wanglab/gogpt-training-data huggingface dataset:
Protein: Alcohol dehydrogenase 1A (EC 1.1.1.1) (Alcohol dehydrogenase subunit alpha) (P28469)
Organism: Macaca mulatta (Rhesus macaque)
Function: Alcohol dehydrogenase. Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate.
Subcellular location: Cytoplasm.
Interaction partners:
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- aldehyde dehydrogenase
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1 family member A2
- S-formylglutathione hydrolase
- Cytochrome P450 2E1
- Aldehyde dehydrogenase 3 family member B2
- All-trans-retinol 13,14-reductase
- aldehyde oxidase
Sequence:
MSTAGKVIKCKAAVLWEVMKPFSIEDVEVAPPKAYEVRIKMVTVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVEPGDKVIPLALPQCGKCRICKTPERNYCLKNDVSNPRGTLQDGTSRFTCRGKPIHHFLGVSTFSQYTVVDENAVAKIDAASPMEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAVYGGFKSKEDIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLRSGKSIRTILTF
Protein: Deoxythymidylate kinase (Dtymk protein) (B0K028)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASRRGALIVLEGVDRAGKTTQCLRLVTALCASGHRAELLRFPERSTEIGKLLSSYLEKKTELEDHSVHLLFSANRWEQVPLIKAKLNQGVTLFWTDTRFLGLPSLAPRRHAGFSRTALYFAFG
Protein: Protein SSX3 (Cancer/testis antigen 5.3) (CT5.3) (Q99909)
Organism: Homo sapiens (Human)
Function: Could act as a modulator of transcription.
Interaction partners:
- Afadin- and alpha-actinin-binding protein
- Protein SSX1
- Protein SSXT
- Protein SSX7
Sequence:
MNGDDTFARRPTVGAQIPEKIQKAFDDIAKYFSKEEWEKMKVSEKIVYVYMKRKYEAMTKLGFKAILPSFMRNKRVTDFQGNDFDNDPNRGNQVQRPQMTFGRLQGIFPKIMPKKPAEEGNVSKEVPEASGPQNDGKQLCPPGKPTTSEKINMISGPKRGEHAWTHRLRERKQLVIYEEISDPEEDDE
Protein: Probable cysteine protease RD19C (EC 3.4.22.-) (RD19-like protein 2) (Q9SUL1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol protease.
Subcellular location: Lytic vacuole {ECO:0000269|PubMed:18708476}. Note=Predominantly vacuolar. From the Golgi apparatus, probably transported to the lytic vacuole (LV) in clathrin-coated vesicles (CCVs) via the prevacuolar compartment (PVC). {ECO:0000269|PubMed:18708476}.
Interaction partners:
- Disease resistance protein RRS1
- UPF0235 protein At5g63440
- Vacuolar-processing enzyme beta-isozyme
- Aspartyl protease UND
- Vacuolar-processing enzyme gamma-isozyme
- Cysteine proteinase RD21A
- Expressed protein
- Probable cysteine protease RD21B
- At1g09850
- Probable cysteine protease RD21C
Sequence:
MDRVVFFFLIAATLLAGSLGSTVISGEVTDGFVNPIRQVVPEENDEQLLNAEHHFTLFKSKYEKTYATQVEHDHRFRVFKANLRRARRNQLLDPSAVHGVTQFSDLTPKEFRRKFLGLKRRGFRLPTDTQTAPILPTSDLPTEFDWREQGAVTPVKNQGMCGSCWSFSAIGALEGAHFLATKELVSLSEQQLVDCDHECDPAQANSCDSGCSGGLMNNAFEYALKAGGLMKEEDYPYTGRDHTACKFDKSKIVASVSNFSVVSSDEDQIAANLVQHGPLAIAINAMWMQTYIGGVSCPYVCSKSQDHGVLLVGFGSSGYAPIRLKEKPYWIIKNSWGAMWGEHGYYKICRGPHNMCGMDTMVSTVAAVHTSPK
Protein: Myosin-2 (Myosin heavy chain 2) (Myosin heavy chain 2a) (MyHC-2a) (Myosin heavy chain IIa) (MyHC-IIa) (Myosin heavy chain, skeletal muscle, adult 2) (Q9UKX2)
Organism: Homo sapiens (Human)
Function: Muscle contraction. Required for cytoskeleton organization (By similarity).
