wanglab/gogpt-training-data huggingface dataset:
Protein: Estrogen-related receptor (GH28308p) (Q9VSE9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MSDGVSILHIKQEVDTPSASCFSPSSKSTATQSGTNGLKSSPSVSPERQLCSSTTSLSCDLHNVSLSNDGDSLKGSGTSGGNGGGGGGGTSGGNATNASAGAGSGSVRDELRRLCLVCGDVASGFHYGVASCEACKAFFKRTIQGNIEYTCPANNECEINKRRRKACQACRFQKCLLMGMLKEGVRLDRVRGGRQKYRRNPVSNSYQTMQLLYQSNTTSLCDVKILEVLNSYEPDALSVQTPPPQVHTTSITNDEASSSSGSIKLESSVVTPNGTCIFQNNNNNDPNEILSVLSDIYDKELVSVIGWAKQIPGFIDLPLNDQMKLLQVSWAEILTLQLTFRSLPFNGKLCFATDVWMDEHLAKECGYTEFYYHCVQIAQRMERISPRREEYYLLKALLLANCDILLDDQSSLRAFRDTILNSLNDVVYLLRHSSAVSHQQQLLLLLPSLRQADDILRRFWRGIARDEVITMKKLFLEMLEPLAR
Protein: Ferulic acid decarboxylase 1 (EC 4.1.1.102) (Phenacrylate decarboxylase) (Q03034)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites. Not essential for ubiquinone synthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Flavin prenyltransferase PAD1, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Uncharacterized protein YDR514C
Sequence:
MRKLNPALEFRDFIQVLKDEDDLIEITEEIDPNLEVGAIMRKAYESHLPAPLFKNLKGASKDLFSILGCPAGLRSKEKGDHGRIAHHLGLDPKTTIKEIIDYLLECKEKEPLPPITVPVSSAPCKTHILSEEKIHLQSLPTPYLHVSDGGKYLQTYGMWILQTPDKKWTNWSIARGMVVDDKHITGLVIKPQHIRQIADSWAAIGKANEIPFALCFGVPPAAILVSSMPIPEGVSESDYVGAILGESVPVVKCETNDLMVPATSEMVFEGTLSLTDTHLEGPFGEMHGYVFKSQGHPCPLYTVKAMSYRDNAILPVSNPGLCTDETHTLIGSLVATEAKELAIESGLPILDAFMPYEAQALWLILKVDLKGLQALKTTPEEFCKKVGDIYFRTKVGFIVHEIILVADDIDIFNFKEVIWAYVTRHTPVADQMAFDDVTSFPLAPFVSQSSRSKTMKGGKCVTNCIFRQQYERSFDYITCNFEKGYPKGLVDKVNENWKRYGYK
Protein: Luteinizing hormone beta (Q800P3)
Organism: Oncorhynchus kisutch (Coho salmon) (Salmo kisutch)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU004069}.
Interaction partners:
Sequence:
VGTLISLFLCILLEPMEGSLMQPCQPINQTVSLEKEGCPTCLVIQTPICSGHCVTKEPVFKSPFSTVYQHVCTYRDVRYETIRLPDCPPWVDPHVTYPVALSCDCSLCNMDTSDCTIESLQPDFCITQRVLTDGDMW
Protein: Propionicin-F (Q6E3K9)
Organism: Propionibacterium freudenreichii subsp. freudenreichii
Function: Bacteriocin with specific antibacterial activity against strains of P.freudenreichii. No antibacterial activity was detected against P.acidipropionici, P.jensenii and P.thoenii.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNTKAVNLKSENTTKLVSYLTENQLDEFIRRIRIDGALVEEVSQNAKQALDNTGLNGWINTDCDEGLLSDFISKIASARWIPLAESIRPAVTDRDKYRVSCWFYQGMNIAIYANIGGVANIIGYTEAAVATLLGAVVAVAPVVPGTPTPPKDKSSQYKEVPLAVRLSETYHEEGVRGLFDELNYSESRMISTLRRASTDGVLINSWNDGQDTILLKKYNFQDLQLTVRSRIVGNQTIIEECKITDGRKTLSDETV
Protein: Fibrinolytic enzyme large subunit (EC 3.4.-.-) (P81802)
Organism: Eisenia fetida (Red wiggler worm)
Function: Cleaves the carboxyl side of basic amino acids, small neutral amino acids, and Met residue. It is also a plasminogen activator.
