wanglab/gogpt-training-data huggingface dataset:
Protein: Neuronal acetylcholine receptor subunit beta-3 (Q8BMN3)
Organism: Mus musculus (Mouse)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:O70174}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O70174}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-6
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit alpha-4
- Acetylcholine receptor subunit gamma
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit delta
- Neuronal acetylcholine receptor subunit alpha-9
Sequence:
MTGFLRVFLALSATLSGSWVTLTATAGLSSVAEHEDALLRHLFQGYQKCVRPVLNSSDIIKVYFGLKISQLVDVDEKNQLMTTNVWLKQEWTDQKLRWNPEDYGGINSIKVPSESLWLPDIVLFENADGRFEGSLMTKAIVKSSGTVSWTPPASYKSSCTMDVTFFPFDKQNCSMKFGSWTYDGTMVDLILINENVDRKDFFDNGEWEILNAKGMKGNRREGFYSYPFVTYSFVLRRLPLFYTLFLIIPCLGLSFLTVLVFYLPSDEGEKLSLSTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLLFIMIFVTLSIIVTVFVINVHHRSSSTYHPMAPWVKRLFLEKLPRWLCMKDPRDRFSFPDGTESKGTVRGKFPGKKKQTPTSDGERVLVAFLEKASESIRYISRHVKKEHFISQVVQDWKFVAQVLDRIFLWLFLTASVLGSVLIFIPALKMWIHRFH
Protein: proton-translocating NAD(P)(+) transhydrogenase (EC 7.1.1.1) (A0A8I6ALS9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAHLLKTVVTGCLCPSVSNLGSCKVLPGKKDFLRTFRTHQALWCKSPAKPGIPYKQLTVGVPKEIFQNEKRVALSPAGVQALVKQGFNVVVESGAGEASKFPDDLYRAAGAQIQGTKEVLASDLVVKVRAPMVNPTLGAHEADFLKPSGTLISFIYPAQNPDLLNKLSERKTTVLAMDQVPRVTIAQGYDALSSMANISGYKAVVLAANHFGRFFTGQITAAGKVPPAKILIVGGGVAGLASAGAAKSMGAVVRGFDTRAAALEQFKSLGAEPLEVDLKESGEGQGGYAKEMSKEFIEAEMKLFAQQCKEVDILISTALIPGGFLVTQRMLDMFKRPTDPPEYNYLYLLPGGTFVGGYLAALYGGYNIEEIMYLGSGLCCVGALGGLSTQGTARLGNALGMIGVAGGLAATLGGLKPDPQLLAQMSGAMAMGGTIGLAIAKRIQISDLPQLVAAFHSLVGLAAVLTCMAEYIVEYPHFAMDATSNFTKIVAYIGTYIGGVTFSGSLVAYGKLQGILKSAPLLLPGRHALNAGLLAASVGGIIPFMADPSFTTGIMCLGSVSALSTLMGVTLTAAIGGADMPVVITVLNSYSGWALCAEGFLLNNNLLTIVGALIGSSGAILSYIMCVAMNRSLANVILGGYGTTSTAGGKPMEISGTHTEINLDNAVEMIREANSIVITPGYGLCAAKAQYPIADLVKMLTEQGKKVRFGIHPVAGRMPGQLNVLLAEAGVPYDIVLEMDEINSDFPDTDLVLVIGANDTVNSAAQEDPNSIIAGMPVLEVWKSKQVIVMKRSLGVGYAAVDNPIFYKPNTAMLLGDAKKTCDALQAKVRESYQK
Protein: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (BPG-dependent PGAM) (PGAM) (Phosphoglyceromutase) (dPGM) (EC 5.4.2.11) (P62707)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
Interaction partners:
- Phosphoglycerate kinase
- Enolase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Probable phosphoglycerate mutase GpmB
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase class 2
- Fructose-bisphosphate aldolase class 1
- Glucose-6-phosphate 1-dehydrogenase
- Transketolase 1
Sequence:
MAVTKLVLVRHGESQWNKENRFTGWYDVDLSEKGVSEAKAAGKLLKEEGYSFDFAYTSVLKRAIHTLWNVLDELDQAWLPVEKSWKLNERHYGALQGLNKAETAEKYGDEQVKQWRRGFAVTPPELTKDDERYPGHDPRYAKLSEKELPLTESLALTIDRVIPYWNETILPRMKSGERVIIAAHGNSLRALVKYLDNMSEEEILELNIPTGVPLVYEFDENFKPLKRYYLGNADEIAAKAAAVANQGKAK
Protein: Collagen adhesin (Q53654)
Organism: Staphylococcus aureus
Function: Collagen-binding adhesin that mediates bacterial adherence to collagenous tissues such as cartilage. Participates in the infectious process by acting as a virulence factor in many different animal models of staphylococcal infections including arthritis, endocarditis and keratitis. Inhibits the activation of the classical complement pathway by interacting with host C1q and interfering with the association between host C1r with C1q.
