ID   S17B_HUMAN     STANDARD;      PRT;   372 AA.
AC   O94768;
DT   16-OCT-2001 (Rel. 40, Created)
DT   16-OCT-2001 (Rel. 40, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Serine/threonine-protein kinase 17B (EC 2.7.1.37) (DAP kinase-related
DE   apoptosis-inducing protein kinase 2).
GN   Name=STK17B; Synonyms=DRAK2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF LYS-62.
RC   TISSUE=Liver, and Placenta;
RX   MEDLINE=99003259; 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.
RC   TISSUE=B-cell;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: Acts as a positive regulator of apoptosis.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with CHP causing CHP to translocate from the
CC       Golgi to the nucleus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nuclear.
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 Ser/Thr protein kinase family. DAP
CC       kinase subfamily.
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DR   EMBL; AB011421; BAA34127.1; -.
DR   EMBL; BC016040; AAH16040.1; -.
DR   HSSP; P53355; 1JKT.
DR   Ensembl; ENSG00000081320; Homo sapiens.
DR   Genew; HGNC:11396; STK17B.
DR   H-InvDB; HIX0002694; -.
DR   MIM; 604727; -.
DR   GO; GO:0005634; C:nucleus; IEP.
DR   GO; GO:0005524; F:ATP binding; IDA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA.
DR   GO; GO:0006917; P:induction of apoptosis; IMP.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IDA.
DR   GO; GO:0007243; P:protein kinase cascade; IDA.
DR   InterPro; IPR011009; Kinase_like.
DR   InterPro; IPR000719; Prot_kinase.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
KW   Apoptosis; ATP-binding; Nuclear protein; Phosphorylation;
KW   Serine/threonine-protein kinase; Transferase.
FT   DOMAIN       33    293       Protein kinase.
FT   DOMAIN      308    311       Poly-Ser.
FT   NP_BIND      39     47       ATP (By similarity).
FT   BINDING      62     62       ATP.
FT   ACT_SITE    158    158       Proton acceptor (By similarity).
FT   MUTAGEN      62     62       K->A: Loss of activity and of apoptotic
FT                                function.
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
//