wanglab/gogpt-training-data huggingface dataset:
Protein: GTP-binding nuclear protein Ran (EC 3.6.5.-) (GTPase Ran) (Ras-related nuclear protein) (P79735)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN, while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensures the directionality of the transport. Interaction with RANBP1 induces a conformation change in the complex formed by XPO1 and RAN that triggers the release of the nuclear export signal of cargo proteins. RAN (GTP-bound form) triggers microtubule assembly at mitotic chromosomes and is required for normal mitotic spindle assembly and chromosome segregation. Required for normal progress through mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62826}. Cytoplasm {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis (By similarity). {ECO:0000250|UniProtKB:P62826}.
Interaction partners:
- Si:ch211-233m11.2.
- Exportin-T
- Exportin 1
- Exportin-1
- Importin subunit beta-1
- Regulator of chromosome condensation
- Si:ch1073-55a19.2.
- Ran GTPase-activating protein 1
- Elongation factor 1-alpha
- FinTRIM family, member 52, pseudogene.
Sequence:
MAENEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGAIKYNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVEMPALAPPEIAMDPTLAAQYEHDLKVASETALPDEDDDL
Protein: Type IV pili, pilus assembly protein (A0Q6G9)
Organism: Francisella tularensis subsp. novicida (strain U112)
Interaction partners:
Sequence:
MQISLKKVISVALLSAVLSSCMTPETPSRNSIKSNSQQQNNTSDNLNPNSAEFISPEQFTASKADYKKATVINAELAIIYSTEGYLERAKTKLIKAQDLAKQHGYDLAIVGYAAGYYYQSIGANSIAKKYYKDTLYKHPKDFEAMNFYAQYLCSQESDYAEAQKLFDKSLYTPDNDDMAQTLFLYSQCMYKQGKKDQALVYMERANRFRQDYRAAKLRLAEMYFERKDYTNCYKVIYSMKDDPAFFNNKRILDLRLKLAEYANNKNQAAEVRLILSSNNYNDEDIQKFFSAADQEDINKNA
Protein: Glutamate receptor ionotropic, kainate 4 (GluK4) (Glutamate receptor KA-1) (KA1) (Q8BMF5)
Organism: Mus musculus (Mouse)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12954862}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000269|PubMed:12954862}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000269|PubMed:12954862}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, kainate 3
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor ionotropic, NMDA 2D
- Disks large homolog 4
- Glutamate receptor ionotropic, NMDA 2A
- Voltage-dependent calcium channel gamma-2 subunit
- Disks large homolog 3
- Glutamate receptor 1
Sequence:
