wanglab/gogpt-training-data huggingface dataset:
Protein: SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein) (Q9Z266)
Organism: Mus musculus (Mouse)
Function: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:12877659}; Peripheral membrane protein {ECO:0000269|PubMed:12877659}; Cytoplasmic side {ECO:0000269|PubMed:12877659}. Cytoplasm, cytosol {ECO:0000269|PubMed:12877659}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12877659}. Golgi apparatus membrane {ECO:0000269|PubMed:17101137}. Lysosome membrane {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11283605}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000250|UniProtKB:O95295}.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- Synaptosomal-associated protein 25
- Dysbindin
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- BLOC-1-related complex subunit 8
- KxDL motif-containing protein 1
- Biogenesis of lysosome-related organelles complex 1 subunit 4
Sequence:
MAAAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGVYPPGSPSK
Protein: tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS (tRNA(Ile2)-agm2C synthetase) (EC 6.3.4.22) (tRNA(Ile2) agmatidine synthetase) (O28025)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- Probable L-aspartate decarboxylase
- Translin
- DNA-directed RNA polymerase
Sequence:
MRVWVGIDDTDSSRGMCTTYLAVLAMERVERELGKVIGFPRLIRLNPTIPYKTRGNGAVSFLVEVDDVGELVDVVNEVIIEHAMLDDEKTNPGAVFVDEELAVKLKPFADKAIKDVLQIDEALFVIGKYFIPHLRHKKGRGLIGALAAVGAELEDFTLELIAYRYPERFGTEREYDEESFFDMDYELYPQTFDNVDWCNDVVVCIPNTPCPVLYGIRGESVEALYKAMESVKTEPVDRRMIFVTNHATDMHLIGEEEVHRLENYRSYRLRGRVTLEPYDIEGGHVFFEIDTKFGSVKCAAFEPTKQFRNVIRLLRKGDVVEVYGSMKKDTINLEKIQIVELAEIWVEKNPICPSCGRRMESAGRGQGFRCKKCRTKADEKLREKVERELQPGFYEVPPSARRHLSKPLIRMNVEGRHIFR
Protein: Cytochrome b6-f complex subunit 4 (17 kDa polypeptide) (P0C317)
Organism: Oryza sativa (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01344}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01344}.
Interaction partners:
Sequence:
MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF
Protein: LD47230p (Tracheal-prostasin (EC 3.4.21.-)) (Q9W2C8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Nuclear pore complex protein Nup153
Sequence:
MNRAWLCLLICLALSCGPSQSASQDRATNQTAASPLLKQSQNTFIQWVLSLLPQRPGSSDSENATLATLSSSSMMPDAASTTSTTTPAPSSSTTTTRRATTPAPPTLNPPRNCSDCVCGIANIQKRIVGGQETEVHQYPWVAMLLYGGRFYCAASLLNDQFLLTASHCVYGFRKERISVRLLEHDRKMSHMQKIDRKVAEVITHPKYNARNYDNDIAIIKLDEPVEFNEVLHPVCMPTPGRSFKGENGIVTGWGALKVGGPTSDTLQEVQVPILSQDECRKSRYGNKITDNMLCGGYDEGGKDSCQGDSGGPLHIVASGTREHQIAGVVSWGEGCAKAGYPGVYARVNRYGTWIKNLTKQACLCQQETKKIK
Protein: 1700016M24Rik protein (Q14DS2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MILCECPSVEKVQCHLASLLDLSHQHSRQREGIALAVGLASTKHLEEVWALLEHLGRTKFLQSVAATEDSQDEILKSSFLSATILLTRSLQAEYSSQRYKFTQTPELIQCLLGILQKEPNSLTNFLRQKIILVIIGLSNLRPRFKPLLKSQILKTCLQTVYMLPPAKDSRNDLFSVEQASDTTVLYKKTVRALDLLLQNFISENPSMDEVCFLLQHIEYWLMSDKIHERSRAVQSIYLLLQYVVDSLKLAKEAVPSLLGHQIGILILLWRDKDKITQQHSHFCVYLLMELVFQQKGKLVESAQWSKMKHFESNVFREWEMKLYHLVKVFKEDLTVAQHTQLILTLVHSLGSYNHLHSDLAAKLLLLICVEPGFRKEQIAELLQGLFQELPNIQSKSVQQAISQATLALGTQHIQEVVEVILSLCQPSERWILPLWKALAANYQVARDVITLLYIKLKLRPPRRLLQSTYRARLVSLMALGTIYELLYTKEYRNTVCWAFSGILLGLLTELYYLLEVGLVQGLFDYQEDDLGSKPLGPCRICLEALKGLFWTTEYWEVFADVKLIQGWELFGQLETFPKGVTLLARAMAHYNCEIKAVLGQALISLKSSEERDNIVGICIITEFLNSPDVSQHMSWKTMYNSLNLGLSSRNQMVRAMSLKGLGSTLMHPKKATLLRSKLMELLDNFLQPEFKDPAGLMKIMGHLLHCLSAQGIGIVSLKIAQHLLSLFTDERAAVREGAIFLFGDVIHYGGKKLRQSLKDVASQATVPLLFNMADPCQEVAMKARFTFLRCAILLKWEFRKELFGKLAWGQGLGAANDIFIYMLESNVGNYQQFLSQALTYLDSSHMTVKLAAMKFIGALLQDYFNDLCIYLRKKDVIFLKNCLEALRHDTDSRTRRFYLNYWNDAVELSYYVQD
Protein: Protein sprouty homolog 2 (F1QU39)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Cbl proto-oncogene, E3 ubiquitin protein ligase.
- non-specific serine/threonine protein kinase
- Growth factor receptor-bound protein 2
- Dual specificity protein phosphatase
- Fibroblast growth factor 8
Sequence:
METRTQNGGSGSSGLLRALRDSGRPQTGDSEPWDGQVLSLDQIRTIRGSNEYTEGPTVAPRPPASEQKTDSQASSPTSTSSIELPEHRNSLRAQQAGQQTPQQAPRGGVSRSISGTSDGSHSTTRASTGSTSSDQRLLGNAGDRVVRVQPKRSEQKQEELKPLSAPVGPAPDGKHSVLCEDCGRCKCEGCTCPRTLPSCWMCGRRCVCSATSAMDYVTCVCCVKCLFYHCSSDDEDVCADKPFSCTQSHCCMRWSAISVLALFLPCLLCYLPAKGCVALCQACYDCTSRPGCRCKNKGVEK
Protein: Homeobox protein HEX homolog pha-2 (Defective pharyngeal development protein 2) (Q21578)
Organism: Caenorhabditis elegans
Function: Transcriptional repressor (By similarity). Involved in pharyngeal development and required for the formation of the pharyngeal isthmus. Plays a role in modulating cytoskeleton in the muscle cells of the isthmus. Regulates expression of the acetylcholinesterase genes ace-1 and ace-2. May regulate its own expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682, ECO:0000269|PubMed:15282157}.
