wanglab/gogpt-training-data huggingface dataset:
Protein: Probable ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (P75476)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0A796}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Pyruvate kinase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Transketolase
- Putative 1-phosphofructokinase
- Enolase
- Mannitol-1-phosphate 5-dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglycerate kinase
Sequence:
MSPKTTKKIAILTSGGDAPGMNATLVYLTRYATSSEIEVFFVKNGYYGLYHDELVPAHQLDLSNSLFSAGTVIGSKRFVEFKELKVREQAAQNLKKRQIDYLVVIGGDGSYMGAKLLSELGVNCYCLPGTIDNDINSSEFTIGFLTALESIKVNVQAVYHTTKSHERVAIVEVMGRHCGDLAIFGALATNADFVVTPSNKMDLKQLESAVKKILQHQNHCVVIVSENIYGFDGYPSLTAIKQHFDANNMKCNLVSLGHTQRGFAPTSLELVQISLMAQHTINLIGQNKVNQVIGNKANVPVNYDFDQAFNMPPVDRSALIAVINKNII
Protein: DNA-repair protein, putative (Q38DK1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair helicase/translocase XPB-R
- TFIIH basal transcription factor complex helicase/translocase XPB subunit
- UV excision repair RAD23 protein, putative
- UV excision repair protein RAD23
- Small ubiquitin protein, putative
- DNA 5'-3' helicase
- DNA repair and transcription factor protein, putative
- DNA damage-binding protein 1
- Centrin, putative
- Centrin, putative
Sequence:
MGQQKKDAAQSVAAVAAQNVDSYLRGVTSRARVPSATGGRGTRRRLASQAEVAAAKIKEQPKSLDDFADADNGDDEWEEVMLPTSFTPSSSTKPEVKVKDEKNGIVETPEFGATGPNPGQGSVKAELVDLTDEENRHNRILASVTPMGGQQSSSPSSGQWRQRDPAYEQMLEQQQLLAAKRRSERTKRAVEEISTLLFALLRGRKIVQQARHPKLVRGLLRLHVVEDAASKTYPLLRAVLQAKGLYAKAMNPAVSTPSLAPCWVTANKDSVNNYTSASISALLRGIECVFVLDGGIEHAALSNWAAPIQPGYLFEQLRKYHYSIGSPGCRIVLPHSLYICAVFLSLAAVSNVSCRLVVAVERMRRGDMSEKSGSDGGSPPKEAMSLFGSGKKRKRGDDAGAKQNTPKRLPSSCFWLEVWCPQRQSYISVNPCGGCATLFAAPYTFSVGGDAIMDVTPRYSIKYSSAFTHRLGRCDRYRHIWKDLQWNDNREASEVIVDLFRRDVGKYTEAQMQREKKQLHSLTYAEEVPKTLTALQKHPLFILENGLSRYEGIYPKDSTTMVGSVKGHIVFKRSAVVSLRSRDGWLREGRTVSGEEEPYKVIPPPPSRPFSKSSALFGVWQTKPFAPEPLGEDGSIPKHGNTQWYILLDKPAPIGLVHMQQPNIIRVARRMNIDFGIVVTGYRRRRLNEARSSGWEVVTDGIIVKETNTGSLVKAYEEWKQLTEEQEAAKRKQRAYRWWMHFVQHRLAYLRIRQQYLEGATHGHLSSH
Protein: Guanine nucleotide exchange factor (Q95V18)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDPYHHIRHHYPPTSIAGTGVVVGSSTTINRPELHQKCNRGSHSSDTSSAYSGSDTMASNYASSLEAEEIDLSGLVESVVDSDEEDLAESMDSLTVRDAVRDCLEKDPAERSEEDVEVLLEFTQGLKAFTNITLAVRRALCSVMVFAVVDKAGTVVMSDGEELDSWSVLINGAVEIEHANGSREELQMGDSFGILPTMDKLYHRGVMRTKCDDCQFVCITQTDYYRIQHQGEENTRRHEDENGFVVMVTELRSIGGVGTDSAGSGGSATGASASLNMKRGHVVIRGTPERLLQQLVEENSMTDPTYVEDFLLTHRIFIQNPQEVTSKLLHWFDLEQVDAHKTQELRDRVTRVVLLWVNNHFTDFEADYEMMEFLEVFEALLERKKLLSQLRLLHIACAAKARMRSCTLTRSSRDEPLNFRIVGGYELRGVAIATGNAAVGIYISHVEPGSKAQDVGLKRGDQIHEVNGQSLDHVTSKRALEILTGTTHLSISVKSNLLGFKEIMQALEHGGGTAGSGSISAGSGSFKSVRSPRRICANDIAKLHGRSDSTTDELSSVSASNRAHMVRLSSVDMLLDQPDCAPPQTPPVSGSGNMASNFMQQLLQSVNNSSAKKSGGNSNSDQQDTKGGFMTLAPKRRLQKALAKMNLLNKQNHGSSLNDSSDTLLNDPKSKLSAVSSCSSSTQSSINGCTVSGGGRLYQSQSNPDLTSLNYDGGSDAGGNGGGRLQVNYLNAHIHRPSAASTLTTNSTQSHLLPDYPDHVLKVYKADQTCKYVLIYKETTAHEVAMLTLQEFGIHDPSSNFSLCEVSVGDGGMVKQRRLPDQLQNLAERISFAARYYLKLNDSTEPLVPDELALELVRESNVHFLHLNAYELAIQLTLQDFGTFRQIESTEYVDELFELRSRYGVPMLSKFAELVNREMFWVVSEICAEHNIVRRMKIVKQFIKIARHCKECRNFNSMFAIVSGLGHGAVSRLRQTWEKLPSKYQRLFNDLQDLMDPSRNMSKYRQLVSAELLAQHPIIPFYPIVKKDLTFIHLGNDTRVDGLINFEKLRMLAKEVRLLTHMCSSPYDLLSILELKGQSPSNALFSLNQMSASQSNAAAGTVIAANAGQATIKRRKKSTAAPNPKKMFEEAQMVRRVKAYLNSLKILSDEDLLHKFSLECEPAHGSTYSGSISHVNTSHRSGGGGSISGGAGGSSGGGGGGSSSLNAGDQLSIYSHTSSSSAPNSSLSLRKRHPSSPTLSTTSSTSSTSDHQRRQMHNNGPKFGTASPQAVKKMLSLSESSKIRPHQPFVPRHGSTMAGVIPPLHHMHAAHGFSTPSPGGVVTSPATSAVANVQCTPSPSPCSHRRLASGGNIIPSRAIHERSHSDTPAPPPPLPSVDLSLESSSVTTFRDLPLRKSVTSGSISSCDSGYVHQQQHYHLQYQQQQQQNSSQHEPSPPVYTAADCRLLQQISNNAVTRNLNSPCQSTNTPPSTPTPPPNQPTATIQLSAPPTAAAYMHARSQHQQLQQQQQSLAMPPPPPPRYNVPPLGSIYSHHQGTAGSRHLNHMHGKTTGPQERWFPDCRPTTKQQMQSGS
Protein: Isocitrate dehydrogenase [NADP] cytoplasmic (IDH) (IDH1) (EC 1.1.1.42) (Cytosolic NADP-isocitrate dehydrogenase) (IDPc) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (O75874)
Organism: Homo sapiens (Human)
Function: Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase. Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways. May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10521434}. Peroxisome {ECO:0000269|PubMed:10521434}.
Interaction partners:
- Cytoplasmic aconitate hydratase
- Aconitate hydratase, mitochondrial
- Isocitrate dehydrogenase subunit gamma, mitochondrial
- Citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
- Malate dehydrogenase, mitochondrial
Sequence:
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVSGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLGENLKIKLAQAKL
Protein: Deubiquitinase SseL (EC 3.4.22.-) (Deubiquitinating enzyme) (DUB) (Deubiquitinating protease) (Salmonella secreted effector L) (Q8ZNG2)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protease targets the host cell ubiquitin pathway by acting as a deubiquitinase in infected host cells. Specifically hydrolyzes mono- and polyubiquitin substrates in vitro with a preference for 'Lys-63'-linked ubiquitin chains, suggesting that it interferes with a signaling pathway rather than inhibiting proteasomal-dependent degradation of its targets. Does not possess desumoylating activity. Is required for the Salmonella-induced delayed cytotoxicity in macrophages and full virulence. Is not required for intracellular bacterial replication.