Interaction partners:
Sequence:
VIGGTNASPGEIPWQLSQQRQSGSW
Protein: Argonaute-binding protein 1 (Q9P7B8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the argonaute siRNA chaperone (ARC) complex which is required for histone H3K9 methylation, heterochromatin assembly and siRNA generation. The ARC complex contains mostly double-stranded siRNA. Inhibits the release of the siRNA passenger strand from ago1 together with arb2. Inhibits the slicer activity of ago1. Required for swi6 localization to the centromeric repeats.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17310250}. Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17310250}. Note=Predominantly nuclear. {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17310250}.
Interaction partners:
- Argonaute-binding protein 2
- Protein argonaute
- RNA-induced transcriptional silencing complex protein tas3
- Chromo domain-containing protein 1
- Protein Dicer
- Meiotic chromosome segregation protein P8B7.28c
- Staphylococcal nuclease domain-containing protein 1
Sequence:
MAEGDFKNDSTGCIGDSVEFTTFKKRTGKSLGNRRKKRGLSGWEPYFQEPELTAEEKLENETLYSRNIPLTVRMERFIQRYRSRRKWSDPTRIRLFTMYLDLGGVSTGQKQFTGGTDINNDAKAREVSAQTTTDYIEYDILDEYDIDFKWVAGVFLSSHILYNAGLTKEEDLQIACQIVRNFLLSVLHNNVAPEFEDNIRDACLLAEQAETELISNKRLSTKLPGRLQRALASIHVDNYKGLWDKSQSDRTSDSSVNFIESNNTKFMPNDELFEPDGISRFSTQQARDYIQRTLGPRYLTGKVVEQEYLTVKLVSKTLLNFSNQSLCKAVFIVWDPPGSKYSQDTNKERLEVILESDLLNNTVDGTHLEGSFTFLDNGLTILDTVLAVLPTFYEEVKDE
Protein: Homeobox protein Meis1a (Meis homeobox 1 a) (Myeloid ecotropic viral integration site 4.1a) (Q7SZP3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MAQRYEDLVHYGMDAVGIPSPMYGDPHAARAMQAVHVSHGPPLHPYPHPATAPGVPPPVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPRESGVTGDVCSSESFDEDITVFSKQIRAEKPFFSSNPDLDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVVDDKEGGSRSDGEEFTRTPGGSEQVFWREDDTASVHSTDTPAACGRRSSSHNGDNSSEHGDFLDQSVASPSTGEEEDPDKERKNNKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKRQLSQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVGHSGPYTPDAQPMGGFVMDGQSHMGIRPPAALGGLGGVNMGLESQWHYM
Protein: dCTP pyrophosphatase 1 (EC 3.6.1.12) (Deoxycytidine-triphosphatase 1) (dCTPase 1) (RS21C6) (XTP3-transactivated gene A protein) (Q9H773)
Organism: Homo sapiens (Human)
Function: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleotide analogs through their catabolism.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24467396}. Nucleus {ECO:0000269|PubMed:24467396}. Cytoplasm, cytosol {ECO:0000269|PubMed:24467396}.
Interaction partners:
- Deoxycytidylate deaminase
- Deoxycytidine kinase
- Nucleoside diphosphate kinase A
- Adenylate kinase 9
- 5'
- Ribonucleoside-diphosphate reductase subunit M2
- 5'
- Ribonucleoside-diphosphate reductase large subunit
- Ribonucleoside-diphosphate reductase subunit M2 B
- Nucleoside diphosphate kinase B
Sequence:
MSVAGGEIRGDTGGEDTAAPGRFSFSPEPTLEDIRRLHAEFAAERDWEQFHQPRNLLLALVGEVGELAELFQWKTDGEPGPQGWSPRERAALQEELSDVLIYLVALAARCRVDLPLAVLSKMDINRRRYPAHLARSSSRKYTELPHGAISEDQAVGPADIPCDSTGQTST
Protein: Lysine--tRNA ligase (EC 2.7.7.-) (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) (Q15046)
Organism: Homo sapiens (Human)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity.