Interaction partners:
- EB domain-containing protein
- Putative protein tag-53
Sequence:
MDQKFYISSLLQEDTPSKEKPETSSESPIPTGSECSLNESSDTTLDQKMEPNKKMFNGTLDFNPWICHVSQQLAAQLSQNGKNRPGAPNQVPLLNMNVNQTMGNMWDPRLSWLYPYMSKSPQKRKGGQIRFTNEQTDALEHKFDSHKYLSPQERKKLAKSLSLSERQVKTWFQNRRAKWRRVRKDGEDEDEMPNGASARSLGQLQSSNPFLSHG
Protein: Probable secreted beta-glucosidase PSU1 (EC 3.2.1.-) (Cell wall synthesis protein psu1) (Q9UR09)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cell wall synthesis. May be required for the activation of 1,3-beta-glucan synthase.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- Polyadenylation factor subunit 2
Sequence:
MRFFETLALALLTTGALAAPFRHPHHLLNKRDVSVVTSKVYAYTTVTLEAAASAISTNGAAKEAATAAGDAETTSSVAASVTPAASSSVAASVTPVASSSVAASVTPVSSSAVVDSATSAAASSSVIPTSSSVVASSSEVASSTTSSAAASATSTGSSSGGFQDGVYDCTDFPSDQSGVVALDYLGYGGYSGIQIGDGAGSSCVEGAYCSYACSPGMLKTQWPSTQPSDGETRGGLLCKGGKLYRTNTAYDNLCENGVGTASVQNTLGQGVAICQTDYPGSENMVIPTYVGGGATSPLSVTDNANYFQWEGKGTSAQYYVNKAGYTAEQGCQWGTSSGDYGNWSPLVFGAGMTDGTTWLSISQNPLTSQLANYNVKIVGADGASVSGTCVFENGAFQNGGSGCTVGITSGSGVFVFY
Protein: DEL-1 (EGF like repeats and discoidin domains 3 L homeolog precursor) (Q6RUW2)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MILKGVSQILLFTSCWLSLITAKGDVCDPNPCENGGICLSSLSDESFSCECPAGFSDLNCPSVMEVDVEVENSTTVGPCHPNPCHNGGICEISEAYRGDTFIGYVCKCSHGFNGIHCQHNVNECEAEPCKNGGICTDLVANYSCECPGEYMGRNCQYRCSGPLGMEGGIISNQQITASSTHRALFGLQKWYPYFARLNKKGLVNAWTSAENDRWPWIQINLQKKMRVTGVITQGAKRIGSPEYIKSYKIAYSDDGKSWSTYKVKRTSEDMIFRGNVDNNTPYANSFTPPIEAQYIRLYPQVCRRHCTLRMELLGCELSGCSEPLGMKSGHIQDHQVTASSVFRTLNMDMFAWEPRKARLDMQGKVNAWTSGKSDQSQWLQVDLLRPAKVTGIITQGAKDFGHVQFVGSYKIAYSNNGEHWAVYQDGKQRKDKVFQGNFDNDTHRKNVMDPPIYARYIRILPWSWYGRITLRAELLGCTEEN
Protein: Calcium-binding EF-hand family protein (F4HZU8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MARLSLFLSFLSLIALISVVNCRVLSSLSEKDSILVSDGVQDGSSYEFLSLDPPNDITKNMCVHVYDFLPCADNVAGYVFQVFSFGCILIIGEYFLTKGRTKLFLIFEVGFYGGIIFPLLTMFPRIALILSTGLVGSREMASSRVGNIIGVTVGYSVFALTIQWGACILFGLSGTKPEQPIDLSAASVEADITNKKSAGIMLLTILPFILVTFSEISSSQYWNDIIVLITLIISASATFAYFFYSYFDRDDQAKSLDHARFELMSEVHKHLQIFSPKSLIRDGQLNQESLKRLFQKIDANGDGKIQVAELKDLTVEFGMIGRVKCHIDKLVHTLVDDFDRDGDREIDEAEFEIGIKKWLNQYKFSFDTTVPPREDQAEGVPILKVEKPEQSLVKKLLSWRTLRASLEVILGMLVVIYLARPFMMNIQLLSESAGVPSFYVVFVVIPLARNLKNTLSAHFCRKKDKAKITSDTFSEIYKDVTMNNLMGISIILAIVYARELVWDYTTEVLIIVIVGLLIGLPAYVRTTYPFWICLLAFALYFISLVVVYFHFMSLEKGTTVTFNK
Protein: Zinc finger and BTB domain-containing protein 26 (Zinc finger protein 481) (Zinc finger protein Bioref) (Q9HCK0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger and BTB domain-containing protein 6
Sequence:
MSERSDLLHFKFENYGDSMLQKMNKLREENKFCDVTVLIDDIEVQGHKIVFAAGSPFLRDQFLLNDSREVKISILQSSEVGRQLLLSCYSGVLEFPEMELVNYLTAASFLQMSHIVERCTQALWKFIKPKQPMDSKEGCEPQSASPQSKEQQGDARGSPKQDSPCIHPSEDSMDMEDSDIQIVKVESIGDVSEVRSKKDQNQFISSEPTALHSSEPQHSLINSTVENRVSEIEQNHLHNYALSYTGSDNIIMASKDVFGPNIRGVDKGLQWHHQCPKCTRVFRHLENYANHLKMHKLFMCLLCGKTFTQKGNLHRHMRVHAGIKPFQCKICGKTFSQKCSLQDHLNLHSGDKPHKCNYCDMVFAHKPVLRKHLKQLHGKNSFDNANERNVQDLTVDFDSFACTTVTDSKGCQPQPDATQVLDAGKLAQAVLNLRNDSTCVN
Protein: ECA polysaccharide chain length modulation protein (P0AG00)
Organism: Escherichia coli (strain K12)
Function: Modulates the polysaccharide chain length of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02025, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02025}.
