ID   GSE1_HUMAN              Reviewed;        1217 AA.
AC   Q14687; D3DUM4; Q8IY61; Q96GA4; Q9BW09;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Genetic suppressor element 1;
GN   Name=GSE1; Synonyms=KIAA0182;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Bone marrow;
RX   PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA   Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. V. The
RT   coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 3:17-24(1996).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   ALA-936.
RC   TISSUE=Lung, and Placenta;
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   [4]
RP   IDENTIFICATION IN THE BHC COMPLEX WITH GTF2I; HDAC1; HDAC2; HMG20B; KDM1A;
RP   PHF21A; RCOR1; ZMYM2; ZMYM3 AND ZNF217.
RX   PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA   Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT   "A candidate X-linked mental retardation gene is a component of a new
RT   family of histone deacetylase-containing complexes.";
RL   J. Biol. Chem. 278:7234-7239(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826; SER-909 AND SER-1101,
RP   AND IDENTIFICATION BY MASS 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-766; SER-857; THR-907
RP   AND SER-909, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-496 AND LYS-739, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-909, AND
RP   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   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-84; THR-433; SER-826;
RP   SER-828; SER-857; SER-909 AND SER-1101, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [13]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-305, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [14]
RP   DOWN-REGULATION BY MIR-489-5P.
RX   PubMed=26828271; DOI=10.1016/j.bbrc.2016.01.168;
RA   Chai P., Tian J., Zhao D., Zhang H., Cui J., Ding K., Liu B.;
RT   "GSE1 negative regulation by miR-489-5p promotes breast cancer cell
RT   proliferation and invasion.";
RL   Biochem. Biophys. Res. Commun. 471:123-128(2016).
RN   [15]
RP   VARIANT [LARGE SCALE ANALYSIS] TRP-627.
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   -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC       PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC       {ECO:0000269|PubMed:12493763}.
CC   -!- INTERACTION:
CC       Q14687; Q6P1W5: C1orf94; NbExp=8; IntAct=EBI-372619, EBI-946029;
CC       Q14687; A2RRN7: CADPS; NbExp=3; IntAct=EBI-372619, EBI-10179719;
CC       Q14687; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-372619, EBI-3866279;
CC       Q14687; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-372619, EBI-749051;
CC       Q14687; Q08379: GOLGA2; NbExp=9; IntAct=EBI-372619, EBI-618309;
CC       Q14687; Q96PV6: LENG8; NbExp=3; IntAct=EBI-372619, EBI-739546;
CC       Q14687; Q15311: RALBP1; NbExp=4; IntAct=EBI-372619, EBI-749285;
CC       Q14687; Q93062: RBPMS; NbExp=3; IntAct=EBI-372619, EBI-740322;
CC       Q14687; Q9P2K3: RCOR3; NbExp=9; IntAct=EBI-372619, EBI-743428;
CC       Q14687; Q9P2K3-2: RCOR3; NbExp=3; IntAct=EBI-372619, EBI-1504830;
CC       Q14687; Q06455-4: RUNX1T1; NbExp=3; IntAct=EBI-372619, EBI-10224192;
CC       Q14687; Q8WW24: TEKT4; NbExp=5; IntAct=EBI-372619, EBI-750487;
CC       Q14687; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-372619, EBI-1105213;
CC       Q14687; Q12933: TRAF2; NbExp=3; IntAct=EBI-372619, EBI-355744;
CC       Q14687; P14373: TRIM27; NbExp=5; IntAct=EBI-372619, EBI-719493;
CC       Q14687; Q15654: TRIP6; NbExp=5; IntAct=EBI-372619, EBI-742327;
CC       Q14687; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-372619, EBI-746595;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14687-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14687-2; Sequence=VSP_021820;
CC       Name=3;
CC         IsoId=Q14687-3; Sequence=VSP_021821;
CC   -!- INDUCTION: Negatively regulated by miR-489-5p.
CC       {ECO:0000269|PubMed:26828271}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11499.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D80004; BAA11499.2; ALT_INIT; mRNA.
DR   EMBL; CH471114; EAW95445.1; -; Genomic_DNA.
DR   EMBL; CH471114; EAW95447.1; -; Genomic_DNA.
DR   EMBL; BC000753; AAH00753.2; -; mRNA.
