ST32C_HUMAN
ID ST32C_HUMAN Reviewed; 486 AA.
AC Q86UX6; Q5T0Q5; Q86UE1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase 32C;
DE EC=2.7.11.1;
DE AltName: Full=PKE;
DE AltName: Full=Yet another novel kinase 3;
GN Name=STK32C {ECO:0000312|EMBL:AAH45760.1}; Synonyms=YANK3;
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] {ECO:0000305, ECO:0000312|EMBL:AAM21719.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ma A.-H., Nelson D.A., Xia L., Ravi L., Chen H.-C., Robinson D.R.,
RA Kung H.-J.;
RT "PKE, a new human AGC group kinase, phosphorylates SET, a PP2A inhibitor.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AL512622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH45760.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-334.
RC TISSUE=Testis {ECO:0000312|EMBL:AAH45760.1};
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] {ECO:0000305}
RP NOMENCLATURE.
RX PubMed=12471243; DOI=10.1126/science.1075762;
RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.;
RT "The protein kinase complement of the human genome.";
RL Science 298:1912-1934(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-18, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-376.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-454 AND LYS-467.
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).
RN [9]
RP VARIANT LEU-151.
RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Expanding the genetic heterogeneity of intellectual disability.";
RL Hum. Genet. 136:1419-1429(2017).
RN [10]
RP ERRATUM OF PUBMED:28940097.
RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Correction to: Expanding the genetic heterogeneity of intellectual
RT disability.";
RL Hum. Genet. 137:105-109(2018).
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 -!- INTERACTION:
CC Q86UX6; O14964: HGS; NbExp=3; IntAct=EBI-1050045, EBI-740220;
CC Q86UX6; P08238: HSP90AB1; NbExp=2; IntAct=EBI-1050045, EBI-352572;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UX6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q86UX6-2; Sequence=VSP_051998;
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; AY098866; AAM21719.1; -; mRNA.
DR EMBL; AL512622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045760; AAH45760.1; -; mRNA.
DR CCDS; CCDS7666.1; -. [Q86UX6-1]
DR CCDS; CCDS81525.1; -. [Q86UX6-2]
DR RefSeq; NP_001305808.1; NM_001318879.1. [Q86UX6-2]
DR RefSeq; NP_775846.2; NM_173575.3. [Q86UX6-1]
DR RefSeq; XP_011537995.1; XM_011539693.2. [Q86UX6-2]
DR RefSeq; XP_011537996.1; XM_011539694.1. [Q86UX6-2]
DR RefSeq; XP_011537997.1; XM_011539695.1. [Q86UX6-2]
DR RefSeq; XP_011537998.1; XM_011539696.1. [Q86UX6-2]
DR AlphaFoldDB; Q86UX6; -.
DR SMR; Q86UX6; -.
DR BioGRID; 129429; 22.
DR IntAct; Q86UX6; 72.
DR MINT; Q86UX6; -.
DR STRING; 9606.ENSP00000298630; -.
DR BindingDB; Q86UX6; -.
DR ChEMBL; CHEMBL5405; -.
DR iPTMnet; Q86UX6; -.
DR PhosphoSitePlus; Q86UX6; -.
DR BioMuta; STK32C; -.
DR DMDM; 74762451; -.
DR EPD; Q86UX6; -.
DR jPOST; Q86UX6; -.
DR MassIVE; Q86UX6; -.
DR MaxQB; Q86UX6; -.
DR PaxDb; Q86UX6; -.
DR PeptideAtlas; Q86UX6; -.
DR PRIDE; Q86UX6; -.
DR ProteomicsDB; 69930; -. [Q86UX6-1]
DR ProteomicsDB; 69931; -. [Q86UX6-2]
DR Antibodypedia; 19318; 142 antibodies from 29 providers.
DR DNASU; 282974; -.
DR Ensembl; ENST00000298630.8; ENSP00000298630.3; ENSG00000165752.17. [Q86UX6-1]
DR Ensembl; ENST00000368622.5; ENSP00000357611.1; ENSG00000165752.17. [Q86UX6-2]
DR GeneID; 282974; -.
DR KEGG; hsa:282974; -.
DR MANE-Select; ENST00000298630.8; ENSP00000298630.3; NM_173575.4; NP_775846.2.
DR UCSC; uc001lld.2; human. [Q86UX6-1]
DR CTD; 282974; -.
DR DisGeNET; 282974; -.
DR GeneCards; STK32C; -.
DR HGNC; HGNC:21332; STK32C.
DR HPA; ENSG00000165752; Tissue enhanced (testis).
DR neXtProt; NX_Q86UX6; -.
DR OpenTargets; ENSG00000165752; -.
DR PharmGKB; PA134888050; -.
DR VEuPathDB; HostDB:ENSG00000165752; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000160573; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q86UX6; -.
DR OMA; MHRRSYY; -.
DR OrthoDB; 668916at2759; -.
DR PhylomeDB; Q86UX6; -.
DR TreeFam; TF313395; -.
DR PathwayCommons; Q86UX6; -.
DR SignaLink; Q86UX6; -.
DR BioGRID-ORCS; 282974; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; STK32C; human.
DR GenomeRNAi; 282974; -.
DR Pharos; Q86UX6; Tbio.
DR PRO; PR:Q86UX6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86UX6; protein.
DR Bgee; ENSG00000165752; Expressed in right testis and 130 other tissues.
DR ExpressionAtlas; Q86UX6; baseline and differential.
DR Genevisible; Q86UX6; HS.
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 Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..486
FT /note="Serine/threonine-protein kinase 32C"
FT /id="PRO_0000232415"
FT DOMAIN 93..353
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 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 99..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
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:0000250|UniProtKB:Q8QZV4"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051998"
FT VARIANT 151
FT /note="V -> L (found in a patient with global developmental
FT delay; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28940097"
FT /id="VAR_084657"
FT VARIANT 334
FT /note="T -> A (in dbSNP:rs17854384)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025900"
FT VARIANT 376
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs764558009)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035637"
FT VARIANT 454
FT /note="A -> T (in dbSNP:rs56109103)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041170"
FT VARIANT 467
FT /note="E -> K (in dbSNP:rs55812591)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041171"
SQ SEQUENCE 486 AA; 54994 MW; 38FEFBB3863B21F3 CRC64;
MRSGAERRGS SAAASPGSPP PGRARPAGSD APSALPPPAA GQPRARDSGD VRSQPRPLFQ
WSKWKKRMGS SMSAATARRP VFDDKEDVNF DHFQILRAIG KGSFGKVCIV QKRDTEKMYA
MKYMNKQQCI ERDEVRNVFR ELEILQEIEH VFLVNLWYSF QDEEDMFMVV DLLLGGDLRY
HLQQNVQFSE DTVRLYICEM ALALDYLRGQ HIIHRDVKPD NILLDERGHA HLTDFNIATI
IKDGERATAL AGTKPYMAPE IFHSFVNGGT GYSFEVDWWS VGVMAYELLR GWRPYDIHSS
NAVESLVQLF STVSVQYVPT WSKEMVALLR KLLTVNPEHR LSSLQDVQAA PALAGVLWDH
LSEKRVEPGF VPNKGRLHCD PTFELEEMIL ESRPLHKKKK RLAKNKSRDN SRDSSQSEND
YLQDCLDAIQ QDFVIFNREK LKRSQDLPRE PLPAPESRDA AEPVEDEAER SALPMCGPIC
PSAGSG
