ID ST17B_HUMAN Reviewed; 372 AA. AC O94768; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 09-DEC-2015, entry version 146. DE RecName: Full=Serine/threonine-protein kinase 17B; DE EC=2.7.11.1; DE AltName: Full=DAP kinase-related apoptosis-inducing protein kinase 2; GN Name=STK17B; Synonyms=DRAK2; 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], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF LYS-62. RC TISSUE=Liver, and Placenta; RX PubMed=9786912; DOI=10.1074/jbc.273.44.29066; RA Sanjo H., Kawai T., Akira S.; RT "DRAKs, novel serine/threonine kinases related to death-associated RT protein kinase that trigger apoptosis."; RL J. Biol. Chem. 273:29066-29071(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [5] RP VARIANT [LARGE SCALE ANALYSIS] PHE-320. 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: Phosphorylates myosin light chains (By similarity). Acts CC as a positive regulator of apoptosis. {ECO:0000250, CC ECO:0000269|PubMed:9786912}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with CHP1; the interaction induces CHP1 to CC translocate from the Golgi to the nucleus. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9786912}. Cell CC membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate CC compartment {ECO:0000250}. Note=Colocalizes with STK17B at the CC plasma membrane. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, lung, pancreas. CC Lower levels in heart, brain, liver, skeletal muscle and kidney. CC {ECO:0000269|PubMed:9786912}. CC -!- PTM: Autophosphorylated. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. DAP kinase subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. 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; AB011421; BAA34127.1; -; mRNA. DR EMBL; BC016040; AAH16040.1; -; mRNA. DR CCDS; CCDS2315.1; -. DR RefSeq; NP_004217.1; NM_004226.3. DR RefSeq; XP_011510470.1; XM_011512168.1. DR RefSeq; XP_011510471.1; XM_011512169.1. DR RefSeq; XP_011510472.1; XM_011512170.1. DR UniGene; Hs.88297; -. DR PDB; 3LM0; X-ray; 2.35 A; A=25-329. DR PDB; 3LM5; X-ray; 2.29 A; A=25-329. DR PDBsum; 3LM0; -. DR PDBsum; 3LM5; -. DR ProteinModelPortal; O94768; -. DR SMR; O94768; 25-335. DR BioGrid; 114684; 13. DR IntAct; O94768; 14. DR STRING; 9606.ENSP00000263955; -. DR BindingDB; O94768; -. DR ChEMBL; CHEMBL3980; -. DR GuidetoPHARMACOLOGY; 2215; -. DR PhosphoSite; O94768; -. DR BioMuta; STK17B; -. DR MaxQB; O94768; -. DR PaxDb; O94768; -. DR PRIDE; O94768; -. DR DNASU; 9262; -. DR Ensembl; ENST00000263955; ENSP00000263955; ENSG00000081320. DR Ensembl; ENST00000409228; ENSP00000386853; ENSG00000081320. DR GeneID; 9262; -. DR KEGG; hsa:9262; -. DR UCSC; uc002utk.3; human. DR CTD; 9262; -. DR GeneCards; STK17B; -. DR HGNC; HGNC:11396; STK17B. DR HPA; HPA034858; -. DR MIM; 604727; gene. DR neXtProt; NX_O94768; -. DR PharmGKB; PA36204; -. DR eggNOG; KOG0032; Eukaryota. DR eggNOG; ENOG410XRMJ; LUCA. DR HOGENOM; HOG000233016; -. DR HOVERGEN; HBG106718; -. DR InParanoid; O94768; -. DR KO; K08804; -. DR OMA; CPHVINL; -. DR OrthoDB; EOG7QZGBH; -. DR PhylomeDB; O94768; -. DR TreeFam; TF314166; -. DR BRENDA; 2.7.11.1; 2681. DR SignaLink; O94768; -. DR ChiTaRS; STK17B; human. DR EvolutionaryTrace; O94768; -. DR GenomeRNAi; 9262; -. DR NextBio; 34721; -. DR PRO; PR:O94768; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; O94768; -. DR CleanEx; HS_STK17B; -. DR ExpressionAtlas; O94768; baseline and differential. DR Genevisible; O94768; HS. DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB. DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IMP:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; ATP-binding; Cell membrane; KW Complete proteome; Kinase; Membrane; Nucleotide-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 372 Serine/threonine-protein kinase 17B. FT /FTId=PRO_0000086706. FT DOMAIN 33 293 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 39 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT COMPBIAS 308 311 Poly-Ser. FT ACT_SITE 158 158 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 62 62 ATP. FT VARIANT 320 320 S -> F (in dbSNP:rs34740616). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_041147. FT MUTAGEN 62 62 K->A: Loss of activity and of apoptotic FT function. {ECO:0000269|PubMed:9786912}. FT HELIX 25 31 {ECO:0000244|PDB:3LM5}. FT STRAND 32 42 {ECO:0000244|PDB:3LM5}. FT STRAND 45 52 {ECO:0000244|PDB:3LM5}. FT TURN 53 55 {ECO:0000244|PDB:3LM5}. FT STRAND 58 68 {ECO:0000244|PDB:3LM5}. FT HELIX 74 86 {ECO:0000244|PDB:3LM5}. FT TURN 87 89 {ECO:0000244|PDB:3LM5}. FT STRAND 96 101 {ECO:0000244|PDB:3LM5}. FT STRAND 103 111 {ECO:0000244|PDB:3LM5}. FT HELIX 118 122 {ECO:0000244|PDB:3LM5}. FT HELIX 124 126 {ECO:0000244|PDB:3LM0}. FT HELIX 132 151 {ECO:0000244|PDB:3LM5}. FT HELIX 161 163 {ECO:0000244|PDB:3LM5}. FT STRAND 164 167 {ECO:0000244|PDB:3LM5}. FT TURN 169 172 {ECO:0000244|PDB:3LM5}. FT STRAND 175 177 {ECO:0000244|PDB:3LM5}. FT HELIX 180 182 {ECO:0000244|PDB:3LM5}. FT HELIX 199 201 {ECO:0000244|PDB:3LM5}. FT HELIX 204 207 {ECO:0000244|PDB:3LM5}. FT HELIX 215 230 {ECO:0000244|PDB:3LM5}. FT HELIX 240 249 {ECO:0000244|PDB:3LM5}. FT TURN 256 261 {ECO:0000244|PDB:3LM5}. FT HELIX 264 273 {ECO:0000244|PDB:3LM5}. FT HELIX 278 280 {ECO:0000244|PDB:3LM5}. FT HELIX 284 287 {ECO:0000244|PDB:3LM5}. FT HELIX 291 293 {ECO:0000244|PDB:3LM5}. SQ SEQUENCE 372 AA; 42344 MW; 7E69FFAED6DC1FF3 CRC64; MSRRRFDCRS ISGLLTTTPQ IPIKMENFNN FYILTSKELG RGKFAVVRQC ISKSTGQEYA AKFLKKRRRG QDCRAEILHE IAVLELAKSC PRVINLHEVY ENTSEIILIL EYAAGGEIFS LCLPELAEMV SENDVIRLIK QILEGVYYLH QNNIVHLDLK PQNILLSSIY PLGDIKIVDF GMSRKIGHAC ELREIMGTPE YLAPEILNYD PITTATDMWN IGIIAYMLLT HTSPFVGEDN QETYLNISQV NVDYSEETFS SVSQLATDFI QSLLVKNPEK RPTAEICLSH SWLQQWDFEN LFHPEETSSS SQTQDHSVRS SEDKTSKSSC NGTCGDREDK ENIPEDSSMV SKRFRFDDSL PNPHELVSDL LC //