wanglab/gogpt-training-data huggingface dataset:
Protein: Rab3 GTPase-activating protein catalytic subunit (RAB3 GTPase-activating protein 130 kDa subunit) (Rab3-GAP p130) (Rab3-GAP) (Q15042)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the Rab3 GTPase-activating (Rab3GAP) complex composed of RAB3GAP1 and RAB3GAP2, which has GTPase-activating protein (GAP) activity towards various Rab3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43, and guanine nucleotide exchange factor (GEF) activity towards RAB18. As part of the Rab3GAP complex, acts as a GAP for Rab3 proteins by converting active RAB3-GTP to the inactive form RAB3-GDP. Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. The Rab3GAP complex, acts as a GEF for RAB18 by promoting the conversion of inactive RAB18-GDP to the active form RAB18-GTP. Required for recruiting and activating RAB18 at the endoplasmic reticulum (ER) membrane where it maintains proper ER structure. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24891604, ECO:0000269|PubMed:9852129}. Endoplasmic reticulum {ECO:0000269|PubMed:24891604}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:26063829}. Note=In neurons, enriched in the synaptic soluble fraction. Localized to the cis-Golgi in fibroblasts (PubMed:26063829). {ECO:0000269|PubMed:26063829, ECO:0000269|PubMed:9852129}.
Interaction partners:
- Rab3 GTPase-activating protein non-catalytic subunit
- Ras-related protein Rab-18
- DmX-like protein 2
- Ras-related protein Rab-3A
- MAP kinase-activating death domain protein
- Vesicle-associated membrane protein-associated protein B/C
- Ras GTPase-activating protein 1
- TBC1 domain family member 20
- DmX-like protein 1
- Vesicle-associated membrane protein-associated protein A
Sequence:
MAADSEPESEVFEITDFTTASEWERFISKVEEVLNDWKLIGNSLGKPLEKGIFTSGTWEEKSDEISFADFKFSVTHHYLVQESTDKEGKDELLEDVVPQSMQDLLGMNNDFPPRAHCLVRWYGLREFVVIAPAAHSDAVLSESKCNLLLSSVSIALGNTGCQVPLFVQIHHKWRRMYVGECQGPGVRTDFEMVHLRKVPNQYTHLSGLLDIFKSKIGCPLTPLPPVSIAIRFTYVLQDWQQYFWPQQPPDIDALVGGEVGGLEFGKLPFGACEDPISELHLATTWPHLTEGIIVDNDVYSDLDPIQAPHWSVRVRKAENPQCLLGDFVTEFFKICRRKESTDEILGRSAFEEEGKETADITHALSKLTEPASVPIHKLSVSNMVHTAKKKIRKHRGVEESPLNNDVLNTILLFLFPDAVSEKPLDGTTSTDNNNPPSESEDYNLYNQFKSAPSDSLTYKLALCLCMINFYHGGLKGVAHLWQEFVLEMRFRWENNFLIPGLASGPPDLRCCLLHQKLQMLNCCIERKKARDEGKKTSASDVTNIYPGDAGKAGDQLVPDNLKETDKEKGEVGKSWDSWSDSEEEFFECLSDTEELKGNGQESGKKGGPKEMANLRPEGRLYQHGKLTLLHNGEPLYIPVTQEPAPMTEDLLEEQSEVLAKLGTSAEGAHLRARMQSACLLSDMESFKAANPGCSLEDFVRWYSPRDYIEEEVIDEKGNVVLKGELSARMKIPSNMWVEAWETAKPIPARRQRRLFDDTREAEKVLHYLAIQKPADLARHLLPCVIHAAVLKVKEEESLENISSVKKIIKQIISHSSKVLHFPNPEDKKLEEIIHQITNVEALIARARSLKAKFGTEKCEQEEEKEDLERFVSCLLEQPEVLVTGAGRGHAGRIIHKLFVNAQRAAAMTPPEEELKRMGSPEERRQNSVSDFPPPAGREFILRTTVPRPAPYSKALPQRMYSVLTKEDFRLAGAFSSDTSFF
Protein: Propionate--CoA ligase (EC 6.2.1.17) (Propionyl-CoA synthetase) (P77495)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity (By similarity).
