SLK_HUMAN
ID SLK_HUMAN Reviewed; 1235 AA.
AC Q9H2G2; D3DRA0; D3DRA1; O00211; Q6P1Z4; Q86WU7; Q86WW1; Q92603; Q9NQL0;
AC Q9NQL1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=STE20-like serine/threonine-protein kinase;
DE Short=STE20-like kinase;
DE Short=hSLK;
DE EC=2.7.11.1;
DE AltName: Full=CTCL tumor antigen se20-9;
DE AltName: Full=STE20-related serine/threonine-protein kinase;
DE Short=STE20-related kinase;
DE AltName: Full=Serine/threonine-protein kinase 2;
GN Name=SLK; Synonyms=KIAA0204, STK2;
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 2), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND MUTAGENESIS OF LYS-63.
RC TISSUE=Lung carcinoma;
RX PubMed=10699464; DOI=10.1016/s0167-4889(99)00164-0;
RA Yamada E., Tsujikawa K., Itoh S., Kameda Y., Kohama Y., Yamamoto H.;
RT "Molecular cloning and characterization of a novel human STE20-like kinase,
RT hSLK.";
RL Biochim. Biophys. Acta 1495:250-262(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-330; SER-565 AND
RP SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-347; SER-348;
RP SER-571; SER-777; SER-779 AND SER-818, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-344 AND SER-565, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-571; SER-779 AND
RP THR-1097, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-347; SER-348; SER-565
RP AND SER-571, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-189; SER-341;
RP SER-518; SER-565; SER-571; SER-779; THR-814 AND SER-818, AND IDENTIFICATION
RP BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372; SER-518; SER-565;
RP THR-569 AND SER-571, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-405; TYR-552; GLN-604; GLY-658;
RP THR-679; ASN-683 AND ILE-697.
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 [18]
RP VARIANT GLU-472--1235-SER DEL.
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 [19]
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 -!- FUNCTION: Mediates apoptosis and actin stress fiber dissolution.
CC {ECO:0000250}.
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 -!- INTERACTION:
CC Q9H2G2; Q9H2G2: SLK; NbExp=3; IntAct=EBI-1022272, EBI-1022272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H2G2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H2G2-2; Sequence=VSP_018100;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression is found
CC in heart and in skeletal muscle. {ECO:0000269|PubMed:10699464}.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:10699464}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47762.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 611.; Evidence={ECO:0000305};
CC Sequence=AAH47885.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 422.; Evidence={ECO:0000305};
CC Sequence=AAH64804.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 614.; Evidence={ECO:0000305};
CC Sequence=BAA13195.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB002804; BAA19655.1; -; mRNA.
DR EMBL; AF273048; AAG34908.1; -; mRNA.
DR EMBL; D86959; BAA13195.2; ALT_SEQ; mRNA.
DR EMBL; AL360170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49615.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49616.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49617.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49618.1; -; Genomic_DNA.
DR EMBL; BC047762; AAH47762.1; ALT_SEQ; mRNA.
DR EMBL; BC047885; AAH47885.1; ALT_SEQ; mRNA.
DR EMBL; BC064804; AAH64804.1; ALT_SEQ; mRNA.
DR EMBL; BC111565; AAI11566.1; -; mRNA.
DR CCDS; CCDS7553.1; -. [Q9H2G2-1]
DR CCDS; CCDS76334.1; -. [Q9H2G2-2]
DR RefSeq; NP_001291672.1; NM_001304743.1. [Q9H2G2-2]
DR RefSeq; NP_055535.2; NM_014720.3. [Q9H2G2-1]
DR PDB; 2J51; X-ray; 2.10 A; A=19-320.
DR PDB; 2JFL; X-ray; 2.20 A; A=19-320.
DR PDB; 2JFM; X-ray; 2.85 A; A=19-320.
DR PDB; 2UV2; X-ray; 2.30 A; A=19-320.
DR PDB; 4USF; X-ray; 1.75 A; A/B=19-320.
DR PDB; 6HVD; X-ray; 1.63 A; A=19-320.
DR PDBsum; 2J51; -.
DR PDBsum; 2JFL; -.
