Full text data of SLK
SLK
(KIAA0204, STK2)
[Confidence: low (only semi-automatic identification from reviews)]
STE20-like serine/threonine-protein kinase; STE20-like kinase; hSLK; 2.7.11.1 (CTCL tumor antigen se20-9; STE20-related serine/threonine-protein kinase; STE20-related kinase; Serine/threonine-protein kinase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
STE20-like serine/threonine-protein kinase; STE20-like kinase; hSLK; 2.7.11.1 (CTCL tumor antigen se20-9; STE20-related serine/threonine-protein kinase; STE20-related kinase; Serine/threonine-protein kinase 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H2G2
ID SLK_HUMAN Reviewed; 1235 AA.
AC Q9H2G2; D3DRA0; D3DRA1; O00211; Q6P1Z4; Q86WU7; Q86WW1; Q92603;
read moreAC Q9NQL0; Q9NQL1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 121.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT kinase, 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.021386498;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D.,
RA Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated
RT 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.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP AND SER-655, AND MASS SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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
RP SER-565, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RP AND THR-1097, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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;
RP SER-565 AND SER-571, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Mediates apoptosis and actin stress fiber dissolution
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-1022272, EBI-1022272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
CC found in heart and in skeletal muscle.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47762.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 611;
CC Sequence=AAH47885.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 422;
CC Sequence=AAH64804.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 614;
CC Sequence=BAA13195.2; Type=Frameshift; Positions=1172;
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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; CAH70403.1; -; Genomic_DNA.
DR EMBL; AL138761; CAH70403.1; JOINED; Genomic_DNA.
DR EMBL; AL360170; CAH70404.1; -; Genomic_DNA.
DR EMBL; AL138761; CAH70404.1; JOINED; Genomic_DNA.
DR EMBL; AL138761; CAI12395.1; -; Genomic_DNA.
DR EMBL; AL360170; CAI12395.1; JOINED; Genomic_DNA.
DR EMBL; AL138761; CAI12396.1; -; Genomic_DNA.
DR EMBL; AL360170; CAI12396.1; JOINED; 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 RefSeq; NP_055535.2; NM_014720.2.
DR RefSeq; XP_005270358.1; XM_005270301.1.
DR UniGene; Hs.591922; -.
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 PDBsum; 2J51; -.
DR PDBsum; 2JFL; -.
DR PDBsum; 2JFM; -.
DR PDBsum; 2UV2; -.
DR ProteinModelPortal; Q9H2G2; -.
DR SMR; Q9H2G2; 21-308.
DR IntAct; Q9H2G2; 5.
DR MINT; MINT-4539212; -.
DR STRING; 9606.ENSP00000358770; -.
DR BindingDB; Q9H2G2; -.
DR ChEMBL; CHEMBL4202; -.
DR GuidetoPHARMACOLOGY; 2200; -.
DR PhosphoSite; Q9H2G2; -.
DR DMDM; 74762732; -.
DR PaxDb; Q9H2G2; -.
DR PRIDE; Q9H2G2; -.
DR Ensembl; ENST00000335753; ENSP00000336824; ENSG00000065613.
DR Ensembl; ENST00000369755; ENSP00000358770; ENSG00000065613.
DR GeneID; 9748; -.
DR KEGG; hsa:9748; -.
DR UCSC; uc001kxo.1; human.
DR CTD; 9748; -.
DR GeneCards; GC10P105716; -.
DR HGNC; HGNC:11088; SLK.
DR HPA; HPA015757; -.
DR neXtProt; NX_Q9H2G2; -.
DR PharmGKB; PA35941; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG052712; -.
DR InParanoid; Q9H2G2; -.
DR KO; K08836; -.
DR OMA; NIMITLE; -.
DR OrthoDB; EOG7CNZF6; -.
DR PhylomeDB; Q9H2G2; -.
DR SignaLink; Q9H2G2; -.
DR EvolutionaryTrace; Q9H2G2; -.
DR GeneWiki; SLK_(gene); -.
DR GenomeRNAi; 9748; -.
DR NextBio; 36684; -.
DR PMAP-CutDB; Q9H2G2; -.
DR PRO; PR:Q9H2G2; -.
DR Bgee; Q9H2G2; -.
DR CleanEx; HS_SLK; -.
DR Genevestigator; Q9H2G2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
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;
KW Coiled coil; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 1235 STE20-like serine/threonine-protein
FT kinase.
FT /FTId=PRO_0000233239.
FT DOMAIN 34 292 Protein kinase.
FT DOMAIN 875 910 UVR.
FT NP_BIND 40 48 ATP (By similarity).
FT COILED 826 1069 Potential.
FT COILED 1109 1183 Potential.
FT COMPBIAS 16 19 Poly-Lys.
FT COMPBIAS 302 652 Glu-rich.
FT ACT_SITE 155 155 Proton acceptor (By similarity).
FT BINDING 63 63 ATP (By similarity).