MPRVSAPLVLLPAWLLMVACSPHSLRIAAILDDPMECSRGERLSITLAKNRINRAPERLGKAKVEVDIFELLRDSEYETAETMCQILPKGVVAVLGPSSSPASSSIISNICGEKEVPHFKVAPEEFVRFQLQRFTTLNLHPSNTDISVAVAGILNFFNCTTACLICAKAECLLNLEKLLRQFLISKDTLSVRMLDDTRDPTPLLKEIRDDKTATIIIHANASMSHTILLKAAELGMVSAYYTYIFTNLEFSLQRMDSLVDDRVNILGFSIFNQSHAFFQEFSQSLNQSWQENCDHVPFTGPALSSALLFDAVYAVVTAVQELNRSQEIGVKPLSCGSAQIWQHGTSLMNYLRMVELEGLTGHIEFNSKGQRSNYALKILQFTRNGFQQIGQWHVAEGLSMDSRLYASNISDSLFNTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRRPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWEGGKCPKEEDHRAKGLGMENIGGIFVVLICGLIVAIFMAMLEFLWTLRHSEASEVSVCQEMVTELRNIILCQDNIHPRRRRSGGLPPQPPVLEERRPRGTATLSNGKLCGAGEPDQLAQRLAQEAALVARGCTHIRVCPECRRFQGLRARPSPARSEESLEWDKTTNSSEPE
Protein: Galectin domain-containing protein (Q20684)
Organism: Caenorhabditis elegans
Interaction partners:
- Serpentine Receptor, class T
- C-type lectin domain-containing protein
Sequence:
MADSSSFFSSAFSSAKNLIPFAKNTEDKPVDADTASDAKDAKDSAIQEAVQNASAAINDVFTDAVDKLEEVKDTVVEQFSNGDEKKEEAVVEEKFDSVHVGVDGETAVQEAKEEVKEAQVVVKGVLADGTQIVEGVTDVAEAPVADEKKEETVAAPLDSAAPVEEHKEESHSSEHTEAPAHTEDSIVQADPEARIVFQGVLADGTQIIEAVSANPPCIQEESAPAAAVSEEVGEAVHVVPVDQAPEAPTSEAQDAAPIEEHVEVVHVAENASTPAATDAHEETKSAEEQTPVVDASPAQEIVKVEEHEHKEEAAPDESAPEAAHDSHVEETAAQVVDEVIEAVHVSANESAPEEHKEEVAAAATSEDQKEPAPASDEHTSESAVEGAIESVHIALTESAPVASDENTTEAAPGTVEEHKNEVHDPVDGASSDAPAEDHREAAASSESVEEPITAVHVEATESAAPADKVHEETKIDSAAETHADAPVVDASPAEDQASEVTEAPHVESAKSAPATSEDHKEDVAQATSEQVETQAPADEHKDDASPAEPTTVQDVIEAIPIVSTESTPAEHSAPAESAPALAEEHKDEAAPSEPVQDVPVEEVIEAVHIAPAESAPASVEEAAPSESTQAPVEEHKDATTAADSSHEEPKAESDAPAAESVETAPVEEHKDEASPTALESVEDVIEAVHVASTESAPAPVEDAASADSTQAPVEEQKDTAAAAEPSHEEAQADHAASVEDVIEAVHIASNESAPTTEAAPSESIQAEDHKDEAASTAEPAHEESVTVVEASHKEPQAESAAPVEENIESVHVASEESAPAPSGDAAPSESAPVSENPVEEVAVAYHVESIESVPTDAQSVEEPVVQQHVGTVEAAPEAAVDEESFDVVHVHSDAAHPETATPESGSEETFEKVEHSQVQEAPSSEEHNSSEPEIVEDVVEKQIVAAVASAPETQPEESPKKPRKLAEMAHESAFPVPYRSKLVEPFEPGQTLIVKGKTGEDSIRFTVNLHTNTADFSGNDVPLHVSVRFDEGKLVFNTFSKGEWGKEERKSNPYKKGDDIDIRIRAHDSKFQIFVDQKEVKEYEHRVPLSSITHFTIDGDVLVNYIHWGGKYYPVPYESGLAGEGLAPGKTLTVFGIPEKKAKRFHINLLKKNGDIALHLNARFDEKHVVRNSLINSAWGNEEREGKMPFEKAVGFDLEIHNEPYAFAVTVNGERFASYAHRLSPDEVNGLQIGGDVEITGIQLA
Protein: GNAT family N-acetyltransferase (Q9HUG2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Uncharacterized protein
- Probable glycosyl transferase
- Probable carbamoyl transferase
- Spore protein YkvP/CgeB glycosyl transferase-like domain-containing protein
- Serine/threonine protein kinase
- Alpha-1,3-rhamnosyltransferase WapR
- Lipopolysaccharide heptosyltransferase 1
- Lipopolysaccharide core heptose
- lipopolysaccharide heptosyltransferase II
Sequence:
MLNRLRAFRERGWREVDAPTYAQAWQRFGGSVATHPLVVEQLAEMAGIPVRYLGWESAGELVAAIPTWGRHLALSKDVLKRRGKKGLYDLGNAELILPVAGDARIALRHAGRYLSALHERNIVTLRPQTEQLAFARAPEDFSKKFRYNQRREVRLVEEAGGQVRQADSFAPAEFAAIYLELFQRRWGFPATGAERMAEVFERLRELLRGSVLLLNDQPIAVQVLYRAEAPGWLSVEYINGGVDPQTREFSPGSVLSYLNTQAAWEDARALGKPLRYSFGRADREYKDRWCHPSPVFQV
