ID G3UXM5_MOUSE Unreviewed; 614 AA. AC G3UXM5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-MAY-2024, entry version 77. DE SubName: Full=BR serine/threonine kinase 2 {ECO:0000313|Ensembl:ENSMUSP00000133750.2}; DE Flags: Fragment; GN Name=Brsk2 {ECO:0000313|Ensembl:ENSMUSP00000133750.2, GN ECO:0000313|MGI:MGI:1923020}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000133750.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000133750.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133750.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000133750.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133750.2}; RG Ensembl; RL Submitted (FEB-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000256|ARBA:ARBA00001433}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR MaxQB; G3UXM5; -. DR PeptideAtlas; G3UXM5; -. DR ProteomicsDB; 312599; -. DR Antibodypedia; 22872; 263 antibodies from 34 providers. DR Ensembl; ENSMUST00000172967.8; ENSMUSP00000133750.2; ENSMUSG00000053046.17. DR AGR; MGI:1923020; -. DR MGI; MGI:1923020; Brsk2. DR VEuPathDB; HostDB:ENSMUSG00000053046; -. DR GeneTree; ENSGT00940000157462; -. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; ENSMUSG00000053046; Expressed in visual cortex and 122 other cell types or tissues. DR ExpressionAtlas; G3UXM5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0050321; F:tau-protein kinase activity; IEA:TreeGrafter. DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:TreeGrafter. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14081; STKc_BRSK1_2; 1. DR CDD; cd14340; UBA_BRSK; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR048622; BRSK1_2-like_UBA. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF99; SERINE_THREONINE-PROTEIN KINASE BRSK2-LIKE ISOFORM X1; 1. DR Pfam; PF21122; KA1_BRSK; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF21115; UBA_BRSK; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Proteomics identification {ECO:0007829|MaxQB:G3UXM5, KW ECO:0007829|PeptideAtlas:G3UXM5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 1..240 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 316..446 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 461..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..354 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..398 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..439 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000133750.2" SQ SEQUENCE 614 AA; 68826 MW; EB293C402C4DDCAE CRC64; XLVKLGIHCV TCQKVAIKIV NREKLSESVL MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG GELFDYLVKK GRLTPKEARK FFRQIISALD FCHSHSICHR DLKPENLLLD ERNNIRIADF GMASLQVGDS LLETSCGSPH YACPEVIRGE KYDGRKADVW SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP PDCQSLLRGM IEVDAARRLT LEHIQKHIWY IGGKNEPEPE QPIPRKVQIR SLPSLEDIDP DVLDSMHSLG CFRDRNKLLQ DLLSEEENQE KMIYFLLLDR KERYPSHEDE DLPPRNEIDP PRKRVDSPML NRHGKRRPER KSMEVLSVTD GGSPVPARRA IEMAQHGQRS RSISGASSGL STSPLSSPRV TPHPSPRGSP LPTPKGTPVH TPKESPAGTP NPTPPSSPSV GGVPWRTRLN SIKNSFLGSP RFHRRKLQVP TPEEMSNLTP ESSPELAKKS WFGNFINLEK EEQIFVVIKD KPLSSIKADI VHAFLSIPSL SHSVISQTSF RAEYKATGGP AVFQKPVKFQ VDITYTEGGE AQKENGIYSV TFTLLSEPPP PAPGLSWGAG LKGQKVATSY ESSL //