Subcellular location: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000269|PubMed:10952987, ECO:0000269|PubMed:19289464, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:28887846}. Cytoplasm {ECO:0000269|PubMed:15220430}. Nucleus {ECO:0000269|PubMed:15220430, ECO:0000269|PubMed:23159739}. Cell membrane {ECO:0000269|PubMed:15220430}; Peripheral membrane protein {ECO:0000269|PubMed:15220430}. Secreted {ECO:0000269|PubMed:15851690}. Note=Secretion is induced by TNF-alpha (PubMed:15851690). Cytosolic in quiescent mast cells. Translocates into the nucleus in response to mast cell activation by immunoglobulin E (PubMed:23159739). {ECO:0000269|PubMed:15851690, ECO:0000269|PubMed:23159739}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:10952987}.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Arginine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
- Eukaryotic translation elongation factor 1 epsilon-1
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Sequence:
MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
Protein: dolichyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.18) (Q7KN63)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
LSEECVVAFQIGYNFRVTGWNWDMNRTPKMLNSKVAGYSSLITFAILLIAWLAGFSSRLFAVIRFESIIHEFDPWFNYRATAYMVQNGWYNFLNWFDERAWYPLGRIVGGTVYPGLMITSGGIHWLLHVLNIPVHIRDICVFLAPIFSGLTSISTYLLTKELWSAGAGLFAASFIAIVPGYISRSVAGSYDNEGIAIFALQFTYFLWVRSVKTGSVFWSAAAALSYFYMVSAWGGYVFIINLIPLHVFVLLIMGRYSPRLLTSYSTFYILGLLFSMQIPFVGFQPIRTSEHMAALGVFVLLMAVATLRHLQSVLSRNEFRKLFIVGGLLVGVGVFVAVVVLTMLGVVAPWSGRFYSLWDTGYAKIHIPIIASVSEHQPTTWFSFFFDLHILVCAFPVGVWYCIKQINDERVFVVLYAISAVYFAGVMVRLMLTLTPVVCMLAGVAFSGLLDVFLQEDSSKRMGTAISAATEVDEAEDSIEKKTLYDKAGKLKHRTKHDAQQDTGVSSNLKSIVILAVLMLLMMFAVHCTWVTSNAYSSPSIVLAFHNSQDGSRNILDDFREAYYWLSQNTADDARVMSWWDYGYQIAGMANRTTLVDNNTWNNSHIALVGKAMSSTEEKSYEIMTSLDVDYVLVIFGGVIGYSGDDINKFLWMVRIAEGEHPKDIKESDYFTDRGEFRVDAEGAPALLNCLMYKLSYYRFGELKLDYRGPSGYDRTRNAVIGNKDFDLTYLEEAYTTEHWLVRIYRVKKPHEFNRPSLKTKERTIPPANFISRKNSKRRKGYIRNRPVVVKGKRTLK
Protein: Auxin response factor 20 (Q9C7I9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Auxin-responsive protein IAA33
- Auxin-responsive protein IAA32
- Auxin-responsive protein IAA11
- Auxin-responsive protein IAA15
- Mitotic spindle checkpoint protein MAD2
- Auxin-responsive protein IAA5
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Winged-helix DNA-binding transcription factor family protein
- Transcription initiation factor TFIID subunit 2
Sequence:
