wanglab/gogpt-training-data huggingface dataset:
Protein: Hsp70/Hsp90 co-chaperone CNS1 (Cyclophilin seven suppressor 1) (STI1 stress-inducible protein homolog) (P33313)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Co-chaperone that binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein HGH1
- Peptidyl-prolyl cis-trans isomerase CYP7
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Peptidyl-prolyl cis-trans isomerase CPR6
- Heat shock protein SSA1
- Co-chaperone protein SBA1
- Hsp70 nucleotide exchange factor FES1
- Heat shock protein 104
- HSP70 co-chaperone SNL1
Sequence:
MSSVNANGGYTKPQKYVPGPGDPELPPQLSEFKDKTSDEILKEMNRMPFFMTKLDETDGAGGENVELEALKALAYEGEPHEIAENFKKQGNELYKAKRFKDARELYSKGLAVECEDKSINESLYANRAACELELKNYRRCIEDCSKALTINPKNVKCYYRTSKAFFQLNKLEEAKSAATFANQRIDPENKSILNMLSVIDRKEQELKAKEEKQQREAQERENKKIMLESAMTLRNITNIKTHSPVELLNEGKIRLEDPMDFESQLIYPALIMYPTQDEFDFVGEVSELTTVQELVDLVLEGPQERFKKEGKENFTPKKVLVFMETKAGGLIKAGKKLTFHDILKKESPDVPLFDNALKIYIVPKVESEGWISKWDKQKALERRSV
Protein: Histidine-rich Ca2+ binding protein (Q9QZV4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGFQGPWLHTCLLWATVAILLVPPVVTQELRGAGLGLGNWNNNAGIPGSSEDLSTEFGHHIHRGYQGEKDRGHREEGEDFSREYGHRVQDHRYPGREVGEENVSEEVFRGHVRQLHGHREHDNEDLGDSAENHLPRQRSHSHEDEDGIVSSEYHRHVPRHAHHGHGEEDDDDDGGEEEERVDVMEDSDDNEHQVHGHQSHSKERDELHHAHSHRHQGHSDDDDDDGVSTEHGHQAHRYQDHEEEDDGDSDEDSHTHRVQGREDENDDEDGDSGEYRHHTQDHQGHNEEQDDDDDDDDDDEDKEDSTEHRHQTQGHRKEEDEDESDEDDHHVSRHGRQGYEEEEDDDDDDGDDDSTEHVHQAHRHRDHEHKDDEDDSEEDYHHVPSHGRQSHQNEEEEDEAVSTEHWHQSPRHAHHDLGRESEEEVAVKYSHHVASHRPQGHNADREEDSLEEHMNEVPGHHHHRASRGDDEDISTEFGHKAPSHRLQDQDERARQGHREPVQGEIAHQPLQPTGPSSRESRKEGDHSSQEGDEDPEQRQAHSEEEEEKEGGHSLPMSQEDDEEEEKDEKESKVDRAAVSAPLSHHRKQGEEEEEEEEEEEEEILEENLLPFTIIPNPLAGREVAREGSSEEESREVTGQQDAQEYENYQPGSLCGYCSFCNRCTECESCHCDEENMGEHCDQCQHCQFCYLCPLVCDTLCTPGSYVDYFSSSLYQALADMLETPEP
Protein: G protein-coupled receptor kinase (EC 2.7.11.-) (A8K8M5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MELENIVANSLLLKARQGGYGKKSGRSKKWKEILTLPPVSQCSELRHSIEKDYSSLCDKQPIGRRLFRQFCDTKPTLKRHIEFLDAVAEYEVADDEDRSDCGLSILDRFFNDKLAAPLPEIPPDVVTECRLGLKEENPSKKAFEECTRVAHNYLRGEPFEEYQESSYFSQFLQWKWLERQPVTKNTFRHYRVLGKGGFGEVCACQVRATGKMYACKKLQKKRIKKRKGEAMALNEKRILEKVQSRFVVSLAYAYETKDALCLVLTIMNGGDLKFHIYNLGNPGFDEQRAVFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLATEIPEGQRVRGRVGTVGYMAPEVVNNEKYTFSPDWWGLGCLIYEMIQGHSPFKKYKEKVKWEEVDQRIKNDTEEYSEKFSEDAKSICRMLLTKNPSKRLGCRGEGAAGVKQHPVFKDINFRRLEANMLEPPFCPDPHAVYCKDVLDIEQFSAVKGIYLDTADEDFYARFATGCVSIPWQNEMIESGCFKDINKSESEEALPLDLDKNIHTPVSRPNRGFFYRLFRRGGCLTMVPSEKEVEPKQC
Protein: Fibroblast growth factor (FGF) (A8K1P5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST
Protein: Zinc finger CCCH domain-containing protein 13 (E9Q784)
Organism: Mus musculus (Mouse)
Function: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs at the 3'-UTR. Controls embryonic stem cells (ESCs) pluripotency via its role in m6A methylation. In the WMM complex, anchors component of the MACOM subcomplex in the nucleus. Also required for bridging WTAP to the RNA-binding component RBM15 (RBM15 or RBM15B).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q5T200}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}.