Subcellular location: Secreted, cell wall {ECO:0000305}; Peptidoglycan-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MNKNVLKFMVFIMLLNIITPLFNKNEAFAARDISSTNVTDLTVSPSKIEDGGKTTVKMTFDDKNGKIQNGDMIKVAWPTSGTVKIEGYSKTVPLTVKGEQVGQAVITPDGATITFNDKVEKLSDVSGFAEFEVQGRNLTQTNTSDDKVATITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHNINANAGIEGTVKGELKVLKQDKDTKAPIANVKFKLSKKDGSVVKDNQKEIEIITDANGIANIKALPSGDYILKEIEAPRPYTFDKDKEYPFTMKDTDNQGYFTTIENAKAIEKTKDVSAQKVWEGTQKVKPTIYFKLYKQDDNQNTTPVDKAEIKKLEDGTTKVTWSNLPENDKNGKAIKYLVKEVNAQGEDTTPEGYTKKENGLVVTNTEKPIETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLADGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVDELTKVNGYTTHVDNNDMGNLIVTNKYTPKKPNKPIYPEKPKDKTPPTKPDHSNKVKPTPPDKPSKVDKDDQPKDNKTKPENPLKELPKTGMKIITSWITWVFIGILGLYLILRKRFNS
Protein: Glutathione S-transferase (EC 2.5.1.18) (A0A3B3IRM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLNLKDFISRFE
Protein: Cyclin E variant ex7del (Cyclin E1) (C9J2U0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKLLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Q9UT41)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase
- GPI transamidase component gaa1
- GPI transamidase component PIG-T homolog
- Endoplasmic reticulum vesicle protein 25
- GPI transamidase component GAB1 homolog
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Geranylgeranyl pyrophosphate synthase
Sequence:
MKDDKGRSDTVNGYYISNSKLSSGFYKRNNANTASNDEKPNLEQNDIPSVTSSGSSTPSSISIEKEIKISKGNVIVKAIRSWSLYVAIIAILLLLVILHSFQGRPQDNGCGKSYVWPSYVRFVDFDERYTRFANKYSLYLYREKSVEESDEPSGIPILFIPGNAGSYKQVRAFAAQAAHVYANAYAEDADGTLNAGKLVPDFFVVDFNEDFSAFHGQTLLDQAEYVNDAIPYILSLYRQNRKISSEYDNEAFPPPTSVILLGHSMGGIVAQATFTMKNYVDGSVNTLITLATPHAMAPLPFDRHLVEFYESIKNFWSQSFLLSPEENSLDDVLLVSIAGGGLDTHVVPEYSSISTFVPPSNGLMVFTSGIPSVWAEIDHQAMAWCENFRRVLIRGIFAIMDARTSKCTVSLNLRKELLSRAYIQGSSFQNDITQISKPIAQYKALDLDLTYVYSEMPGQLLFLNQLGVSYIRHHIFPIPKPTSSIDRFELLTDQPIDLSSSNIKVLACRLDPKIDNTISALLENGNNKVINANCHLLRELVTLLPASTAYTSSPYGGDSFYNYVLPKEKMDDYHFILVSDDSKAPASGFVVGGFSNVSLDPKTIKGSQIELFKSGRKFQFDTKGSISKRFRFPGIQSSIMAYTISVTYELYPGAVPQKEFTPMLKQSIESPFETKYHVNMSNTELSVHGISPFMEFFGKESEKSLTLEFFLNPAIYKSVYVSIQPSYYRSAGRLLMRYRTLLASFPVVVISLAAYNQFRYFHYGSAYLSMSAALEVMIRKGLIKLLFLVSILSIAFSYLISRVELIVADGADPVASWKIFAMMVPKSFWKQNHLLFGLQTAQFWFLAPLLTLMFVGLVITASVIILCVMHLLAFIYGIYLRYKGLTFTGVCQAVKFSFQCLRTRNTRKLDHGEFKKLSSFLSQRNMYYANPSLCYVYGKKHMQARIIGIMLLLLMAMTVVPFQLVYGVALCTQTVTTAKALHLARFCTKSSHYRKKLWDFYNFSCTITILMLLLAPLDFPVLIVWARNLSMHWSIPFPTHHNFFSIIPFILLTEILRTGKMLPRLNDVEYYINNVFLFLLSFYSLIYGAEKPYLIHNVVGLYFFWLLFLYAKNGFFVQNISKWPIIPRMKYFIKHKFLRSIS
Protein: Ribonuclease VapC10 (RNase VapC10) (EC 3.1.-.-) (Toxin VapC10) (P9WFA7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. The cognate antitoxin is VapB10 (By similarity).
Interaction partners:
- Putative antitoxin VapB10
- Probable endoribonuclease MazF7
- Ribonuclease VapC31
- Ribonuclease VapC12
Sequence:
MILVDSDVLIAHLRGVVAARDWLVSARKDGPLAISVVSTAELIGGMRTAERREVWRLLASFRVQPATEVIARRAGDMMRRYRRSHNRIGLGDYLIAATADVQDLQLATLNVWHFPMFEQLKPPFAVPGHRPRA
Protein: Valine--tRNA ligase (EC 6.1.1.9) (Protein G7a) (Valyl-tRNA synthetase) (ValRS) (Q9Z1Q9)
Organism: Mus musculus (Mouse)
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Elongation factor 1-gamma
- Lysine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Elongation factor 1-delta
- Leucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Elongation factor 1-beta
- Isoleucine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, mitochondrial
Sequence:
MSILYVSPHPDAFPSLRALIAARYGEAGDGPGWGGPHPRICLQPPPSSRTPFPPPRLPALEQGPGGLWVWGAPAVAQLLWPAGLGGPGGSRAAVLVQQWVSYADTELIPAACGATLPALGLRGPGQDPQAALGALGKALNPLEDWLRLHTYLAGDAPTLADLAAVTALLLPFRYVLDPSARRIWGNVTRWFNTCVRQPEFRAVLGEVALYSGARSVTQQPGSEVIAPQKTPAQLKKEAKKREKLEKFQQKQKTQQQPPHGEKKPKPEKKEKRDPGVITYDLPTPPGEKKDVSGAMPDSYSPQYVEAAWYPWWERQGFFKPEYGRPSVSAPNPRGVFMMCIPPPNVTGSLHLGHALTNAIQDSLTRWHRMRGETTLWNPGCDHAGIATQVVVEKKLWKERGLNRHQLGREAFLEEVWKWKAEKGDRIYHQLKKLGSSLDWDRACFTMDPKLSATVTEAFVRLHEEGVIYRSTRLVNWSCTLNSAISDIEVDKKELTGRTLLPVPGYKEKVEFGVLVSFAYKVQGSDSDEEVVVATTRIETMLGDVAVAVHPKDPRYQHLKGKCVVHPFLSRSLPIVFDDFVDMEFGTGAVKITPAHDQNDYEVGQRHRLEAISIMDSKGALINVPPPFLGLPRFEARKAVLAALKERGLFRGVKDNPMVVPLCNRSKDVVEPLLRPQWYVRCGEMAQAASAAVTRGDLRILPEAHQRTWHSWMDNIRDWCISRQLWWGHRIPAYFITVHDPAVPPGEDPDGRYWVSGRTEAEAREKAAREFGVSPDKISLQQDEDVLDTWFSSGLFPFSIFGWPNQSEDLSVFYPGTLLETGHDILFFWVARMVMLGLKLTGKLPFREVYLHAIVRDAHGRKMSKSLGNVIDPLDVIHGVSLQGLYDQLLNSNLDPSEVEKAKEGQKADFPAGIPECGTDALRFGLCAYTSQGRDINLDVNRILGYRHFCNKLWNATKFALRGLGKGFVPSATSKPEGHESLVDRWIRSRLTEAVRLSNEGFQAYDFPAITTAQYSFWLYELCDVYLECLKPVLNGVDQVAAECARQTLYTCLDVGLRLLSPFMPFVTEELFQRLPRRTPKAPASLCVTPYPEPSECSWKDPEAEAALELALSITRAVRSLRADYNLTRTRPDCFLEVADEATGALASAVSGYVQALASAGVVAVLALGAPAPQGCAVAVASDRCSIHLQLQGLVDPARELGKLQAKRSEAQRQAQRLQERRAASSYSAKVPLEVQEADEAKLQQTEAELRKVDEAIALFQKML
Protein: Lactoperoxidase (LPO) (WBLP) (EC 1.11.1.7) (A5JUY8)
Organism: Bubalus bubalis (Domestic water buffalo)
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism. Shows antibacterial properties against E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis and S.dysenteriae. May protect the udder from infection and may promote growth in newborns (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:12071645, ECO:0000269|PubMed:19339248, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}.
Interaction partners:
Sequence:
MWVCLQLPVFLASVTLFEVAASDTIAQAASTTTISDAVSKVKIQVNKAFLDSRTRLKTTLSSEAPTTQQLSEYFKHAKGQTRTAIRNGQVWEESFKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLALPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSNEHSKTQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLAREQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYLPFNNKKPSPCEFINTTARVPCFLAGDFRASEQILLATAHTLLLREHNRLARELKKLNPHWNGEKLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLTRGLLAKKSKLMNQDKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQTVLKNKILAKKLMDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKFSFSRLICDNTHITKVPLHAFQANNYPHDFVDCSTVDKLDLSPWASREN
Protein: Thioredoxin reductase 1, mitochondrial (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase 1) (NTR1) (NADPH-dependent thioredoxin reductase B) (AtNTRB) (Q39243)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NADPH-dependent thioredoxin-disulfide reductase that reduces thioredoxins O1, O2 and F3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11717467, ECO:0000269|PubMed:15642341}. Mitochondrion {ECO:0000269|PubMed:15642341, ECO:0000305|PubMed:25732537}.