METGNVVNAQPELSGIIDGSKSYMYEQLWKLCAGPLCDIPKLGENVYYFPQGNIELVDASTREELNELQPICDLPSKLQCRVIAIHLKVENNSDETYAEITLMPDTTQVVIPTQSENQFRPLVNSFTKVLTASDTSAYGGFFVPKKHAIECLPPLPLPAQELLAKDLHGNQWRFRHSYRGTPQRHSLTTGWNEFTTSKKLVKGDVIVFVRGETGELRVGIRRARHQQGNIPSSIVSIDCMRHGVIASAKHALDNQCIFIVVYKPSIRSSQFIVSYDKFLDAMNNKFIVGSRFTMRFEGDDFSERRYFGTIIGVNDFSPHWKCSEWRSLEVQWDEFASFSRPNKVSPWEIEHLMSALNVPRSSLLKNKRLREVNEFGQEIGQLSVASPMNTSLRYRDTTEDAMNPSRLLMSYPVQPMPKLNYNNQMVTQIEENITTKAVTNFRLFGVSLAIPLVIKDPIEEIGSDISKLTEGKKFGQSQTLRSPIEIQSKQFGSTRTCTKVQMQGVTIGRAVDLSVLNGYDQLILELEKLFDLKGQLQTRNQWKIAFTDSDGYEMLVGDDPWPEFCKMVKKILIYSKEEVKNLKSSKSLSS
Protein: Heat shock 70 kDa protein, putative (Q57VR7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Heat shock protein 70, putative
- Heat shock protein 70
- Heat shock protein 83
- Heat shock protein, mitochondrial, putative
- Ankyrin repeat protein
- GrpE protein homolog
- Lipophosphoglycan biosynthetic protein, putative
- Nucleotide exchange factor Fes1 domain-containing protein
- Chaperone protein DNAJ, putative
Sequence:
MPAPAIGIDLGTTYSCVGVFKNDQVEIVANDQGNRTTPSYVSFSETERLVGDAAKNQVAMNPTNTVFDAKRIIGRKYDDPDLQADMKHWPFKVTVKEGKPVVEVEYQGERRTFFPEEISAMVLQKMKEIAESYLGEKVSKAVVTVPAYFNDSQRQATKDAGSIAGLEVLRIVNEPTAAAIAYGMDRSSEGAMKTVLIFDLGGGTFDVTLLNIDGGLFEVRATAGDTHLGGEDFDSRLVDYFATEFRTRTGKDLRGNARAMRRLRTACERVKRTLSSSASTNIEIDALYEGFDFFSKITRARFEEMCRDQFERCLEPVRKVLKDAEVDASAVDDVVLVGGSTRIPRVQQLVQNFFNGKEPNRSINPDEAVAYGAAVQAHIVSGGKSKQTKDLLLVDVTPLSLGVETAGGVMSVLIPRNTSVPAQKSQTFSTNADNQRSVEIKVYEGERPLVSQCQCLGTFTLTDIPPAPRGKPRITVSFDVNVDGILVVTAVEETAGKTQAITISNDKGRLSREQIDKMVAEAEKFAEEDRANAEKIEARNSVENYTFSLRSTLSDPDVQQNISQEDQQKIQTVVNAVVNWLDENRDATKEEYDAKNKEIEQVAHPILSAYYVKRAMEQAPPAPPSGEGEGNAPVPDDVD
Protein: Protein S100-A7-like 2 (S100 calcium-binding protein A7-like 2) (Q5SY68)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNIPLGEKVMLDIVAMFRQYSGDDGRMDMPGLVNLMKENFPNFLSGCEKSDMDYLSNALEKKDDNKDKKVNYSEFLSLLGDITIDHHKIMHGVAPCSGGSQ
Protein: Bcl-2-binding component 3, isoforms 3/4 (JFY-1) (p53 up-regulated modulator of apoptosis) (Q96PG8)
Organism: Homo sapiens (Human)
Function: Does not affect cell growth.
Subcellular location: Note=Contrary to isoforms 1 and 2, isoform 3 does not localize to the mitochondria.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Induced myeloid leukemia cell differentiation protein Mcl-1
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-like protein 2
- Bcl-2-like protein 11
- BH3-interacting domain death agonist
- Cellular tumor antigen p53
- Apoptosis regulator BAX
- Bcl-2 homologous antagonist/killer
Sequence:
MKFGMGSAQACPCQVPRAASTTWVPCQICGPRERHGPRTPGGQLPGARRGPGPRRPAPLPARPPGALGSVLRPLRARPGCRPRRPHPAARCLPLRPHRPTRRHRRPGGFPLAWGSPQPAPRPAPGRSSALALAGGAAPGVARAQRPGGSGGRSHPGGPGSPRGGGTVGPGDRGPAAADGGRPQRTVRAAETRGAAAAPPLTLEGPVQSHHGTPALTQGPQSPRDGAQLGACTRPVDVRDSGGRPLPPPDTLASAGDFLCTM
Protein: Cannabinoid receptor 1 (V5KA96)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}. Presynapse {ECO:0000256|ARBA:ARBA00034106}.
