ID SBK1_HUMAN Reviewed; 424 AA. AC Q52WX2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 03-MAR-2009, entry version 38. DE RecName: Full=Serine/threonine-protein kinase SBK1; DE EC=2.7.11.1; DE AltName: Full=SH3-binding kinase 1; GN Name=SBK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang P.Z., Wang X., Wang F., Wu J.; RT "Cloning of human SBK1 cDNA and screening of its interaction RT proteins."; RL Zhongguo Sheng Wu Hua Xue Yu Fen Zi Sheng Wu Xue Bao 22:313-321(2006). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63 AND TYR-64, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [3] RP VARIANTS [LARGE SCALE ANALYSIS] GLU-92; THR-250 AND SER-261. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: May be involved in signal-transduction pathways related CC to the control of brain development (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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 EMBL; AY874862; AAX59898.1; -; mRNA. DR IPI; IPI00399180; -. DR RefSeq; NP_001019572.1; -. DR UniGene; Hs.97837; -. DR PRIDE; Q52WX2; -. DR Ensembl; ENSG00000188322; Homo sapiens. DR GeneID; 388228; -. DR KEGG; hsa:388228; -. DR GeneCards; GC16P028211; -. DR HGNC; HGNC:17699; SBK1. DR PharmGKB; PA134887617; -. DR HOGENOM; Q52WX2; -. DR HOVERGEN; Q52WX2; -. DR BRENDA; 2.7.11.1; 247. DR NextBio; 101893; -. DR ArrayExpress; Q52WX2; -. DR Bgee; Q52WX2; -. DR CleanEx; HS_SBK1; -. DR GermOnline; ENSG00000188322; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR016234; Ser/Thr_prot_kinase_Sbk1. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000566; Ser/Thr_PK_Sbk1; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; KW Polymorphism; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 424 Serine/threonine-protein kinase SBK1. FT /FTId=PRO_0000238451. FT DOMAIN 53 318 Protein kinase. FT NP_BIND 59 67 ATP (By similarity). FT COMPBIAS 332 400 Pro-rich. FT ACT_SITE 174 174 Proton acceptor (By similarity). FT BINDING 82 82 ATP (By similarity). FT MOD_RES 63 63 Phosphothreonine. FT MOD_RES 64 64 Phosphotyrosine. FT VARIANT 12 12 R -> H (in dbSNP:rs35448675). FT /FTId=VAR_051665. FT VARIANT 92 92 K -> E (in an ovarian mucinous carcinoma FT sample; somatic mutation). FT /FTId=VAR_041068. FT VARIANT 250 250 N -> T. FT /FTId=VAR_041069. FT VARIANT 261 261 A -> S. FT /FTId=VAR_041070. SQ SEQUENCE 424 AA; 46252 MW; 2E07FFDA5693311F CRC64; MSVGCPEPEP PRSLTCCGPG TAPGPGAGVP LLTEDMQALT LRTLAASDVT KHYELVRELG KGTYGKVDLV VYKGTGTKMA LKFVNKSKTK LKNFLREVSI TNSLSSSPFI IKVFDVVFET EDCYVFAQEY APAGDLFDII PPQVGLPEDT VKRCVQQLGL ALDFMHGRQL VHRDIKPENV LLFDRECRRV KLADFGMTRR VGCRVKRVSG TIPYTAPEVC QAGRADGLAV DTGVDVWAFG VLIFCVLTGN FPWEAASGAD AFFEEFVRWQ RGRLPGLPSQ WRRFTEPALR MFQRLLALEP ERRGPAKEVF RFLKHELTSE LRRRPSHRAR KPPGDRPPAA GPLRLEAPGP LKRTVLTESG SGSRPAPPAV GSVPLPVPVP VPVPVPVPVP EPGLAPQGPP GRTDGRADKS KGQVVLATAI EICV //