Interaction partners:
- NADPH-dependent thioredoxin reductase 3
- Methionine gamma-lyase
- Cysteine desulfurase 1, chloroplastic
- Thioredoxin reductase 2
- Thioredoxin O1, mitochondrial
- Thioredoxin O2, mitochondrial
- Selenoprotein O
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- p-hydroxybenzoic acid efflux pump subunit
- Glutathione reductase, cytosolic
Sequence:
MNCVSRLKCLISKARSFARLGGESTLSQPPSLASAAFSSSAVMNGLETHNTRLCIVGSGPAAHTAAIYAARAELKPLLFEGWMANDIAPGGQLTTTTDVENFPGFPEGILGVELTDKFRKQSERFGTTIFTETVTKVDFSSKPFKLFTDSKAILADAVILATGAVAKRLSFVGSGEASGGFWNRGISACAVCDGAAPIFRNKPLAVIGGGDSAMEEANFLTKYGSKVYIIHRRDAFRASKIMQQRALSNPKIDVIWNSSVVEAYGDGERDVLGGLKVKNVVTGDVSDLKVSGLFFAIGHEPATKFLDGGVELDSDGYVVTKPGTTQTSVPGVFAAGDVQDKKYRQAITAAGTGCMAALDAEHYLQEIGSQQGKSD
Protein: Interleukin-17B (IL-17B) (Cytokine Zcyto7) (Interleukin-20) (IL-20) (Neuronal interleukin-17-related factor) (Q9UHF5)
Organism: Homo sapiens (Human)
Function: Stimulates the release of tumor necrosis factor alpha and IL-1-beta from the monocytic cell line THP-1.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-17 receptor B
- Interleukin-25
- Interleukin-17 receptor A
- Interleukin-17 receptor E
- Interleukin-17 receptor D
- Interleukin-17 receptor C
Sequence:
MDWPHNLLFLLTISIFLGLGQPRSPKSKRKGQGRPGPLAPGPHQVPLDLVSRMKPYARMEEYERNIEEMVAQLRNSSELAQRKCEVNLQLWMSNKRSLSPWGYSINHDPSRIPVDLPEARCLCLGCVNPFTMQEDRSMVSVPVFSQVPVRRRLCPPPPRTGPCRQRAVMETIAVGCTCIF
Protein: 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha) (Q9LPL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). Required during sugar starvation.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, chloroplastic
Sequence:
MAIWFARSKTLVSSLRHNLNLSTILIKRDYSHRPIFYTTSQLSSTAYLSPFGSLRHESTAVETQADHLVQQIDEVDAQELDFPGGKVGYTSEMKFIPESSSRRIPCYRVLDEDGRIIPDSDFIPVSEKLAVRMYEQMATLQVMDHIFYEAQRQGRISFYLTSVGEEAINIASAAALSPDDVVLPQYREPGVLLWRGFTLEEFANQCFGNKADYGKGRQMPIHYGSNRLNYFTISSPIATQLPQAAGVGYSLKMDKKNACTVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVRSAREMAVTEQRPVLIEMMTYRVGHHSTSDDSTKYRAADEIQYWKMSRNPVNRFRKWVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEQELGLKELVKKQPQDYPPGFHV
Protein: Acetyltransferase PA2578 (EC 2.3.1.-) (GCN5-related N-acetyltransferase) (GNAT) (Q9I0Q8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers the antibiotic chloramphenicol.
