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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
 
 
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