Interaction partners:
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- UDP-N-acetyl-D-mannosamine dehydrogenase
- UDP-N-acetylglucosamine 2-epimerase
- Probable ECA polymerase
- Lipid III flippase
- dTDP-glucose 4,6-dehydratase 2
- Putative O-antigen transporter
- UDP-N-acetyl-D-mannosaminuronic acid transferase
- dTDP-4-amino-4,6-dideoxygalactose transaminase
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Sequence:
MTQPMPGKPAEDAENELDIRGLFRTLWAGKLWIIGMGLAFALIALAYTFFARQEWSSTAITDRPTVNMLGGYYSQQQFLRNLDVRSNMASADQPSVMDEAYKEFVMQLASWDTRREFWLQTDYYKQRMVGNSKADAALLDEMINNIQFIPGDFTRAVNDSVKLIAETAPDANNLLRQYVAFASQRAASHLNDELKGAWAARTIQMKAQVKRQEEVAKAIYDRRMNSIEQALKIAEQHNISRSATDVPAEELPDSEMFLLGRPMLQARLENLQAVGPAFDLDYDQNRAMLNTLNVGPTLDPRFQTYRYLRTPEEPVKRDSPRRAFLMIMWGIVGGLIGAGVALTRRCSK
Protein: Pex20p (Q3ZJZ2)
Organism: Pichia angusta (Yeast) (Hansenula polymorpha)
Interaction partners:
Sequence:
MSFSNAFGDSCGANNALNKFTQRANVDNSLANQLRANSDSQRLQAQPHQTVDQQLESEYRAFQQQTPSYQASFQTLPTPAFIEENQWVNHFRDMNLHDTPGAQHLQQVPTQSLHSQQWRHEFAQSQQQQQQQETADTYSSAFRMRTGAPQLATSLAPQVVSAATVREDFSAVDAAFDELEHEMHDEKMEEQQAEQVKPQNEDDKIKFAQLARSVFLTMSQPPADISKQTSDKFQKSNFLKLMNRISTREVEMNEDRDRFVDAQGRDIRDMLPDPLKDIKEEGLAGMGPFASAQQVYSQMGDDLRPSMWQ
Protein: Ent-kaur-16-ene synthase, chloroplastic (EC 4.2.3.19) (Ent-kaurene synthase) (AtKS) (Ent-kaurene synthase B) (KSB) (Protein GA REQUIRING 2) (Q9SAK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products and in the production of gibberellins phytohormones. Catalyzes the conversion of ent-copalyl diphosphate to the gibberellin precursor ent-kaur-16-ene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Ent-kaurene oxidase, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
- Gibberellin 3-beta-dioxygenase 1
- Gibberellin 20 oxidase 1
- Gibberellin 2-beta-dioxygenase 1
- Gibberellin 2-beta-dioxygenase 2
- Gibberellin 2-beta-dioxygenase 3
- Gibberellin 2-beta-dioxygenase 6
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 2-beta-dioxygenase 4
Sequence:
MSINLRSSGCSSPISATLERRLDSEVQTRANNVSFEQTKEKIRKMLEKVELSVSAYDTSWVAMVPSPSSQNAPLFPQCVKWLLDNQHEDGSWGLDNHDHQSLKKDVLSSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQKPTGFDIIFPGMIKYARDLNLTIPLGSEVVDDMIRKRDLDLKCDSEKFSKGREAYLAYVLEGTRNLKDWDLIVKYQRKNGSLFDSPATTAAAFTQFGNDGCLRYLCSLLQKFEAAVPSVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCALAFRLLLAHGYDVSYDPLKPFAEESGFSDTLEGYVKNTFSVLELFKAAQSYPHESALKKQCCWTKQYLEMELSSWVKTSVRDKYLKKEVEDALAFPSYASLERSDHRRKILNGSAVENTRVTKTSYRLHNICTSDILKLAVDDFNFCQSIHREEMERLDRWIVENRLQELKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGVPEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFKRESAEGKLNAVSLHMKHERDNRSKEVIIESMKGLAERKREELHKLVLEEKGSVVPRECKEAFLKMSKVLNLFYRKDDGFTSNDLMSLVKSVIYEPVSLQEESLT
Protein: Transcription elongation factor A N-terminal and central domain-containing protein 2 (Q96MN5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000255|PROSITE-ProRule:PRU00651}.