Protein: Transcription/mRNA export factor (B3H7K2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MELVRDRLVECGWKDEMRIACREHVKKKGRKDVTVDELIRVITPKGRGKIYNEQSVSVSVNSLLVTLTLFLWMFVVYVCSFSTRFCEGRAVEQNSKLHCISCSLMVF
Protein: Rho-type guanine nucleotide exchange factor, isoform F (Rho-type guanine nucleotide exchange factor, isoform I) (A8DZ19)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Cdc42 homolog
- ARF GTPase-activating protein Git
- GH23568p
- non-specific serine/threonine protein kinase
- Rho-related BTB domain containing, isoform B
- Pebble, isoform B
- Guanine nucleotide exchange factor MSS4 homolog
- Protein lap4
- Myoblast city, isoform B
Sequence:
MDQPLVVQAEYSFMGSNNDELCFQKGDVITVTQREDGGWWEGTLNDKTGWFPSNYVNECKVQLPLTETIRPPEEIQEYRSVVLKDLLDSERAHVAELQGLLENFLEPMQQTQILSQDEYAQLMCNFVEIVRTHEDLLIQIEECNDRVGKLFLTSAPLMKKVHQAYCAAHPKAIVILDKYKDELEKYMERQGAATPGLLVLTTGLSKPFRRLDKYSAMLQELERHMESSHPDRGDTQRSVAVYKDIAATCSATRRQKELELQVLTGPVRGWQGQELSTLGDIIHMGSVAVGADHRDRYFVLFPQTLLFLSVSQRMSAFIYEGKLPLTGIIVNRLEDTDALKNAFEISSPLIDRIVAVCQGPNEANKWVELLNANNPSLPMGIKRQLSNLSNSSLGHLNAAHLSQHLDSRGYCTRFSLCAYYSSPPCHVRPLRVTLPPSNYPATAPYANLSAHFARLVKGGGLRSAIVKMLLYPQARQSIDLKRIALRKRRCHKASAKLKDLNTNQDSGQSELERQDAIELPTDSESYDDDFEDDFLHSCDSDPFEYVQFYQNKRNDSMCNSTGTFVDHGTGARRHCSSINLIKLDSADTDEVLALNELKKESLVIGSRALRALARKSTTRNSSVHTSTATLELGVGGSITNCVEEEPILKVKPSFSLQQQSSDASSIFAARLGGAFTACENLASMPDDLSRESSIQEPPTPLPASPTERHSMPTIFVGNRFNHSKNTEVYVPTWRDRQEMQNQSVDAKQDEELHSSSIDLPAACLSAPDKLQAELLYNYDEILEKPLQLHRELTPFPGHNLNSDKRVSHKSDSPSTGNAKTDPNLATRSSSTTELCIDTTSKKRTTPSERSRDSIRRCISYQFLQMSNRPPPPPPPRRDPDLHLDTKCRCCENSQCPSPRSSDSGMAGSCTITSPDPPNPESYFPMEAAGHDMLDNVEPERFDVCGMFREKFLTPEATQDVVDLSEEQPQLSDEPTTPTNRKEEPTCITSAQVQVNTRSIFLPSSSSMDETNRNVPANNILFSSSSADQLEPQATFRSGMYAHWWKKERLPPEVVRGIAHAYNKSLPSKDSKDSGSVCSSCFCSLGASGYSEGALYCSVCQNCADYYNGSVTSTTNTTTTTSSASCPLCSEDEGMIAPTHDSSSLDCPICNGRIASGAEEGKQSEMDRRPDVAAIKPHTPTARRPSASHSQQHPGRQQQRREPQPPGVSGHQLDVASQTEPVVQPPSQLQSVHAHSASTTSSASTTTTKSAKSSGGIRPQIKFSPDTKQQDSSSTPGVIHGRQSSNSGSGSSSGGSGGNGGAKRKERKHKG
Protein: Trypsin-2 (EC 3.4.21.4) (Anionic trypsinogen) (Serine protease 2) (Trypsin II) (P07478)
Organism: Homo sapiens (Human)
Function: In the ileum, may be involved in defensin processing, including DEFA5.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Trypsin-3
- Mannose-binding protein C
- Alpha-1-antitrypsin
- Serine protease inhibitor Kazal-type 1
- Amyloid-beta precursor protein
- Defensin alpha 5
- Chymotrypsinogen B
- Protein AMBP
- Cystic fibrosis transmembrane conductance regulator
- Serine protease 1
Sequence:
MNLLLILTFVAAAVAAPFDDDDKIVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS
Protein: alcohol dehydrogenase (EC 1.1.1.1) (A0A1D8PP43)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Pyruvate decarboxylase
- Pdc12p
- catechol O-methyltransferase
- S-