Interaction partners:
- 2-methylcitrate synthase
- 2-methylcitrate dehydratase
- Propanoyl-CoA:succinate CoA transferase
- Probable acrylyl-CoA reductase AcuI
- Methylmalonyl-CoA decarboxylase
- Probable dehydratase PflD
- Propionate kinase
- Phosphate acetyltransferase
- Probable dehydratase YbiW
- Acetyl-coenzyme A synthetase
Sequence:
MSFSEFYQRSINEPEQFWAEQARRIDWQTPFTQTLDHSNPPFARWFCEGRTNLCHNAIDRWLEKQPEALALIAVSSETEEERTFTFRQLHDEVNAVASMLRSLGVQRGDRVLVYMPMIAEAHITLLACARIGAIHSVVFGGFASHSVAARIDDAKPVLIVSADAGARGGKIIPYKKLLDDAISQAQHQPRHVLLVDRGLAKMARVSGRDVDFASLRHQHIGARVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGSVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTWPDCGVWWTIVEKYQVSRMFSAPTAIRVLKKFPTAEIRKHDLSSLEVLYLAGEPLDEPTASWVSNTLDVPVIDNYWQTESGWPIMAIARGLDDRPTRLGSPGVPMYGYNVQLLNEVTGEPCGVNEKGMLVVEGPLPPGCIQTIWGDDGRFVKTYWSLFSRPVYATFDWGIRDADGYHFILGRTDDVINVAGHRLGTREIEESISSHPGVAEVAVVGVKDALKGQVAVAFVIPKESDSLEDRDVAHSQEKAIMALVDSQIGNFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLDQIRQAMEE
Protein: Chitin-binding protein 2 (Mo-CBP2) (C0HKC5)
Organism: Moringa oleifera (Horseradish tree) (Moringa pterygosperma)
Function: Chitin-binding protein. Has antifungal activity against C.krusei, C.albicans, C.tropicalis and C.parapsilosis. Inhibits C.albicans by increasing cell membrane permeability and production of reactive oxygen species. Has no hemagglutinating activity.
Interaction partners:
Sequence:
QPDFQRCPSLRCCQQLRQAVQLTHQQQGQVGPQQVRQQFQTHQRIPAICNLQPMRQAVQLAHQQQQGQVGPQQVRCCQQLRQAVQSQAAAAGQVGPQQVGHMYR
Protein: Dynamin-1 (EC 3.6.5.5) (Dynamin) (Dynamin I) (Q05193)
Organism: Homo sapiens (Human)
Function: Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15703209}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:8101525}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P21575, ECO:0000250|UniProtKB:P39053}. Presynapse {ECO:0000250|UniProtKB:P21575}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:Q08DF4}. Note=Associated to the membrane in a helical polymer shape in a GTP bound state (PubMed:30069048). Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation (PubMed:15703209). {ECO:0000269|PubMed:15703209, ECO:0000269|PubMed:30069048}.
Interaction partners:
- Dynamin-3
- Mitochondrial fission 1 protein
- Amphiphysin
- Myc box-dependent-interacting protein 1
- Dynamin-2
- Intersectin-1
- Hematopoietic lineage cell-specific protein
- Growth factor receptor-bound protein 2
- Sorting nexin-9
- Endophilin-A1
Sequence:
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL
Protein: Vesicle-associated membrane protein 7B (Q86AQ7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Late endosome membrane; Single-pass type IV membrane protein. Lysosome membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Note=During macropinocytosis highest levels are found in endosomes with lower levels observed in the lysosomes. {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q54NW7, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}.