DR   EMBL; BC009854; AAH09854.2; -; mRNA.
DR   EMBL; BC037556; AAH37556.1; -; mRNA.
DR   EMBL; BQ214916; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS10952.1; -. [Q14687-1]
DR   CCDS; CCDS45539.1; -. [Q14687-2]
DR   CCDS; CCDS62007.1; -. [Q14687-3]
DR   RefSeq; NP_001127945.1; NM_001134473.2. [Q14687-2]
DR   RefSeq; NP_001265113.1; NM_001278184.1. [Q14687-3]
DR   RefSeq; NP_055430.1; NM_014615.3. [Q14687-1]
DR   AlphaFoldDB; Q14687; -.
DR   SMR; Q14687; -.
DR   BioGRID; 116808; 154.
DR   CORUM; Q14687; -.
DR   IntAct; Q14687; 84.
DR   MINT; Q14687; -.
DR   STRING; 9606.ENSP00000253458; -.
DR   GlyGen; Q14687; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q14687; -.
DR   MetOSite; Q14687; -.
DR   PhosphoSitePlus; Q14687; -.
DR   BioMuta; GSE1; -.
DR   DMDM; 126302550; -.
DR   EPD; Q14687; -.
DR   jPOST; Q14687; -.
DR   MassIVE; Q14687; -.
DR   MaxQB; Q14687; -.
DR   PaxDb; 9606-ENSP00000253458; -.
DR   PeptideAtlas; Q14687; -.
DR   ProteomicsDB; 60121; -. [Q14687-1]
DR   ProteomicsDB; 60122; -. [Q14687-2]
DR   ProteomicsDB; 60123; -. [Q14687-3]
DR   Pumba; Q14687; -.
DR   Antibodypedia; 30633; 57 antibodies from 19 providers.
DR   DNASU; 23199; -.
DR   Ensembl; ENST00000253458.12; ENSP00000253458.6; ENSG00000131149.19. [Q14687-1]
DR   Ensembl; ENST00000393243.5; ENSP00000376934.1; ENSG00000131149.19. [Q14687-3]
DR   Ensembl; ENST00000405402.6; ENSP00000384839.2; ENSG00000131149.19. [Q14687-2]
DR   GeneID; 23199; -.
DR   KEGG; hsa:23199; -.
DR   MANE-Select; ENST00000253458.12; ENSP00000253458.6; NM_014615.5; NP_055430.1.
DR   UCSC; uc002fiw.4; human. [Q14687-1]
DR   AGR; HGNC:28979; -.
DR   CTD; 23199; -.
DR   DisGeNET; 23199; -.
DR   GeneCards; GSE1; -.
DR   HGNC; HGNC:28979; GSE1.
DR   HPA; ENSG00000131149; Low tissue specificity.
DR   MIM; 616886; gene.
DR   neXtProt; NX_Q14687; -.
DR   OpenTargets; ENSG00000131149; -.
DR   PharmGKB; PA143485512; -.
DR   VEuPathDB; HostDB:ENSG00000131149; -.
DR   eggNOG; ENOG502QR0Q; Eukaryota.
DR   GeneTree; ENSGT00700000104539; -.
DR   HOGENOM; CLU_009387_0_0_1; -.
DR   InParanoid; Q14687; -.
DR   OMA; CLSCWSP; -.
DR   OrthoDB; 3268655at2759; -.
DR   PhylomeDB; Q14687; -.
DR   TreeFam; TF332496; -.
DR   PathwayCommons; Q14687; -.
DR   SignaLink; Q14687; -.
DR   BioGRID-ORCS; 23199; 36 hits in 1162 CRISPR screens.
DR   ChiTaRS; GSE1; human.
DR   GeneWiki; KIAA0182; -.
DR   GenomeRNAi; 23199; -.
DR   Pharos; Q14687; Tdark.
DR   PRO; PR:Q14687; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q14687; Protein.
DR   Bgee; ENSG00000131149; Expressed in corpus epididymis and 212 other cell types or tissues.
DR   ExpressionAtlas; Q14687; baseline and differential.
DR   InterPro; IPR022207; GSE-like.
DR   InterPro; IPR042337; GSE1.
DR   PANTHER; PTHR17608; GENETIC SUPPRESSOR ELEMENT 1; 1.