- Phosphoglycerate kinase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase domain-containing protein
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Aldehyde dehydrogenase
Sequence:
MSEQIPKTQKAVVFDTNGGQLVYKDYPVPTPKPNELLIHVKYSGVCHTDLHAWKGDWPLATKLPLVGGHEGAGVVVGMGENVKGWKIGDFAGIKWLNGSCMSCEFCQQGAEPNCGEADLSGYTHDGSFEQYATADAVQAAKIPAGTDLANVAPILCAGVTVYKALKTADLAAGQWVAISGAGGGLGSLAVQYARAMGLRVVAIDGGDEKGEFVKSLGAEAYVDFTKDKDIVEAVKKATDGGPHGAINVSVSEKAIDQSVEYVRPLGKVVLVGLPAHAKVTAPVFDAVVKSIEIKGSYVGNRKDTAEAIDFFSRGLIKCPIKIVGLSDLPEVFKLMEEGKILGRYVLDTSK
Protein: Odorant-binding protein 22 (AeOBP22) (OBP22) (Q1HRL7)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKVFIAVFALIAVAAAEFTVSTTEDLQRYRTECVSSLNIPADYVEKFKKWEFPEDDTTMCYIKCVFNKMQLFDDTEGPLVDNLVHQLAHGRDAEEVRTEVLKCVDKNTDNNACHWAFRGFKCFQKNNLSLIKASIKKD
Protein: LD11008p (Q961D6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MNEGKRLEATATLNVNYYPRVEVGPENPLRVERDRTAKLECNVDAKPKVPNVRWNRNGRFISSSLVHTIHRVSVQDAGKYTCIADNGLGKTGEQELILDILYPPMVVIESKTREAEEGDTVTIRCNVTANPAPVTIEWLKENSPDFRYNGDVLTLTSVRADHAGNYICRAVNIMQSQGMERSERVGNSTVALLVRHRPGQAYITPNKPVVHVGNGVTLTCSANPPGWPVPQYRWFRDMDGEFSSTQKILAQGPQYSIPKAHLGNEGKYHCHAVNELGIGMMATIVLEIHQPPQFLAKLQQHMTRRVADTDYTVTCSAKGKPAPSVKWLKDAVEILPEENLYEVQTNPDQGLNGMVTVQSQLKFRGKARPNGNALVPGDRGLYTCLYQNEVNSANSSMQLRIEHEPIVLHQYNKVAFDIRETAEVVCKVQAYPKPEFQWQFGNNPSPLTMSSDGHYEISTTTDNNDIYTSVLKINSLTHSDYGEYTCRVANTLDTIRAPIRLQQKGPPEKPTNLRATEVGHNYVSLSWDPGFDGGLSKTKFFVSYRRVAMPREEQLIPDCATLANSNSAWVEVDCQRDIPCKVTALEQHQSYAFKVKALNPKSDSPYSSEIMVTTKVSRIPPPLQVTYEPNTRTLGIDVGATCLNLVAVVESMVNADSPMAAWEVVTTMDNLQLSGNGPTHKEKIIDRIIGARRVGGGRALGHTISEDEDDNGLNSLALEDENSPTVRVKLCLRTNPEHCGDYTDAEIGRPYIAEANALATPTLIAIIVSCVVFALFAGLILMFCRCKRNQSKKSAAAKDYEMDSVRPSIVAAQQNQAPPPYYPASGLDNKALEHSMDLALSMEDQKTALYATQNGYSYHPGSGVVGVGMGGGVVGVGVGGSVVSGMGGGVGGIGGSGVGVNGIPGLSAHTMPGNEWVNMGYMENNYSNSNNGGSVNSQDSLWQVKMSAAAVGNQQGMVQAPMNQYVEQQPAYGYDPLTHGGYGAVDDYAPYPHLTATPSQVGDEYHNLRNSQNPSRQDYCSDPYASVQKPKKRVDQHLDSPYHDVSGLPNPYNMEHLEQDEVLPPQQHMSLSYDDSFEGEYSTTPNARNRRVIREIIV
Protein: Dapper 1-A (Dapper1b) (XDpr1b) (Functional regulator of dsh in ontogenesis) (Frodo) (Q8JJ48)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. Binds to dvl2/dsh and impedes the degradation of beta-catenin (ctnnb1-A and possibly ctnnb1-B), thereby enhancing the transcriptional activation of target genes of the Wnt signaling pathway. Also promotes catenin delta/ctnnd1 stability which in turn promotes zbtb33/kaiso sequestration and thus is involved in the regulation of zbtb33/kaiso-mediated transcriptional repression. May also bind to and directly stimulate the transcriptional activity of tcf7l1-A. Required for eye development and neural patterning.