CREST_HUMAN
ID CREST_HUMAN Reviewed; 396 AA.
AC O75177; A6NNE3; A8K620; B3KWR8; E1P5H7; Q5JXJ3; Q6MZV9; Q6NTH3; Q6XYD9;
AC Q8NE69; Q9BR55; Q9H4K6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Calcium-responsive transactivator;
DE AltName: Full=SS18-like protein 1;
DE AltName: Full=SYT homolog 1;
GN Name=SS18L1; Synonyms=CREST, KIAA0693;
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 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Wan D.F., Qin W.X., Zhou X.M., Zhang P.P., Jiang H.Q., Gu J.R.;
RT "Novel Homo sapiens cDNA clones with function of promoting mice NIH/3T3
RT cells' growth.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND VARIANT
RP ILE-189.
RC TISSUE=Lymph, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18331714; DOI=10.1016/j.devcel.2007.12.007;
RA Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W.;
RT "sSgo1, a major splice variant of Sgo1, functions in centriole cohesion
RT where it is regulated by Plk1.";
RL Dev. Cell 14:331-341(2008).
CC -!- FUNCTION: Transcriptional activator which is required for calcium-
CC dependent dendritic growth and branching in cortical neurons. Recruits
CC CREB-binding protein (CREBBP) to nuclear bodies. Component of the
CC CREST-BRG1 complex, a multiprotein complex that regulates promoter
CC activation by orchestrating a calcium-dependent release of a repressor
CC complex and a recruitment of an activator complex. In resting neurons,
CC transcription of the c-FOS promoter is inhibited by BRG1-dependent
CC recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium
CC influx, RB1 is dephosphorylated by calcineurin, which leads to release
CC of the repressor complex. At the same time, there is increased
CC recruitment of CREBBP to the promoter by a CREST-dependent mechanism,
CC which leads to transcriptional activation. The CREST-BRG1 complex also
CC binds to the NR2B promoter, and activity-dependent induction of NR2B
CC expression involves a release of HDAC1 and recruitment of CREBBP (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Dimerization may be necessary for its function in
CC neuronal dendritic development. Interacts (via C-terminus) with CREBBP
CC (via N-terminus), EP300 and SMARCA4/BRG1. Interacts with the nBAF
CC complex. Association with CREBBP facilitates transcription while the
CC association with SMARCA4/BRG1 suppresses CREST-mediated transcription
CC in resting neurons (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O75177; P33240: CSTF2; NbExp=3; IntAct=EBI-744674, EBI-711360;
CC O75177; Q92567: FAM168A; NbExp=4; IntAct=EBI-744674, EBI-7957930;
CC O75177; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-744674, EBI-16429135;
CC O75177; P17931: LGALS3; NbExp=3; IntAct=EBI-744674, EBI-1170392;
CC O75177; Q6NVH9: LGALS3; NbExp=3; IntAct=EBI-744674, EBI-10187804;
CC O75177; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-744674, EBI-741424;
CC O75177; Q96PC5: MIA2; NbExp=3; IntAct=EBI-744674, EBI-1050253;
CC O75177; Q15427: SF3B4; NbExp=4; IntAct=EBI-744674, EBI-348469;
CC O75177; P14678-2: SNRPB; NbExp=3; IntAct=EBI-744674, EBI-372475;
CC O75177; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-744674, EBI-10246938;
CC O75177-5; Q86V38: ATN1; NbExp=3; IntAct=EBI-12035119, EBI-11954292;
CC O75177-5; O95429: BAG4; NbExp=3; IntAct=EBI-12035119, EBI-2949658;
CC O75177-5; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-12035119, EBI-1012434;
CC O75177-5; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-12035119, EBI-946029;
CC O75177-5; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-12035119, EBI-747776;
CC O75177-5; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-12035119, EBI-16429135;
CC O75177-5; O14964: HGS; NbExp=3; IntAct=EBI-12035119, EBI-740220;
CC O75177-5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-12035119, EBI-1055254;
CC O75177-5; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-12035119, EBI-741424;
CC O75177-5; Q96HR8: NAF1; NbExp=3; IntAct=EBI-12035119, EBI-2515597;
CC O75177-5; Q06710: PAX8; NbExp=3; IntAct=EBI-12035119, EBI-2683132;
CC O75177-5; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-12035119, EBI-746118;
CC O75177-5; Q15427: SF3B4; NbExp=3; IntAct=EBI-12035119, EBI-348469;
CC O75177-5; Q9BWW4: SSBP3; NbExp=3; IntAct=EBI-12035119, EBI-2902395;
CC O75177-5; Q13470-2: TNK1; NbExp=3; IntAct=EBI-12035119, EBI-11018037;
CC O75177-5; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-12035119, EBI-11975223;
CC O75177-5; Q8NF64-3: ZMIZ2; NbExp=3; IntAct=EBI-12035119, EBI-12011330;
CC O75177-5; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-12035119, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Note=Localizes to nuclear bodies.
