KPSH2_HUMAN
ID KPSH2_HUMAN Reviewed; 385 AA.
AC Q96QS6; A0AV22;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase H2;
DE EC=2.7.11.1;
DE AltName: Full=Protein serine kinase H2;
DE Short=PSK-H2;
GN Name=PSKH2;
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].
RA Scharm B.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 VARIANTS [LARGE SCALE ANALYSIS] ASP-72; LYS-79; GLN-114; ILE-116; ARG-132;
RP GLN-148; SER-176; ARG-211; ILE-212; ALA-225; ARG-266 AND VAL-336.
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 -!- 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 -!- INTERACTION:
CC Q96QS6; Q16543: CDC37; NbExp=3; IntAct=EBI-6424813, EBI-295634;
CC Q96QS6; P07900: HSP90AA1; NbExp=2; IntAct=EBI-6424813, EBI-296047;
CC Q96QS6; P08238: HSP90AB1; NbExp=3; IntAct=EBI-6424813, EBI-352572;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Asn-183 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AY037806; AAK59985.1; -; mRNA.
DR EMBL; BC126180; AAI26181.1; -; mRNA.
DR EMBL; BC126182; AAI26183.1; -; mRNA.
DR CCDS; CCDS6240.1; -.
DR RefSeq; NP_149117.1; NM_033126.2.
DR AlphaFoldDB; Q96QS6; -.
DR SMR; Q96QS6; -.
DR BioGRID; 124556; 12.
DR IntAct; Q96QS6; 65.
DR STRING; 9606.ENSP00000276616; -.
DR iPTMnet; Q96QS6; -.
DR PhosphoSitePlus; Q96QS6; -.
DR BioMuta; PSKH2; -.
DR DMDM; 74762688; -.
DR MassIVE; Q96QS6; -.
DR PaxDb; Q96QS6; -.
DR PeptideAtlas; Q96QS6; -.
DR PRIDE; Q96QS6; -.
DR Antibodypedia; 12608; 125 antibodies from 27 providers.
DR DNASU; 85481; -.
DR Ensembl; ENST00000276616.3; ENSP00000276616.2; ENSG00000147613.8.
DR GeneID; 85481; -.
DR KEGG; hsa:85481; -.
DR MANE-Select; ENST00000276616.3; ENSP00000276616.2; NM_033126.3; NP_149117.1.
DR UCSC; uc011lfy.3; human.
DR CTD; 85481; -.
DR DisGeNET; 85481; -.
DR GeneCards; PSKH2; -.
DR HGNC; HGNC:18997; PSKH2.
DR HPA; ENSG00000147613; Tissue enriched (retina).
DR neXtProt; NX_Q96QS6; -.
DR PharmGKB; PA134961168; -.
DR VEuPathDB; HostDB:ENSG00000147613; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162917; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q96QS6; -.
DR OMA; DHPWVIT; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q96QS6; -.
DR TreeFam; TF314166; -.
DR PathwayCommons; Q96QS6; -.
DR SignaLink; Q96QS6; -.
DR BioGRID-ORCS; 85481; 10 hits in 1093 CRISPR screens.
DR ChiTaRS; PSKH2; human.
DR GenomeRNAi; 85481; -.
DR Pharos; Q96QS6; Tdark.
DR PRO; PR:Q96QS6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96QS6; protein.
DR Bgee; ENSG00000147613; Expressed in adult mammalian kidney and 11 other tissues.
DR Genevisible; Q96QS6; HS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..385
FT /note="Serine/threonine-protein kinase H2"
FT /id="PRO_0000086171"
FT DOMAIN 63..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 342..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 72
FT /note="G -> D (in dbSNP:rs56407605)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040615"
FT VARIANT 79
FT /note="R -> K (in dbSNP:rs35315725)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040616"
FT VARIANT 114
FT /note="R -> Q (in dbSNP:rs35915498)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040617"
FT VARIANT 116
FT /note="S -> I (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040618"
FT VARIANT 132
FT /note="Q -> R (in dbSNP:rs16879427)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040619"
FT VARIANT 148
FT /note="R -> Q (in dbSNP:rs56356246)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040620"
FT VARIANT 176
FT /note="A -> S (in dbSNP:rs6998760)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040621"
FT VARIANT 211
FT /note="G -> R (in dbSNP:rs36074412)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040622"
FT VARIANT 212
FT /note="K -> I (in a lung adenocarcinoma sample; somatic
FT mutation; dbSNP:rs778066815)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040623"
FT VARIANT 225
FT /note="T -> A (in dbSNP:rs34457516)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040624"
FT VARIANT 266
FT /note="S -> R (in dbSNP:rs34037815)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040625"
FT VARIANT 336
FT /note="I -> V (in dbSNP:rs16876805)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040626"
SQ SEQUENCE 385 AA; 43027 MW; 6472D63BC7688334 CRC64;
MGCGASRKVV PGPPALAWAK HEGQNQAGVG GAGPGPEAAA QAAQRIQVAR FRAKFDPRVL
ARYDIKALIG TGSFSRVVRV EQKTTKKPFA IKVMETRERE GREACVSELS VLRRVSHRYI
VQLMEIFETE DQVYMVMELA TGGELFDRLI AQGSFTERDA VRILQMVADG IRYLHALQIT
HRNLKPENLL YYHPGEESKI LITDFGLAYS GKKSGDWTMK TLCGTPEYIA PEVLLRKPYT
SAVDMWALGV ITYALLSGFL PFDDESQTRL YRKILKGKYN YTGEPWPSIS HLAKDFIDKL
LILEAGHRMS AGQALDHPWV ITMAAGSSMK NLQRAISRNL MQRASPHSQS PGSAQSSKSH
YSHKSRHMWS KRNLRIVESP LSALL