Interaction partners:
Sequence:
MKSILDGLADTTFRTITTDLLGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL
Protein: Actin (Q9U1E8)
Organism: Leishmania major
Interaction partners:
- ADF/Cofilin
- C2 domain-containing protein
- Tubulin alpha chain
- Profilin
- Helicase-like protein
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Actin-like protein 4
- Arp2/3 complex 41 kDa subunit
Sequence:
MADNEQSSIVCDNGSGMVKAGFSGDDAPRHVFPSIVGRPKNMQAMMGSANKTVYVGDEAQSKRGVLSLKYPIEHGIVTNWDDMEKIWHHTFYNELRVNPEQHNVLLTEAPMNPKQNREKMTQIMFETFNVPSLYIGIQAVLSLYSSGRTTGIVLDAGDGVTHTVPIYEGYSLPHAVRRVDMAGRDLTEYLMKIMMETGTTFTTTAEKEIVRNVKEQLCYVALDFEEEMTNSAKSANEEAFELPDGNVMMVGNQRFRCPEVLFKPSLIGLDEAPGFPEMVYQSINKCDIDVRRELYGNIVLSGGSTMFLNLPERLAKEISNLAPSSIKPKVVAPPERKYSVWIGGSILSSLTTFQTMWVKKSEYDESGPSIVHNKCF
Protein: Rac family small GTPase 3 (M0R5T4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- TIAM Rac1 associated GEF 1
- Proto-oncogene vav
- Plexin-A1
- Nck-associated protein 1
- Rho, GDP dissociation inhibitor
- Serine/threonine-protein kinase PAK 1
- Intersectin 2
- Cytoplasmic FMR1-interacting protein
- Rho GDP-dissociation inhibitor 1
- Intersectin-1
Sequence:
ARAHLMLPGLCPVAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTVGGKRADSRDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
Protein: Isochorismatase domain-containing protein 2B (Q9DCC7)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the nucleus in the presence of CDKN2A. {ECO:0000250}.
Interaction partners:
Sequence:
MGAAKASLGRIFPESSILFLCDMQEKLRDRILYFPQIVSKAARMLKVAQMLEIPVLLTEHYPQGLGPTVPELGAQGLRTMSKTSFSMVPPLQQELDKLPQLQSVLLCGIETQGCILHTALDLLDRGLQVHVAVDACSSQSEMNRLVALARMQQSGVFLSTSEVLILQLVKDAAHPQFKEIQKILKEPVTDIGLLGFFQGKKNSLLPNSRT
Protein: Hydroxymethylglutaryl-CoA lyase, mitochondrial (HL) (HMG-CoA lyase) (EC 4.1.3.4) (3-hydroxy-3-methylglutarate-CoA lyase) (P35914)
Organism: Homo sapiens (Human)
Function: Mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis. Terminal step in leucine catabolism. Ketone bodies (beta-hydroxybutyrate, acetoacetate and acetone) are essential as an alternative source of energy to glucose, as lipid precursors and as regulators of metabolism.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P38060}. Peroxisome {ECO:0000250|UniProtKB:P38060}. Note=Unprocessed form is peroxisomal. {ECO:0000250|UniProtKB:P38060}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Methylglutaconyl-CoA hydratase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 2, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKL
Protein: Glutathione S-transferase T3 (AtGSTT3) (EC 2.5.1.18) (GST class-theta member 3) (Glutathione S-transferase 10C) (Q9FHE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Nucleus {ECO:0000269|PubMed:19174456}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Subtilisin-like protease SBT4.9
- Subtilisin-like protease SBT4.4
- Putative defensin-like protein 3
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Probable serine/threonine-protein kinase PBL7
- Glutathione S-transferase DHAR2
- Glutathione S-transferase 3, mitochondrial
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MKLKVYADRMSQPSRAVLIFCKVNEIQFDEILIYLANRQQLSPEFKDINPMGKVPAIVDGKLKLSESHAILIYLSSAYPSVVDHWYPTDLSKRARIHSVLDWHHTNLRPGAAGYVLNSVLGPALGLPLNPKAAAEAEQLLTKSLTTLDTFWLKGNAMFLLGSNQPSIADLSLVCELTQLQVLDDKDRLRLLSPHKNVEQWIENTRKATMPHFDEVHEVLFRAKDRCQKQREMATASKPGPQSKIIQFSTIGEKSDDPNLVQNTTDRRKHRRKWSRAEDAILISAWLNTSKDPIVDNEHKACAFWKRIGAYFNNSASLANLPKREPSHCKQRWSKLNDKVCKFVGCYDQALNQRSSGQSEDDVFQVAYQVYTNNYKSNFTLEHAWRELRHSKKWCSLYPFENSKGGGSSKRTKLNNGDRVYSSSSNPESVPIALDEEEQVMDLPLGVKSSKQKEKKVATIITIEEREADSGSRLENLWVLDEEEQVMDRPLGVKSLEQKENKVAPKPTIEEREAADSRSRLENLWALKEKEEREADSRSRLENLWALKEKDIEEQKKLTRMEVLKSLLGRTTDQLSEKEDILKNKLIDEML
Protein: Thioredoxin domain-containing protein 17 (14 kDa thioredoxin-related protein) (TRP14) (Protein 42-9-9) (Thioredoxin-like protein 5) (Q9BRA2)
Organism: Homo sapiens (Human)
Function: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14607844}.