Interaction partners:
- Transcription initiation factor TFIID subunit 8
Sequence:
MDKFVIRTPRIQNSPQKKDSGGKVYKQATIESLKRVVVVEDIKRWKTMLELPDQTKENLVEALQELKKKIPSREVLKSTRIGHTVNKMRKHSDSEVASLAREVYTEWKTFTEKHSNRPSIEVRSDPKTESLRKNAQKLLSEALELKMDHLLVENIERETFHLCSRLINGPYRRTVRALVFTLKHRAEIRAQVKSGSLPVGTFVQTHKK
Protein: POU class 5 homeobox 1 (A0A1W2PP83)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGHLASDFAFSPPPGGGGDGPGGPEPGWVDPRTWLSFQGPPGGPGIGPGVGPGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLVPQGGLETSQPEGEAGVGVETPMGPPRSPAPSPLPLSGS
Protein: Cold-inducible RNA-binding protein B (Cold-inducible RNA-binding protein 2) (xCIRP2) (Glycine-rich RNA-binding protein CIRP-B) (Q9DED4)
Organism: Xenopus laevis (African clawed frog)
Function: Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by binding to them and inhibiting their deadenylation. Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesion molecules, and cell movement during embryogenesis. Required for pronephros development.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:12466543}. Cytoplasm {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:12466543}. Note=Shuttles between the nucleus and cytoplasm. Predominantly cytoplasmic in oocytes. Translocates from the nucleus to the cytoplasm upon arginine methylation. {ECO:0000269|PubMed:11095679, ECO:0000269|PubMed:12466543}.
Interaction partners:
Sequence:
MSDEGKLFIGGLNFDTNEESLEQVFSKYGQISEVVVVKDRETKRSRGFGFVTFENPDDAKDAMMAMNGKAVDGRQIRVDQAGKSSGDRRGGYRGGSSGGRGFFRGGRGRGGGDRGYGSSRFDNRSGGYGGSSGSRDYYSSGRSQGSYGDRAGGSYRDSYDSYATHE
Protein: O-methyltransferase gsfB (EC 2.1.1.-) (Griseofulvin synthesis protein B) (D7PI16)
Organism: Penicillium aethiopicum
Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of griseofulvin, an important antifungal drug that has been in use for a long time for treating dermatophyte infections. The first step of the pathway is the formation of the heptaketide backbone by gsfA which is initiated by priming with acetyl-CoA, followed by sequential condensations of 6 malonyl-CoA units. The resulting benzophenone can undergo a spontaneous dehydration to form norlichexanthone. However, the true precursor for the griseofulvin biosynthesis is not norlichexanthone, but the heptaketide benzophenone that is O-methylated at 3-OH by gsfB to produce griseophenone D which is further methylated at 9-OH by gsfC to yield griseophenone C. Griseophenone C is then substrate of halogenase gsfI which is responsible for the regio-specific chlorination at the C13 position to form griseophenone B. The cytochrome P450 gsfF catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A which is further methylated at 5-OH by gsfD to yield dehydrogriseofulvin. Finally, gsfE performs stereospecific reduction of enone 18 of dehydrogriseofulvin to afford the final product griseofulvin.