Interaction partners:
- Vesicle-associated membrane protein 7A
- Syntaxin-7A
- Syntaxin-8A
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Vacuolar protein sorting-associated protein 16 homolog
- Probable syntaxin-8B
- t-SNARE family protein
- t-SNARE family protein
- AP-3 complex subunit mu
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MPIIYSLVARGSSVLAEFTSTNGNFVTITRRILDLIPPNDTKMSYVYEKYIFHYLVSDTLTYLCMADEEFGRRIPFTFLDDVKNRFKSMYGDKGKTAIAYGMNSDFSRTLENLMDHYSNTTRVDTMSRTMAEIDEVKNILVSDIAPQLLKRGEKIEMLVERTDTLNQQSFKFKKQSKQLKCAMWWKNVKLMLVLGAIVLIIIFIIVMSYCDGFRSGSKCRSSPSSNSTPTPTPTETPTPTPTPTSTPTPSQLLETLLNQF
Protein: ABC-type transporter, ATPase component and permease component (Q8NNV2)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- ABC-type transporter, ATPase component and permease component
- ABC-type multidrug/protein/lipid transport system, ATPase component
- Glutamate transport ATP-binding protein GluA
- ABC-type transporter, ATPase component and permease component
- Siderophore-interacting protein
- Arginine transport ATP-binding protein ArgV
- Phosphate import ATP-binding protein PstB
Sequence:
MISRLLQLAKKVWPELGASTLLRLLNQLLTAALIVFPAWVLSRKPDISLLAVAIIMALIALTAAVCRWGEQVCGHRAAFGLLAHMRVMLYDALVHKGSPSPIHGSGSIMSVATRDINSIEVFFAHTIGPTVTAVLLSAGGVITLATLDPVAGLIGLLGVLIAWLIPLIGKQSSSSEATSRGHIAQHLTEDAAGRLEINSHGAQATRLNALEVKEQQLEQVVTRQGLIVGIRQGAALLWPWISAVLLVALVPHVGIVAAAIILGISPALDAVEGFARTMPTALNSAQRYFQIIDAPVAIAEPDEPKPLPKGPLKLRISRVPVSAKGTVSLEVAAGEHIGIIGSSGSGKSTLAKLILKLAQLRSGTITIGGVDIAEVSSAELRKSVTLVEQKSVLFRASVLENLRMGNPELSEDEAREALRLASISELPLDADALRLSGGQQQRLCLARALARTPQVLIVDEATSHQDALNQADLSQTLATLKDTTVIIIAHRTAALTHVDRIIDLEEIKNP
Protein: Large ribosomal subunit protein uL14c (50S ribosomal protein L14, chloroplastic) (P56792)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to 23S rRNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein uL16c
- Small ribosomal subunit protein uS8c
- Large ribosomal subunit protein uL2cz/uL2cy
- Large ribosomal subunit protein bL36c
- Large ribosomal subunit protein bL20c
- Large ribosomal subunit protein uL22c
- Small ribosomal subunit protein uS7cz/uS7cy
- DNA-directed RNA polymerase subunit alpha
- Small ribosomal subunit protein bS16cz
- Small ribosomal subunit protein uS3c
Sequence:
MIQPQTYLNVADNSGARELMCIRIIGASNRRYAHIGDVIVAVIKEAIPNTPLERSEVIRAVIVRTCKELKRNNGTIIRYDDNAAVVIDQEGNPKGTRVFGAIPRELRQLNFTKIVSLAPEVL