Interaction partners:
- Thioredoxin
- Mitochondrial import inner membrane translocase subunit Tim8 B
- Short transient receptor potential channel 7
- Thioredoxin-like protein 1
- Large ribosomal subunit protein mL51
Sequence:
MARYEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFRKNLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSED
Protein: Uncharacterized protein At2g39795, mitochondrial (Q8W487)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Serine/arginine-rich splicing factor RS2Z32
- At3g48120
Sequence:
MALAWCVVRRSASKFASVYGGRVRSISAVANRASLARNPSSIRPFVSRALNYSTAIDRISSEQTLIRVIDSEINSALQSDNIDSDEEMTPGSFPFRIEDKPGNQNVTLTRDYNGEHIKVVVSMPSLVSDENDDDDDDDEGPSNESSIPLVVTVTKKSGLTLEFSCMAFPDEIAIDALSVKHPGDSLEDQLANEGPDFEDLDENLKKTFYKFLEIRGVKASTTNFLHEYMTRKVNREYFLWLKNVKEFMEQ
Protein: Alanine racemase, biosynthetic (EC 5.1.1.1) (Q9HUN4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis.
Interaction partners:
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- D-alanine--D-alanine ligase A
- D-alanine--D-alanine ligase B
- Alanine racemase, catabolic
- Glutamate racemase
- Glycolipid-binding domain-containing protein
- Glutamate-pyruvate aminotransferase AlaA
- D-amino acid dehydrogenase 1
- Glycine oxidase
- UDP-N-acetylmuramate--L-alanine ligase
Sequence:
MRPLVATVDLSAIRHNYALAKRCAPQRQAFAVVKANAYGHGAREVVTALHDDADGFAVACLEEAAEVRALHASARILLLEGCFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFACADERNHPLTEQQLESFLGLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAELGLKPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPEARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRYSH
Protein: Inner kinetochore subunit fta6 (Constitutive centromere-associated network protein fta6) (Sim4 complex subunit fta6) (Sim4-mal2-associated protein 6) (Q9UTP3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Inner kinetochore subunit cnl2
- Inner kinetochore subunit fta7
- Inner kinetochore subunit fta4
- Inner kinetochore subunit fta2
- Inner kinetochore subunit fta1
- Inner kinetochore subunit fta3
- Inner kinetochore subunit mis17
- Inner kinetochore subunit mal2
- Inner kinetochore subunit mis15
- Inner kinetochore subunit mis6
Sequence:
MEDKYILLSAVETFKSRLEELLMQSAKVQKQTMLRKELASSMNDMASTVQEALNKKKSS
Protein: Beadex, isoform B (RE72043p) (Q8IQX7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEYLYNASMHCEDEERVNFYNMDKFFVPHVQSIELEQQAILRQYVPQYAYQWPWGFAPSAYSYYQGFGSLNMMTMDITKTEPGLVGLSSNQQQQQQQQSQQSNAGMNSGGQNNGPNPNGNGNVVNVVNSGGAGGGNNGNGNVQSIAAAANNNNNNNNNGSQLCAGCGKHIQDRYLLRALDMLWHEDCLKCGCCDCRLGEVGSTLYTKGNLMLCKRDYLRLFGNTGYCAACSKVIPAFEMVMRARTNVYHLECFACQQCNHRFCVGDRFYLCENKILCEYDYEERLVFASMANHPMLKRHVSSLGQGSPTGAAGAQNTAGGLLGGGPGGGNVNGVGMVNGPRTPGDHNNNNNGPQTPTGGGSPFAAAAAAAAAAAHMKNQLGASS