KPSH1_HUMAN
ID KPSH1_HUMAN Reviewed; 424 AA.
AC P11801; Q9NY19;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Serine/threonine-protein kinase H1;
DE EC=2.7.11.1;
DE AltName: Full=Protein serine kinase H1;
DE Short=PSK-H1;
GN Name=PSKH1;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, HOMODIMERIZATION, AND MUTAGENESIS OF ASP-218.
RX PubMed=11087665; DOI=10.1006/geno.2000.6365;
RA Brede G., Solheim J., Troen G., Prydz H.;
RT "Characterization of PSKH1, a novel human protein serine kinase with
RT centrosomal, Golgi, and nuclear localization.";
RL Genomics 70:82-92(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 199-348.
RX PubMed=2948189; DOI=10.1073/pnas.84.2.388;
RA Hanks S.K.;
RT "Homology probing: identification of cDNA clones encoding members of the
RT protein-serine kinase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:388-392(1987).
RN [4]
RP FUNCTION.
RX PubMed=12466556; DOI=10.1093/nar/gkf648;
RA Brede G., Solheim J., Prydz H.;
RT "PSKH1, a novel splice factor compartment-associated serine kinase.";
RL Nucleic Acids Res. 30:5301-5309(2002).
RN [5]
RP MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND SUBCELLULAR LOCATION.
RX PubMed=14644153; DOI=10.1016/j.yexcr.2003.07.009;
RA Brede G., Solheim J., Stang E., Prydz H.;
RT "Mutants of the protein serine kinase PSKH1 disassemble the Golgi
RT apparatus.";
RL Exp. Cell Res. 291:299-312(2003).
RN [6]
RP VARIANT [LARGE SCALE ANALYSIS] SER-301.
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: May be a SFC-associated serine kinase (splicing factor
CC compartment-associated serine kinase) with a role in intranuclear SR
CC protein (non-snRNP splicing factors containing a serine/arginine-rich
CC domain) trafficking and pre-mRNA processing.
CC {ECO:0000269|PubMed:12466556}.
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 -!- ACTIVITY REGULATION: Activity depends on Ca(2+) concentration.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC P11801; P08238: HSP90AB1; NbExp=3; IntAct=EBI-3922781, EBI-352572;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Nucleus speckle. Endoplasmic
CC reticulum membrane; Lipid-anchor. Cell membrane; Lipid-anchor.
CC Cytoplasm. Note=Localized in the brefeldin A-sensitive Golgi
CC compartment, at centrosomes, in the nucleus with a somewhat speckle-
CC like presence, membrane-associated to the endoplasmic reticulum (ER)
CC and the plasma membrane (PM), and more diffusely in the cytoplasm.
CC Found to concentrate in splicing factor compartments (SFCs) within the
CC nucleus of interphase cells. The acylation-negative form may be only
CC cytoplasmic and nuclear. Acylation seems to allow the sequestering to
CC the intracellular membranes. Myristoylation may mediate targeting to
CC the intracellular non-Golgi membranes and palmitoylation may mediate
CC the targeting to the Golgi membranes. Dual acylation is required to
CC stabilize the interaction with Golgi membranes.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues and cell lines tested with
CC the highest level of abundance in testis.
CC {ECO:0000269|PubMed:11087665}.
CC -!- PTM: Autophosphorylated on serine residues.
CC {ECO:0000269|PubMed:11087665}.
CC -!- PTM: Myristoylated. Required for membrane association. Prerequisite for
CC palmitoylation to occur. {ECO:0000269|PubMed:14644153}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:14644153}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AJ272212; CAB91984.1; -; mRNA.
DR EMBL; BC062616; AAH62616.1; -; mRNA.
DR EMBL; M14504; AAA36519.1; -; mRNA.
DR CCDS; CCDS10851.1; -.
DR PIR; B26368; B26368.
DR PIR; I38138; I38138.