Interaction partners:
Sequence:
MASNTSRSAHLAQIITENTANIETYRREQGLPPLSLGPDAPLDVKYPPNVEKCRRAVIDATLELGELATGPVELRLVPGWAIMTMFGVTQFICDFDIARQIPLAGDISYEDLSKAINVAVPVLRQVLRAGMPYHMFYESRPGHVAHTATTKVMASESLISDWTSLYTDVLFPASAGLSKALREEPTASDPSKTGFMVTKGDGESGMYMYFEKHPEEARRFAGVMEAFQKDEAYAVRHLTDSWPSDSQTGKLVDLGGSTGAVAFALAEKFPGLEIVVQDLPGALEAAHVREGKNVSFMPHDFFNEQPVKDADVYMFRWILHNWPDGHVQRILRALVPSLKPGAKVIVFDEIMPPAGTLPLSIERYQRNIDFGMLTLFNSKIRDIVEWKEIITQSDQRFNVTGVRYPENSRLSLIEIVWQP
Protein: Putative colanic acid biosynthesis glycosyl transferase WcaE (P71239)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative colanic acid biosynthesis glycosyl transferase WcaC
- Putative colanic acid polymerase
- Putative colanic acid biosynthesis acetyltransferase WcaF
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- Putative colanic acid biosynthesis acetyltransferase WcaB
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- GDP-L-fucose synthase
- GDP-mannose 4,6-dehydratase
- Putative polysaccharide export protein Wza
- GDP-mannose mannosyl hydrolase
Sequence:
MLLSIITVAFRNLEGIVKTHASLAHLAQVEDISFEWIVVDGGSNDGTREYLENLNGIFNLRFVSEPDNGIYDAMNKGIAMAQGKFALFLNSGDIFHQNAANFVRKLKMQKDNVMITGDALLDFGDGHKIKRSAKPGWYIYHSLPASHQAIFFPVSGLKKWRYDLEYKVSSDYALAAKMYKAGYAFKKLNGLVSEFSMGGVSTTNNMELCADAKKVQRQILHVPGFWAELSWHLRQRTTSKTKALYNKV
Protein: Probable glucose sensor protein SLC5A4 (Solute carrier family 5 member 4) (Q9NY91)
Organism: Homo sapiens (Human)
Function: Has electrogenic activity in response to glucose, and may function as a glucose sensor. Mediates influx of sodium ions into the cell but does not transport sugars. Also potently activated by imino sugars such as deoxynojirimycin (DNJ).
Subcellular location: Cell membrane {ECO:0000269|PubMed:13130073, ECO:0000305|PubMed:17110502, ECO:0000305|PubMed:20421923, ECO:0000305|PubMed:22766068}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Regulatory solute carrier protein family 1 member 1
Sequence:
MASTVSPSTIAETPEPPPLSDHIRNAADISVIVIYFLVVMAVGLWAMLKTNRGTIGGFFLAGRDMAWWPMGASLFASNIGSNHYVGLAGTGAASGVATVTFEWTSSVMLLILGWIFVPIYIKSGVMTMPEYLKKRFGGERLQVYLSILSLFICVVLLISADIFAGAIFIKLALGLDLYLAIFILLAMTAVYTTTGGLASVIYTDTLQTIIMLIGSFILMGFAFNEVGGYESFTEKYVNATPSVVEGDNLTISASCYTPRADSFHIFRDAVTGDIPWPGIIFGMPITALWYWCTNQVIVQRCLCGKDMSHVKAACIMCAYLKLLPMFLMVMPGMISRILYTDMVACVVPSECVKHCGVDVGCTNYAYPTMVLELMPQGLRGLMLSVMLASLMSSLTSIFNSASTLFTIDLYTKMRKQASEKELLIAGRIFVLLLTVVSIVWVPLVQVSQNGQLIHYTESISSYLGPPIAAVFVLAIFCKRVNEQGAFWGLMVGLAMGLIRMITEFAYGTGSCLAPSNCPKIICGVHYLYFSIVLFFGSMLVTLGISLLTKPIPDVHLYRLCWVLRNSTEERIDIDAEEKSQEETDDGVEEDYPEKSRGCLKKAYDLFCGLQKGPKLTKEEEEALSKKLTDTSERPSWRTIVNINAILLLAVVVFIHGYYA
Protein: Protease 4 (EC 3.4.21.-) (Endopeptidase IV) (Protease IV) (Signal peptide peptidase) (P08395)
Organism: Escherichia coli (strain K12)
Function: Digests cleaved signal peptides in vitro, its in vivo function is unknown. This activity is necessary to maintain proper secretion of mature proteins across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:3522590}; Single-pass membrane protein {ECO:0000269|PubMed:18476724, ECO:0000269|PubMed:3522590}.