Interaction partners:
- E3 ubiquitin-protein ligase Hakai
- N
- N
- Protein virilizer homolog
- Putative RNA-binding protein 15B
- Pre-mRNA-splicing regulator WTAP
- RNA-binding protein 15
- RNA N
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 4
Sequence:
MSKIRRKVTVENTKTISESTSRRPSVFERLGPSTGSTTETQCRNWLKTGSCLYGNTCRFIHGPSPRGKGYSSNYRRSPERPTGDLRERMKNKRQDVDSESQKRNTEEPSSPVRKESSRGRHRDKEDIKIVKERTPESEEENVEWETNRDDSDNGDINYDYVHELSLEMKRQKIQRELMKLEQENMDKREEIIIQKEVSPEVVRSKLSPSPSLRKSSKSPKRKSSPKASSAGKKERKAAVVASPLLDQQRNSKGNQSKKKGPRTPSPPPPILEDIILGKKYKEKYKVKDRIEEKPRDGKDRGRDFEKQREKRDKPRSSSPGQHHSPLSSRHHSSSSQSGSSIQRHSPSPRRKRTPSPSYQRTLTPSLRRSASPYPTHCLSSPQRKQSPPRHRSPMREKGRHDHERTSQSHDRRHERREETRGKRDREKDTREERESEHDHRDDREPRDSRDRRDTRDRRELRDSRDMRDSREMRDYSRDAKESRDPRDSRSARDVHDYRDREARDAHARDVRDARDARDARDARDIRDVRDVRDVRDVRDVRDVRDVRDVRDVRDARDVRDVRDARDVRDVRDVRDGHRKEDVYQEEARSYGRNHLREESSRVELRNDSRNESRSEIRNDRMGRSRGRGPELPEKGSRGTRGSQMDSHSSGSNYHDSWETRSSYPERDRYPERDTRDPARDSSFERRHGERDRRDNRERDQRPSSPIRHQGRSEELERDERREERRIDRVDERRDDRVRDRDRDREREREREREREREREKERERELERERAREREREREKERERERERERDQRDRDHDREREREREREREKEREREREERERERERERERERERERERERERERERERERAREREKERERQREWEDKDKGRDDRREKREDIHVREDRIPRDSHEERKSKKRYRNEGSPSPRQSPKRRREHSPDSDTYHSGDDKNEKHRLLSQVVRPQESRSLSPSHLTEDRQGRWKEEDRKSERKESSRRYEEQELKEKLSCGDRQREQAESVDSSRVRAQDLLSHRQAEDRDRDGSDRAHDEKKKAKAPKKPVKKKKEEDVGVERGNLETHEDSQVFSPKKGQKKKNIEKKRKRSKGDSDVSDEEAAPQNKKKRGPRTPPLAIKEELADISTDKDGVLEDPLKKENTAFSDWSDEDVPDRTEGLEAEHTAATATPGSTPSPLSSLLPPPPPVAAASTAATALASSAVSATTSATSSSSAATSNTNGSEDSHRKCHRARGEKVEVSHVTLEDTPHRKLVDQKRSSSLGSNRSHRSHTSGRLRSPSNDSAHRSGDDQGSRKRVLHSGSRDREKTKSLEITGERKSRIDQLKRGEPSRSTSSDRQDSRSHSSRRSSPESDRQVHSRSGSFDSRDRLQERDRYEHDRERERDRRDPRQREWDREAEKEWPRTRDRDRLRERDRDRDRRRDLDRERERLISDPMERDRERERTFETSQLESGKRSEVKLESEHERDLEGSSRDSVALDKERMDRDLGSVQGFEDVSKAERTESLEGDDESKLDDAHSLGSGAGEGYEPISDDELDEILAGDAEKREDQQEEEKMPDPLDVIDVDWSGLMPKHPKEPREPGAALLKFTPGAVLLRVGISKKLAGSELFTKVKETCQQLVEKPKDADSLFEHELGALNMAALLRKEERASLLSDLGPCCKALCFRRDSAIRKQLVKNEKGTVKQAYTNTPMVDNELLRLSLRLFKKKATCHAPGQEKTEDGKLGPCSIQQELCVS