Subcellular location: Secreted. Host cytoplasm. Note=Secreted via type III secretion system 2 (SPI-2 T3SS), and delivered into the host cytoplasm. In phagocytic cells localizes to the Salmonella-containing vacuole (SCV). In epithelial cells localizes to the Salmonella-containing vacuole (SCV) and to the Salmonella-induced filaments (Sifs), which are tubular membrane extensions from the SCV that are formed at late stages of infection.
Interaction partners:
- Secreted effector protein SseJ
- Inner membrane protein
- Secreted effector protein PipB2
- Secreted effector protein SifA
- Secreted effector protein sopD2
- Secreted effector kinase SteC
- Secreted effector protein SptP
- E3 ubiquitin-protein ligase SspH2
- Secretion system effector
- Secretion system effector
Sequence:
MNICVNSLYRLSIPQFHSLYTEEVSDEALTLLFSAVENGDQNCIDLLCNLALRNDDLGHRVEKFLFDLFSGKRTGSSDIDKKINQACLVLHQIANNDITKDNTEWKKLHAPSRLLYMAGSATTDLSKKIGIAHKIMGDQFAQTDQEQVGVENLWCGARMLSSDELAAATQGLVQESPLLSVNYPIGLIHPTTKENILSTQLLEKIAQSGLSHNEVFLVNTGDHWLLCLFYKLAEKIKCLIFNTYYDLNENTKQEIIEAAKIAGISESDEVNFIEMNLQNNVPNGCGLFCYHTIQLLSNAGQNDPATTLREFAENFLTLSVEEQALFNTQTRRQIYEYSLQ
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8 (Gamma-9) (P63077)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This subunit may have a very specific role in the development and turnover of olfactory and vomeronasal neurons.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Protein kinase C epsilon type
- Apelin receptor
- 5-hydroxytryptamine receptor 7
- Melatonin receptor type 1A
- C-C chemokine receptor type 5
- Phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1
- C-X-C chemokine receptor type 4
Sequence:
MSNNMAKIAEARKTVEQLKLEVNIDRMKVSQAAAELLAFCETHAKDDPLVTPVPAAENPFRDKRLFCTLL
Protein: Heat shock factor A4e (A0A024DAJ6)
Organism: Triticum aestivum (Wheat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEMDMEGGSQPQPQGASLSPAPFLIKTYEMVEDPATSRVVSWGPGGASFVVWNPPDFSRDLLPKYFKHNNFSSFIRQLNTYGFRKIDPELWEFANDDFIRGHMHLLKNIHRRKPVHSHSPQNQVNGPLAESERREYEEEISRLKHENGLLVAELQRQAQQQCGLSWLMQSLEDRLTAMEQRQANVVASVRDTLQRRRGGVHPRQETMMLELEPTDHFSKKRRVPTIGFFVEEPAEEQRVPHLRAMGGETPGMVMVNAEPFEKMELALVSMEKLVRRAGDYASSSEDMYNAAAAAAPSTDDPAHADLQAAPVETGANLQPSSPELAESPGYAVQSPMLLFPEIHEDKRNTTAEVDMSSEASTTDASQDETTAEAEAETGVPHEPAVANDLFWERFLTDTPKPLAVEESHGPEDDVKTGLDCYWFGHRNNVDQITEQMGHLASAQKT
Protein: THO complex subunit 7 (Functional spliceosome-associated protein 24) (fSAP24) (Ngg1-interacting factor 3-like protein 1-binding protein 1) (NIF3L1-binding protein 1) (hTREX30) (Q6I9Y2)
Organism: Homo sapiens (Human)
Function: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12951069}. Nucleus {ECO:0000269|PubMed:12951069, ECO:0000269|PubMed:19059247}. Nucleus speckle {ECO:0000305}. Note=Interaction with THOC5 is required for nuclear localization. {ECO:0000269|PubMed:19059247}.