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MKPIPSPEPPGQLRLTPRRKDKGEAEWERHRTRERLEATLAGLAELDCLRHRQQLLVQNVLSPGTHGQDAAPTGDSPRSDEQKLLEENISLLKKQLNCLRKRDAGLLSQLHELDKQINDLKIDSEKTEETDSRPSSGFYELSDGTSGSLSNSSNSVFSECLSSCHSSTCFCNPLETSLNLTDGQAKSAEDFLEWLDYRESQHETGTVRCSFSAPHSNSVEVTADVHPKYQCDLVSKNGNDVYRYPSPLHAVAVQSPMFLISVMGNIKAEEPEEEIGPNDNDDCIVPELDHLKDEDSFLHQSSLCSLPLSSGKKMDGYILSIIHKKAHPVRTNKPRTSVNADPGKGILRHGSICVKQTVGVSQSNAVNLKNSKQTCLHSAGMISVDNSTYPSLKPCSKESLSEQLESKRMPSISTYPSCNVNELQSQNNSRNTVKSVCQGLARGSVAMTSNVQKENVTPNAPANLPNASSSVCNGSPRESTQNSALLPQEIKVVPPVKRVSLKNTLLSYHESSSFEERPPLDFKSEGSSSQSLDEGMLVNAHYIPAQQHGVKLHKNTKNVKIVKSSTLKHRADVQYVLENGSQTLKEKSKVVGKKCRFPEDLDTNKKVKKSTPRVKKIVHPHFEPAAVGRNPVAVRSGIKSHGHPKDVVLAKPKHKRSDYRRWKSSAEISYEEALRRARRRVQREMMGVCAQVPFSHASPYAYIASDSEYSAECESLFHSTVVDTSEDEQSNYTTNCFGDSESSLSEVEFVGESTTSSDTDESGGLIWSQFVHTLPMQATATAELQTTAKAFIKIKASHNLKKKILRFRSGSLKLMTTV
Protein: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (SBCAD) (EC 1.3.8.5) (2-methyl branched chain acyl-CoA dehydrogenase) (2-MEBCAD) (2-methylbutyryl-coenzyme A dehydrogenase) (2-methylbutyryl-CoA dehydrogenase) (P45954)
Organism: Homo sapiens (Human)
Function: Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA. Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:11013134}.
Interaction partners:
- Enoyl-CoA hydratase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Trifunctional enzyme subunit alpha, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal bifunctional enzyme
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Isobutyryl-CoA dehydrogenase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Sequence:
MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
Protein: Cytosolic phospholipase A2 epsilon (cPLA2-epsilon) (EC 3.1.1.4) (Calcium-dependent N-acyltransferase) (Phospholipase A2 group IVE) (Q3MJ16)
Organism: Homo sapiens (Human)
Function: Calcium-dependent N-acyltransferase involved in the biosynthesis of N-acyl ethanolamines (NAEs) in the brain. Transfers the sn-1 fatty acyl chain of phosphatidylcholine (fatty acyl donor) to the amine group of phosphatidylethanolamine (fatty acyl acceptor) to generate N-acyl phosphatidylethanolamine (NAPE). Similarly can use plasmenylethanolamine as a fatty acyl acceptor to form N-acyl plasmenylethanolamine (N-Acyl-PlsEt). Both NAPE and N-Acyl-PlsEt can serve as precursors of bioactive NAEs like N-arachidonoyl phosphatidylethanolamine also called anandamide. Has weak phospholipase A2 and lysophospholipase activities (By similarity). Regulates intracellular membrane trafficking that requires modulation of membrane curvature as it occurs by enrichment in lysophospholipids. Promotes tubule formation involved in clathrin-independent endocytotic trafficking and cargo recycling (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q50L42}. Early endosome membrane {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q50L42}; Cytoplasmic side {ECO:0000250|UniProtKB:Q50L42}. Lysosome membrane {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q50L42}; Cytoplasmic side {ECO:0000250|UniProtKB:Q50L42}. Cell membrane {ECO:0000250|UniProtKB:Q50L42}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q50L42}. Note=Targeted to clathrin-independent endocytotic vesicles through binding to phosphoinositides, especially phosphatidylinositol 4,5-bisphosphates. {ECO:0000250|UniProtKB:Q50L42}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Mitogen-activated protein kinase 3
- Guanine nucleotide-binding protein G
- Mitogen-activated protein kinase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Guanine nucleotide-binding protein G
- Patatin-like phospholipase domain-containing protein 7
- Patatin-like phospholipase domain-containing protein 6
- Lysosomal phospholipase A and acyltransferase
- Platelet-activating factor acetylhydrolase
Sequence:
MSLQASEGCPGLGTNVFVPQSPQTDEEGSRSGRSFSEFEDTQDLDTPGLPPFCPMAPWGSEEGLSPCHLLTVRVIRMKNVRQADMLSQTDCFVSLWLPTASQKKLRTRTISNCPNPEWNESFNFQIQSRVKNVLELSVCDEDTVTPDDHLLTVLYDLTKLCFRKKTHVKFPLNPQGMEELEVEFLLEESPSPPETLVTNGVLVSRQVSCLEVHAQSRRRRKREKMKDLLVMVNESFENTQRVRPCLEPCCPTSACFQTAACFHYPKYFQSQVHVEVPKSHWSCGLCCRSRKKGPISQPLDCLSDGQVMTLPVGESYELHMKSTPCPETLDVRLGFSLCPAELEFLQKRKVVVAKALKQVLQLEEDLQEDEVPLIAIMATGGGTRSMTSMYGHLLGLQKLNLLDCASYITGLSGATWTMATLYRDPDWSSKNLEPAIFEARRHVVKDKLPSLFPDQLRKFQEELRQRSQEGYRVTFTDFWGLLIETCLGDERNECKLSDQRAALSCGQNPLPIYLTINVKDDVSNQDFREWFEFSPYEVGLQKYGAFIPSELFGSEFFMGRLVKRIPESRICYMLGLWSSIFSLNLLDAWNLSHTSEEFFHRWTREKVQDIEDEPILPEIPKCDANILETTVVIPGSWLSNSFREILTHRSFVSEFHNFLSGLQLHTNYLQNGQFSRWKDTVLDGFPNQLTESANHLCLLDTAFFVNSSYPPLLRPERKADLIIHLNYCAGSQTKPLKQTCEYCTVQNIPFPKYELPDENENLKECYLMENPQEPDAPIVTFFPLINDTFRKYKAPGVERSPEELEQGQVDIYGPKTPYATKELTYTEATFDKLVKLSEYNILNNKDTLLQALRLAVEKKKRLKGQCPS
Protein: Proteasome subunit beta (Q6IAT9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MAATLLAARGAGPAPAWGPEAFTPDWESREVSTGTTIMAVQFDGGVVLGADSRTTTGSYIANRVTDKLTPIHDRIFCCRSGSAADTQAVADAVTYQLGFHSIELNEPPLVHTAASLFKEMCYRYREDLMAGIIIAGWDPQEGGQVYSVPMGGMMVRQSFAIGGSGSSYIYGYVDATYREGMTKEECLQFTANALALAMERDGSSGGVIRLAAIAESGVERQVLLGDQIPKFAVATLPPA
Protein: DNA-directed RNA polymerase II subunit 7 (RNA polymerase II subunit B7) (P38421)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. NRPB7 is part of a subcomplex with NRPB4 that binds to a pocket formed by NRPB1, NRPB2 and NRPB6 at the base of the clamp element. The NRBP4-NRPB7 subcomplex seems to lock the clamp via NRPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The NRPB4-NRPB7 subcomplex binds single-stranded DNA and RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 3