Interaction partners:
- Probable transcriptional regulator
- EamA domain-containing protein
- N-acetyltransferase domain-containing protein
- N-acetyltransferase domain-containing protein
- N-acetyltransferase domain-containing protein
- HAD family hydrolase
- Acetyltransferase PA3944
Sequence:
MPTPGTGSVPELQLVPFQLGHFPILQRWFATEKELVQWAGPALRHPLSLEQMHEDLAESRRRPPLRLLWSACRDDQVIGHCQLLFDRRNGVVRLARIVLAPSARGQGLGLPMLEALLAEAFADADIERVELNVYDWNAAARHLYRRAGFREEGLRRSATRVGRERWNVVLMGLLRQEWAAGGAGND
Protein: Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (BRL-BP) (P12843)
Organism: Rattus norvegicus (Rat)
Function: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000269|PubMed:2426267, ECO:0000269|PubMed:2480123, ECO:0000269|PubMed:2538475}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-2
- Insulin-1
- Insulin-like growth factor 1 receptor
- Insulin-like growth factor-binding protein 4
- Receptor-type tyrosine-protein phosphatase beta
Sequence:
MLPRLGGPALPLLLPSLLLLLLLGAGGCGPGVRAEVLFRCPPCTPERLAACGPPPDAPCAELVREPGCGCCSVCARQEGEACGVYIPRCAQTLRCYPNPGSELPLKALVTGAGTCEKRRVGATPQQVADSEDDHSEGGLVENHVDGTMNMLGGSSAGRKPPKSGMKELAVFREKVNEQHRQMGKGAKHLSLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDDRGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKPIQGAPTIRGDPECHLFYNEQQENDGAHAQRVQ
Protein: ATP-dependent RNA helicase DHX33 (EC 3.6.4.13) (DEAH box protein 33) (Q9H6R0)
Organism: Homo sapiens (Human)
Function: Implicated in nucleolar organization, ribosome biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By similarity). Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment. In the cytoplasm, promotes elongation-competent 80S ribosome assembly at the late stage of mRNA translation initiation. Senses cytosolic dsRNA mediating NLRP3 inflammasome formation in macrophages and type I interferon production in myeloid dendritic cells. Required for NLRP3 activation induced by viral dsRNA and bacterial RNA. In dendritic cells, required for induction of type I interferon production induced by cytoplasmic dsRNA via the activation of MAPK and NF-kappa-B signaling pathways (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:26100019}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21930779}. Cytoplasm {ECO:0000269|PubMed:23871209, ECO:0000269|PubMed:26100019}. Nucleus {ECO:0000269|PubMed:23871209}. Inflammasome {ECO:0000269|PubMed:23871209}. Note=Predominantly in the nucleolus. During mitosis, localizes with the nucleolar organizing regions (PubMed:21930779). Upon dsRNA-binding, localizes in the inflammasome (PubMed:23871209). {ECO:0000269|PubMed:21930779, ECO:0000269|PubMed:23871209}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 3
- Mitochondrial antiviral-signaling protein
- 2-5A-dependent ribonuclease
- NACHT, LRR and PYD domains-containing protein 6
- Caspase-1
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 9
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 1
- Caspase recruitment domain-containing protein 8
Sequence:
MPEEAGFPPAKRFRPGSGPPSRAGSFPPGRQVVMLLTAGSGGRGGGGGRRQQPPLAQPSASPYPEAVELQRRSLPIFQARGQLLAQLRNLDNAVLIGETGSGKTTQIPQYLYEGGISRQGIIAVTQPRRVAAISLATRVSDEKRTELGKLVGYTVRFDDVTSEDTRIKFLTDGMLLREAISDSLLRKYSCVILDEAHERTIHTDVLFGVVKAAQKRRKELGKLPLKVIVMSATMDVDLFSQYFNGAPVLYLEGRQHPIQVFYTKQPQNDYLHAALVSVFQIHQEAPSSQDILVFLTGQEEIEAMSKTCRDIAKHLPDGCPAMLVLPLYASLPYAQQLRVFQGAPKGYRKVIISTNIAETSITITGIKYVVDTGMVKAKKYNPDSGLEVLAVQRVSKTQAWQRTGRAGREDSGICYRLYTEDEFEKFDKMTVPEIQRCNLASVMLQLLAMKVPNVLTFDFMSKPSPDHIQAAIAQLDLLGALEHKDDQLTLTPMGRKMAAFPLEPKFAKTILMSPKFHCTEEILTIVSLLSVDSVLHNPPSRREEVQGVRKKFISSEGDHMTLLNIYRTFKNLGGNKDWCKENFVNSKNMTLVAEVRAQLRDICLKMSMPIASSRGDVESVRRCLAHSLFMSTAELQPDGTYATTDTHQPVAIHPSSVLFHCKPACVVYTELLYTNKCYMRDLCVIDAQWLYEAAPEYFRRKLRTARN
Protein: DNA topoisomerase 3-beta (EC 5.6.2.1) (F4ISQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).