Interaction partners:
- THO complex subunit 5
- THO complex subunit 6
- THO complex subunit 2
- THO complex subunit 3
- THO complex subunit 1
- Spliceosome RNA helicase DDX39B
- THO complex subunit 4
- SAP domain-containing ribonucleoprotein
- Chromatin target of PRMT1 protein
- NIF3-like protein 1
Sequence:
MGAVTDDEVIRKRLLIDGDGAGDDRRINLLVKSFIKWCNSGSQEEGYSQYQRMLSTLSQCEFSMGKTLLVYDMNLREMENYEKIYKEIECSIAGAHEKIAECKKQILQAKRIRKNRQEYDALAKVIQHHPDRHETLKELEALGKELEHLSHIKESVEDKLELRRKQFHVLLSTIHELQQTLENDEKLSEVEEAQEASMETDPKP
Protein: Large ribosomal subunit protein bL21 (50S ribosomal protein L21) (P0AG48)
Organism: Escherichia coli (strain K12)
Function: This protein binds to 23S rRNA in the presence of protein L20.
Interaction partners:
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein bL20
- Elongation factor G
- Small ribosomal subunit protein bS20
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL15
Sequence:
MYAVFQSGGKQHRVSEGQTVRLEKLDIATGETVEFAEVLMIANGEEVKIGVPFVDGGVIKAEVVAHGRGEKVKIVKFRRRKHYRKQQGHRQWFTDVKITGISA
Protein: Ethylene-responsive transcription factor RAP2-13 (Ethylene-responsive transcription factor ERF058) (Protein RELATED TO APETALA2 13) (Q9LM15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine-type endopeptidase inhibitor
- VQ motif-containing protein
Sequence:
MTTSMDFYSNKTFQQSDPFGGELMEALLPFIKSPSNDSSAFAFSLPAPISYGSDLHSFSHHLSPKPVSMKQTGTSAAKPTKLYRGVRQRHWGKWVAEIRLPRNRTRLWLGTFDTAEEAALAYDKAAYKLRGDFARLNFPDLRHNDEYQPLQSSVDAKLEAICQNLAETTQKQVRSTKKSSSRKRSSTVAVKLPEEDYSSAGSSPLLTESYGSGGSSSPLSELTFGDTEEEIQPPWNENALEKYPSYEIDWDSILQCSSLVN
Protein: Orexin receptor type 2 (Ox-2-R) (Ox2-R) (Ox2R) (Hypocretin receptor type 2) (P58308)
Organism: Mus musculus (Mouse)
Function: Nonselective, high-affinity receptor for both orexin-A and orexin-B neuropeptides. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O43614}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43614}.
Interaction partners:
- Hypocretin neuropeptide precursor
- Orexin/Hypocretin receptor type 1
- Oxidation resistance protein 1
- Guanine nucleotide-binding protein G
Sequence:
MSSTKLEDSLSRRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVVIWIVSCIIMIPQAIVMECSSMLPGLANKTTLFTVCDEHWGGEVYPKMYHICFFLVTYMAPLCLMILAYLQIFRKLWCRQIPGTSSVVQRKWKQQQPVSQPRGSGQQSKARISAVAAEIKQIRARRKTARMLMVVLLVFAICYLPISILNVLKRVFGMFTHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCLGVHHRQGDRLARGRTSTESRKSLTTQISNFDNVSKLSEHVVLTSISTLPAANGAGPLQNWYLQQGVPSSLLSTWLEV
Protein: Cytochrome P450 monooxygenase iccC (EC 1.-.-.-) (Ilicicolin H biosynthesis cluster protein C) (A0A482NAF7)