Sequence:
MFFHIVLERNMQLHPRFFGRNLKENLVSKLMKDVEGTCSGRHGFVVAITGIDTIGKGLIRDGTGFVTFPVKYQCVVFRPFKGEILEAVVTLVNKMGFFAEAGPVQIFVSKHLIPDDMEFQAGDMPNYTTSDGSVKIQKECEVRLKIIGTRVDATAIFCVGTIKDDFLGVINDPAAA
Protein: Putative lysine N-acyltransferase C17G9.06c (EC 2.3.1.-) (Q9UUE3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- L-ornithine N
- Hydroxamate-type ferrichrome siderophore peptide synthetase
- Putative amidase PB8B6.03
- Putative uncharacterized protein C23C4.04c
- Uncharacterized protein C685.08
- Uncharacterized mitochondrial membrane protein C800.14c
- Uncharacterized protein PB1A10.16
- Putative uncharacterized protein C27E2.12
- Uncharacterized protein C16G5.19
- Fluoride export protein 2
Sequence:
MSFTVWSKTEPFKLSAVQESLITLEHDNKRLLLTYREESKTWDIDLNGFQDMDVNEILQLAFLSIFYVFPTLRTEVVLQWANIESQKGTLSLPVEYNELEGNVSIDRMSFWQIPSPWMYTRCSDWPLSYLPNQVIRRPKCPKPGSTLYERFIPSLNETLSFVSLDIEQHLQYFHEWQNKPRVEYFWNESGSWDQHHEYLTTLQNDPHSFGVIGCFNDVPFAYFEVYWVPEDRIAPFAQPWHTHDRGFHALVGNDKFRGPHRVPVWLSSITHMLFLDDPRTQRVLLEPRIDNSKFINYLIEENYSKRLEFNFPHKRAAFMEITRNMFFSCLGPRI
Protein: Histone-lysine N-methyltransferase ATX3 (EC 2.1.1.-) (Protein SET DOMAIN GROUP 14) (Trithorax-homolog protein 3) (TRX-homolog protein 3) (Q9M364)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein TRAUCO
- Protein RBL
- Histone-lysine N-methyltransferase ATX2
- Histone H3-lysine
- Histone-lysine N-methyltransferase ATX5
- Histone-lysine N-methyltransferase ATX4
- Lysine-specific demethylase JMJ26
- E3 ubiquitin-protein ligase JMJ24
- Lysine-specific demethylase JMJ28
- COMPASS-like H3K4 histone methylase component WDR5A
Sequence:
MILKRTLTTFENQNLKRCKIDSEIEYGRKKGEIIVYKKRQRATVDQPCSKEPELLTSSSSSLTSKEESQQVCSDQSKSSRGRVRAVPSRFKDSIVGTWKSSRRKGESTESSHDDDDVSLGKKVKGFSGSSKLHRSKDSKVFPRKDNGDSSEVDCDYWDVQISYDDANFGMPKKSDASRKGVYKPEEFTVGDLVWAKCGKRFPAWPAVVIDPISQAPDGVLKHCVPGAICVMFFGYSKDGTQRDYAWVRQGMVYPFTEFMDKFQDQTNLFNYKASEFNKALEEAVLAENGNFGDAEIISPDSSATESDQDYGPASRFQGSYHEDIRTCDGCGSVMPLKSLKRTKDSQPEELLCKHCSKLRKSNQYCGICKRIWHPSDDGDWVCCDGCDVWVHAECDNITNERFKELEHNNYYCPDCKVQHELTPTILEEQNSVFKSTEKTTETGLPDAITVVCNGMEGTYIRKFHAIECKCGSCGSRKQSPSEWERHTGCRAKKWKYSVRVKDTMLPLEKWIAEFSTYTLETQMLDKQKMLSLLEEKYEPVRAKWTTERCAVCRWVEDWEENKMIICNRCQVAVHQECYGVSKSQDLTSWVCRACETPDIERDCCLCPVKGGALKPSDVEGLWVHVTCAWFRPEVGFLNHENMEPAVGLFKIPANSFLKVCTICKQTHGSCVHCCKCATHFHAMCASRAGYNMELHCLEKNGVQRTRKSVYCSFHRKPDPDSVVVVHTPSGVFGSRNLLQNQYGRAKGSRLVLTKKMKLPGFQTQTQAEQSRVFDSLSAARCRIYSRSNTKIDLEAISHRLKGPSHHSLSAIENLNSFKASFSFRAPFMSVFCFLGATFSEYLRKILISIYLVTHQEADFTSFRERLKHLQRTENFRVCFGKSGIHGWGLFARKSIQEGEMIIEYRGVKVRRSVADLREANYRSQGKDCYLFKISEEIVIDATDSGNIARLINHSCMPNCYARIVSMGDGEDNRIVLIAKTNVAAGEELTYDYLFEVDESEEIKVPCLCKAPNCRKFMN