Protein: Protocadherin gamma A1 (Protocadherin gamma subfamily A, 1) (Q91XZ0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAIPEKLTGWSLLVLVCLSLELLLEAGAGNIRYSVPEETDKGSFVGSIAKDLGLETRELMERGIRIVSRGRSQLFSLNPRSGSLVTAGRIDREELCAQSTPCVVSFNILMEDEMKLLPIEVEIIDINDNTPQFQLEELELKMSEITTPGTRIPLPLGQDLDVGINSLQSYQLSANPHFSLDVQQGPEGPQQPEMVLQRPLDREKDAVHYLVLTASDGGSPIHSGTLQIHVQVVDVNDNPPAFTKAEYHVSVPENVPLGTRLLKVNATDPDEGANGRVTYSFHKVDHSVVRKFQLDAYTGELSNKEPLDFEEYKVYPMEIQAQDGAGLMARAKVLVTVLDVNDNAPEVGITSVTNTVPENFPPGTTIALISVHDQDADNNGHITCSIPGNLPFKLEKLVDNYYRLVTERTLDREQSSRHNITITATDQGTPPLSTQAHISLLVTDINDNPPVFEQDSYSVYIPENNPRGASIFSVKAQDADHNENALVTYALVEDTIQGVPLSSYFSINSDTGVVYALQSFDYEQFRDLQLRVMAHDSGNPQLSSNVSLSLFMIDQNDNAPEILYPVLPTDGSTGVELAPRSAEPGYLVTKVVAVDKDSGQNSWLSYRLLKASEPGLFSVGLHTGEVRTARALLERDALKQSLVVAVQDHGQPPLSTTVTFTIAVADSIPDLLADLGSMGTPADPQDSDLTLYLVVAVAVVSCIFLAFVIVLLVLKLRHWYSSRLLQTEANGLTGLPASNFVGVDGVHAFLQTYSREISLTADSRKSHLIFPQPNYADTLISHESCEKQEFLSAPQSLLEDKEEIFSQQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: LD18706p (Q8T098)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAVQGFVTMSFIIVFLVLALLSLTIIRLPLKAVLQYEWLLVRLSYMGTAISSLFMFLAVCIFGGCAYRRDWMMYPKFNVLGWSYALAVVTFMLLGLAALILQREARQAYDARGEQKNLVMQMEMQEPGYQPPRHHHSQSRSLQGYI
Protein: Steroid 5-alpha-reductase DET2 (GhDET2) (EC 1.3.1.22) (Q2QDF6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Involved in a reduction step in the biosynthesis of the plant steroid, brassinolide (BL). Promotes cotton fibers (seed trichomes) initiation and elongation.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein BZR1 homolog
Sequence:
MASDQTLFHYCLLTLYIIALPTWISLYFLQAPYGKHNRPGWGPTISPPLAWFLMESPTLWLTFFLFPSGQHFYNPKSFLLISPFLFHYFNRTVLYPLRLARNTTQTRGFPVSVAFMAFGFNLLNGYLQARWVSHYKDDYENEELFWWRFLAGLLIFVVGMWVNVRADKVLVGLKKQGDGGYKIPRGGLFELVSCPNYFGEIMEWFGWAVMTWSWVGFGFFLYTCANLMPRARATRLWYLEKFKDDYPKDRKAVIPFIY
Protein: phosphoserine phosphatase (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) (Q6FND4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Histidine biosynthesis trifunctional protein
- Phosphoserine aminotransferase
- Serine hydroxymethyltransferase, cytosolic
- alanine--glyoxylate transaminase
- Serine hydroxymethyltransferase, mitochondrial
- Tryptophan synthase
- Cystathionine beta-synthase
- Threonine dehydratase
- L-serine dehydratase
- CDP-diacylglycerol--serine O-phosphatidyltransferase
Sequence:
MSFVVTVIAHGDALRSEKELVDRVVGALDAELIKTETLSKRAVDIFVKAPGEVLQLKQKLDQLDVDGADLAVQVVDEQLQRRPLKLCVFDMDSTLIYQEVIELIAAYAGVEPQVHEITERAMNNEIDFKQSLRERVRLLKGLKIDNLYEEIKQKLQITEGVPQLCSTLKQHGIKLAVLSGGFIQFASYIKDQLSLDYARANLLEMDDSGVLTGEVIGEIVDGQCKAETIKQLCKDWSIDLENVCMIGDGGNDLPSMHVSGYGIAWNAKPTVQKQAPSKLNTKSLADALYIFGIIE
Protein: Aldehyde decarbonylase (AD) (EC 4.1.99.5) (Fatty aldehyde decarbonylase) (Q54764)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.