Protein: Ubiquinone biosynthesis O-methyltransferase, mitochondrial (3-demethylubiquinol 3-O-methyltransferase) (EC 2.1.1.64) (3-demethylubiquinone 3-O-methyltransferase) (EC 2.1.1.-) (Polyprenyldihydroxybenzoate methyltransferase) (EC 2.1.1.114) (Q8BMS4)
Organism: Mus musculus (Mouse)
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03190}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Atypical kinase COQ8A, mitochondrial
- Atypical kinase COQ8B, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- All trans-polyprenyl-diphosphate synthase PDSS1
Sequence:
MWRGGRLGSRGVRLLETLGFGCPSAVAQPPRLTSRSAYSGTQLTRNLQIKPWELGEHGTMCFRSYRMALSCLSRVKTYRTPWKRLYSTSQTTVDSREVKNFQALAHTWWDEYGKFAPLHSMNDLRVPFIRDNLLKTSASHHPGKPLSGMKILDVGCGGGLLTEPLGRLGASVVGIDPVAENIKIAQHHKSFDPVLDKRIQYKVCSLEEAVDESAECFDAVVASEVVEHVSHLEMFIQCCYQVLKPGGSLFITTVNKTQLSYALGIVFAEQIAGIVPKGTHTWEKFVSPEKLESILEPNGLSVETVAGLVYNPFSGYWHWSENTSLNYAAHAVRSRAQEHQEPAESALKGETGALHANTSGSPSVREEQRT
Protein: Tubulin-like protein TubZ (EC 3.6.5.-) (FtsZ-like protein TubZ-Bt) (Q8KNP3)
Organism: Bacillus thuringiensis subsp. israelensis
Function: A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBtoxis plasmid. Filaments may seed from the centromere-like site (tubC) when bound by DNA-binding protein TubR; the tubC-TubR complex stabilizes the TubZ filament. Filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell. Required for pBtoxis plasmid replication/partition. Binds the TubR-tubC complex; GTP is not required for binding to TubR-tubC. TubZ alone does not bind DNA. Has a high GTPase activity in the presence of Mg(2+); in the presence of GTP assembles into dynamic filaments which upon polymerization bind almost exclusively GDP. Filament formation is cooperative, requiring a critical concentration. Formation occurs very quickly and is followed by disassembly as GTP is consumed.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17510284}. Note=Forms long, dynamic filaments. {ECO:0000269|PubMed:17510284, ECO:0000269|PubMed:18198178, ECO:0000269|PubMed:20974911}.
