ST17B_HUMAN
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 03-AUG-2022, entry version 185.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 protein
RT 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 project:
RT 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., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA 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 as a
CC positive regulator of apoptosis. {ECO:0000250,
CC ECO:0000269|PubMed:9786912}.
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 -!- 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;
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 plasma
CC membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, lung, pancreas. Lower
CC 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 Ser/Thr
CC protein kinase family. DAP kinase subfamily. {ECO:0000305}.
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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_011512168.2.
DR RefSeq; XP_011510471.1; XM_011512169.1.
DR RefSeq; XP_011510472.1; XM_011512170.1.
DR PDB; 3LM0; X-ray; 2.35 A; A=25-329.
DR PDB; 3LM5; X-ray; 2.29 A; A=25-329.
DR PDB; 6QF4; X-ray; 2.50 A; A=18-329.
DR PDB; 6Y6F; X-ray; 1.98 A; A=25-329.
DR PDB; 6Y6H; X-ray; 1.95 A; A=25-329.
DR PDB; 6ZJF; X-ray; 1.75 A; A=25-329.
DR PDB; 7AKG; X-ray; 2.08 A; A=25-329.
DR PDBsum; 3LM0; -.
DR PDBsum; 3LM5; -.
DR PDBsum; 6QF4; -.
DR PDBsum; 6Y6F; -.
DR PDBsum; 6Y6H; -.
DR PDBsum; 6ZJF; -.
DR PDBsum; 7AKG; -.
DR AlphaFoldDB; O94768; -.
DR SMR; O94768; -.
DR BioGRID; 114684; 37.
DR IntAct; O94768; 27.
DR STRING; 9606.ENSP00000263955; -.
DR BindingDB; O94768; -.
DR ChEMBL; CHEMBL3980; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB04216; Quercetin.
DR DrugCentral; O94768; -.
DR GlyGen; O94768; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O94768; -.
DR PhosphoSitePlus; O94768; -.
DR BioMuta; STK17B; -.
DR CPTAC; CPTAC-1034; -.
DR EPD; O94768; -.
DR jPOST; O94768; -.
DR MassIVE; O94768; -.
DR PaxDb; O94768; -.
DR PeptideAtlas; O94768; -.
DR PRIDE; O94768; -.
DR ProteomicsDB; 50432; -.
DR Antibodypedia; 19872; 436 antibodies from 44 providers.
DR DNASU; 9262; -.
DR Ensembl; ENST00000263955.9; ENSP00000263955.4; ENSG00000081320.11.
DR Ensembl; ENST00000409228.5; ENSP00000386853.1; ENSG00000081320.11.
DR GeneID; 9262; -.
DR KEGG; hsa:9262; -.
DR MANE-Select; ENST00000263955.9; ENSP00000263955.4; NM_004226.4; NP_004217.1.
DR CTD; 9262; -.
DR DisGeNET; 9262; -.
DR GeneCards; STK17B; -.
DR HGNC; HGNC:11396; STK17B.
DR HPA; ENSG00000081320; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 604727; gene.
DR neXtProt; NX_O94768; -.
DR OpenTargets; ENSG00000081320; -.
DR PharmGKB; PA36204; -.
DR VEuPathDB; HostDB:ENSG00000081320; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000154014; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O94768; -.
DR OMA; FYMLESK; -.
DR OrthoDB; 1156450at2759; -.
DR PhylomeDB; O94768; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; O94768; -.
DR SignaLink; O94768; -.
DR SIGNOR; O94768; -.
DR BioGRID-ORCS; 9262; 9 hits in 1116 CRISPR screens.
DR ChiTaRS; STK17B; human.
DR EvolutionaryTrace; O94768; -.
DR GenomeRNAi; 9262; -.
DR Pharos; O94768; Tchem.
DR PRO; PR:O94768; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O94768; protein.
DR Bgee; ENSG00000081320; Expressed in epithelium of nasopharynx and 172 other tissues.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
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:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
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 CDD; cd14198; STKc_DRAK2; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR042763; ST17B_STKc.
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; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..372
FT /note="Serine/threonine-protein kinase 17B"
FT /id="PRO_0000086706"
FT DOMAIN 33..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 305..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT VARIANT 320
FT /note="S -> F (in dbSNP:rs34740616)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041147"
FT MUTAGEN 62
FT /note="K->A: Loss of activity and of apoptotic function."
FT /evidence="ECO:0000269|PubMed:9786912"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6ZJF"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:6ZJF"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:6ZJF"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3LM5"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:6ZJF"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6ZJF"
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