DR PDBsum; 2JFM; -.
DR PDBsum; 2UV2; -.
DR PDBsum; 4USF; -.
DR PDBsum; 6HVD; -.
DR AlphaFoldDB; Q9H2G2; -.
DR PCDDB; Q9H2G2; -.
DR SMR; Q9H2G2; -.
DR BioGRID; 115096; 75.
DR IntAct; Q9H2G2; 36.
DR MINT; Q9H2G2; -.
DR STRING; 9606.ENSP00000358770; -.
DR BindingDB; Q9H2G2; -.
DR ChEMBL; CHEMBL4202; -.
DR DrugBank; DB07853; 2-[4-[4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl]iminocyclohexa-2,5-dien-1-yl]acetonitrile.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB07664; K-00546.
DR DrugCentral; Q9H2G2; -.
DR GuidetoPHARMACOLOGY; 2200; -.
DR GlyGen; Q9H2G2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2G2; -.
DR MetOSite; Q9H2G2; -.
DR PhosphoSitePlus; Q9H2G2; -.
DR SwissPalm; Q9H2G2; -.
DR BioMuta; SLK; -.
DR DMDM; 74762732; -.
DR EPD; Q9H2G2; -.
DR jPOST; Q9H2G2; -.
DR MassIVE; Q9H2G2; -.
DR MaxQB; Q9H2G2; -.
DR PaxDb; Q9H2G2; -.
DR PeptideAtlas; Q9H2G2; -.
DR PRIDE; Q9H2G2; -.
DR ProteomicsDB; 80544; -. [Q9H2G2-1]
DR ProteomicsDB; 80545; -. [Q9H2G2-2]
DR Antibodypedia; 18194; 294 antibodies from 34 providers.
DR DNASU; 9748; -.
DR Ensembl; ENST00000335753.8; ENSP00000336824.4; ENSG00000065613.15. [Q9H2G2-2]
DR Ensembl; ENST00000369755.4; ENSP00000358770.3; ENSG00000065613.15. [Q9H2G2-1]
DR GeneID; 9748; -.
DR KEGG; hsa:9748; -.
DR MANE-Select; ENST00000369755.4; ENSP00000358770.3; NM_014720.4; NP_055535.2.
DR UCSC; uc001kxo.2; human. [Q9H2G2-1]
DR CTD; 9748; -.
DR DisGeNET; 9748; -.
DR GeneCards; SLK; -.
DR HGNC; HGNC:11088; SLK.
DR HPA; ENSG00000065613; Low tissue specificity.
DR MIM; 616563; gene.
DR neXtProt; NX_Q9H2G2; -.
DR OpenTargets; ENSG00000065613; -.
DR PharmGKB; PA35941; -.
DR VEuPathDB; HostDB:ENSG00000065613; -.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156184; -.
DR HOGENOM; CLU_001965_3_0_1; -.
DR InParanoid; Q9H2G2; -.
DR OMA; HEAYFIE; -.
DR OrthoDB; 851098at2759; -.
DR PhylomeDB; Q9H2G2; -.
DR TreeFam; TF351445; -.
DR PathwayCommons; Q9H2G2; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q9H2G2; -.
DR SIGNOR; Q9H2G2; -.
DR BioGRID-ORCS; 9748; 21 hits in 1109 CRISPR screens.
DR ChiTaRS; SLK; human.
DR EvolutionaryTrace; Q9H2G2; -.
DR GeneWiki; SLK_(gene); -.
DR GenomeRNAi; 9748; -.
DR Pharos; Q9H2G2; Tchem.
DR PRO; PR:Q9H2G2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9H2G2; protein.
DR Bgee; ENSG00000065613; Expressed in esophagus squamous epithelium and 211 other tissues.
DR ExpressionAtlas; Q9H2G2; baseline and differential.
