SMTN_HUMAN
ID SMTN_HUMAN Reviewed; 917 AA.
AC P53814; O00569; O95769; O95937; Q8N4H8; Q8WWW1; Q8WWW2; Q9P1S8; Q9UIT1;
AC Q9UIT2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 7.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Smoothelin;
GN Name=SMTN; Synonyms=SMSMO;
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 A).
RC TISSUE=Colon smooth muscle;
RX PubMed=8707825; DOI=10.1083/jcb.134.2.401;
RA van der Loop F.T.L., Schaart G., Timmer E.D.J., Ramaekers F.C.S.,
RA van Eys G.J.J.M.;
RT "Smoothelin, a novel cytoskeletal protein specific for smooth muscle
RT cells.";
RL J. Cell Biol. 134:401-411(1996).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Rensen S.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND VARIANTS ASP-455 AND PRO-547.
RC TISSUE=Fetus;
RX PubMed=10023782; DOI=10.1007/s001090050352;
RA Kraemer J., Aguirre-Arteta A.M., Thiel C., Gross M.C., Dietz R.,
RA Cardoso M.C., Leonhardt H.;
RT "A novel isoform of the smooth muscle cell differentiation marker
RT smoothelin.";
RL J. Mol. Med. 77:294-298(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND B2), AND VARIANT ASP-455.
RX PubMed=11316948; DOI=10.1159/000051039;
RA Kraemer J., Quensel C., Meding J., Cardoso M.C., Leonhardt H.;
RT "Identification and characterization of novel smoothelin isoforms in
RT vascular smooth muscle.";
RL J. Vasc. Res. 38:120-132(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; B2 AND B3),
RP ALTERNATIVE PROMOTER USAGE, AND VARIANT ASP-455.
RC TISSUE=Vascular smooth muscle;
RX PubMed=12176134; DOI=10.1016/s0008-6363(02)00491-1;
RA Rensen S.S., Thijssen V.L., De Vries C.J., Doevendans P.A.,
RA Detera-Wadleigh S.D., Van Eys G.J.J.M.;
RT "Expression of the smoothelin gene is mediated by alternative promoters.";
RL Cardiovasc. Res. 55:850-863(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B2), AND VARIANTS ASP-455 AND PRO-547.
RA Kraemer J., Arteta-Aguirre A.M., Cardoso M.C., Leonhardt H.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-547.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B2), AND VARIANT PRO-547.
RC TISSUE=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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-304; SER-341;
RP THR-373; SER-503; SER-514; SER-576 AND SER-729, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND THR-360, AND
RP IDENTIFICATION BY 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-299; SER-301; SER-304;
RP THR-351; SER-357; THR-360; THR-373 AND SER-514, AND IDENTIFICATION BY MASS
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-304; SER-341;
RP SER-514; SER-523; SER-729 AND SER-792, AND IDENTIFICATION BY MASS
RP 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 [15]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-637 AND VAL-763.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Structural protein of the cytoskeleton.
CC -!- INTERACTION:
CC P53814-5; Q4L180-3: FILIP1L; NbExp=3; IntAct=EBI-11100581, EBI-12221557;
CC P53814-5; O76024: WFS1; NbExp=3; IntAct=EBI-11100581, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Exhibits a
CC filamentous organization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=B; Synonyms=Long, B1, L1;
CC IsoId=P53814-1; Sequence=Displayed;
CC Name=A; Synonyms=Short;
CC IsoId=P53814-2; Sequence=VSP_004398;
CC Name=B2; Synonyms=L2;
CC IsoId=P53814-5; Sequence=VSP_007020;
CC Name=B3;
CC IsoId=P53814-6; Sequence=VSP_031242;
CC -!- TISSUE SPECIFICITY: Smooth muscle; contractile or vascular (for the
CC long form).
CC -!- MISCELLANEOUS: [Isoform A]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the smoothelin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL36149.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL36150.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA73884.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49989; CAA90281.2; -; mRNA.
DR EMBL; AJ010306; CAA09077.2; -; mRNA.
DR EMBL; Y13492; CAA73884.2; ALT_FRAME; mRNA.
DR EMBL; AY061971; AAL36149.1; ALT_FRAME; mRNA.
DR EMBL; AY061972; AAL36150.1; ALT_FRAME; mRNA.
DR EMBL; AF115570; AAF03562.1; -; Genomic_DNA.
DR EMBL; AF115552; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115553; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115554; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115555; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115556; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115557; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115558; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115559; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115560; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115561; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115562; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115563; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115564; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115565; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115566; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115567; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115568; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115569; AAF03562.1; JOINED; Genomic_DNA.
DR EMBL; AF115570; AAF03563.1; -; Genomic_DNA.