Subcellular location: Cytoplasm, myofibril {ECO:0000250|UniProtKB:G3UW82}. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin-1
- Myosin regulatory light chain 11
- Myosin-7
- Actin, alpha skeletal muscle
- Myosin-6
- Myosin-13
- Myosin light chain 3
- Myosin-8
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Sequence:
MSSDSELAVFGEAAPFLRKSERERIEAQNRPFDAKTSVFVAEPKESFVKGTIQSREGGKVTVKTEGGATLTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKIQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVVFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVEQVSNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFALIHYAGVVDYNITGWLEKNKDPLNETVVGLYQKSAMKTLAQLFSGAQTAEGEGAGGGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFKAGLLGLLEEMRDDKLAQLITRTQARCRGFLARVEYQRMVERREAIFCIQYNIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKIKDELAKSEAKRKELEEKMVTLLKEKNDLQLQVQAEAEGLADAEERCDQLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKIKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESIMDIENEKQQLDEKLKKKEFEISNLQSKIEDEQALGIQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAATLRKKHADSVAELGEQIDNLQRVKQKLEKEKSEMKMEIDDLASNVETVSKAKGNLEKMCRTLEDQLSELKSKEEEQQRLINDLTAQRGRLQTESGEFSRQLDEKEALVSQLSRGKQAFTQQIEELKRQLEEEIKAKNALAHALQSSRHDCDLLREQYEEEQESKAELQRALSKANTEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQAAEEHVEAVNAKCASLEKTKQRLQNEVEDLMLDVERTNAACAALDKKQRNFDKILAEWKQKCEETHAELEASQKEARSLGTELFKIKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKRIHELEKIKKQVEQEKCELQAALEEAEASLEHEEGKILRIQLELNQVKSEVDRKIAEKDEEIDQLKRNHIRIVESMQSTLDAEIRSRNDAIRLKKKMEGDLNEMEIQLNHANRMAAEALRNYRNTQGILKDTQIHLDDALRSQEDLKEQLAMVERRANLLQAEIEELRATLEQTERSRKIAEQELLDASERVQLLHTQNTSLINTKKKLETDISQMQGEMEDILQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQLRLDEAEQLALKGGKKQIQKLEARVRELEGEVESEQKRNAEAVKGLRKHERRVKELTYQTEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQSNTNLAKFRKLQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE
Protein: GH15984p (Rho GTPase activating protein at 1A, isoform A) (Rho GTPase activating protein at 1A, isoform B) (Q29QE1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
Interaction partners:
Sequence:
MSVFDDFQRLWMQRFPQSSLSDAWEQDVRASLERHKVRINELSKELEQETLYVEYLERLLSDVERYRVSGGDPKALFEAASGSCASSNNSNCSSTTNGATQEESNTNLDKDFKSSLNLRESPSSTGAKDKDRLSLNPDNKYTTHTNAVIGGIGSEKVSGPLHSTQITADGKRTGELYLKREEDKCKDSNSEDTDGALQQCITELAASLKAQPDNVAGGRLENDVDIDKPLRKSTSQYVTVIQVKEAKDKESADGTTSSSGIGEPQQQPTPPSTFSRYSEATAPPLSPSLTSYAAHVEAKKKMPPRPPPKNIRRVEPPTIPSQQLSSSPKRETYMINTMPSSSSGSLCIDSLGNSLERNIKPSDILRQKSSDNLDSKYSAKRKTTPELSKFVNVNNPELMEELGRKMVSKADSLEQTRRNDSSPSGCGSLGRTSSTPGRSLTPGRTGVGASPTGSLSKTGKLAMADSSSTSSLERRSCLQAVDADIGTESRESGANQRSVGSKESLTSQGISEVIKSYESVSSLSSESAKAVASQQSAAAGGALAECEPYYDSVPLDNGDGEYVFIKPGRTGSSSSRDDLSTPGSSILPLPNVADPESPGRTSNYVNIDFFLQQGIETRSSSLDSDGEYEGPPILRTISHDDQTTTQTTPGAIRKNLVSAILVCGNARGAKIRSILSSIIQSETIYVECLNKMMQYKKAIHATLTTSQPVIREEEENTIFFKIDELYDLHTGFLSDLKTIVSHEGGDVLIGEPFRRLAEMFDLYSAFLHNYKNAIETVKKCSANNPQFKKIVSTIVLNLQTEQSLTLEDLLHKPVARVQINALVFNDLLRETPNAHPDHQPLRQAQKIIQMFLNQFNVVNQRLPIESNRNLRRMVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGAFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLKQKCNLPGANTINSLEVTAFIVAMQKGMKTEMGSYLMRNTNDESLLVGDLYMGVHGLEGLEQANDLYICVEVDSYGHYFRKATTKKICRSQTPLWNESFMLELEGSQNVRILLYEAKERPLLKAKHILKLSLSWLTETTQPKSIKLTETLELGCSFRFIPGELFRGSTKPGALFGAKMSQVLKREKRDIPFIIGACIREVERRGMLEVGCYRVSGSASDLAKLKKAFESDAYEAEQLLREVDIHSVTGILKTFLRELPEALFTDQLYPRFFDTFSAFSNNNESTRINELLKVFEELPQANKASITSILDHLIRVHEKETDNKMSLHNLAMVFGPTLLRPGQTQVKQKDPLAASTVDVMAQAGILYCFLQARIKKD
Protein: Guanine nucleotide exchange factor DBS (DBL's big sister) (MCF2-transforming sequence-like protein) (Q64096)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways. Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17000758}. Cell membrane {ECO:0000269|PubMed:17000758}; Peripheral membrane protein {ECO:0000269|PubMed:17000758}; Cytoplasmic side {ECO:0000269|PubMed:17000758}.
Interaction partners:
- Cell division control protein 42 homolog
- Transforming protein RhoA
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MSDCWCFIFCKEHVRSNPLSPQHDGASREEADHQVDVSDGIRLVPDKAEATAATASDEIMHQDIVPLCAADIQEQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRQDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDEFKMKVPVMMLSSVPELHGYIDKSQLTEDLGGTLDYCHSRWLCHRTAIESFALMVKQTAQMLQAFGTELAETELPNDVQSTSLVLSAHTEKKAKVKEDLQLALKEGNSILESLREPLAESAAHSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGFREVKTTLDSMSQKIAAFTDVGNSLAHVQHLLKDLTAFEEKSSVAVDKARALSLEGQQLIENRHYAVDSIHPKCEELQHLCDHFASEVTRRRGLLSKSLELHSLLETSMKWSDEGIFLLASQPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNEIYKEYECILNQDLLEHVQKVFQKQESTEEMFHRRQASLKKLAAKQTRPVQPVAPRPEALTKSPSPSPGSWRSSENSSSEGNALRRGPYRRAKSEMSEPRQGRTSSTGEEEESLAILRRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHLISTGLQNKKNILFGNMEEIYHFHNRNIPAGLESCIDCPELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQCSDCPFFQECQKKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMTAVGITENVKGDTKKFEIWYNAREEVYIIQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSHSLPLPTPSSTSPTKGNTRNVKKLEDRKTDPLSLEGYVSSSLPKPPEKGKGWSKTSHSLEAPEEDGGWSSAEELINSSDAEEDGGVGPKKLVPGKYTVVMDDEKGGPDTLAMRSGDMVEVVEEGAEGLWYVRDLTSSKEGWVPASSLSTLLGKSSSAQCLSSSGKIHCARQLCPEPAEILSPEPV
Protein: 60 kDa heat shock protein, mitochondrial (C9JL25)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKTCWTREQLQGKRQGEVVKGKQGGEYRHPDPARQAGWQETEMLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISK
Protein: E3 ubiquitin-protein ligase TRIM47 (EC 2.3.2.27) (Tripartite motif-containing protein 47) (Q8C0E3)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates the ubiquitination and proteasomal degradation of CYLD.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96LD4}. Nucleus {ECO:0000250|UniProtKB:Q96LD4}.
