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   19-MAR-2014, entry version 131.
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.
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cell membrane (By similarity).
CC       Endoplasmic reticulum-Golgi intermediate compartment (By
CC       similarity). Note=Colocalizes with STK17B at the plasma membrane
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta, lung, pancreas.
CC       Lower levels in heart, brain, liver, skeletal muscle and kidney.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. DAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AB011421; BAA34127.1; -; mRNA.
DR   EMBL; BC016040; AAH16040.1; -; mRNA.
DR   RefSeq; NP_004217.1; NM_004226.3.
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; 25-357.
DR   BioGrid; 114684; 4.
DR   IntAct; O94768; 4.
DR   STRING; 9606.ENSP00000263955; -.
DR   BindingDB; O94768; -.
DR   ChEMBL; CHEMBL3980; -.
DR   GuidetoPHARMACOLOGY; 2215; -.
DR   PhosphoSite; 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; GC02M196964; -.
DR   HGNC; HGNC:11396; STK17B.
DR   HPA; HPA034858; -.
DR   MIM; 604727; gene.
DR   neXtProt; NX_O94768; -.
DR   PharmGKB; PA36204; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000233016; -.
DR   HOVERGEN; HBG106718; -.
DR   InParanoid; O94768; -.
DR   KO; K08804; -.
DR   OMA; KRFRFDN; -.
DR   OrthoDB; EOG7QZGBH; -.
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   ArrayExpress; O94768; -.
DR   Bgee; O94768; -.
DR   CleanEx; HS_STK17B; -.
DR   Genevestigator; O94768; -.
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: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   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_dom.
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.
FT   NP_BIND      39     47       ATP (By similarity).
FT   COMPBIAS    308    311       Poly-Ser.
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   BINDING      62     62       ATP.
FT   VARIANT     320    320       S -> F (in dbSNP:rs34740616).
FT                                /FTId=VAR_041147.
FT   MUTAGEN      62     62       K->A: Loss of activity and of apoptotic
FT                                function.
FT   HELIX        25     31
FT   STRAND       32     42
FT   STRAND       45     52
FT   TURN         53     55
FT   STRAND       58     68
FT   HELIX        74     86
FT   TURN         87     89
FT   STRAND       96    101
FT   STRAND      103    111
FT   HELIX       118    122
FT   HELIX       124    126
FT   HELIX       132    151
FT   HELIX       161    163
FT   STRAND      164    167
FT   TURN        169    172
FT   STRAND      175    177
FT   HELIX       180    182
FT   HELIX       199    201
FT   HELIX       204    207
FT   HELIX       215    230
FT   HELIX       240    249
FT   TURN        256    261
FT   HELIX       264    273
FT   HELIX       278    280
FT   HELIX       284    287
FT   HELIX       291    293
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
//