DR Genevisible; Q9H2G2; HS.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001943; UVR_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
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.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Coiled coil;
KW Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1235
FT /note="STE20-like serine/threonine-protein kinase"
FT /id="PRO_0000233239"
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 875..910
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT REGION 309..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 826..1069
FT /evidence="ECO:0000255"
FT COILED 1109..1183
FT /evidence="ECO:0000255"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 438..439
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08815"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54988"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 814
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1097
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 929..959
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10699464,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9039502"
FT /id="VSP_018100"
FT VARIANT 405
FT /note="Q -> K (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041080"
FT VARIANT 472..1235
FT /note="Missing (found in a patient with global
FT developmental delay; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28940097"
FT /id="VAR_084656"
FT VARIANT 552
FT /note="C -> Y (in dbSNP:rs805657)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041081"
FT VARIANT 604
FT /note="E -> Q (in an ovarian serous carcinoma sample;
FT somatic mutation; dbSNP:rs190220654)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041082"
FT VARIANT 658
FT /note="A -> G (in dbSNP:rs56400929)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041083"
FT VARIANT 666
FT /note="G -> E (in dbSNP:rs7071400)"
FT /id="VAR_051666"
FT VARIANT 679
FT /note="I -> T (in dbSNP:rs34326537)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041084"
FT VARIANT 683
FT /note="K -> N (in dbSNP:rs35389916)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041085"
FT VARIANT 697
FT /note="T -> I (in dbSNP:rs3740469)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041086"
FT MUTAGEN 63
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10699464"
FT CONFLICT 5
FT /note="N -> S (in Ref. 3; BAA13195)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6HVD"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6HVD"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:2J51"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:6HVD"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 263..272
FT /evidence="ECO:0007829|PDB:6HVD"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6HVD"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:6HVD"
SQ SEQUENCE 1235 AA; 142695 MW; 53A43E7CA29B0ED3 CRC64;
MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EDFWEIIGEL GDGAFGKVYK AQNKETSVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTES QIQVVCKQTL DALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP
MRVLLKIAKS EPPTLAQPSR WSSNFKDFLK KCLEKNVDAR WTTSQLLQHP FVTVDSNKPI
RELIAEAKAE VTEEVEDGKE EDEEEETENS LPIPASKRAS SDLSIASSEE DKLSQNACIL
ESVSEKTERS NSEDKLNSKI LNEKPTTDEP EKAVEDINEH ITDAQLEAMT ELHDRTAVIK
ENEREKRPKL ENLPDTEDQE TVDINSVSEG KENNIMITLE TNIEHNLKSE EEKDQEKQQM
FENKLIKSEE IKDTILQTVD LVSQETGEKE ANIQAVDSEV GLTKEDTQEK LGEDDKTQKD
VISNTSDVIG TCEAADVAQK VDEDSAEDTQ SNDGKEVVEV GQKLINKPMV GPEAGGTKEV
PIKEIVEMNE IEEGKNKEQA INSSENIMDI NEEPGTTEGE EITESSSTEE MEVRSVVADT
DQKALGSEVQ DASKVTTQID KEKKEIPVSI KKEPEVTVVS QPTEPQPVLI PSININSDSG
ENKEEIGSLS KTETILPPES ENPKENDNDS GTGSTADTSS IDLNLSISSF LSKTKDSGSI
SLQETRRQKK TLKKTRKFIV DGVEVSVTTS KIVTDSDSKT EELRFLRRQE LRELRFLQKE
EQRAQQQLNS KLQQQREQIF RRFEQEMMSK KRQYDQEIEN LEKQQKQTIE RLEQEHTNRL
RDEAKRIKGE QEKELSKFQN MLKNRKKEVI NEVEKAPKEL RKELMKRRKE ELAQSQHAQE
QEFVQKQQQE LDGSLKKIIQ QQKAELANIE RECLNNKQQL MRAREAAIWE LEERHLQEKH
QLLKQQLKDQ YFMQRHQLLK RHEKETEQMQ RYNQRLIEEL KNRQTQERAR LPKIQRSEAK
TRMAMFKKSL RINSTATPDQ DRDKIKQFAA QEEKRQKNER MAQHQKHENQ MRDLQLQCEA
NVRELHQLQN EKCHLLVEHE TQKLKELDEE HSQELKEWRE KLRPRKKTLE EEFARKLQEQ
EVFFKMTGES ECLNPSTQSR ISKFYPIPSL HSTGS