Interaction partners:
Sequence:
MDGSGPFSCPICLEPLREPVTLPCGHNFCLACLGALWPHRSAGGTGGSGGPARCPLCQEPFPDGLQLRKNHTLSELLQLRQGSVPGPMSAPASGSTRGATPEPSAPSAPPPAPEPSAPCAPEQWPAGEEPVRCDACPEGAALPAALSCLSCLASFCSAHLAPHERSPALRGHRLVPPLRRLEESLCPRHLRPLERYCRVERVCLCEACATQDHRGHELVPLEQERALQEVEQSKVLSAAEDRMDELGAGIAQSRRTVALIKSAAVAERERVSQMFAEATATLQSFQNEVMGFIEEGEATMLGRSQGDLRRQEEQRSRLSKARHNLGQVPEADSVSFLQELLALRLALEEGCGPGPGPPRELSFTKSSQVVKAVRDTLISACASQWEQLRGLGSNEDGLQKLGSEDVESQDPDSTSLLESEAPRDYFLKFAYIVDLDSDTADKFLQLFGTKGVKRVLCPINYPESPTRFTHCEQVLGEGALDRGTYYWEVEIIEGWVSVGVMAEGFSPQEPYDRGRLGRNAHSCCLQWNGRGFSVWFCGLEAPLPHAFSPTVGVCLEYADHALAFYAVRDGKLSLLRRLKASRPRRSGALASPTDPFQSRLDSHFSGLFNHRLKPAFFLESVDAHLQIGPLKKSCITVLKRR
Protein: Diacylglycerol kinase alpha (DAG kinase alpha) (EC 2.7.1.107) (EC 2.7.1.93) (80 kDa diacylglycerol kinase) (Diglyceride kinase alpha) (DGK-alpha) (P23743)
Organism: Homo sapiens (Human)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids (Probable). Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:2175712}.
Interaction partners:
- Lipoprotein lipase
- RAS guanyl-releasing protein 1
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipase D2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Ceramide kinase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Diacylglycerol O-acyltransferase 1
Sequence:
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNLSTSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPMLMGPPPRSTNFFGFLS
Protein: Cytosolic Fe-S cluster assembly factor NUBP1 (Nucleotide-binding protein 1) (NBP 1) (P53384)
Organism: Homo sapiens (Human)
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Implicated in the regulation of centrosome duplication (By similarity). Negatively regulates cilium formation and structure (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03038, ECO:0000269|PubMed:18573874, ECO:0000269|PubMed:29848660}. Nucleus {ECO:0000250|UniProtKB:Q9R060}. Cell projection {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9R060}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis. Localized at centrioles and in the nucleus at interphase. Colocalizes with nubp-2 at prometaphase. Specifically localizes to the axenome of motile cilia as opposed to primary non-motile cilia. Localization is independent of NUBP2 and KIFC1. {ECO:0000250|UniProtKB:Q9R060}.
Interaction partners:
- Probable cytosolic iron-sulfur protein assembly protein CIAO1
- Anamorsin
- Cytosolic iron-sulfur assembly component 3
- Iron-sulfur clusters transporter ABCB7, mitochondrial
- MMS19 nucleotide excision repair protein homolog
- Cytosolic Fe-S cluster assembly factor NUBP2
- Cytosolic iron-sulfur assembly component 2B
- NADPH-dependent diflavin oxidoreductase 1
- FAD-dependent oxidoreductase domain-containing protein 1
- Iron-sulfur cluster assembly enzyme ISCU
Sequence:
MEEVPHDCPGADSAQAGRGASCQGCPNQRLCASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVMSVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLATAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPPTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPATLAYRSIIQRIQEFCNLHQSKEENLISS
Protein: Equilibrative nucleoside transporter 4 (hENT4) (Plasma membrane monoamine transporter) (PMAT) (Solute carrier family 29 member 4) (Q7RTT9)
Organism: Homo sapiens (Human)
Function: Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15448143, ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17121826, ECO:0000269|PubMed:20858707}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:17018840, ECO:0000269|PubMed:23255610}; Multi-pass membrane protein {ECO:0000305}. Note=Located to the plasma membranes of ventricular myocytes and vascular endothelial cells (PubMed:16873718). Targeted to the apical membranes of differentiated kidney epithelial cells (PubMed:17018840). Localized to the apical blood-cerebrospinal fluid (CSF)-facing membrane of the choroid plexus epithelium (PubMed:23255610). {ECO:0000269|PubMed:16873718, ECO:0000269|PubMed:17018840, ECO:0000269|PubMed:23255610}.
