STK25_HUMAN
ID STK25_HUMAN Reviewed; 426 AA.
AC O00506; A8K6Z3; A8K7D2; B7Z9K1; Q15522; Q5BJF1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Serine/threonine-protein kinase 25;
DE EC=2.7.11.1;
DE AltName: Full=Ste20-like kinase;
DE AltName: Full=Sterile 20/oxidant stress-response kinase 1;
DE Short=SOK-1;
DE Short=Ste20/oxidant stress response kinase 1;
GN Name=STK25; Synonyms=SOK1, YSK1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8887545; DOI=10.1002/j.1460-2075.1996.tb00831.x;
RA Pombo C.M., Bonventre J.V., Molnar A., Kyriakis J., Force T.;
RT "Activation of a human Ste20-like kinase by oxidant stress defines a novel
RT stress response pathway.";
RL EMBO J. 15:4537-4546(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9160885; DOI=10.1038/sj.onc.1201043;
RA Osada S., Izawa M., Saito R., Mizuno K., Suzuki A., Hirai S., Ohno S.;
RT "YSK1, a novel mammalian protein kinase structurally related to Ste20 and
RT SPS1, but is not involved in the known MAPK pathways.";
RL Oncogene 14:2047-2057(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
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 [9]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-174, SUBCELLULAR
RP LOCATION, INTERACTION WITH GOLGA2, AND MUTAGENESIS OF LYS-49 AND ASP-158.
RX PubMed=15037601; DOI=10.1083/jcb.200310061;
RA Preisinger C., Short B., De Corte V., Bruyneel E., Haas A., Kopajtich R.,
RA Gettemans J., Barr F.A.;
RT "YSK1 is activated by the Golgi matrix protein GM130 and plays a role in
RT cell migration through its substrate 14-3-3zeta.";
RL J. Cell Biol. 164:1009-1020(2004).
RN [10]
RP INTERACTION WITH CTTNBP2NL.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Oxidant stress-activated serine/threonine kinase that may
CC play a role in the response to environmental stress. Targets to the
CC Golgi apparatus where it appears to regulate protein transport events,
CC cell adhesion, and polarity complexes important for cell migration.
CC {ECO:0000269|PubMed:15037601}.
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 -!- 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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Interaction with Golgi matrix protein GOLGA2 leads
CC to autophosphorylation on Thr-174, possibly as a consequence of
CC stabilization of dimer formation. The C-terminal non-catalytic region
CC inhibits the kinase activity. {ECO:0000269|PubMed:15037601}.
CC -!- SUBUNIT: Homodimer. Interacts with CTTNBP2NL.
CC {ECO:0000269|PubMed:15037601, ECO:0000269|PubMed:18782753}.
CC -!- INTERACTION:
CC O00506; Q9Y376: CAB39; NbExp=4; IntAct=EBI-618295, EBI-306905;
CC O00506; O95273: CCNDBP1; NbExp=3; IntAct=EBI-618295, EBI-748961;
CC O00506; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-618295, EBI-739624;
CC O00506; Q08379: GOLGA2; NbExp=16; IntAct=EBI-618295, EBI-618309;
CC O00506; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-618295, EBI-5916454;
CC O00506; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-618295, EBI-8638439;
CC O00506; Q9BUL8: PDCD10; NbExp=30; IntAct=EBI-618295, EBI-740195;
CC O00506; O43815: STRN; NbExp=5; IntAct=EBI-618295, EBI-1046642;
CC O00506; P14373: TRIM27; NbExp=6; IntAct=EBI-618295, EBI-719493;
CC O00506; P63104: YWHAZ; NbExp=2; IntAct=EBI-618295, EBI-347088;
CC O00506; Q62839: Golga2; Xeno; NbExp=2; IntAct=EBI-618295, EBI-618335;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15037601}. Golgi
CC apparatus {ECO:0000269|PubMed:15037601}. Note=Localizes to the Golgi
CC apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O00506-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00506-2; Sequence=VSP_054397;
CC Name=3;
CC IsoId=O00506-3; Sequence=VSP_054683;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels are found in
CC testis, large intestine, brain and stomach followed by heart and lung.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/stk25/";
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DR EMBL; X99325; CAA67700.1; -; mRNA.