Organism: Talaromyces variabilis (Penicillium variabile)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IccC catalyzes the ring expansion of the tetramate intermediate to the acyclic 2-pyridone intermediate that contains the trans bis-diene chain. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MITLQNLPWILLYTGFLAIFLSRLFSNGKQSRDEKANGCQPPARYPQWDPIMGLDLVYSQVSALKNNRYLEWLRDLHAKMPKTFSLNFFGQRWIYSIEPEILKAVYATNFRDFGVEPIRRHSKGSMPFADKGVNTTDGEDWEFSRLLIKPFFERNVYTDTDRIKVHADHFLSLIPADGETFDAQPLVQRWFLDLTTEFIFGESMGSLAHPERADIAWTMLDVLRGGRLRAQMHRFMWARDWTWWLKAVYKVHDYVNPYIRSTLKELAEREERIKQGLPVGPERTDLVWSMATHLRDEELLRSQLCLIIVPNNDTTSIFISNCLWHLARHPEVWKKLREEVFALGEETPLTFEILRNMKYLNGVLNETHRVIPNNVTQVRACVQDTVLPVGGGPDGKWPVQVRKGDIVSVTKTVMYRDPDYWGSDADEFRPERFDGLRGTWNFLPFGGGPRRCPAQMMSQTEAAYMLCRLARTYSRIEARDPEPYTAVMRIGPSNKTGVKIALYK
Protein: Regulatory protein zeste (Q8MLR4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKIAANWQNSNHNLLEGVDIKTEMTQYMNSPSMNMYKKRERTQNWNHQEKKYLLDLCRKDMRIIENKRLDAGLTAVKNKAWKIIHQKFSNQFGTDRTCNRLKEQWRRMKACTRNEILDYNNRLARFGAEVADRKKPSPFTFEVWDFMQEAKKACKSEALDGIDYSKIPLALEEGFEYREDYKFNPEDHDMDDSRTPPQELCDVDIKEEENNETFNETFNHHHLNQSDILGSGERLSVSPNHSISRNGIHEAESPATISTSNVLDSSGAYMAGGGDMSGFQANFNMNNISATLEALNALRSGQFPSAAAAAAAAIHQHQAQAQVAMHHQHNNNNNNNNNNEDDEDSMKPQSKRQRTSSGSMLGSEDQAPVLAPSVPASSDSQALERSGSSNGLTMPGTAVSTNANSSSSNNNNFELRMFMEMQSKEHMMRMKILEVQLQAAKHSRDLVEINKTLALQKLQLELASKRLPS
Protein: E3 ubiquitin-protein ligase pellino homolog 3 (Pellino-3) (EC 2.3.2.27) (Q8BXR6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1. Can activate AP1/JUN and ELK1. Not required for NF-kappa-B activation.
Interaction partners:
- Interleukin-1 receptor-associated kinase 1
- TNF receptor-associated factor 6
- Interleukin-1 receptor-associated kinase 4
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MVLEGNPDVGSPRTSDLQHPGSQGSCILSCPGEEALAGEEPIKYGELIVLGYNGCLASGDKGRRRSRLALSRRPHANGVKPDVMHHISTPLVSKALSNRGQHSISFTLSRSHSVIVEYTHDSDKDMFQIGRSTENMIDFVVTDTSPGGGATEGPSAQSTISRYACRILCDRRPPYTARIYAAGFDASSNIFLGERAAKWRTPDGLMDGLTTNGVLVMHPAGGFSEDSAPGVWREISVCGNVYTLRDSRSAQQRGKLVENESNVLQDGSLIDLCGATLLWRTPAGLLRAPTLKQLEAQRQEANAARPQCPVGLSTLAFPSPARGRTAPDKQQPWVYVRCGHVHGYHGWGCRRERGPQERECPLCRLVGPYVPLWLGQEAGLCLDPGPPSHAFAPCGHVCSEKTARYWAQTPLPHGTHAFHAACPFCGAWLTGELGCVRLIFQGPLD
Protein: Chromodomain helicase DNA binding protein 8 (G3V303)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVTQDPIEEALGLPSSLDSLDQMNQDGGGGDVGNSSASELVPPPEETAPTELSKESTAPAPESITLHDYTTQPASQEQPAQPVLQTSTPTSGLLQVSKSQEILSQGNPFMGVSATAVSSSSAGGQPPQSAPKIVILKAPPSSSVTGAHVA
Protein: RNA helicase (EC 3.6.4.13) (Q95QN2)
Organism: Caenorhabditis elegans
Interaction partners:
- Pre-mRNA-splicing factor 8 homolog