DR RefSeq; NP_006733.1; NM_006742.2.
DR AlphaFoldDB; P11801; -.
DR SMR; P11801; -.
DR BioGRID; 111654; 8.
DR IntAct; P11801; 55.
DR STRING; 9606.ENSP00000291041; -.
DR ChEMBL; CHEMBL4524035; -.
DR iPTMnet; P11801; -.
DR PhosphoSitePlus; P11801; -.
DR SwissPalm; P11801; -.
DR BioMuta; PSKH1; -.
DR DMDM; 17379144; -.
DR MassIVE; P11801; -.
DR PaxDb; P11801; -.
DR PeptideAtlas; P11801; -.
DR PRIDE; P11801; -.
DR ProteomicsDB; 52804; -.
DR Antibodypedia; 29669; 142 antibodies from 30 providers.
DR DNASU; 5681; -.
DR Ensembl; ENST00000291041.6; ENSP00000291041.4; ENSG00000159792.10.
DR GeneID; 5681; -.
DR KEGG; hsa:5681; -.
DR MANE-Select; ENST00000291041.6; ENSP00000291041.4; NM_006742.3; NP_006733.1.
DR UCSC; uc002euv.3; human.
DR CTD; 5681; -.
DR DisGeNET; 5681; -.
DR GeneCards; PSKH1; -.
DR HGNC; HGNC:9529; PSKH1.
DR HPA; ENSG00000159792; Low tissue specificity.
DR MIM; 177015; gene.
DR neXtProt; NX_P11801; -.
DR OpenTargets; ENSG00000159792; -.
DR PharmGKB; PA33874; -.
DR VEuPathDB; HostDB:ENSG00000159792; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000157041; -.
DR InParanoid; P11801; -.
DR OMA; CPGAPTT; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; P11801; -.
DR TreeFam; TF314166; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P11801; -.
DR SignaLink; P11801; -.
DR BioGRID-ORCS; 5681; 13 hits in 1115 CRISPR screens.
DR ChiTaRS; PSKH1; human.
DR GeneWiki; PSKH1; -.
DR GenomeRNAi; 5681; -.
DR Pharos; P11801; Tbio.
DR PRO; PR:P11801; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P11801; protein.
DR Bgee; ENSG00000159792; Expressed in stromal cell of endometrium and 143 other tissues.
DR ExpressionAtlas; P11801; baseline and differential.
DR Genevisible; P11801; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
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 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 ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Golgi apparatus; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..424
FT /note="Serine/threonine-protein kinase H1"
FT /id="PRO_0000086167"
FT DOMAIN 98..355
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 104..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 380
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 381
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:14644153"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:14644153"
FT VARIANT 301
FT /note="N -> S (in dbSNP:rs35552721)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040614"
FT MUTAGEN 218
FT /note="D->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:11087665"
SQ SEQUENCE 424 AA; 48035 MW; B357757DDC12388D CRC64;
MGCGTSKVLP EPPKDVQLDL VKKVEPFSGT KSDVYKHFIT EVDSVGPVKA GFPAASQYAH
PCPGPPTAGH TEPPSEPPRR ARVAKYRAKF DPRVTAKYDI KALIGRGSFS RVVRVEHRAT
RQPYAIKMIE TKYREGREVC ESELRVLRRV RHANIIQLVE VFETQERVYM VMELATGGEL
FDRIIAKGSF TERDATRVLQ MVLDGVRYLH ALGITHRDLK PENLLYYHPG TDSKIIITDF
GLASARKKGD DCLMKTTCGT PEYIAPEVLV RKPYTNSVDM WALGVIAYIL LSGTMPFEDD
NRTRLYRQIL RGKYSYSGEP WPSVSNLAKD FIDRLLTVDP GARMTALQAL RHPWVVSMAA
SSSMKNLHRS ISQNLLKRAS SRCQSTKSAQ STRSSRSTRS NKSRRVRERE LRELNLRYQQ
QYNG
