIVADRFGTNGYSTLWGVLTTGGVFSVSVFTDILGRDFKANTGDDDGNCKKGVLCYSYTFMVTKYCAAFNLLFVLGIIGYTYYRRRATANSL
Protein: 1,3-beta-glucanosyltransferase (EC 2.4.1.-) (Q6FTR7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}. Cell membrane {ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
Interaction partners:
Sequence:
MQYSLVSFIIAATLLLSSVMADDLPAIEIKGNKFFFSNNGSQFYMKGIAYQADTANVTGGATINDPLADWDTCSRDIPYLQQLATNVIRVYAVNTSLDHSRCMNALNDAGIYVIADLSSPKVSVNRKSPSWDLEIFDRYKSVVDMFANYSNVLGFFAGNEVTNDATNTDASAFVKAAIRDTKSYIKEKGYRGIPVGYSSNDDADTRVDIADYFACGDDAERADFYGINMYEWCGNSTFQKSGYADRTKEFANLSIPLFFSEYGCNEVQPREFTEVQALYGPDMTDVWSGGIVYMYFQEANNYGLVSIDGSSVKTLEDFNYYSKEIHSISPSSVNSKTYTPTATSLACPSTNQYWKAATNLPPTPQLDLCECMDAANSCIVQDDVDEDDYQDLFSYLCGKIDCGGITGNGTTGKYGSYSFCSPKEKLNFVLNLYYNAQGGSKSNCDFSGSATLRSGTTQAGCASALKEIGSVGTNSATDSVTFSGGSTGTSKASATGSNSSKSGSSKSGSSTSSSAKSSSSGKSNKKSNSSSSVQVGLYQLLFSAFITLGAVAGAGFALI
Protein: ArsR (Helix-turn-helix transcriptional regulator) (B5LWZ9)
Organism: Campylobacter jejuni
Interaction partners:
Sequence:
MQKFLTIISAINDESRVLILHHLLRYKELCVCDLQELLNMGQSRLSRHLKILKDAGFLYVKRKGTWAYYGINNELLKLHSDLFENIKNLDIDNIVLEQNTCENDK
Protein: Paired amphipathic helix protein pst1 (SIN3 homolog 1) (Q09750)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in modulating the nuclear import of TF1 virus-like particles. Essential for viability.
Subcellular location: Nucleus.
Interaction partners:
- Histone deacetylase clr6
- Transcriptional regulatory protein sds3
- Chromatin modification-related protein png2
- RbAp48-related WD40 repeat-containing protein prw1
- Chromatin modification-related protein eaf3
- Uncharacterized protein C2F7.07c
- Transcriptional regulatory protein rxt3
- Uncharacterized protein C16C9.05
- Putative histone deacetylase complex subunit cti6
- Transcriptional regulatory protein rxt2
Sequence:
MAKDWQDARLGQCHRLEDYSNVAINYTGPYLTPSGTMAYHPGNAPLFTQAPPHTNPQGPPPFPLFNSISPVYDPATGRLLYRNVNTQVSHTAIPNPANGYAAVYGGPPSQLPPPPQPQSHPNVTVISASPARAIEQQPTILSSTDSNIPRPGTVKSSASPFVPNQNPSAPPPPPQEYRQLNVTDALSYLDLVKLQFHQEPEIYNEFLDIMKEFKSQAIETPEVITRVSKLFAGYPNLIQGFNTFLPPGYSIEISSADPGSLAGIHITTPQGPLMINDLGKTTAPPPPHGSTTPLPAAASYTSMNMKQSSASHPVLQPPAPSTLQFNPSPSPAAPSYPPVDASVKQAADLDQAINFVNNVKNRFSHKPEAYNSFLDILKSYQHDQRPIQLVYFQVSQLFAEAPDLLEEFKRFLPDVSVNAPAETQDKSTVVPQESATATPKRSPSATPTSALPPIGKFAPPTTAKAQPAPEKRRGEPAVQTRNHSKRTRTATSSVEETTPRAFNVPIAQNKNPSELEFLEHARQYLANESKYNEFIKLLELYSQEVFDKNALVERCYVFFGSNEHLMNWLKDLVKYNPANPIPVPRPRVDLTQCKSCGPSYRLLPKIELLLPCSGRDDLCWTILNDAWVSFPTLASEDSGFIAHRKNQFEENLHKLEEERYEYDRHIGANMRFIELLQIHADKMLKMSEVEKANWTLPSNLGGKSVSIYHKVIKKVYGKEHAQQIIENLQKNPSVTIPIVLERLKKKDREWRSLQNHWNELWHDIEEKNFYRSLDHQGVSFKSVDKKSTTPKFLISELRNLAQQQKVELSEGKVTPSHQFLFSYKDPNIITDIARLFGVFLIHGSTHSAEDNEKMSNFLRSFLSLFFDVPYDSFIPYLPTHFNEEESDIDSLSSSLIEKPRASSSPIHHANNNGLRLLKDVLKKTYRGARENRSSVKEDYVSESTERTPDASEIDEHISEHEENDDESSSVFSTGEVWVNCKFTDTDGSLLDDGTKLSDRSVYNLFGNMSLYCFFRLFHTLYSRLEEIKNLEQMAYSKQHDVKSNPVAVELGLVRHPSERLGFALPTADTVYEQAIQLCERLMEGEIDQNGFEDALRCLYGIHAFRLYTVEKLVTSIIKQLHSVTTNRRLAQVFMYYEKDRVQRRTSPRQQIMYRIQTETAFGPDENLCCIDWNSQTRQSAIRLMGREDLTMGTLKSDAEKWCYYIGSYIMSSPTEGILPEHVRIPFLRKCLPSDEGNEDDESSSVVKSANAIITSFLESGLALTIPINTVKIRYENGTEDVFARNSEQVYNGPYDKIRDYRQSKWREWLNSDEGWTQGLSKDKVRRIKPCTIESLFNESTLRSGKAERFSENAGVESIGKKGKNLLNESGNGKKLDKGLPPKVNGKSSVTRGNKTNLKARNGRNNDDSSNKINLSEKEKEKESIEDEEKNREGSMSPVAKHASDVEDDHDVAKSTAPDFETSSHRPERSSEKKSPSPVFTSVKQTAENDADNEDDKTDMDDQTEETLDADNTMEEEPSKDDL
Protein: Cytochrome P450 monooxygenase helB1 (EC 1.-.-.-) (Helvolic acid biosynthesis cluster protein B1) (Q4WR17)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid. Protostadienol synthase helA cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid. Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton. This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid. Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order. The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21. C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation. The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protostadienol synthase helA
- Acyltransferase helD2
- 3-ketosteroid 1-dehydrogenase helE
- Acyltransferase helD1
Sequence:
MRTYAIRPVSNRLPGPIEPKKHRRDRDNSTTGSLYNALIHPVQGEKTITSTMIRVAEFQPFLNTISVLQVLAAIFIGALTYRLIDAFFLSPLRSIPGPLLARLTTKRANVDTFSGKVTQTVDKDVARYGDVYVYKPRAVCINHPDDIRAVLGSQEFRKAAFFDIFNDGNTPNIVSLREPELANRRRRQLGPFFNYAYLGRAEPLILQHGYQAIRTKWDALIQANSGRPTEVNYRTDTQLVTFDIMSALAFGRNFNAISRGSSSIMKWAGLIMEMLESPAVLALLSLLPFSLIMRPWKIMYRELAAFSSDAVDMRKQLLAEDSTEKPLDMLQAFIDAEDPESKIKMSPHEVQAESIMMMLAGSETTSSAIMWTFHLLLLYPETLRRAVHEVRSAFSLNHLVTYKDVRSSLPYVEACVYEALRHSPTTAGLTPRISHSTGITLQGYYIPPGTEIYVNLRSPSMHPSLWDDPARFNPDRFLDSDNNKRLLFTFSYGPRNCLGRNLAWVEMLTIVANVLKDYDIALTEDSLFGPHCTDENGLPVLMPAKCFIASFPAKPERDCRMVITRRMAGVKACAREYSPC
Protein: Transport and Golgi organization protein 6 (Q9VJ29)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in protein secretion and Golgi organization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16452979}. Golgi apparatus {ECO:0000269|PubMed:16452979}.