Interaction partners:
- L-asparaginase 1
- Signal peptidase I
- Protease HtpX
Sequence:
MRTLWRFIAGFFKWTWRLLNFVREMVLNLFFIFLVLVGVGIWMQVSGGDSKETASRGALLLDISGVIVDKPDSSQRFSKLSRQLLGASSDRLQENSLFDIVNTIRQAKDDRNITGIVMDLKNFAGGDQPSMQYIGKALKEFRDSGKPVYAVGENYSQGQYYLASFANKIWLSPQGVVDLHGFATNGLYYKSLLDKLKVSTHVFRVGTYKSAVEPFIRDDMSPAAREADSRWIGELWQNYLNTVAANRQIPAEQVFPGAQGLLEGLTKTGGDTAKYALENKLVDALASSAEIEKALTKEFGWSKTDKNYRAISYYDYALKTPADTGDSIGVVFANGAIMDGEETQGNVGGDTTAAQIRDARLDPKVKAIVLRVNSPGGSVTASEVIRAELAAARAAGKPVVVSMGGMAASGGYWISTPANYIVANPSTLTGSIGIFGVITTVENSLDSIGVHTDGVSTSPLADVSITRALPPEAQLMMQLSIENGYKRFITLVADARHSTPEQIDKIAQGHVWTGQDAKANGLVDSLGDFDDAVAKAAELAKVKQWHLEYYVDEPTFFDKVMDNMSGSVRAMLPDAFQAMLPAPLASVASTVKSESDKLAAFNDPQNRYAFCLTCANMR
Protein: Nuclear migration protein nudC (Nuclear distribution protein C homolog) (Q57UQ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Rab-GAP TBC domain-containing protein
Sequence:
MATDERFDTMLLAIAQQHDGIDSILNTFFSFLGRKTDFFSQPAMARTAVQRALDRHLAQAEEKQRQKRKEAPVSRVEEVEDEEEVKAKAAAQAAAEAAKRKADLERKKEELANAKEDEDGAKPKGLPPTVGNGFDYEHYMFSQTLKEVEVRVPLLVARAKGKDVDVVLQQRRLRVGMKGKPPIVDGELFASVKTEESMWTIEDGHTVVVTLTKQNQMEWWKTVMVGDAEIDLQKVMPENSKLDDLDGDTRQTVEKMMYDQRQKAMGLPTSEEQKKREMLAKFMAAHPEMDFSQAKIC
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2 (3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II) (3-beta-HSD II) (3-beta-HSD adrenal and gonadal type) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] (P26439)
Organism: Homo sapiens (Human)
Function: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25322271}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Cytochrome P450 11B1, mitochondrial
- 17-beta-hydroxysteroid dehydrogenase type 3
- Steroid 21-hydroxylase
- Cytochrome P450 11B2, mitochondrial
- Aldo-keto reductase family 1 member C3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Aromatase
- Cytochrome P450 7A1
Sequence:
MGWSCLVTGAGGLLGQRIVRLLVEEKELKEIRALDKAFRPELREEFSKLQNRTKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVFGVTHRESIMNVNVKGTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEEEPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCALRPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNPVYVGNVAWAHILALRALRDPKKAPSVRGQFYYISDDTPHQSYDNLNYILSKEFGLRLDSRWSLPLTLMYWIGFLLEVVSFLLSPIYSYQPPFNRHTVTLSNSVFTFSYKKAQRDLAYKPLYSWEEAKQKTVEWVGSLVDRHKETLKSKTQ