SLK_MOUSE
ID SLK_MOUSE Reviewed; 1233 AA.
AC O54988; A2RRK4; Q80U65; Q8CAU2; Q8CDW2; Q9WU41;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=STE20-like serine/threonine-protein kinase;
DE Short=STE20-like kinase;
DE Short=mSLK;
DE EC=2.7.11.1;
DE AltName: Full=Etk4;
DE AltName: Full=STE20-related kinase SMAK;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=9808774; DOI=10.1006/abbi.1998.0907;
RA Pytowski B., Hicklin D.J., Kornhaber G., Dellaratta D.V., Witte L.;
RT "Identification and initial characterization of mSLK, a murine member of
RT the STE20 family of kinases.";
RL Arch. Biochem. Biophys. 359:310-319(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, CLEAVAGE BY
RP CASPASE-3, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-436.
RC STRAIN=BALB/cJ;
RX PubMed=10611247; DOI=10.1128/mcb.20.2.684-696.2000;
RA Sabourin L.A., Seale P., Wagner J., Rudnicki M.A.;
RT "Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates
RT an apoptosis-inducing kinase domain and an actin-disassembling region.";
RL Mol. Cell. Biol. 20:684-696(2000).
RN [3]
RP ERRATUM OF PUBMED:10611247.
RA Sabourin L.A., Seale P., Wagner J., Rudnicki M.A.;
RL Mol. Cell. Biol. 20:2949-2949(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-784 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 157-201, AND TISSUE SPECIFICITY.
RX PubMed=8346215; DOI=10.1073/pnas.90.15.7044;
RA Biesecker L.G., Gottschalk L.R., Emerson S.G.;
RT "Identification of four murine cDNAs encoding putative protein kinases from
RT primitive embryonic stem cells differentiated in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7044-7048(1993).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183; SER-189; SER-344;
RP SER-347; SER-348; SER-354; SER-543; SER-643; SER-647; SER-666; SER-777;
RP THR-812 AND SER-816, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Mediates apoptosis and actin stress fiber dissolution.
CC {ECO:0000269|PubMed:10611247}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10611247,
CC ECO:0000269|PubMed:9808774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O54988-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54988-2; Sequence=VSP_018101;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10611247, ECO:0000269|PubMed:8346215,
CC ECO:0000269|PubMed:9808774}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed from day 7 to 17 dpc.
CC {ECO:0000269|PubMed:9808774}.
CC -!- PTM: Proteolytically cleaved by caspase-3.
CC {ECO:0000269|PubMed:10611247}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9808774}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF039574; AAB96682.1; -; mRNA.
DR EMBL; AF112855; AAD28717.1; -; mRNA.
DR EMBL; AK037798; BAC29874.1; -; mRNA.
DR EMBL; AK122218; BAC65500.1; ALT_INIT; mRNA.
DR EMBL; BC131675; AAI31676.1; -; mRNA.
DR EMBL; AK029491; BAC26474.1; -; mRNA.
DR CCDS; CCDS38017.1; -. [O54988-1]
DR CCDS; CCDS50465.1; -. [O54988-2]
DR PIR; T14157; T14157.
DR RefSeq; NP_001158111.1; NM_001164639.1. [O54988-2]
DR RefSeq; NP_033315.2; NM_009289.3. [O54988-1]
DR AlphaFoldDB; O54988; -.
DR SMR; O54988; -.
DR BioGRID; 203546; 4.
DR IntAct; O54988; 1.
DR STRING; 10090.ENSMUSP00000049977; -.
DR ChEMBL; CHEMBL2176844; -.
DR iPTMnet; O54988; -.
DR PhosphoSitePlus; O54988; -.
DR SwissPalm; O54988; -.
DR EPD; O54988; -.
DR jPOST; O54988; -.
DR MaxQB; O54988; -.
DR PaxDb; O54988; -.
DR PeptideAtlas; O54988; -.
DR PRIDE; O54988; -.
DR ProteomicsDB; 261081; -. [O54988-1]
DR ProteomicsDB; 261082; -. [O54988-2]
DR Antibodypedia; 18194; 294 antibodies from 34 providers.
DR DNASU; 20874; -.
DR Ensembl; ENSMUST00000026043; ENSMUSP00000026043; ENSMUSG00000025060. [O54988-2]
DR Ensembl; ENSMUST00000051691; ENSMUSP00000049977; ENSMUSG00000025060. [O54988-1]
DR GeneID; 20874; -.
