ST32B_HUMAN
ID ST32B_HUMAN Reviewed; 414 AA.
AC Q9NY57; Q6UXH3; Q8IY14;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase 32B;
DE EC=2.7.11.1;
DE AltName: Full=Yet another novel kinase 2;
GN Name=STK32B {ECO:0000312|EMBL:AAH38238.1}; Synonyms=YANK2;
GN ORFNames=UNQ3003/PRO9744;
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:CAB76471.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:CAB76471.1};
RX PubMed=10700184; DOI=10.1038/73508;
RA Ruiz-Perez V.L., Ide S.E., Strom T.M., Lorenz B., Wilson D., Woods K.,
RA King L., Francomano C., Freisinger P., Spranger S., Marino B.,
RA Dallapiccola B., Wright M., Meitinger T., Polymeropoulos M.H., Goodship J.;
RT "Mutations in a new gene in Ellis-van Creveld syndrome and Weyers
RT acrodental dysostosis.";
RL Nat. Genet. 24:283-286(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAQ88719.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH38238.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-198.
RC TISSUE=Brain {ECO:0000312|EMBL:AAH38238.1};
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 VARIANTS [LARGE SCALE ANALYSIS] GLU-35; GLY-198; HIS-244; VAL-310 AND
RP THR-342.
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10700184, ECO:0000269|PubMed:15489334};
CC IsoId=Q9NY57-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12975309};
CC IsoId=Q9NY57-2; Sequence=VSP_051997;
CC -!- MISCELLANEOUS: [Isoform 2]: It is unsure whether Met-1 or Met-3 is the
CC initiator. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ250839; CAB76471.1; -; mRNA.
DR EMBL; AY358353; AAQ88719.1; ALT_INIT; mRNA.
DR EMBL; BC038238; AAH38238.1; -; mRNA.
DR CCDS; CCDS3380.1; -. [Q9NY57-1]
DR CCDS; CCDS77895.1; -. [Q9NY57-2]
DR RefSeq; NP_001293011.1; NM_001306082.1. [Q9NY57-2]
DR RefSeq; NP_060871.1; NM_018401.2. [Q9NY57-1]
DR AlphaFoldDB; Q9NY57; -.
DR SMR; Q9NY57; -.
DR BioGRID; 120631; 1.
DR IntAct; Q9NY57; 15.
DR MINT; Q9NY57; -.
DR STRING; 9606.ENSP00000282908; -.
DR BindingDB; Q9NY57; -.
DR ChEMBL; CHEMBL5912; -.
DR DrugCentral; Q9NY57; -.
DR iPTMnet; Q9NY57; -.
DR PhosphoSitePlus; Q9NY57; -.
DR BioMuta; STK32B; -.
DR DMDM; 74761811; -.
DR MassIVE; Q9NY57; -.
DR PaxDb; Q9NY57; -.
DR PeptideAtlas; Q9NY57; -.
DR PRIDE; Q9NY57; -.
DR ProteomicsDB; 83178; -. [Q9NY57-1]
DR ProteomicsDB; 83179; -. [Q9NY57-2]
DR Antibodypedia; 9281; 125 antibodies from 23 providers.
DR DNASU; 55351; -.
DR Ensembl; ENST00000282908.10; ENSP00000282908.5; ENSG00000152953.13. [Q9NY57-1]
DR Ensembl; ENST00000510398.1; ENSP00000420984.1; ENSG00000152953.13. [Q9NY57-2]
DR GeneID; 55351; -.
DR KEGG; hsa:55351; -.
DR MANE-Select; ENST00000282908.10; ENSP00000282908.5; NM_018401.3; NP_060871.1.
DR UCSC; uc003gih.2; human. [Q9NY57-1]
DR CTD; 55351; -.
DR DisGeNET; 55351; -.
DR GeneCards; STK32B; -.
DR HGNC; HGNC:14217; STK32B.
DR HPA; ENSG00000152953; Tissue enhanced (kidney, lymphoid tissue).
DR neXtProt; NX_Q9NY57; -.
DR OpenTargets; ENSG00000152953; -.
DR PharmGKB; PA128394683; -.
DR VEuPathDB; HostDB:ENSG00000152953; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000160490; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q9NY57; -.
DR OMA; KQRIIHR; -.
DR PhylomeDB; Q9NY57; -.
DR TreeFam; TF313395; -.
DR PathwayCommons; Q9NY57; -.
DR SignaLink; Q9NY57; -.
DR BioGRID-ORCS; 55351; 9 hits in 1105 CRISPR screens.
DR ChiTaRS; STK32B; human.
DR GenomeRNAi; 55351; -.
DR Pharos; Q9NY57; Tchem.
DR PRO; PR:Q9NY57; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NY57; protein.
DR Bgee; ENSG00000152953; Expressed in secondary oocyte and 109 other tissues.
DR ExpressionAtlas; Q9NY57; baseline and differential.
DR Genevisible; Q9NY57; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..414
FT /note="Serine/threonine-protein kinase 32B"
FT /id="PRO_0000232413"
FT DOMAIN 23..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_051997"
FT VARIANT 35
FT /note="G -> E (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041166"
FT VARIANT 198
FT /note="R -> G (in dbSNP:rs3733182)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_025899"
FT VARIANT 244
FT /note="R -> H (in dbSNP:rs35207488)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041167"
FT VARIANT 310
FT /note="D -> V (in dbSNP:rs56259884)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041168"
FT VARIANT 342
FT /note="K -> T (in dbSNP:rs55961955)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041169"
SQ SEQUENCE 414 AA; 47883 MW; 8FCD58A67EF09B0E CRC64;
MGGNHSHKPP VFDENEEVNF DHFQILRAIG KGSFGKVCIV QKRDTKKMYA MKYMNKQKCI
ERDEVRNVFR ELQIMQGLEH PFLVNLWYSF QDEEDMFMVV DLLLGGDLRY HLQQNVHFTE
GTVKLYICEL ALALEYLQRY HIIHRDIKPD NILLDEHGHV HITDFNIATV VKGAERASSM
AGTKPYMAPE VFQVYMDRGP GYSYPVDWWS LGITAYELLR GWRPYEIHSV TPIDEILNMF
KVERVHYSST WCKGMVALLR KLLTKDPESR VSSLHDIQSV PYLADMNWDA VFKKALMPGF
VPNKGRLNCD PTFELEEMIL ESKPLHKKKK RLAKNRSRDG TKDSCPLNGH LQHCLETVRE
EFIIFNREKL RRQQGQGSQL LDTDSRGGGQ AQSKLQDGCN NNLLTHTCTR GCSS