FT SITE 438 439 Cleavage; by caspase-3 (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 330 330 Phosphoserine.
FT MOD_RES 344 344 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 348 348 Phosphoserine.
FT MOD_RES 354 354 Phosphoserine (By similarity).
FT MOD_RES 565 565 Phosphoserine.
FT MOD_RES 571 571 Phosphoserine.
FT MOD_RES 655 655 Phosphoserine.
FT MOD_RES 777 777 Phosphoserine.
FT MOD_RES 779 779 Phosphoserine.
FT MOD_RES 818 818 Phosphoserine.
FT MOD_RES 1097 1097 Phosphothreonine.
FT VAR_SEQ 929 959 Missing (in isoform 2).
FT /FTId=VSP_018100.
FT VARIANT 405 405 Q -> K (in a lung adenocarcinoma sample;
FT somatic mutation).
FT /FTId=VAR_041080.
FT VARIANT 552 552 C -> Y (in dbSNP:rs805657).
FT /FTId=VAR_041081.
FT VARIANT 604 604 E -> Q (in an ovarian serous carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_041082.
FT VARIANT 658 658 A -> G (in dbSNP:rs56400929).
FT /FTId=VAR_041083.
FT VARIANT 666 666 G -> E (in dbSNP:rs7071400).
FT /FTId=VAR_051666.
FT VARIANT 679 679 I -> T (in dbSNP:rs34326537).
FT /FTId=VAR_041084.
FT VARIANT 683 683 K -> N (in dbSNP:rs35389916).
FT /FTId=VAR_041085.
FT VARIANT 697 697 T -> I (in dbSNP:rs3740469).
FT /FTId=VAR_041086.
FT MUTAGEN 63 63 K->R: Loss of activity.
FT CONFLICT 5 5 N -> S (in Ref. 3; BAA13195).
FT STRAND 25 28
FT HELIX 30 32
FT STRAND 34 43
FT STRAND 46 53
FT TURN 54 56
FT STRAND 59 66
FT STRAND 68 70
FT HELIX 73 85
FT STRAND 94 100
FT STRAND 103 109
FT HELIX 116 123
FT HELIX 129 148
FT HELIX 158 160
FT STRAND 161 163
FT STRAND 169 171
FT HELIX 181 187
FT HELIX 199 202
FT TURN 207 209
FT TURN 212 214
FT HELIX 215 230
FT TURN 234 237
FT HELIX 240 242
FT HELIX 243 249
FT HELIX 258 260
FT HELIX 263 272
FT TURN 277 279
FT HELIX 283 286
FT HELIX 290 292
FT HELIX 298 307
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
//
ID SLK_HUMAN Reviewed; 1235 AA.
AC Q9H2G2; D3DRA0; D3DRA1; O00211; Q6P1Z4; Q86WU7; Q86WW1; Q92603;
read moreAC Q9NQL0; Q9NQL1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 121.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT kinase, 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.021386498;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D.,
RA Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated
RT 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.
RT The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
RT analysis of 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RP AND SER-655, AND MASS SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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
RP SER-565, AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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
RP AND THR-1097, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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;
RP SER-565 AND SER-571, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Mediates apoptosis and actin stress fiber dissolution
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-1022272, EBI-1022272;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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
CC found in heart and in skeletal muscle.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC -!- PTM: Autophosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47762.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 611;
CC Sequence=AAH47885.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 422;
CC Sequence=AAH64804.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 614;
CC Sequence=BAA13195.2; Type=Frameshift; Positions=1172;
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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; CAH70403.1; -; Genomic_DNA.
DR EMBL; AL138761; CAH70403.1; JOINED; Genomic_DNA.
DR EMBL; AL360170; CAH70404.1; -; Genomic_DNA.
DR EMBL; AL138761; CAH70404.1; JOINED; Genomic_DNA.
DR EMBL; AL138761; CAI12395.1; -; Genomic_DNA.
DR EMBL; AL360170; CAI12395.1; JOINED; Genomic_DNA.
DR EMBL; AL138761; CAI12396.1; -; Genomic_DNA.
DR EMBL; AL360170; CAI12396.1; JOINED; 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 RefSeq; NP_055535.2; NM_014720.2.
DR RefSeq; XP_005270358.1; XM_005270301.1.
DR UniGene; Hs.591922; -.
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 PDBsum; 2J51; -.
DR PDBsum; 2JFL; -.
DR PDBsum; 2JFM; -.
DR PDBsum; 2UV2; -.
DR ProteinModelPortal; Q9H2G2; -.
DR SMR; Q9H2G2; 21-308.
DR IntAct; Q9H2G2; 5.
DR MINT; MINT-4539212; -.
DR STRING; 9606.ENSP00000358770; -.
DR BindingDB; Q9H2G2; -.
DR ChEMBL; CHEMBL4202; -.
DR GuidetoPHARMACOLOGY; 2200; -.