Interaction partners:
- Long-chain acyl-[acyl-carrier-protein] reductase
- Biosynthetic arginine decarboxylase
- Aldehyde dehydrogenase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
- Uncharacterized protein
- Cob
- Protein splicing
- PH domain-containing protein
Sequence:
MPQLEASLELDFQSESYKDAYSRINAIVIEGEQEAFDNYNRLAEMLPDQRDELHKLAKMEQRHMKGFMACGKNLSVTPDMGFAQKFFERLHENFKAAAAEGKVVTCLLIQSLIIECFAIAAYNIYIPVADAFARKITEGVVRDEYLHRNFGEEWLKANFDASKAELEEANRQNLPLVWLMLNEVADDARELGMERESLVEDFMIAYGEALENIGFTTREIMRMSAYGLAAV
Protein: GPN-loop GTPase 2 (ATP-binding domain 1 family member B) (Q9H9Y4)
Organism: Homo sapiens (Human)
Function: Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Interaction partners:
- GPN-loop GTPase 1
- RNA polymerase II-associated protein 1
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase II subunit GRINL1A
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- GPN-loop GTPase 3
- DNA-directed RNA polymerase II subunit RPB11-b2
Sequence:
MAGAAPTTAFGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPHINLLSKMDLIEHYGKLAFNLDYYTEVLDLSYLLDHLASDPFFRHYRQLNEKLVQLIEDYSLVSFIPLNIQDKESIQRVLQAVDKANGYCFRAQEQRSLEAMMSAAMGADFHFSSTLGIQEKYLAPSNQSVEQEAMQL
Protein: Valerianol synthase TPS1C (EC 4.2.3.204) (Terpene synthase 1c) (ChTps1c) (A0A348AUV7)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNCEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVEGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAGLTKIMLLLSVTDDTYDAYGTYNELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRAYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM
Protein: Protein IMPACT (Imprinted and ancient gene protein homolog) (Q9P2X3)
Organism: Homo sapiens (Human)
Function: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O55091}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- Thymidine kinase, cytosolic
- UMP-CMP kinase 2, mitochondrial
- Thymidylate kinase
- Dihydrofolate reductase 2, mitochondrial
- Dihydrofolate reductase
- C-terminal-binding protein 2
Sequence:
MAEGDAGSDQRQNEEIEAMAAIYGEEWCVIDDCAKIFCIRISDDIDDPKWTLCLQVMLPNEYPGTAPPIYQLNAPWLKGQERADLSNSLEEIYIQNIGESILYLWVEKIRDVLIQKSQMTEPGPDVKKKTEEEDVECEDDLILACQPESSLKALDFDISETRTEVEVEELPPIDHGIPITDRRSTFQAHLAPVVCPKQVKMVLSKLYENKKIASATHNIYAYRIYCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNYTNSPEESSKALGKNKKVRKDKKRNEH
Protein: V-type proton ATPase subunit E 2 (V-ATPase subunit E 2) (Vacuolar proton pump subunit E 2) (Q9D593)
Organism: Mus musculus (Mouse)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Interaction partners:
- V-type proton ATPase subunit F
- V-type proton ATPase subunit D
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit B, kidney isoform
- V-type proton ATPase 116 kDa subunit a 2
Sequence:
MALTDIDVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMDYFEKKEKQIEQQKKIQLSTMRNQARITVLRARDNLILELLKDAKMRLSRIVSDEEIYQDLLDKLVLQALLRLLEPVMIVRCRPQDLHLVESAVLRAIPQYMRLCQKHLEVQVDQTEHLPSNAAGGVEVYSSDQKIKVSNTLESRLNLAAMQKMPEIRGILFGDNTSRKFFT
Protein: Septin (A0A1D8PD83)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Bud neck {ECO:0000256|ARBA:ARBA00004266}.