Interaction partners:
Sequence:
MINTAKYFALLESLRFSKALANTANNSGTAEALEINLRILEKYAKLEIGQQLHELCLEYQLTDDHESSIDPDSDRTICYIIRLQHVLHSIMRNINFHSDAKEDLISVAHLKLCIQASQELSYYSLRCQLHEDFYKSPIFCEAQGKIKANFSLMLLSIQFFINLLHIRQYHIANSMELVQRDLLAAIVSLRVQQDSPLLDKAIAYLWQYESKADFFRNILLFKATTLCPTLAQLLHRQLLGKLHLPQGFASLVEALHQNPNVNSSRNAEIVASIVARKGFSQLAQEKMVLQVLEYCKFYLQNADKMCAGVLSLRRLYDLSDTNQKLIKEILFKHWETLCNPEDIINGLILMDHQELCNRILLWQHLFCSSTVACLPSNLLVPYLPLLLQLYDGLPMELPASSQISAIILRCLDNREMKNELPAILQKLFKWEIEKEPPWKCLNPRIIILPSMNTTQIQVKVAHKDHLADHDMGRILPGLLTSSSHHSLTCKVFLSLLGFIAKQINDKSSASVDFISSEAELKDFLHSKYQLKLDLLIALNQMVAHQPLRAQLSQHTKELLHILKDLLVHRSREQDTTDQILLLVLNLLQEILEGSENIQLSEACKELKEQLHLLGTRSSNPLIQQSVKSLLTIIHGAWRPSEAVKIQPFQRARSLIEEKQSHMQVYGIQMMIDLLKKRDPATLAQGQLIIALALTTLKDKESYTFLNCVRLFVSLVHVMESDVLDKLSDEYLSETAHLDYRLVVGEAILKVAQELGPLCFRYKAVLLNCFMYGSRSPVHEFRMSAFANLAQLCRLLAFQVQNFFHELLQLVNSELTTGGYVPSKRAAVLVLAELLNGMENLLDYQEMLLPIYRLLKAIEADESCDPQMRQHAANGLKILNKKCTKLIQSALEEKSLQKQIKVLGIKDDDSPQRRNRHILELN
Protein: DNA-directed RNA polymerase subunit beta'' (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta'') (RNA polymerase subunit beta'') (Q6ENI2)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01324}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- Uncharacterized protein
- RNA polymerase Rpb4/RPC9 core domain-containing protein
- DNA-directed RNA polymerase RBP11-like dimerisation domain-containing protein
- DNA-directed RNA polymerase I subunit rpa49
- DNA-directed RNA polymerase III subunit RPC5
- Uncharacterized protein
Sequence:
MAERANLVFQNKEIDGTAMKRLISRLIDHFGMGYTSHILDQIKTLGFHQATTTSISLGIEDLLTIPSKGWLVQDAEQQSFLLEKHYYYGAVHAVEKLRQSVEIWYATSEYLKHEMNSNFRITDPSNPVYLMSFSGARGNASQVHQLVGMRGLMADPQGQMIDLPIQSNLREGLSLTEYIISCYGARKGVVDTAVRTADAGYLTRRLVEVVQHIIVRRRDCGTIQAISVSPQNGMTEKLFVQTLIGRVLANDIYIGSRCIATRNQDIGIGLVNRFITTFRAQPFRAQPIYIRTPFTCRSTSWICQLCYGRSSTHGDLVELGEAVGVIAGQSIGEPGTQLTLRTFHTGGVFTGGTADLVRSPSNGKIQFNGDLVHPTRTRHGQPAFLCYIDLHITIQSQDILHSVTIPSKSLILVQNDQYVESEQVIAEIRAGTSALHFKEKVQKHIYSESDGEMHWSTDVYHAPEYQYGNLRRLPKTSHLWILSVSMCRSSIASFSLHKDQDQMNTYSFSVDGRYIFGLSMADDEVRHRLLDTFGKKDREILDYSTPDRIMSNGHWNFVYPSILQNNFDLLAKKRRNRFAIPLQYHQEQEKEPISCFGISIEIPFMGVLRRNTIVAYFDDPRYKKDKKGSGIVKFRYRTLEDEYRTREKDSENEYGSPENEYRTREEECKTLEDEYRTREEEYETLEDEYGIPENEYETLEDEYGILEDEYRTREEESEDEYGSPENKYRPREDKYGTLEEDSEDEHGTLEEDSEEDSEDEYGNPEEDSVLKKGVLIEHRGTKEFSLKYQKEVDRFFFILQELHILPRSSSLKVLDNSIIGVDTQLTKNTRSRLGGLVRVKRKKSHTELKIFSGDIHFPEEADKILGGSLIPLEREKKDSKESKKRENWVYVQWKKILKSKEKYFVLVRPAVAYEMNEGRNLATLFPQDLLQEEGNLQLRLVNFISHENSKLTQRIYHTNSQFVRTCLVLNWEQEEKEEARASLVEIRANGLIRDFLRIGLIKSTISYTRKRYDSRSAGLILHNRLDRTNTNSFYSKAKIQSLSQHQEAIGTLLNRNKEYQSLMVLSASNCSRIGFFKNSKNPNGVKESNPRIPIPKFFGLFRNFSGLLGTIAPSISNFSSSYYLLTYNQILLKKHLLLDNLKQNFKVLQGLKHSLINENQRTSNFDSNIMLDPFQLNWHFLPHDSWEETSAKIHLGQFICENVCLFKSHIKKSGQIFIVNIDSFVIRAAKPYLATTGATVHGHYGEILYKGDRLVTFIYEKARSSDITQGLPKVEQIFEARSIDSLSPNLERRIEDWNERIPRILGGPWGFLIGAELTIAQSRISLVNKIQKVYRSQGVQIHNRHIEIIIRQVTSKVRVSEDGMSNVFSPGELIGLLRAERAGRALDESIYYRAILLGITRVSLNTQSFISEASFQETARVLAKAALRGRIDWLKGLKENVVLGGIIPVGTGFQKFVHRYPQDKNLYFEIQKKKLFASEMRDILFLHTELVSSDSDVTNNFYETSESPFTPFI