CC Colocalizes with SGO1 at kinetochore (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=O75177-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75177-2; Sequence=VSP_038700;
CC Name=3;
CC IsoId=O75177-3; Sequence=VSP_038698;
CC Name=4;
CC IsoId=O75177-4; Sequence=VSP_038697;
CC Name=5;
CC IsoId=O75177-5; Sequence=VSP_038699;
CC -!- TISSUE SPECIFICITY: Ubiquitous; with lowest levels in spleen.
CC -!- DOMAIN: The MFD (multi-functional domain) domain is involved in
CC transcription transactivation, nuclear body targeting and dimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SS18L1ID474ch20q13.html";
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DR EMBL; AB014593; BAA31668.1; ALT_INIT; mRNA.
DR EMBL; BX640848; CAE45918.1; -; mRNA.
DR EMBL; AY203931; AAP34454.1; -; mRNA.
DR EMBL; AK125656; BAG54230.1; -; mRNA.
DR EMBL; AK291485; BAF84174.1; -; mRNA.
DR EMBL; AL078633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75393.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75392.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75395.1; -; Genomic_DNA.
DR EMBL; BC034494; AAH34494.1; -; mRNA.
DR EMBL; BC068993; AAH68993.1; -; mRNA.
DR CCDS; CCDS13491.1; -. [O75177-1]
DR RefSeq; NP_001288707.1; NM_001301778.1. [O75177-4]
DR RefSeq; NP_945173.1; NM_198935.2. [O75177-1]
DR RefSeq; XP_005260448.1; XM_005260391.1. [O75177-2]
DR RefSeq; XP_011527066.1; XM_011528764.2. [O75177-2]
DR RefSeq; XP_011527069.1; XM_011528767.1. [O75177-5]
DR AlphaFoldDB; O75177; -.
DR SMR; O75177; -.
DR BioGRID; 117505; 98.
DR IntAct; O75177; 65.
DR MINT; O75177; -.
DR STRING; 9606.ENSP00000333012; -.
DR iPTMnet; O75177; -.
DR PhosphoSitePlus; O75177; -.
DR BioMuta; SS18L1; -.
DR EPD; O75177; -.
DR jPOST; O75177; -.
DR MassIVE; O75177; -.
DR MaxQB; O75177; -.
DR PaxDb; O75177; -.
DR PeptideAtlas; O75177; -.
DR PRIDE; O75177; -.
DR ProteomicsDB; 49845; -. [O75177-1]
DR ProteomicsDB; 49846; -. [O75177-2]
DR ProteomicsDB; 49847; -. [O75177-3]
DR ProteomicsDB; 49848; -. [O75177-4]
DR ProteomicsDB; 49849; -. [O75177-5]
DR Antibodypedia; 44341; 156 antibodies from 23 providers.
DR DNASU; 26039; -.
DR Ensembl; ENST00000331758.8; ENSP00000333012.3; ENSG00000184402.15. [O75177-1]
DR Ensembl; ENST00000370848.8; ENSP00000359885.5; ENSG00000184402.15. [O75177-3]
DR GeneID; 26039; -.
DR KEGG; hsa:26039; -.
DR MANE-Select; ENST00000331758.8; ENSP00000333012.3; NM_198935.3; NP_945173.1.
DR UCSC; uc002ycb.4; human. [O75177-1]
DR CTD; 26039; -.
DR DisGeNET; 26039; -.
DR GeneCards; SS18L1; -.
DR HGNC; HGNC:15592; SS18L1.
DR HPA; ENSG00000184402; Low tissue specificity.
DR MIM; 606472; gene.
DR neXtProt; NX_O75177; -.
DR OpenTargets; ENSG00000184402; -.
DR PharmGKB; PA37989; -.
DR VEuPathDB; HostDB:ENSG00000184402; -.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000159853; -.
DR HOGENOM; CLU_054580_1_0_1; -.
DR InParanoid; O75177; -.
DR OMA; SAQQYMG; -.
DR PhylomeDB; O75177; -.
DR TreeFam; TF330999; -.
DR PathwayCommons; O75177; -.
DR SignaLink; O75177; -.
DR SIGNOR; O75177; -.
DR BioGRID-ORCS; 26039; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; SS18L1; human.
DR GeneWiki; SS18L1; -.
DR GenomeRNAi; 26039; -.
DR Pharos; O75177; Tbio.
DR PRO; PR:O75177; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O75177; protein.
DR Bgee; ENSG00000184402; Expressed in lateral nuclear group of thalamus and 206 other tissues.
DR ExpressionAtlas; O75177; baseline and differential.
DR Genevisible; O75177; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0071565; C:nBAF complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Calcium; Centromere; Chromatin regulator;
KW Chromosome; Kinetochore; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..396
FT /note="Calcium-responsive transactivator"
FT /id="PRO_0000181825"
FT REGION 1..148
FT /note="N-terminal auto-inhibitory domain; necessary for
FT interaction with SMARCA4/BRG1"
FT /evidence="ECO:0000250"
FT REGION 72..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..232
FT /note="Methionine-rich intra-molecular domain"
FT /evidence="ECO:0000250"
FT REGION 192..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..317
FT /note="MFD domain"
FT /evidence="ECO:0000250"
FT REGION 311..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..396
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 387..396
FT /note="Necessary for interaction with CREBBP and for the
FT recruitment of CREBBP to the nuclear bodies"
FT /evidence="ECO:0000250"
FT MOTIF 50..53
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 353..356
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 371..379
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 391..394
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038697"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038698"
FT VAR_SEQ 1..49
FT /note="MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILEYQSKGKTAECTQ ->
FT MQSLSTEARYVPRVPQHRDQISPRSPQHGGQICPRSPLHRGQICPRSPPARR (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038699"
FT VAR_SEQ 1..23
FT /note="MSVAFASARPRGKGEVTQQTIQK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_038700"
FT VARIANT 189
FT /note="M -> I (in dbSNP:rs17853304)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_062534"
FT VARIANT 321
FT /note="A -> T (in dbSNP:rs36106901)"
FT /id="VAR_053691"
FT CONFLICT 128
FT /note="S -> G (in Ref. 2; CAE45918)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="T -> S (in Ref. 4; BAF84174)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="T -> A (in Ref. 4; BAG54230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42990 MW; B76B7D61C7DF5592 CRC64;
MSVAFASARP RGKGEVTQQT IQKMLDENHH LIQCILEYQS KGKTAECTQY QQILHRNLVY
LATIADSNQN MQSLLPAPPT QNMNLGPGAL TQSGSSQGLH SQGSLSDAIS TGLPPSSLLQ
GQIGNGPSHV SMQQTAPNTL PTTSMSISGP GYSHAGPASQ GVPMQGQGTI GNYVSRTNIN
MQSNPVSMMQ QQAATSHYSS AQGGSQHYQG QSSIAMMGQG SQGSSMMGQR PMAPYRPSQQ
GSSQQYLGQE EYYGEQYSHS QGAAEPMGQQ YYPDGHGDYA YQQSSYTEQS YDRSFEESTQ
HYYEGGNSQY SQQQAGYQQG AAQQQTYSQQ QYPSQQSYPG QQQGYGSAQG APSQYPGYQQ
GQGQQYGSYR APQTAPSAQQ QRPYGYEQGQ YGNYQQ