Interaction partners:
- Synaptic vesicular amine transporter
- Multidrug and toxin extrusion protein 1
- Solute carrier family 22 member 3
- Multidrug and toxin extrusion protein 2
- Solute carrier family 22 member 1
- Sodium/nucleoside cotransporter 1
- Sodium/nucleoside cotransporter 2
- Solute carrier family 28 member 3
Sequence:
MGSVGSQRLEEPSVAGTPDPGVVMSFTFDSHQLEEAAEAAQGQGLRARGVPAFTDTTLDEPVPDDRYHAIYFAMLLAGVGFLLPYNSFITDVDYLHHKYPGTSIVFDMSLTYILVALAAVLLNNVLVERLTLHTRITAGYLLALGPLLFISICDVWLQLFSRDQAYAINLAAVGTVAFGCTVQQSSFYGYTGMLPKRYTQGVMTGESTAGVMISLSRILTKLLLPDERASTLIFFLVSVALELLCFLLHLLVRRSRFVLFYTTRPRDSHRGRPGLGRGYGYRVHHDVVAGDVHFEHPAPALAPNESPKDSPAHEVTGSGGAYMRFDVPRPRVQRSWPTFRALLLHRYVVARVIWADMLSIAVTYFITLCLFPGLESEIRHCILGEWLPILIMAVFNLSDFVGKILAALPVDWRGTHLLACSCLRVVFIPLFILCVYPSGMPALRHPAWPCIFSLLMGISNGYFGSVPMILAAGKVSPKQRELAGNTMTVSYMSGLTLGSAVAYCTYSLTRDAHGSCLHASTANGSILAGL
Protein: Duplicated homeodomain-like superfamily protein (MYB transcription factor) (MYB-family transcription factor, putative; alternative splicing isoform 2 of 2;71559-70643 (Myb-family transcription factor, putative; alternative splicing isoform 1 of 2;71559-70643)) (Putative MYB-family transcription factor) (Q9C773)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METLHPFSHLPISDHRFVVQEMVSLHSSSSGSWTKEENKMFERALAIYAEDSPDRWFKVASMIPGKTVFDVMKQYSKLEEDVFDIEAGRVPIPGYPAASSPLGFDTDMCRKRPSGARGSDQDRKKGVPWTEEEHRRFLLGLLKYGKGDWRNISRNFVVSKTPTQVASHAQKYYQRQLSGAKDKRRPSIHDITTGNLLNANLNRSFSDHRDILPDLGFIDKDDTEEGVIFMGQNLSSENLFSPSPTSFEAAINFAGENVFSAGA
Protein: Serine palmitoyltransferase small subunit B (Protein ADMP) (Small subunit of serine palmitoyltransferase B) (ssSPTb) (Q925E8)
Organism: Mus musculus (Mouse)
Function: Stimulates the activity of serine palmitoyltransferase (SPT). The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference, complexes with this subunit showing a clear preference for longer acyl-CoAs. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 3
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase small subunit A
- ORM1-like protein 3
- ORM1-like protein 1
- ORM1-like protein 2
Sequence:
MDFKRVKEYFAWLYYQYQIITCCAVMEPWEQSMLNTIILTIVAMVVYTAYVFIPIHIRLAWEFFSKICGYDSSISN