DR EMBL; AF115560; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115561; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115562; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115563; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115564; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115565; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115566; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115567; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115568; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF115569; AAF03563.1; JOINED; Genomic_DNA.
DR EMBL; AF064238; AAF01481.3; -; mRNA.
DR EMBL; AC005005; AAD15619.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59930.1; -; Genomic_DNA.
DR EMBL; BC034237; AAH34237.1; -; mRNA.
DR CCDS; CCDS13886.1; -. [P53814-1]
DR CCDS; CCDS13887.1; -. [P53814-6]
DR CCDS; CCDS13888.1; -. [P53814-5]
DR PIR; T09575; T09575.
DR RefSeq; NP_001193946.1; NM_001207017.1.
DR RefSeq; NP_001193947.1; NM_001207018.1.
DR RefSeq; NP_008863.3; NM_006932.4. [P53814-1]
DR RefSeq; NP_599031.1; NM_134269.2. [P53814-5]
DR RefSeq; NP_599032.2; NM_134270.2. [P53814-6]
DR PDB; 2D87; NMR; -; A=801-868.
DR PDBsum; 2D87; -.
DR AlphaFoldDB; P53814; -.
DR SMR; P53814; -.
DR BioGRID; 112416; 32.
DR IntAct; P53814; 27.
DR MINT; P53814; -.
DR STRING; 9606.ENSP00000484398; -.
DR GlyGen; P53814; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53814; -.
DR PhosphoSitePlus; P53814; -.
DR BioMuta; SMTN; -.
DR DMDM; 338817991; -.
DR EPD; P53814; -.
DR jPOST; P53814; -.
DR MassIVE; P53814; -.
DR MaxQB; P53814; -.
DR PaxDb; P53814; -.
DR PeptideAtlas; P53814; -.
DR PRIDE; P53814; -.
DR ProteomicsDB; 56630; -. [P53814-1]
DR ProteomicsDB; 56631; -. [P53814-2]
DR ProteomicsDB; 56632; -. [P53814-5]
DR ProteomicsDB; 56633; -. [P53814-6]
DR Antibodypedia; 3445; 177 antibodies from 24 providers.
DR DNASU; 6525; -.
DR Ensembl; ENST00000333137.12; ENSP00000329532.7; ENSG00000183963.19. [P53814-5]
DR Ensembl; ENST00000347557.6; ENSP00000328635.5; ENSG00000183963.19. [P53814-1]
DR Ensembl; ENST00000358743.5; ENSP00000351593.1; ENSG00000183963.19. [P53814-6]
DR GeneID; 6525; -.
DR KEGG; hsa:6525; -.
DR MANE-Select; ENST00000333137.12; ENSP00000329532.7; NM_134269.3; NP_599031.1. [P53814-5]
DR UCSC; uc003ajk.3; human. [P53814-1]
DR CTD; 6525; -.
DR DisGeNET; 6525; -.
DR GeneCards; SMTN; -.
DR HGNC; HGNC:11126; SMTN.
DR HPA; ENSG00000183963; Tissue enhanced (intestine, urinary bladder).
DR MIM; 602127; gene.
DR neXtProt; NX_P53814; -.
DR OpenTargets; ENSG00000183963; -.
DR PharmGKB; PA35975; -.
DR VEuPathDB; HostDB:ENSG00000183963; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000161655; -.
DR HOGENOM; CLU_014660_0_0_1; -.
DR InParanoid; P53814; -.
DR TreeFam; TF316716; -.
DR PathwayCommons; P53814; -.
DR SignaLink; P53814; -.
DR BioGRID-ORCS; 6525; 23 hits in 1076 CRISPR screens.
DR ChiTaRS; SMTN; human.
DR EvolutionaryTrace; P53814; -.
DR GeneWiki; SMTN; -.
DR GenomeRNAi; 6525; -.
DR Pharos; P53814; Tbio.
DR PRO; PR:P53814; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P53814; protein.
DR Bgee; ENSG00000183963; Expressed in lower esophagus muscularis layer and 161 other tissues.
DR ExpressionAtlas; P53814; baseline and differential.