Interaction partners:
- AT5G19950 protein
- DNA topoisomerase 3-alpha
- Uncharacterized protein
- Crossover junction endonuclease MUS81
- Crossover junction endonuclease MUS81
- DNA repair protein RAD50
- DNA topoisomerase 1 beta
- DNA repair endonuclease UVH1
- ATP-dependent DNA helicase Q-like 1
- ATP-dependent DNA helicase Q-like 4B
Sequence:
MANLLRVLMVAEKPSIALSIASVLSHGQMSTRRGSTEVHEFDGMFRGFKAHYRVTSVIGHVFSVDFPEKYQNWATIDPQDLFDAPIIKKESNPKAHICRHLSNEARGCSYMVLWLDCDREGENICFEVIESTGFDMKDSKRKVYRARFSSVTEKDISKAMDNLVEPNRDEALAVDARQEIDLKVGVAFSRFQTSYFQGKYQNLDCRVISYGPCQTPTLGFCVQRYMHINTFKPEKFWALRPYIRKDGYELQLEWERRRLFDLEAATVFQKLVVEGRTAKVMDVSEKQEVKGRPAGLNTVNLLKVASSALGFGPQTAMHLAERLYTQGFISYPRTESTAYPSSFDFTDTLRAQVSNPVWGGYVQRLLSDGFHMPKSGTDAGDHPPITPMRAATEVMVGGDAWRLYQYVCQHFLGTVSPNCKYIRTKVELSIGGETFHCTGQRVTEKGFTAIMPWSAVDEKKLPSFLKGERIEVLRVELYEGNTAPPDYLTESELISLMEKHGIGTDASIAVHINNIGERNYVQVQSGRKMVPTALGITLIRGYQCIDPDLCLPDIRSFIEQQITLVAKGQADHSHVVQHVIQQFRRKFSYFVQQIEHMDALFEAQFSPLADSGRALSKCGKCLRYMKHITAVPPRLFCGTCEEVYYLPQKGTVKLYKELTCPLDNFELVIYSVPGPEGKSFPLCPYCYNSPPFEGIDTLFGASKTPNAPAKTKTGAGMPCSLCPHPTCQHSVRNQGVCACPECEGTLVLDPVSFPKWKLNCNLCSCIVLLPEGAHRITTTSNRCPECDSAIIEIDFNKKTTPLENGATLHQGCVLCDELLLSLVEVKHGRSFVRRGGRGRGRGRGRGRGGRRGSKSVDPKMSFRDF
Protein: cAMP-dependent protein kinase (EC 2.7.11.11) (Q9HFW0)
Organism: Cryptococcus neoformans var. neoformans
Interaction partners:
Sequence:
MFQKVSDKFHRKQQSSTSPGKTQQVPNSPSSVLAKANSQAQQAYSSQDHSPMEGIQSDSTHIQQPMATQKAPIVGPSTSTSLSTVPVQDGTLPLTPGAQGMLAGTTDGHRQVQSPVSRSSSAGEDKMREKARDAQEQAAQAQANLHRVTQQARVAAINAAATQAALETATQLPATARVPTSGTGAEPGQARRKTAGRYALSDFLIERTLGTGSFGRVHLVRSRHNGRFYAVKVLNKEKVIKMKQVEHTNSEREMLVRVRHPFLVNLWGTFQDVNNLYMVMDFVAGGELFSLLRKSQRFPNSVAKFYAAEVALALDYLHSLDIIYRDLKPENLLLGADGHVKVTDFGFAKYVPDITWTLCGTPDYLAPEVVQSKGYNKSVDWYALGVLIFEMLAGYPPFFTEDGNPMKLYEKIIAGKVRYPTYFDVLAKELLKNLLIGDLTKRYGNLRAGSSDIFAHGWFAEVDWDKLYRREIPAPYVPKIDGEGDASQFDRYQEADVSAYGKVGNGPYDHFFVEF