Interaction partners:
- Septin
- Septation protein 7
- Cell division control protein 10
- Septin CDC11
- Septin
- Elongation factor 3
- Serine/threonine-protein kinase GIN4
- Bud site selection protein BUD4
Sequence:
MAAVDHSTTGEIVPQNIKIIKKVLNGYVGFANLPKQWHRKSIRRGFSLNIMAIGESGLGKATLINTLFNRDIITSQHDSDEFDEGEEEDVSVKIKSTQAEIEEDGVKLKVSVITAPGFGESINNVEAWKPIVDEINSRFDSYLEAESRINRTAVVDNRVHAFLYFIEPTGHSLRALDIALMKQVHEKVNLIPVIAKSDTLTDEEILEFKHRILADISHQGIKIFKPTDFEYDEEESANTRSIIDSFPFAVVGSTNEVQTPDGRLVRGRKYPWGVIEVDNENHNDFVKLRQLLVRNFLEELKEHTANVLYENYRTEKLKRMGIEQDNTVFREFDPAAKQEEERALHEAKLAKMEAEMKSVFQQKVSEKEKKLQRSEADLFARHKEMKDKLTKQIKLLEEKKAQLEKQKLLPQDPPAQPAPQKSRKGFLR
Protein: Protein IMPAIRED IN BABA-INDUCED STERILITY 1 (EC 2.7.11.-) (F4ICB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for beta-aminobutyric acid (BABA)-induced resistance (BABA-IR) against bacteria (e.g. P.syringae) and oomycetes (e.g. H.parasitica) via priming for salicylate (SA)-dependent defense responses such as pathogenesis-related PR-1 gene expression and trailing necrosis. Involved in BABA-mediated sterility. Necessary for the inheritance of BABA-priming to next generation, especially for the primed to be primed phenotype which consists in an enhanced second BABA-priming in transgenerationally primed plants.
Interaction partners:
- Phosphoinositide phosphatase SAC6
- UDP-glucose:glycoprotein glucosyltransferase
- Cyclin-dependent kinase-like protein
- HVA22-like protein i
- Cytosolic sulfotransferase 13
- Protein RER1B
Sequence:
MGCVNSKQTVSVTPAIDHSGVFRDNVCSGSGRIVVEDLPPVTETKLLSWWSKSGKKSSSKKSGSELGSDFGELSESGRASSNCRSESVSFRLGNLSKYLEAEQVAAGWPAWLSNVAGEAIHGWVPFRSDAFEKLEKIGQGTYSSVFRARETETGRIVALKKVRFDNFEPESVRFMAREILILRKLNHPNIIKLEGIVTSKLSCSIHLVFEYMEHDLTGLLSSPDIDFTTPQIKCYMKQLLSGLDHCHARGVMHRDIKGSNLLVNNEGILKVADFGLANFCNASGNKQPLTSRVVTLWYRPPELLLGATEYGASVDLWSVGCVFAELLIGKPVLQGRTEVEQLHKIFKLCGSPPEDYWKKSKLPHAMLFKPQQHYDGCLRETLKLKGLSDADINLIETLLSIQPHKRGTASTALVSQYFTSKPFACDPSSLPVYSPSKEIDAKHREDTTRKKISGNGRRGTESRKPTRKPPAFAKLAPAEDVRHHSQKFQKRNGHSVHNSIDSDSTLFEKMQKPSNHEKDEASHVKNASQGDVPFSGPLQVSVSSGFAWAKRRKDDICVRSHNRSLSRGHIPNLLGPSPAFSENTDVDSKNNEKEKEEKHGERTDSQDREAYEMLKLSMLKKWRQLERPDSFGGSDEYHSQELSLELYQREEKAAKLGHLGYEDNDEKIEFSGPLLSKSYGVDELLERHERQIRQLVRKSWFQKGKKQGK
Protein: Musculin (activated B-cell factor-1) (Musculin isoform X1) (A0A2R8QBT6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Zinc finger and BTB domain-containing 49.
Sequence:
MSTGSVSDPEDLQSISHCLDDSEDDFSLDDGLKPKPKSKTPRGAASNTNKPQMKLAKDGRQSQRNAANARERARMRVLSKAFSRLKTSLPWVPADTKLSKLDTLRLASSYISHLRQLLQDDTYHNNLAHPANLTWPFVVSARSEDTKDISAAVRLCGATA
Protein: FI11475p (FI13101p) (Paxillin, isoform C) (Q8INW7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDDLDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLKELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG