ST32C_MOUSE
ID ST32C_MOUSE Reviewed; 488 AA.
AC Q8QZV4; Q9JJG4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Serine/threonine-protein kinase 32C;
DE EC=2.7.11.1;
GN Name=Stk32c {ECO:0000312|EMBL:AAH26457.1, ECO:0000312|MGI:MGI:2385336};
GN Synonyms=Pkek {ECO:0000312|MGI:MGI:2385336}; ORFNames=MNCb-1563;
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] {ECO:0000312|EMBL:BAA95027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAA95027.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAA95027.1};
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAC32730.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32730.1};
RC TISSUE=Corpora quadrigemina {ECO:0000312|EMBL:BAC32730.1};
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 [3] {ECO:0000312|EMBL:AAH26457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye {ECO:0000312|EMBL:AAH26457.1};
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Evidence={ECO:0000250|UniProtKB:Q60592};
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; Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB041542; BAA95027.1; -; mRNA.
DR EMBL; AK046439; BAC32730.1; -; mRNA.
DR EMBL; BC026457; AAH26457.1; -; mRNA.
DR CCDS; CCDS21952.1; -.
DR RefSeq; NP_001156012.1; NM_001162540.1.
DR RefSeq; NP_067277.2; NM_021302.3.
DR AlphaFoldDB; Q8QZV4; -.
DR SMR; Q8QZV4; -.
DR BioGRID; 208304; 3.
DR IntAct; Q8QZV4; 3.
DR STRING; 10090.ENSMUSP00000016125; -.
DR iPTMnet; Q8QZV4; -.
DR PhosphoSitePlus; Q8QZV4; -.
DR EPD; Q8QZV4; -.
DR MaxQB; Q8QZV4; -.
DR PaxDb; Q8QZV4; -.
DR PeptideAtlas; Q8QZV4; -.
DR PRIDE; Q8QZV4; -.
DR ProteomicsDB; 254571; -.
DR Antibodypedia; 19318; 142 antibodies from 29 providers.
DR DNASU; 57740; -.
DR Ensembl; ENSMUST00000016125; ENSMUSP00000016125; ENSMUSG00000015981.
DR GeneID; 57740; -.
DR KEGG; mmu:57740; -.
DR UCSC; uc009kfl.2; mouse.
DR CTD; 282974; -.
DR MGI; MGI:2385336; Stk32c.
DR VEuPathDB; HostDB:ENSMUSG00000015981; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000160573; -.
DR InParanoid; Q8QZV4; -.
DR OMA; MHRRSYY; -.
DR OrthoDB; 668916at2759; -.
DR PhylomeDB; Q8QZV4; -.
DR TreeFam; TF313395; -.
DR BioGRID-ORCS; 57740; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Stk32c; mouse.
DR PRO; PR:Q8QZV4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8QZV4; protein.
DR Bgee; ENSMUSG00000015981; Expressed in striatum and 54 other tissues.
DR ExpressionAtlas; Q8QZV4; baseline and differential.
DR Genevisible; Q8QZV4; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..488
FT /note="Serine/threonine-protein kinase 32C"
FT /id="PRO_0000232416"
FT DOMAIN 94..354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 100..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86UX6"
FT CONFLICT 30
FT /note="D -> E (in Ref. 1; BAA95027)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 55263 MW; 2B6A927BE6B78EF2 CRC64;
MRSGAERRGS SAAAPPSSPP PGRARPAGSD VSPALPPPAA SQPRARDAGD ARAQPRPLFQ
WSKWKKRMSM SSISSGSARR PVFDDKEDVN FDHFQILRAI GKGSFGKVCI VQKRDTEKMY
AMKYMNKQQC IERDEVRNVF RELEILQEIE HVFLVNLWYS FQDEEDMFMV VDLLLGGDLR
YHLQQNVQFS EDTVRLYICE MALALDYLRS QHIIHRDVKP DNILLDEQGH AHLTDFNIAT
IIKDGERATA LAGTKPYMAP EIFHSFVNGG TGYSFEVDWW SVGVMAYELL RGWRPYDIHS
SNAVESLVQL FSTVSVQYVP TWSKEMVALL RKLLTVNPEH RFSSLQDMQT APSLAHVLWD
DLSEKKVEPG FVPNKGRLHC DPTFELEEMI LESRPLHKKK KRLAKNKSRD SSRDSSQSEN
DYLQDCLDAI QQDFVIFNRE KLKRSQELMS EPPPGPETSD MTDSTADSEA EPTALPMCGS
ICPSSGSS