Protein: Transcription initiation factor TFIID subunit 4 (TBP-associated factor 4) (Q9P7S4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by taf1), facilitation of DNA opening and initiation of transcription (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf6
- Transcription initiation factor TFIID subunit 13
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf10
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 2
- TATA-box-binding protein
- Putative transcription initiation factor TFIID 111 kDa subunit
Sequence:
MDLNNPPSKRFGDDDDIPANKRPKNEEYPEIPGYLGNRKPSYTQNPNSGPGKLHYASPRPNNVSSSVGVASGGDRQEADQLQDALISCGIQLKEEELNLSTSFYDPSSLNTFALTTEDRSRKSDFLNSFVLMQTVSNIVNLHRLKSMDSDIHALISMAVRDYLANLLQKMIVESHHRTSQLHTDNYKQVDNVRQTLANFAYKEYESEERRRTVLNIRRAEHEARLAELNSASTNEEGSSRRRKEQSSSAAAKNISEDAQNRMTNATASIMAGSALPSGGKKYSWMATDMTPMTPAVGGGFGIRKKDSNSLKPSSRDGVLPLQQEEKGIITIRDALAVLEMDREGAGRIFGRGAKAMMRAYIRLKD
Protein: Clustered mitochondria protein 1 (Translation initiation factor 31) (eIF3-associated protein p135) (Q03690)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- mRNA-binding protein PUF3
- Protein TMA108
Sequence:
MSEKKEEVKNATVKVTVKLPKEDNHSHNTKHLKKTQSSKNNDISFEIGKESKIQTVLDVLAMIPSSKYLTNVGLKTIEGDSQLSDEMSIKEIVGEKSELKLQLILKPYSAREALKHVITVRDFIGFAQETSDGLSEFAISTGSSFSSLPLGPIKERSKQEEKDEKSDPEEKKNTFKDVTDEEKLKFNEMVHEVFSSFKNSSINKLLTSESNIITPCVRSLSFAPYNPVPPFYRSKGHLFYLQIVTLEGESFYITAIPSGFYVNKSNSTKFDPSPKENTDENAHSSLIYYSLFDLIASRSKKFISHVQAFEKKLSALDSTSYVRPSNTFLHKPWFVSSLPPNNPDYLRLQTAALDTTPERNFNDEFQAIKDLTTSTLQDRIEMERLFSKVVHEFSVTAASGAMSIFYSDFVAMNPESPTRDQIFLKDNIFYSYVSDVSGNYEGKGGDEAAIAASNQDLKTINILNRLHMHEVRYLLTTVVEFAGRRILAQTPVPGLLATMGNKIVKDANTGEEVTEDFVNDINVKYGLDEGLGKIVYDADFDSVLEKKFVKAFHLKKHKVNGTELAFSSQSKGIVGFDKRRYILDLANTYPLDINFARQNFDNIEETGNRYPHRQTLLRPELVEKWWNNKVEKEGVEFEKAYEENLFSYNPDAYQVEGIEDANVDEMSNYLQKEVIPSVIQDYLSGNLSTPYNGEHLADTLHKNGINMRYLGKIIELSQKELDSQIVHYEQNLKAVEQDNKEYEDWEKSYLQKIENMIKERQAKINKLVQEGKEVPKELTEDLKLNDEEIKKPTDGKPVVVAYDELVPLIKISELEIVSRSLKHVLKDLSKDVPVFLVPSLVAYVFNMLVGINYNADPKPEPVDEFYPVNKCSFAKLTRSELLEAVSKQAFLRFRHQLPSNWIEAYMENPFTLIRSVSYKFGIQLLNKEYFFTREQLESYKQSLDKKIRNKFVEPPTTFSLSDLTIIPRVKFSEYTSSVSEEFWAQGASMINEDKQSALTLLAQSITVLEDVNNILHPAVAEKYLSLSAIYNKLALYPEAIAFCRKACTIYERVSGIDSFEMMRALTNLAILEFSNESPYNATVVYNRLAEILKVYELPKIHHPAPTSIFNHLEQLALGVQDTKLAIEVLGQLSSYVVELEGKDSLAYGYTESRLGNLFAALKDFHRALEHITVTQGIFTKQLGMNHTHSAQSRQWVNGLSSLIMDLKQKKQLAQDQMSTTGSNSAGHKKTNHRQKKDDVKPELANKSVDELLTFIEGDSSNSKSKNKTNNKKKHGKK