DR EMBL; D63780; BAA20420.1; -; mRNA.
DR EMBL; AK291808; BAF84497.1; -; mRNA.
DR EMBL; AK291947; BAF84636.1; -; mRNA.
DR EMBL; AK315966; BAH14337.1; -; mRNA.
DR EMBL; BT019961; AAV38764.1; -; mRNA.
DR EMBL; AC110299; AAY14683.1; -; Genomic_DNA.
DR EMBL; DQ093965; AAY88740.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71265.1; -; Genomic_DNA.
DR EMBL; BC007852; AAH07852.1; -; mRNA.
DR EMBL; BC091505; AAH91505.1; -; mRNA.
DR CCDS; CCDS2549.1; -. [O00506-1]
DR CCDS; CCDS63199.1; -. [O00506-3]
DR CCDS; CCDS63200.1; -. [O00506-2]
DR PIR; S71886; S71886.
DR RefSeq; NP_001258906.1; NM_001271977.1. [O00506-1]
DR RefSeq; NP_001258907.1; NM_001271978.1. [O00506-1]
DR RefSeq; NP_001258908.1; NM_001271979.1. [O00506-2]
DR RefSeq; NP_001258909.1; NM_001271980.1. [O00506-2]
DR RefSeq; NP_001269234.1; NM_001282305.1. [O00506-3]
DR RefSeq; NP_001269236.1; NM_001282307.1. [O00506-3]
DR RefSeq; NP_001269237.1; NM_001282308.1. [O00506-3]
DR RefSeq; NP_006365.2; NM_006374.4. [O00506-1]
DR PDB; 2XIK; X-ray; 1.97 A; A=1-293.
DR PDB; 3W8H; X-ray; 2.43 A; B=355-426.
DR PDB; 4NZW; X-ray; 3.58 A; B=1-293.
DR PDB; 7Z4V; X-ray; 1.64 A; A=1-294.
DR PDBsum; 2XIK; -.
DR PDBsum; 3W8H; -.
DR PDBsum; 4NZW; -.
DR PDBsum; 7Z4V; -.
DR AlphaFoldDB; O00506; -.
DR SMR; O00506; -.
DR BioGRID; 115757; 78.
DR DIP; DIP-34269N; -.
DR IntAct; O00506; 64.
DR MINT; O00506; -.
DR STRING; 9606.ENSP00000325748; -.
DR BindingDB; O00506; -.
DR ChEMBL; CHEMBL5552; -.
DR DrugCentral; O00506; -.
DR GlyGen; O00506; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00506; -.
DR PhosphoSitePlus; O00506; -.
DR SwissPalm; O00506; -.
DR BioMuta; STK25; -.
DR EPD; O00506; -.
DR jPOST; O00506; -.
DR MassIVE; O00506; -.
DR MaxQB; O00506; -.
DR PaxDb; O00506; -.
DR PeptideAtlas; O00506; -.
DR PRIDE; O00506; -.
DR ProteomicsDB; 1868; -.
DR ProteomicsDB; 47947; -. [O00506-1]
DR ProteomicsDB; 7036; -.
DR Antibodypedia; 34565; 264 antibodies from 32 providers.
DR DNASU; 10494; -.
DR Ensembl; ENST00000316586.9; ENSP00000325748.4; ENSG00000115694.15. [O00506-1]
DR Ensembl; ENST00000401869.5; ENSP00000385687.1; ENSG00000115694.15. [O00506-1]
DR Ensembl; ENST00000403346.7; ENSP00000384162.3; ENSG00000115694.15. [O00506-1]
DR Ensembl; ENST00000405585.5; ENSP00000385541.1; ENSG00000115694.15. [O00506-2]
DR Ensembl; ENST00000405883.7; ENSP00000384444.3; ENSG00000115694.15. [O00506-2]
DR Ensembl; ENST00000535007.5; ENSP00000446008.1; ENSG00000115694.15. [O00506-3]
DR Ensembl; ENST00000543554.5; ENSP00000444886.1; ENSG00000115694.15. [O00506-3]
DR GeneID; 10494; -.