DR   PANTHER; PTHR17608:SF4; GENETIC SUPPRESSOR ELEMENT 1; 1.
DR   Pfam; PF12540; DUF3736; 1.
DR   Genevisible; Q14687; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Methylation;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1217
FT                   /note="Genetic suppressor element 1"
FT                   /id="PRO_0000050730"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          948..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          321..403
FT                   /evidence="ECO:0000255"
FT   COILED          1127..1201
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        11..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..437
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1098..1115
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U3C9"
FT   MOD_RES         305
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         433
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         496
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         739
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         766
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         826
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         828
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         857
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         907
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         909
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         1101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..104
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021820"
FT   VAR_SEQ         3..75
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8724849"
FT                   /id="VSP_021821"
FT   VARIANT         627
FT                   /note="R -> W (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs757859891)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035926"
FT   VARIANT         936
FT                   /note="V -> A (in dbSNP:rs17853763)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_029546"
FT   VARIANT         1153
FT                   /note="R -> Q (in dbSNP:rs2303203)"
FT                   /id="VAR_029547"
FT   CONFLICT        444
FT                   /note="G -> S (in Ref. 1; BAA11499)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1217 AA;  136164 MW;  4291FBE301B70F36 CRC64;
     MKGMSHEPKS PSLGMLSTAT RTTATVNPLT PSPLNGALVP SGSPATSSAL SAQAAPSSSF
     AAALRKLAKQ AEEPRGSSLS SESSPVSSPA TNHSSPASTP KRVPMGPIIV PPGGHSVPST
     PPVVTIAPTK TVNGVWRSES RQDAGSRSSS GGRERLIVEP PLPQEKAGGP AIPSHLLSTP
     YPFGLSPSSV VQDSRFPPLN LQRPVHHVVP PSTVTEDYLR SFRPYHTTDD LRMSSLPPLG
     LDPATAAAYY HPSYLAPHPF PHPAFRMDDS YCLSALRSPF YPIPTPGSLP PLHPSAMHLH
     LSGVRYPPEL SHSSLAALHS ERMSGLSAER LQMDEELRRE RERERERERE READREREKE
     REREREKERE QEKEREREKE RERELERQRE QRAREKELLA AKALEPSFLP VAELHGLRGH
     ATEERGKPSE QLTPTRAEKL KDAGLQAPKP VQHPLHPVPT PHHTVPSLIS NHGIFSLPSS
     SAATALLIQR TNEEEKWLAR QRRLRQEKED RQSQVSEFRQ QVLEQHLDMG RPPVPAEAEH
     RPESTTRPGP NRHEPGGRDP PQHFGGPPPL ISPKPQLHAA PTALWNPVSL MDNTLETRRA
     ESHSLHSHPA AFEPSRQAAV PLVKVERVFC PEKAEEGPRK REPAPLDKYQ PPPPPPREGG
     SLEHQPFLPG PGPFLAELEK STQTILGQQR ASLPQAATFG ELSGPLKPGS PYRPPVPRAP
     DPAYIYDEFL QQRRRLVSKL DLEERRRREA QEKGYYYDLD DSYDESDEEE VRAHLRCVAE
     QPPLKLDTSS EKLEFLQLFG LTTQQQKEEL VAQKRRKRRR MLRERSPSPP TIQSKRQTPS
     PRLALSTRYS PDEMNNSPNF EEKKKFLTIF NLTHISAEKR KDKERLVEML RAMKQKALSA
     AVADSLTNSP RDSPAVSLSE PATQQASLDV EKPVGVAASL SDIPKAAEPG KLEQVRPQEL
     SRVQELAPAS GEKARLSEAP GGKKSLSMLH YIRGAAPKDI PVPLSHSTNG KSKPWEPFVA
     EEFAHQFHES VLQSTQKALQ KHKGSVAVLS AEQNHKVDTS VHYNIPELQS SSRAPPPQHN
     GQQEPPTARK GPPTQELDRD SEEEEEEDDE DGEDEEEVPK RKWQGIEAVF EAYQEHIEEQ
     NLERQVLQTQ CRRLEARHYS LSLTAEQLSH SVAELRSQKQ KMVSERERLQ AELDHLRKCL
     ALPAMHWPRG YLKGYPR
//