KPSH1_MOUSE
ID KPSH1_MOUSE Reviewed; 424 AA.
AC Q91YA2; Q3U3V3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129S6/SvEvTac; TISSUE=Spleen;
RA Bjoernslett M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trophoblast stem 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).
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. {ECO:0000250}.
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 {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Nucleus speckle {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Localized in
CC the brefeldin A- sensitive Golgi compartment, at centrosomes, in the
CC nucleus with a somewhat speckle-like presence, membrane-associated to
CC the endoplasmic reticulum (ER) and the plasma membrane (PM), and more
CC diffusely in the cytoplasm. Found to concentrate in splicing factor
CC compartments (SFCs) within the nucleus of interphase cells. The
CC acylation-negative form may be only cytoplasmic and nuclear. Acylation
CC seems to allow the sequestering to the intracellular membranes.
CC Myristoylation may mediate targeting to the intracellular non-Golgi
CC membranes and palmitoylation may mediate the targeting to the Golgi
CC membranes. Dual acylation is required to stabilize the interaction with
CC Golgi membranes (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine residues. {ECO:0000250}.
CC -!- PTM: Myristoylated. Required for membrane association. Prerequisite for
CC palmitoylation to occur (By similarity). {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK053397; BAC35374.1; -; mRNA.
DR EMBL; AK153861; BAE32217.1; -; mRNA.
DR EMBL; AF236365; AAL11033.1; -; Genomic_DNA.
DR EMBL; AF236364; AAL11033.1; JOINED; Genomic_DNA.
DR EMBL; AK154570; BAE32682.1; -; mRNA.
DR EMBL; BC050128; AAH50128.1; -; mRNA.
DR CCDS; CCDS22619.1; -.
DR RefSeq; NP_775608.1; NM_173432.2.
DR AlphaFoldDB; Q91YA2; -.
DR SMR; Q91YA2; -.
DR STRING; 10090.ENSMUSP00000061700; -.
DR iPTMnet; Q91YA2; -.
DR PhosphoSitePlus; Q91YA2; -.
DR PaxDb; Q91YA2; -.
DR PRIDE; Q91YA2; -.
DR ProteomicsDB; 265021; -.
DR Antibodypedia; 29669; 142 antibodies from 30 providers.
DR DNASU; 244631; -.
DR Ensembl; ENSMUST00000049699; ENSMUSP00000061700; ENSMUSG00000048310.
DR GeneID; 244631; -.
DR KEGG; mmu:244631; -.
DR UCSC; uc009nen.1; mouse.
DR CTD; 5681; -.
DR MGI; MGI:3528383; Pskh1.
DR VEuPathDB; HostDB:ENSMUSG00000048310; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000157041; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q91YA2; -.
DR OMA; CPGAPTT; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q91YA2; -.
DR TreeFam; TF314166; -.
DR BioGRID-ORCS; 244631; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Pskh1; mouse.
DR PRO; PR:Q91YA2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91YA2; protein.
DR Bgee; ENSMUSG00000048310; Expressed in manus and 181 other tissues.
DR Genevisible; Q91YA2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
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; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
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 2: Evidence at transcript 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 CHAIN 2..424
FT /note="Serine/threonine-protein kinase H1"
FT /id="PRO_0000086168"
FT DOMAIN 98..355
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 59..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..408
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:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 213
FT /note="G -> S (in Ref. 1; BAE32682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48095 MW; 81B7A29543C39F47 CRC64;
MGCGTSKVLP EPPKDVQLDL VKKVEPFSGT KNDVYKHFIT EVDSVGPLKA GFPATSQYAP
PCPGVPNTGH TAPPSEPPRR ARVAKYRAKF DPRVTAKYDI KALIGRGSFS RVVRVEHRAT
RQPYAIKMIE TKYREGREVC ESELRVLRRV RHANIIQLVE VFETQERVYM VMELATGGEL
FDRIIAKGSF TERDATRVLQ MVLDGVRYLH ALGITHRDLK PENLLYYHPG TDSKIIITDF
GLASARKKGD DCLMKTTCGT PEYIAPEVLV RKPYTNSVDM WALGVIAYIL LSGTMPFEDD
NRTRLYRQIL RGKYSYLGEP WPSVSNLAKD FIDRLLTVDP GARMTALQAL RHPWVVSMAA
SSSMKNLHRS ISQNLLKRAS SRCQSTKSSQ STRSSRSTRS NKSRRVRERE LRELNLRYQQ
QYNG