DR KEGG; mmu:20874; -.
DR UCSC; uc008hvf.2; mouse. [O54988-1]
DR CTD; 9748; -.
DR MGI; MGI:103241; Slk.
DR VEuPathDB; HostDB:ENSMUSG00000025060; -.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156184; -.
DR HOGENOM; CLU_001965_3_0_1; -.
DR InParanoid; O54988; -.
DR OMA; HEAYFIE; -.
DR OrthoDB; 851098at2759; -.
DR PhylomeDB; O54988; -.
DR TreeFam; TF351445; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 20874; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slk; mouse.
DR PRO; PR:O54988; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O54988; protein.
DR Bgee; ENSMUSG00000025060; Expressed in ileal epithelium and 268 other tissues.
DR ExpressionAtlas; O54988; baseline and differential.
DR Genevisible; O54988; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS: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 Alternative splicing; Apoptosis; ATP-binding; Coiled coil; Cytoplasm;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1233
FT /note="STE20-like serine/threonine-protein kinase"
FT /id="PRO_0000233240"
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 873..908
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..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 824..1067
FT /evidence="ECO:0000255"
FT COILED 1107..1181
FT /evidence="ECO:0000255"
FT COMPBIAS 315..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
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 436..437
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000305"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 183
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08815"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 812
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1095
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2G2"
FT VAR_SEQ 927..957
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10611247,
FT ECO:0000303|PubMed:12693553"
FT /id="VSP_018101"
FT MUTAGEN 436
FT /note="D->N: No change in caspase-3-induced cleavage
FT product."
FT /evidence="ECO:0000269|PubMed:10611247"
FT CONFLICT 164
FT /note="T -> N (in Ref. 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="A -> V (in Ref. 1; AAB96682)"
FT /evidence="ECO:0000305"
FT CONFLICT 1098
FT /note="Q -> K (in Ref. 2; BAC29874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1233 AA; 141457 MW; B1A5230666C58A73 CRC64;
MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EEFWEIIGEL GDGAFGKVYK AQNKETNVLA
AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
LELERPLTES QIQVVCKQTL EALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP
MRVLLKIAKS EPPTLAQPSK WSSNFKDFLR KCLEKNVDAR WTTSQLLQHP FVTVDSNKPV
RELIAEAKAE VTEEVEDGKE EDEEEEAENA LPIPANKRAS SDLSIASSEE DKLSQNACIL
ESVSERTEQS TSEDKFSNKI LNEKPTTDGP EKAVDEHASD VNLETGAELN DQTVGIHENG
REKKRPKLEN LPDTQDQQTV DVNSVSEENE NNRVTLETNT DCLKPEEDRN KENQETLESK
LIQSEEINDT HIQTMDLVSQ ETGEKEADFQ AVDNEVGLTK EETQEKLGKD GTAQKVITSD
RSSEVGTDEA LDDTQKAAEL SKAAQSGEGD EALAPTQTLA EKPTEGPEAG GAEEEPPGGE
RVEDKQPEQQ PAVCEAEGQL TSTSETTRAT LEQPETDEVE QVSESNSIEE LERLVVTGAE
ARALGSEGEA AATEVDLERK ENAQKVPVKA ESQAPAASQP SEPHPVLIPS ININSETTEN
KEEMGALPKP ETILPPEPEH EKGNDTDSGT GSTVENSSGD LNLSISSFLS KAKDSGSVSL
QETRRQKKTL KKTRKFIVDG VEVSVTTSKI VTDSDSKTEE LRFLRRQELR ELRLLQKEEQ
RAQQQLNGKL QQQREQIFRR FEQEMLSKKR QYDQEIENLE KQQKQTIERL EQEHTNRLRD
EAKRIKGEQE KELSKFQNVL KNRKKEVMNE VEKAPRELRR ELTKRRKEEL AQSQHAQEQE
FVQKQQQELD GSLKKIIQQQ KAELANIERE CLNNKQQLMR AREAAIWELE ERHLQEKHQL
LKQQLKDQYF MQRHQLLKRH EKETEQMQRY NQRLIEELKN RQTQERARLP KIQRSEAKTR
MAMFKKSLRI NSTATPDQDR EKIKQFAAQE EKRQKNERMA QHQKHESQMR DLQLQCEANV
RELHQLQNEK CHLLVEHETQ KLKELDEEHS QELKEWREKL RPRKKTLEEE FARKLQEQEV
FFKMTGESEC LNPSAQSRIS KFYPIPTLHS TGS