Interaction partners:
Sequence:
MLLNSNELEHIHSTNHSVNDISIRWGVIGAGQKGNKEADLFAGYKFSNGTTCYPTLAVNFAESDMMHLQNIIKEDRIHFDGLKGAARTPSVVTDLFDPETNPNANGYLDKLAQELGRKFTNEEGEVIVDQFLICLGAGGGVGTGWGSLVLQLIREQFFPCPVSMLISLPSGDPDEINNALVLLSEIDEFMREQDRLFGNSDIKPLANVIVNDNTQMQRIIESQKGTKDLKNRYVNWKEVANDNVVSTLHEINIIPENYGSDNVTYDPSDLIKLLSIPGRFLTIGKARIAKFDLHSLENSIKRSLDEGFFSAEHQFETATMYGGFVLRPSNADFFKDVNTENRIRNTLGEYKRLDEIAGKFGDPIWDNEYAVCYTIFAGMTMPKRYISLAREGKELAEKQEQLRAEAQRKQDEEKVDISFATNRVQKNTFNPYNKNQGFGGASRFSGGKNSAFKRQTSEATSTQNQQEEENIISTLKTSNPFKKR
Protein: Proteasome subunit alpha type-5 (Q95083)
Organism: Drosophila melanogaster (Fruit fly)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 6
- Proteasome subunit beta type-1
- Proteasome subunit beta type-3
- Proteasome subunit beta
- Proteasome subunit alpha type-7-1
- Proteasome subunit alpha type-2
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasome subunit alpha type-3
Sequence:
MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGICTPEGVVLAVEKRITSPLMVPSTVEKIVEVDKHIGCATSGLMADARTLIERARVECQNHWFVYNERMSIESCAQAVSTLAIQFGDSGDSDGAAAMSRPFGVAILFAGIEAGQPQLWHMDPSGTFVRHGAKAIGSGSEGAQQNLQDLFRPDLTLDEAIDISLNTLKQVMEEKLNSTNVEVMTMTKEREFYMFTKEEVEQHIKNIA
Protein: PCTK1 protein (Q9BRL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRMKKIKRQLSMTLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNIINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEIQLQKEASLRSSSMPDSGRPAFRVVDTEF
Protein: guanylate kinase (EC 2.7.4.8) (A0A1D8PNS0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- GMP synthase
- Adenine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase
- Hypoxanthine phosphoribosyltransferase
- Ribonucleoside-diphosphate reductase
- Pyruvate kinase
- Ribonucleoside-diphosphate reductase
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- 3'\5'-cyclic-nucleotide phosphodiesterase PDE1
Sequence:
MSSSANRPIVISGPSGTGKSTLLKKLFAEYPDKFGFSVSNTTRKPRPGEVNGKDYNFSTVEEFKQLIDENKFIEWAQFSGNYYGTTIKAVKDVAEQGRTCLLDIDMQGVKSVKKTDLNARYLFISPPSIEELKSRLTGRGTETEDSLQKRIAAASDEMEYAQTGAHDKIIVNDDLDKAYAEFKKFIVDEQ
Protein: Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) (Cobalamin-independent methionine synthase) (Methionine synthase, vitamin-B12 independent isozyme) (Q9UT19)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenosylhomocysteinase
- S-adenosylmethionine synthase
- Cystathionine beta-lyase
- Uncharacterized protein C57A7.07c
- Probable cystathionine gamma-synthase
- Homocysteine synthase
- Methylenetetrahydrofolate reductase 1
- Homoserine dehydrogenase
- Methylenetetrahydrofolate reductase 2
- Uncharacterized trans-sulfuration enzyme C23A1.14c
Sequence:
MVKSAVLGFPRIGKNRELKKATEAYWSGKTSAEELLATAKQLRLEHWKLQKAQGVDIIPSNDFSLYDQIMDHSFSFNVIPPRYRLSGLSSLDTYFAMGRGMQRAATADKAAVDVPAGEMVKWFDSNYHFLRPEVSEETDFKLSSTKALDEFLEAKEAGIITRPVLVGPVTYLFIAKAAKGSSIKPIELLPKLLPVYVELIKKLTEAGAEYIQIDEPILTLDLPQEILASYKEAYETLGKIGKLILTTYFGSLQSNADVLKGLPIAGVHVDVVRAPENLDRALAVLGENQIISVGVVSGRNIWKTDFQKATAIIEKAISAVGSERVQVASSSSILHIPHSLSGEDQINPEIKRWFAFAVEKCAELAILTKAANDGPASVRAELEANAADCKARAESPITNVEAVRERQSKVTPQMHERKSPFETRYAKQQASLKLPLFPTTTIGSFPQTKEIRVTRNRFAKGLISQEEYDAFIRKEISDVVKFQEEVGLDVLVHGEPERNDMVQYFGERMEGFVFTVNGWVQSYGSRCVRPPIIVGDVYRPAPMTVKESQYAQSITSKPMKGMLTAPITILRWSFPRDDVHDSVQAQQIALGLRDEVLDLEKAGIKVIQCDEPALREGLPLRRAEWDEYLKWAIDAFRLATAAVQDDTQIHSHFCYSDFNDIFDAIQRLDADVVSIENSKSDMKLLNVLSRYTSCIGPGLFDIHSPRVPPVSEFKERIDAIVKHVPKDHLWLNPDCGLKTRGWPETTADLKNMIAAAREAREQYA
Protein: Importin subunit alpha-3 (Karyopherin subunit alpha-3) (Q19969)
Organism: Caenorhabditis elegans
Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs. Necessary for correct nucleoporin localization within the germline. Essential gene for embryonic and larval development. May be dispensable for axon development, but required for axon regeneration in both mechanosensory and motor neurons. Required for oogenic development, ima-1 and ima-2 cannot functionally compensate for loss of ima-3.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11311162}. Nucleus {ECO:0000269|PubMed:11311162}.
Interaction partners:
- Importin N-terminal domain-containing protein
- Regulator of chromosome condensation
- F-box domain-containing protein
- Exportin-2
- Nsp1_C domain-containing protein
- Nuclear cap-binding protein subunit 2
- GTP-binding nuclear protein ran-1
- Nuclear cap-binding protein subunit 1
- Sentrin-specific protease
- Nuclear pore complex protein npp-16
Sequence:
MSSNRQAYYKNNAKEQIGKEKRNEEVVSIRKDKREEAISKRRNINTQIEDDSETSTTPPGPFDANLLRLTVAAAQSSDPAEQLTAVQQARKMLSTDRNPPIDDLIGSGILPVLVQCLSSTDPNLQFEAAWALTNIASGTSEQTQAVVNAGAVPLFLQLLSCGNLNVCEQSVWALGNIIGDGPHFRDYCLELGILQPLLQFINPEIPIGFLRNVTWVIVNLCRCKDPAPSPAVVRTILPALSLLIHHQDTNILIDTVWALSYLTDGGNEHIQMVIEAQVVTHLVPLLGHVDVKVQTAALRAVGNIVTGTDEQTQLVLDSGVLRFMPGLLAHYKEKINKEAVWFVSNITAGNQQQVQDVFDAGIMPMIIHLLDRGDFPTQKEAAWAISNVTISGRPNQVEQMVKLGVLRPFCAMLSCTDSQIIQVVLDGINNILKMAGEAAEQVTSEIEECGGLDKIENLQNHENEDIYKLAFEIIDNFFSSDDETGNVEGAQSSAFGGDVPPVPDAPNGGWNFGK
Protein: Serine/threonine-protein kinase 36 (EC 2.7.11.1) (Fused homolog) (Q69ZM6)
Organism: Mus musculus (Mouse)
Function: Serine/threonine protein kinase which plays an important role in the sonic hedgehog (Shh) pathway by regulating the activity of GLI transcription factors. Controls the activity of the transcriptional regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and promoting their nuclear localization. GLI2 requires an additional function of STK36 to become transcriptionally active, but the enzyme does not need to possess an active kinase catalytic site for this to occur. Required for postnatal development, possibly by regulating the homeostasis of cerebral spinal fluid or ciliary function. Essential for construction of the central pair apparatus of motile cilia.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19305393}. Nucleus {ECO:0000250|UniProtKB:Q9NRP7}. Cytoplasm, cytoskeleton, cilium axoneme. Note=Low levels also present in the nucleus. {ECO:0000250|UniProtKB:Q9NRP7}.