- Pre-mRNA-processing factor 6
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Tr-type G domain-containing protein
- Thioredoxin-like protein
- GYF domain-containing protein
- SNU homolog
- U4/U6 small nuclear ribonucleoprotein Prp31
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Probable small nuclear ribonucleoprotein Sm D2
Sequence:
MAAEPPSLEELLEKKKREEDELAKPKFLSKAERAALALKRREEEVAKLRETQKQAEEARKNWGRTEKTSDDRRDRGLDRGNDRDRDRERERDRDRRRDRRERSGSRDRRRRSRSRDRDGGRRRDRSRSRDRRDRNDDRKRDRNEDSDNEEDVSKMADAVKDRYLGKQKEKKKRGRRLHEKKFVFDWDAGEDTSQDYNKLYQSRHEIQFFGRGSVAGTDVNAQKKEKNSFYQEMMENRRTVDEKEQEMHRLEKELKKEKKVAHDDRHWRMKELSEMSDRDWRIFREDFNISIKGGRVPRPLRNWEEAGFPDEVYQAVKEIGYLEPTPIQRQAIPIGLQNRDVIGVAETGSGKTAAFLLPLLVWITSLPKMERQEHRDLGPYAIIMAPTRELAQQIEEETNKFGKLLGIKTVSVIGGASREDQGMKLRMGVEVVIATPGRLLDVLENRYLLLNQCTYVILDEADRMLDMGFEPDVQKVLEYMPDTNMKKDTDEFDNEEALMKGFSTREKYRQTVMFTATMSSAIERLARQYLRRPAVVHIGSAGKPTERVEQVVYMVPEDRKRKKLVEVLESQFQPPIIIFVNQKKGADMLSKGLTKLGFKPTVLHGGKGQDQREYALQALKEGTSDILVATDVAGRGIDVKDVSLVLNYDMAKSIEDYTHRIGRTGRAGKHGKAITFLTPDDTAVYFDLKQVLVESPVSSCPPELANHPDAQSKPGVFTSKKRQDETLFLK
Protein: ORF 6 (P88904)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MALKGPQTLEENIGSAAPTGPCGYLYAYLTHNFPIGEASLLGNGYPEAKVFSLPLLHGLTVESDFPLNVKAVHKKIDATTASVKLTSYHREAIVFHNTHLFQPIFQGKGLEKLCRESRELFGFSTFVEQQHKGTLWSPEACPQLPCANEIFMAVIVTEGFKERLYGGKLVPVPSQTTPVHIGEHQAFKIPLYDEDLFGPSRAQELCRFYNPDISRYLHDSIFTGIAQALRVKDVSTVIQASERQFVHDQYKIPKLVQAKDFPQCASRGTDGSTLMVIDSLVAELGMSYGLSFIEGPQDSCEVLNYDTWPIFENCETPDARLRALEVWHAEQALHIGAQLFAANSVLYLTRVAKLPQKNQRGDANMYNSFYLQHGLGYLSEATVKENGASAFKGVPVSALDGSSYTLQHLAYASSFSPHLLARMCYYLQFLPHHKNTNSQSYNVVDYVGTAAPSQMCDLCQGQCPAVCINTLFYRMKDRFPPVLSNVKRDPYVITGTAGTYNDLEILGNFATFREREEEGNPVEDAPKYTYWQLCQNITEKLASMGISEGGDALRTLIVDIPSFVKVFKGIDSTVEAELLKFINCMIKNNYNFRENIKSVHHILQFACNVYWQAPCPVFLTLYYKSLLTVIQDICLTSCMMYEQDNPAVGIVPSEWLKMHFQTMWTNFKGACFDKGAITGGELKIVHQSMFCDLFDTDAAIGGMFAPARMQVRIARAMLMVPKTIKIKNRIIFSNSTGAESIQAGFMKPASQRDSYIVGGPYMKFLNALHKTLFPSTKTSALYLWHKIGQTTKNPILPGVSGEHLTELCNYVKASSQAFEEINVLDLVPDTLTSYAKIKLNSSILRACGQTQFYATTLSCLSPVTQLVPAEEYPHVLGPVGLSSPDEYRAKVAGRSVTIVQSTLKQAVSTNGRLRPIITVPLVVNKYTGSNGNTNVFHCANLGYFSGRGVDRNLRPESVPFKKNNVSSMLRKRHVIMTPLVDRLVKRIVGINSGEFEAEAVKRSVQNVLEDRDNPNLPKTVVLELVKPPRWSSCASLTEEDVIYYLGPYAVLGDEVLSLLSTVGQAGVPWTAEGVASVIQDIIDDCELQFVGPEEPCLIQGQSVVEELFPSPGVPSLTVGKKRKIASLLSDLDL
Protein: 2,6-dihydroxypyridine 3-monooxygenase (2,6-DHPH) (EC 1.14.13.10) (Q93NG3)
Organism: Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans)
Function: Catalyzes the conversion of 2,6-dihydroxypyridine into 2,3,6-trihydroxypyridine in the nicotine degradation pathway.
