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   27-MAR-2024, entry version 198.
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 472-GLU--SER-1235 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   PDB; 8BEM; X-ray; 2.60 A; A/B/D/G=19-319.
DR   PDBsum; 2J51; -.
DR   PDBsum; 2JFL; -.
DR   PDBsum; 2JFM; -.
DR   PDBsum; 2UV2; -.
DR   PDBsum; 4USF; -.
DR   PDBsum; 6HVD; -.
DR   PDBsum; 8BEM; -.
DR   AlphaFoldDB; Q9H2G2; -.
DR   PCDDB; Q9H2G2; -.
DR   SMR; Q9H2G2; -.
DR   BioGRID; 115096; 168.
DR   IntAct; Q9H2G2; 37.
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   CPTAC; CPTAC-2845; -.
DR   CPTAC; CPTAC-2948; -.
DR   EPD; Q9H2G2; -.
DR   jPOST; Q9H2G2; -.
DR   MassIVE; Q9H2G2; -.
DR   MaxQB; Q9H2G2; -.
DR   PaxDb; 9606-ENSP00000358770; -.
DR   PeptideAtlas; Q9H2G2; -.
DR   ProteomicsDB; 80544; -. [Q9H2G2-1]
DR   ProteomicsDB; 80545; -. [Q9H2G2-2]
DR   Pumba; Q9H2G2; -.
DR   Antibodypedia; 18194; 316 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   AGR; HGNC:11088; -.
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; KTRAQMF; -.
DR   OrthoDB; 2880940at2759; -.
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; 24 hits in 1189 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 213 other cell types or tissues.
DR   ExpressionAtlas; Q9H2G2; baseline and differential.
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: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   CDD; cd06643; STKc_SLK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF12474; PKK; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
DR   Genevisible; Q9H2G2; HS.
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; uncertain 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
//