Interaction partners:
- Suppressor of fused homolog
- Kinesin-like protein KIF27
- Zinc finger protein GLI1
- Kinesin-like protein KIF7
- Protein smoothened
- Transcriptional activator GLI3
- Zinc finger protein GLI2
Sequence:
MEKYHVLEMIGEGSFGRVYKGRKKYSAQVVALKFIPKLGRSEKELRNLQREIEIMRGLWHPNIVHMLDSFETDKEVVVVTDYAEGELFQILEDDGKLPEDQVQAIAAQLVSALYYLHSHRILHRDMKPQNILLAKGGGIKLCDFGFARAMSTNTMVLTSIKGTPLYMSPELVEERPYDHTADLWSVGCILYELAVGTPPFYTTSIFQLVSLILKDPVRWPSTISSCFKNFLQGLLTKDPRQRLSWPDLLHHPFIAGRVTIITEPAGSDLGTPFTSRLPPELQVLKDEQAHRLAPKGNQSRILRQACKLMAEEAKQKEDQNAGSALEQEDGLCKVTPSTAPVPGLKATPQESSLLAGILASEMKNNWEDWGAGEAPRTSRENHINLECEQGFPEPRPEAMGRQSTDVVDPENEEPDSDDEWQRLLETSEPGPVQLKSPLTLLCNPDFCQRIQSQLRGTGEQILKGVLDGVSHLLPVLRILSSLLSSCNDSVLLYSFCQEAGLPELPLSLLRYSQESSSIQQQPWYGALLRDLVAVVQAYFSCTFNLERSQTGDSLQVFQEAASLFLDLLGKLLAQSDDSEQTFRRDSLMCFAVLCEAVDGNSWAVSKAFYSSLLTTQRAVLDGLLHGLTVPQLPFHTPPGAPQVSQPLREQSEDVPGAISSALAAMCTAPVGLPSCWDAKEQVSWHLANQLTEDSSQLRPSLISGLRHHVLCLHLLKVLYACCYISERLCHILGQEPLALESLLMLVQGKVKVADWEESTEVALYLLSLLVFRLQDLPSGMEKLGSEVATLFTHSHVVSLVNAAACLLGQLGQQGVTFDLQPREWIAAAAHALSAPAEVRLTPPYSCGFYDGLLILLLQLLMQVQGKPGLIRDVVGSEVWTILWHRFSMALRLPEEVSAQEDDLLLSSPSSLEPDWTLISPQGMAALLSLAMAIFTQESQLCLSHLSQHGSVLMLTLKHLLSPSFLHHLSQAPQGPEFLPVVVLSVCKLLCFPFALDVDADLLVGVLADLRASEVVVCLLQVCCHHLSLLQAELPIGLLTRLALTDSASLKQFVNTVATSSRAIISFLSVVLLSDQPLMISDLLSLLTHTARILSPSHLSFIQELLSGSDESYRPLRSLLGHSENTVRVRAYGLLGHLLQHSMALRGALQSQSGLLNLLLLGLGDKDPAVRRSASFAVGNAAYQAGPLGPALAAAVPSMTQLLGDAQDGIRRNAASALGNLGPEGLGKELLKCQVPQRLLEMACGDPQPTVKEAALIALRSLQQESCIHQVLVSLGASEKLALLSLGNQLLPNSSNRPASVRHCRKLIQLLRPTHST
Protein: Regulator of chromosome condensation domain-containing protein (Q54D12)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- HECT-type E3 ubiquitin transferase
Sequence:
MIKTIVNQTILNKNFINKNVYNNINKCYHHHHYTTTTTNTTTDKSRQKLFSFGSFDNLKLGVPGNNDKLIPTQITHLPPFLKIKQFGSSWLNSFLLTDEQNENDPTISNKVYMWGTNKSGNMSLPSEQYRFPTTIDLLKNTFVEKVIGGRSFTLVLTRDGKVLGFGENNFGQLGLGDTRNRTAPTPVETLNNQHIIDIGVGLDHSIAVTKAGHVFGWGYNVEGQIGQKVVEYTRMNSTTEVMDGEEEGGAGSLREQMIPDVEYTLPTLVPGLEQIKISNVFCGYDSTFLLSARGNVYSFGSNEIGTLGLGSELKGRVTKPTKIKFTETNEKIKQLSSGASHTLFLTSGGNVYSCGWGTEGRLGLGMDTSNRDSPTLLKYFNQNKIKIVKVAAGGSHSMALDDQGRVYTWGNGSNGKLGHGNESDENLPKQINFFSHSNVIDIFAGIDNSLVLIKE
Protein: Translational activator of cytochrome c oxidase 1 (Coiled-coil domain-containing protein 44) (Translational activator of mitochondrially-encoded cytochrome c oxidase I) (Q9BSH4)
Organism: Homo sapiens (Human)
Function: Acts as a translational activator of mitochondrially-encoded cytochrome c oxidase 1.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19503089}.