Interaction partners:
Sequence:
MSPTTDRIAVVGGSISGLTAALMLRDAGVDVDVYERSPQPLSGFGTGIVVQPELVHYLLEQGVELDSISVPSSSMEYVDALTGERVGSVPADWRFTSYDSIYGGLYELFGPERYHTSKCLVGLSQDSETVQMRFSDGTKAEANWVIGADGGASVVRKRLLGIEPTYAGYVTWRGVLQPGEVADDVWNYFNDKFTYGLLDDGHLIAYPIPGRENAESPRLNFQWYWNVAEGPDLDELMTDVRGIRLPTSVHNNSLNPHNLRQFHSKGESLFKPFRDLVLNASSPFVTVVADATVDRMVHGRVLLIGDAAVTPRPHAAAGGAKACDDARTLAEVFTKNHDLRGSLQSWETRQLQQGHAYLNKVKKMASRLQHGGSFEPGNPAFAFGLPKVDEPSVVTNS
Protein: Protein BOLA4, chloroplastic/mitochondrial (Q9LF68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act either alone or in interaction with glutaredoxin as a redox-regulated transcriptional regulator, or as a factor regulating Fe-S cluster biogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24203231}. Mitochondrion {ECO:0000269|PubMed:24203231}.
Interaction partners:
- Protein BOLA2
- Bifunctional monothiol glutaredoxin-S16, chloroplastic
- Monothiol glutaredoxin-S14, chloroplastic
- Monothiol glutaredoxin-S15, mitochondrial
- Monothiol glutaredoxin-S17
- Anamorsin homolog
- SufE-like protein 1, chloroplastic/mitochondrial
- Lipoyl synthase, chloroplastic
- Lipoyl synthase, mitochondrial
- NifU-like protein 4, mitochondrial
Sequence:
MAQTLMATTRPYVLLSSTRASLYRLFQSSKRPFASFSAPLVRFTNSRCVSAVLSRKETAPSSIYGNRVSRVSGFGALDIRSLNFSTKSSQINDAGSIDQTLMQSMELKIKEQLNAESVTVTDMSGDGRHVCINVVSSAFEGQSAVNRQRMVYKAIWEELQNVVHAVDQMTTKTPSEV
Protein: Sad1 and UNC84 domain containing 1 (A0A8I6A5M4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHRLEPVFDSPRMSRRSLRLITTTAAYSSGDGQTVDTHISTSRATPAKGRETRTVKQRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAVHGPTSRVYSRDRTLRPRDLLVRALRRTRAAGWSVAEAMWSVLWLAVTAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGFSLWGQGNFFSLLPMLNWTAMQPAQRVDNPKDMHRPGPLSPSPPLKVDPMASQWPQESDMGQKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMVGQHLQEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLRSSCEQADARIQETVQLMFSEDQPGGSLEWLLQKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAMSQAGISGITEAQAHIIVNNALRLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPRDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