DR KEGG; hsa:10494; -.
DR MANE-Select; ENST00000316586.9; ENSP00000325748.4; NM_001271977.2; NP_001258906.1.
DR UCSC; uc002wbm.5; human. [O00506-1]
DR CTD; 10494; -.
DR DisGeNET; 10494; -.
DR GeneCards; STK25; -.
DR HGNC; HGNC:11404; STK25.
DR HPA; ENSG00000115694; Group enriched (skeletal muscle, tongue).
DR MIM; 602255; gene.
DR neXtProt; NX_O00506; -.
DR OpenTargets; ENSG00000115694; -.
DR PharmGKB; PA36211; -.
DR VEuPathDB; HostDB:ENSG00000115694; -.
DR eggNOG; KOG0201; Eukaryota.
DR GeneTree; ENSGT00940000153476; -.
DR InParanoid; O00506; -.
DR OMA; REFANQH; -.
DR OrthoDB; 1115738at2759; -.
DR PhylomeDB; O00506; -.
DR TreeFam; TF354217; -.
DR PathwayCommons; O00506; -.
DR SignaLink; O00506; -.
DR SIGNOR; O00506; -.
DR BioGRID-ORCS; 10494; 11 hits in 1114 CRISPR screens.
DR ChiTaRS; STK25; human.
DR GeneWiki; STK25; -.
DR GenomeRNAi; 10494; -.
DR Pharos; O00506; Tchem.
DR PRO; PR:O00506; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O00506; protein.
DR Bgee; ENSG00000115694; Expressed in hindlimb stylopod muscle and 181 other tissues.
DR ExpressionAtlas; O00506; baseline and differential.
DR Genevisible; O00506; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; 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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
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:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0051683; P:establishment of Golgi localization; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0051645; P:Golgi localization; IDA:UniProtKB.
DR GO; GO:0090168; P:Golgi reassembly; IMP:UniProtKB.
DR GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IGI:UniProtKB.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd06642; STKc_STK25; 1.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035060; STK_STK25.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW Golgi apparatus; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..426
FT /note="Serine/threonine-protein kinase 25"
FT /id="PRO_0000086713"
FT DOMAIN 20..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 291..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15037601"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W1"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054683"
FT VAR_SEQ 11..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054397"
FT VARIANT 64
FT /note="Q -> H (in dbSNP:rs34341643)"
FT /id="VAR_051674"
FT MUTAGEN 49
FT /note="K->R: Loss of kinase activity and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15037601"
FT MUTAGEN 158
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:15037601"
FT CONFLICT 347..348
FT /note="EP -> DA (in Ref. 1; CAA67700)"
FT /evidence="ECO:0000305"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:2XIK"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:2XIK"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 114..133
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2XIK"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:2XIK"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:2XIK"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 281..291
FT /evidence="ECO:0007829|PDB:2XIK"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3W8H"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:3W8H"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3W8H"
FT HELIX 381..396
FT /evidence="ECO:0007829|PDB:3W8H"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:3W8H"
SQ SEQUENCE 426 AA; 48112 MW; 183CE5700FCEA716 CRC64;
MAHLRGFANQ HSRVDPEELF TKLDRIGKGS FGEVYKGIDN HTKEVVAIKI IDLEEAEDEI
EDIQQEITVL SQCDSPYITR YFGSYLKSTK LWIIMEYLGG GSALDLLKPG PLEETYIATI
LREILKGLDY LHSERKIHRD IKAANVLLSE QGDVKLADFG VAGQLTDTQI KRNTFVGTPF
WMAPEVIKQS AYDFKADIWS LGITAIELAK GEPPNSDLHP MRVLFLIPKN SPPTLEGQHS
KPFKEFVEAC LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW KSEGHGEESS
SEDSDIDGEA EDGEQGPIWT FPPTIRPSPH SKLHKGTALH SSQKPAEPVK RQPRSQCLST
LVRPVFGELK EKHKQSGGSV GALEELENAF SLAEESCPGI SDKLMVHLVE RVQRFSHNRN
HLTSTR