Interaction partners:
- Heme A synthase COX15
- Leucine-rich PPR motif-containing protein, mitochondrial
- Protoheme IX farnesyltransferase, mitochondrial
- Elongation factor Ts, mitochondrial
- Surfeit locus protein 1
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase assembly factor 3 homolog, mitochondrial
- Protein SCO1 homolog
- Protein SCO2 homolog
- Mitochondrial chaperone BCS1
Sequence:
MSAWAAASLSRAAARCLLARGPGVRAAPPRDPRPSHPEPRGCGAAPGRTLHFTAAVPAGHNKWSKVRHIKGPKDVERSRIFSKLCLNIRLAVKEGGPNPEHNSNLANILEVCRSKHMPKSTIETALKMEKSKDTYLLYEGRGPGGSSLLIEALSNSSHKCQADIRHILNKNGGVMAVGARHSFDKKGVIVVEVEDREKKAVNLERALEMAIEAGAEDVKETEDEEERNVFKFICDASSLHQVRKKLDSLGLCSVSCALEFIPNSKVQLAEPDLEQAAHLIQALSNHEDVIHVYDNIE
Protein: Toxin Rv0299 (O07226)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin Rv0298/MT0312.
Interaction partners:
- Antitoxin Rv0298
- Putative ribonuclease VapC50
- Putative antitoxin VapB50
- Putative ribonuclease VapC45
- Antitoxin VapB2
Sequence:
MIAPGDIAPRRDSEHELYVAVLSNALHRAADTGRVITCPFIPGRVPEDLLAMVVAVEQPNGTLLPELVQWLHVAALGAPLGNAGVAALREAASVVTALLC
Protein: Ubiquitin-conjugating enzyme E2 B (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme B) (E214K) (RAD6 homolog B) (HR6B) (mHR6B) (Ubiquitin carrier protein B) (Ubiquitin-protein ligase B) (P63147)
Organism: Mus musculus (Mouse)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P63149}. Nucleus {ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons, expressed both at the plasma membrane and in nuclei. {ECO:0000250|UniProtKB:P63149}.
Interaction partners:
- E3 ubiquitin-protein ligase RAD18
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- E3 ubiquitin-protein ligase UBR2
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-conjugating enzyme E2 variant 1
- Ubiquitin-conjugating enzyme E2 A
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase UBR1
Sequence:
MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQENKREYEKRVSAIVEQSWNDS
Protein: Pentacotripeptide-repeat region of PRORP domain-containing protein (Q387I7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRASAMTFRGRMDVKPWMGVGCYPVTPSFIGGMLSVKPAYNHYKMMRPQRPLRAIGTNVTLPPVLYNRLDQIVQIENAIALQRVERQVEMTLSQLALGIRNAEDFLEKHLLHAPVRPSLHMLWFHEDGIRKNQHILSTLGAHHLVPLFSLLAYDVERGRMSLHMAEELYDELMDCSVAQPKVVQRELTNQMVRAYCLHDEFEKALDVVSEMKAKGIRRTFVTYAPIFRMIRSKEEVETHLKLEQFMRDAEGGRLQKLCFIDVPRIFYVFGVFIRYNWAAINSIFTAICTIAALHLFNYGI