DR Genevisible; P53814; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; TAS:ProtInc.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0006939; P:smooth muscle contraction; TAS:ProtInc.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR022189; SMTN.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12510; Smoothelin; 3.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative promoter usage;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..917
FT /note="Smoothelin"
FT /id="PRO_0000071976"
FT DOMAIN 799..906
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 157..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..89
FT /evidence="ECO:0000255"
FT COILED 603..630
FT /evidence="ECO:0000255"
FT COMPBIAS 169..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 373
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..456
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12176134,
FT ECO:0000303|PubMed:8707825"
FT /id="VSP_004398"
FT VAR_SEQ 868
FT /note="E -> ETHADCPQLLDTEDMVRLREPDWK (in isoform B3)"
FT /evidence="ECO:0000303|PubMed:12176134"
FT /id="VSP_031242"
FT VAR_SEQ 869..917
FT /note="MLVDCVPLVEVDDMMIMGKKPDPKCVFTYVQSLYNHLRRHELRLRGKNV ->
FT THADCPQLLDTEDMVRLREPDWKCVYTYIQEFYRCLVQKGLVKTKKS (in isoform
FT B2)"
FT /evidence="ECO:0000303|PubMed:11316948,
FT ECO:0000303|PubMed:12176134, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.6"
FT /id="VSP_007020"
FT VARIANT 455
FT /note="G -> D (in dbSNP:rs1064178)"
FT /evidence="ECO:0000269|PubMed:10023782,
FT ECO:0000269|PubMed:11316948, ECO:0000269|PubMed:12176134,
FT ECO:0000269|Ref.6"
FT /id="VAR_038785"
FT VARIANT 547
FT /note="A -> P (in dbSNP:rs3205187)"
FT /evidence="ECO:0000269|PubMed:10023782,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.8"
FT /id="VAR_038786"
FT VARIANT 559
FT /note="A -> V (in dbSNP:rs5997872)"
FT /id="VAR_038787"
FT VARIANT 580
FT /note="A -> T (in dbSNP:rs12158015)"
FT /id="VAR_038788"
FT VARIANT 637
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs777851029)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035657"
FT VARIANT 642
FT /note="R -> C (in dbSNP:rs34292278)"
FT /id="VAR_062223"
FT VARIANT 763
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035658"
FT CONFLICT 279
FT /note="T -> P (in Ref. 5; AAF03562/AAL36149/AAL36150/
FT CAA73884)"
FT /evidence="ECO:0000305"
FT HELIX 801..812
FT /evidence="ECO:0007829|PDB:2D87"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:2D87"
FT TURN 824..829
FT /evidence="ECO:0007829|PDB:2D87"
FT HELIX 832..841
FT /evidence="ECO:0007829|PDB:2D87"
FT TURN 843..845
FT /evidence="ECO:0007829|PDB:2D87"
FT HELIX 856..871
FT /evidence="ECO:0007829|PDB:2D87"
FT HELIX 879..884
FT /evidence="ECO:0007829|PDB:2D87"
FT HELIX 891..905
FT /evidence="ECO:0007829|PDB:2D87"
SQ SEQUENCE 917 AA; 99059 MW; EC508A8239AA6B36 CRC64;
MADEALAGLD EGALRKLLEV TADLAERRRI RSAIRELQRQ ELEREEEALA SKRFRAERQD
NKENWLHSQQ REAEQRAALA RLAGQLESMN DVEELTALLR SAGEYEERKL IRAAIRRVRA
QEIEAATLAG RLYSGRPNSG SREDSKGLAA HRLEQCEVPE REEQEQQAEV SKPTPTPEGT
SQDVTTVTLL LRAPPGSTSS SPASPSSSPT PASPEPPLEP AEAQCLTAEV PGSPEPPPSP
PKTTSPEPQE SPTLPSTEGQ VVNKLLSGPK ETPAAQSPTR GPSDTKRADV AGPRPCQRSL
SVLSPRQPAQ NRESTPLASG PSSFQRAGSV RDRVHKFTSD SPMAARLQDG TPQAALSPLT
PARLLGPSLT STTPASSSSG SSSRGPSDTS SRFSKEQRGV AQPLAQLRSC PQEEGPRGRG
LAARPLENRA GGPVARSEEP GAPLPVAVGT AEPGGSMKTT FTIEIKDGRG QASTGRVLLP
TGNQRAELTL GLRAPPTLLS TSSGGKSTIT RVNSPGTLAR LGSVTHVTSF SHAPPSSRGG
CSIKMEAEPA EPLAAAVEAA NGAEQTRVNK APEGRSPLSA EELMTIEDEG VLDKMLDQST
DFEERKLIRA ALRELRQRKR DQRDKERERR LQEARGRPGE GRGNTATETT TRHSQRAADG
SAVSTVTKTE RLVHSNDGTR TARTTTVESS FVRRSENGSG STMMQTKTFS SSSSSKKMGS
IFDREDQASP RAGSLAALEK RQAEKKKELM KAQSLPKTSA SQARKAMIEK LEKEGAAGSP
GGPRAAVQRS TSFGVPNANS IKQMLLDWCR AKTRGYEHVD IQNFSSSWSD GMAFCALVHN
FFPEAFDYGQ LSPQNRRQNF EVAFSSAEML VDCVPLVEVD DMMIMGKKPD PKCVFTYVQS
LYNHLRRHEL RLRGKNV