DR PhosphoSite; Q9H2G2; -.
DR DMDM; 74762732; -.
DR PaxDb; Q9H2G2; -.
DR PRIDE; Q9H2G2; -.
DR Ensembl; ENST00000335753; ENSP00000336824; ENSG00000065613.
DR Ensembl; ENST00000369755; ENSP00000358770; ENSG00000065613.
DR GeneID; 9748; -.
DR KEGG; hsa:9748; -.
DR UCSC; uc001kxo.1; human.
DR CTD; 9748; -.
DR GeneCards; GC10P105716; -.
DR HGNC; HGNC:11088; SLK.
DR HPA; HPA015757; -.
DR neXtProt; NX_Q9H2G2; -.
DR PharmGKB; PA35941; -.
DR eggNOG; COG0515; -.
DR HOVERGEN; HBG052712; -.
DR InParanoid; Q9H2G2; -.
DR KO; K08836; -.
DR OMA; NIMITLE; -.
DR OrthoDB; EOG7CNZF6; -.
DR PhylomeDB; Q9H2G2; -.
DR SignaLink; Q9H2G2; -.
DR EvolutionaryTrace; Q9H2G2; -.
DR GeneWiki; SLK_(gene); -.
DR GenomeRNAi; 9748; -.
DR NextBio; 36684; -.
DR PMAP-CutDB; Q9H2G2; -.
DR PRO; PR:Q9H2G2; -.
DR Bgee; Q9H2G2; -.
DR CleanEx; HS_SLK; -.
DR Genevestigator; Q9H2G2; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
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;
KW Coiled coil; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1 1235 STE20-like serine/threonine-protein
FT kinase.
FT /FTId=PRO_0000233239.
FT DOMAIN 34 292 Protein kinase.
FT DOMAIN 875 910 UVR.
FT NP_BIND 40 48 ATP (By similarity).
FT COILED 826 1069 Potential.
FT COILED 1109 1183 Potential.
FT COMPBIAS 16 19 Poly-Lys.
FT COMPBIAS 302 652 Glu-rich.
FT ACT_SITE 155 155 Proton acceptor (By similarity).
FT BINDING 63 63 ATP (By similarity).
FT SITE 438 439 Cleavage; by caspase-3 (By similarity).
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 330 330 Phosphoserine.
FT MOD_RES 344 344 Phosphoserine.
FT MOD_RES 347 347 Phosphoserine.
FT MOD_RES 348 348 Phosphoserine.
FT MOD_RES 354 354 Phosphoserine (By similarity).
FT MOD_RES 565 565 Phosphoserine.
FT MOD_RES 571 571 Phosphoserine.
FT MOD_RES 655 655 Phosphoserine.
FT MOD_RES 777 777 Phosphoserine.
FT MOD_RES 779 779 Phosphoserine.
FT MOD_RES 818 818 Phosphoserine.
FT MOD_RES 1097 1097 Phosphothreonine.
FT VAR_SEQ 929 959 Missing (in isoform 2).
FT /FTId=VSP_018100.
FT VARIANT 405 405 Q -> K (in a lung adenocarcinoma sample;
FT somatic mutation).
FT /FTId=VAR_041080.
FT VARIANT 552 552 C -> Y (in dbSNP:rs805657).
FT /FTId=VAR_041081.
FT VARIANT 604 604 E -> Q (in an ovarian serous carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_041082.
FT VARIANT 658 658 A -> G (in dbSNP:rs56400929).
FT /FTId=VAR_041083.
FT VARIANT 666 666 G -> E (in dbSNP:rs7071400).
FT /FTId=VAR_051666.
FT VARIANT 679 679 I -> T (in dbSNP:rs34326537).
FT /FTId=VAR_041084.
FT VARIANT 683 683 K -> N (in dbSNP:rs35389916).
FT /FTId=VAR_041085.
FT VARIANT 697 697 T -> I (in dbSNP:rs3740469).
FT /FTId=VAR_041086.
FT MUTAGEN 63 63 K->R: Loss of activity.
FT CONFLICT 5 5 N -> S (in Ref. 3; BAA13195).
FT STRAND 25 28
FT HELIX 30 32
FT STRAND 34 43
FT STRAND 46 53
FT TURN 54 56
FT STRAND 59 66
FT STRAND 68 70
FT HELIX 73 85
FT STRAND 94 100
FT STRAND 103 109
FT HELIX 116 123
FT HELIX 129 148
FT HELIX 158 160
FT STRAND 161 163
FT STRAND 169 171
FT HELIX 181 187
FT HELIX 199 202
FT TURN 207 209
FT TURN 212 214
FT HELIX 215 230
FT TURN 234 237
FT HELIX 240 242
FT HELIX 243 249
FT HELIX 258 260
FT HELIX 263 272
FT TURN 277 279
FT HELIX 283 286
FT HELIX 290 292
FT HELIX 298 307
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
//