ST32A_HUMAN
ID ST32A_HUMAN Reviewed; 396 AA.
AC Q8WU08; B3KSY0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Serine/threonine-protein kinase 32A;
DE EC=2.7.11.1;
DE AltName: Full=Yet another novel kinase 1;
GN Name=STK32A; Synonyms=YANK1;
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}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND 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 [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala {ECO:0000269|PubMed:15489334};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
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 [5]
RP MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-2.
RX PubMed=25043870; DOI=10.1016/j.ab.2014.07.006;
RA Takamitsu E., Fukunaga K., Iio Y., Moriya K., Utsumi T.;
RT "Cell-free identification of novel N-myristoylated proteins from
RT complementary DNA resources using bioorthogonal myristic acid analogues.";
RL Anal. Biochem. 464:83-93(2014).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-58; PHE-89 AND ILE-316.
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 -!- INTERACTION:
CC Q8WU08-2; Q16543: CDC37; NbExp=3; IntAct=EBI-13046508, EBI-295634;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
CC {ECO:0000269|PubMed:25043870}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000305};
CC IsoId=Q8WU08-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8WU08-2; Sequence=VSP_051992, VSP_051993;
CC Name=3 {ECO:0000305};
CC IsoId=Q8WU08-3; Sequence=VSP_051994, VSP_051995;
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; AK094580; BAG52892.1; -; mRNA.
DR EMBL; AC008740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61827.1; -; Genomic_DNA.
DR CCDS; CCDS47299.1; -. [Q8WU08-1]
DR CCDS; CCDS54931.1; -. [Q8WU08-2]
DR RefSeq; NP_001106195.1; NM_001112724.1. [Q8WU08-1]
DR RefSeq; NP_659438.1; NM_145001.3. [Q8WU08-2]
DR PDB; 4FR4; X-ray; 2.29 A; A/B/C/D/E/F=9-390.
DR PDBsum; 4FR4; -.
DR AlphaFoldDB; Q8WU08; -.
DR SMR; Q8WU08; -.
DR BioGRID; 128429; 5.
DR IntAct; Q8WU08; 15.
DR STRING; 9606.ENSP00000381535; -.
DR BindingDB; Q8WU08; -.
DR ChEMBL; CHEMBL6150; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8WU08; -.
DR iPTMnet; Q8WU08; -.
DR PhosphoSitePlus; Q8WU08; -.
DR BioMuta; STK32A; -.
DR DMDM; 93140693; -.
DR MassIVE; Q8WU08; -.
DR PaxDb; Q8WU08; -.
DR PeptideAtlas; Q8WU08; -.
DR PRIDE; Q8WU08; -.
DR ProteomicsDB; 74618; -. [Q8WU08-1]
DR ProteomicsDB; 74619; -. [Q8WU08-2]
DR ProteomicsDB; 74620; -. [Q8WU08-3]
DR Antibodypedia; 27607; 235 antibodies from 27 providers.
DR DNASU; 202374; -.
DR Ensembl; ENST00000397936.8; ENSP00000381030.3; ENSG00000169302.16. [Q8WU08-1]
DR Ensembl; ENST00000626951.2; ENSP00000487441.1; ENSG00000169302.16. [Q8WU08-2]
DR GeneID; 202374; -.
DR KEGG; hsa:202374; -.
DR MANE-Select; ENST00000397936.8; ENSP00000381030.3; NM_001112724.2; NP_001106195.1.
DR UCSC; uc010jgn.2; human. [Q8WU08-1]
DR CTD; 202374; -.
DR DisGeNET; 202374; -.
DR GeneCards; STK32A; -.
DR HGNC; HGNC:28317; STK32A.
DR HPA; ENSG00000169302; Tissue enhanced (brain).
DR neXtProt; NX_Q8WU08; -.
DR OpenTargets; ENSG00000169302; -.
DR PharmGKB; PA134932545; -.
DR VEuPathDB; HostDB:ENSG00000169302; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000158185; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q8WU08; -.
DR OMA; MRITTMA; -.
DR OrthoDB; 923710at2759; -.
DR PhylomeDB; Q8WU08; -.
DR TreeFam; TF313395; -.
DR PathwayCommons; Q8WU08; -.
DR SignaLink; Q8WU08; -.
DR BioGRID-ORCS; 202374; 11 hits in 1105 CRISPR screens.
DR ChiTaRS; STK32A; human.
DR GenomeRNAi; 202374; -.
DR Pharos; Q8WU08; Tchem.
DR PRO; PR:Q8WU08; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8WU08; protein.
DR Bgee; ENSG00000169302; Expressed in sural nerve and 123 other tissues.
DR ExpressionAtlas; Q8WU08; baseline and differential.
DR Genevisible; Q8WU08; HS.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Kinase;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25043870"
FT CHAIN 2..396
FT /note="Serine/threonine-protein kinase 32A"
FT /id="PRO_0000232411"
FT DOMAIN 23..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 373..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Polar residues"
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25043870"
FT VAR_SEQ 158..166
FT /note="GHVHITDFN -> DTWLSYKSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051992"
FT VAR_SEQ 167..396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051993"
FT VAR_SEQ 345..358
FT /note="TCLLQEHLDSVQKE -> VSRSPPNSGSWVSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051994"
FT VAR_SEQ 359..396
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_051995"
FT VARIANT 58
FT /note="K -> M (in dbSNP:rs35852718)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041163"
FT VARIANT 89
FT /note="S -> F (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041164"
FT VARIANT 316
FT /note="M -> I (in a lung neuroendocrine carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041165"
FT MUTAGEN 2
FT /note="G->A: Localizes to cytoplasm."
FT /evidence="ECO:0000269|PubMed:25043870"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:4FR4"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:4FR4"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 343..358
FT /evidence="ECO:0007829|PDB:4FR4"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:4FR4"
SQ SEQUENCE 396 AA; 46369 MW; 5ED718F0D3A7A48C CRC64;
MGANTSRKPP VFDENEDVNF DHFEILRAIG KGSFGKVCIV QKNDTKKMYA MKYMNKQKCV
ERNEVRNVFK ELQIMQGLEH PFLVNLWYSF QDEEDMFMVV DLLLGGDLRY HLQQNVHFKE
ETVKLFICEL VMALDYLQNQ RIIHRDMKPD NILLDEHGHV HITDFNIAAM LPRETQITTM
AGTKPYMAPE MFSSRKGAGY SFAVDWWSLG VTAYELLRGR RPYHIRSSTS SKEIVHTFET
TVVTYPSAWS QEMVSLLKKL LEPNPDQRFS QLSDVQNFPY MNDINWDAVF QKRLIPGFIP
NKGRLNCDPT FELEEMILES KPLHKKKKRL AKKEKDMRKC DSSQTCLLQE HLDSVQKEFI
IFNREKVNRD FNKRQPNLAL EQTKDPQGED GQNNNL
