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   27-MAR-2024, entry version 160.
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}.
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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   BioGRID; 232668; 1.
DR   STRING; 10090.ENSMUSP00000061700; -.
DR   iPTMnet; Q91YA2; -.
DR   PhosphoSitePlus; Q91YA2; -.
DR   PaxDb; 10090-ENSMUSP00000061700; -.
DR   ProteomicsDB; 265021; -.
DR   Antibodypedia; 29669; 160 antibodies from 30 providers.
DR   DNASU; 244631; -.
DR   Ensembl; ENSMUST00000049699.9; ENSMUSP00000061700.9; ENSMUSG00000048310.9.
DR   GeneID; 244631; -.
DR   KEGG; mmu:244631; -.
DR   UCSC; uc009nen.1; mouse.
DR   AGR; MGI:3528383; -.
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; FAHEPWK; -.
DR   OrthoDB; 1121238at2759; -.
DR   PhylomeDB; Q91YA2; -.
DR   TreeFam; TF314166; -.
DR   BioGRID-ORCS; 244631; 1 hit in 79 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 184 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14087; STKc_PSKH1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24347:SF254; SERINE_THREONINE-PROTEIN KINASE H1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q91YA2; MM.
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
//