ELF2_HUMAN
ID ELF2_HUMAN Reviewed; 593 AA.
AC Q15723; E9PCX3; Q15724; Q15725; Q6P1K5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=ETS-related transcription factor Elf-2;
DE AltName: Full=E74-like factor 2;
DE AltName: Full=New ETS-related factor;
GN Name=ELF2 {ECO:0000312|EMBL:AAF67195.1};
GN Synonyms=NERF {ECO:0000303|PubMed:8756667};
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] {ECO:0000305, ECO:0000312|EMBL:AAB37759.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain {ECO:0000269|PubMed:8756667},
RC Fetal liver {ECO:0000269|PubMed:8756667}, and
RC Spleen {ECO:0000312|EMBL:AAB37759.1};
RX PubMed=8756667; DOI=10.1128/mcb.16.9.5091;
RA Oettgen P., Akbarali Y., Boltax J., Best J., Kunsch C., Libermann T.A.;
RT "Characterization of NERF, a novel transcription factor related to the Ets
RT factor ELF-1.";
RL Mol. Cell. Biol. 16:5091-5106(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF67195.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Chronic myeloid leukemia cell;
RA Wilkinson D.A., Neale G.A.M., Mao S., Fernandes E.R., Davenport J.W.,
RA Naeve C.W., Goorha R.M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAH34951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH34951.1};
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 [5] {ECO:0000305}
RP INTERACTION WITH RUNX1.
RX PubMed=10207087; DOI=10.1128/mcb.19.5.3635;
RA Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
RT "Functional and physical interactions between AML1 proteins and an ETS
RT protein, MEF: implications for the pathogenesis of t(8;21)-positive
RT leukemias.";
RL Mol. Cell. Biol. 19:3635-3644(1999).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RUNX1.
RX PubMed=14970218; DOI=10.1074/jbc.m309074200;
RA Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y.,
RA Oettgen P., Zhang D.-E., Libermann T.A.;
RT "Isoforms of the Ets transcription factor NERF/ELF-2 physically interact
RT with AML1 and mediate opposing effects on AML1-mediated transcription of
RT the B cell-specific blk gene.";
RL J. Biol. Chem. 279:19512-19522(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-430, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-185; SER-191;
RP SER-363 AND THR-521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 IDENTIFICATION BY 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-494, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-536, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
CC -!- FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK
CC promoters and acts synergistically with RUNX1 to transactivate the BLK
CC promoter.
CC -!- FUNCTION: Isoform 2 may function in repression of RUNX1-mediated
CC transactivation.
CC -!- SUBUNIT: Interacts with the LIM domains of LMO2 (By similarity).
CC Interacts via its N-terminal region with RUNX1.
CC {ECO:0000250|UniProtKB:Q9JHC9, ECO:0000269|PubMed:10207087,
CC ECO:0000269|PubMed:14970218}.
CC -!- INTERACTION:
CC Q15723; Q01196: RUNX1; NbExp=2; IntAct=EBI-956941, EBI-925904;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=5 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2b
CC {ECO:0000303|PubMed:8756667};
CC IsoId=Q15723-5; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2
CC {ECO:0000303|PubMed:8756667}, NERF-2a {ECO:0000303|PubMed:8756667};
CC IsoId=Q15723-1; Sequence=VSP_014155;
CC Name=2 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1a
CC {ECO:0000303|PubMed:8756667};
CC IsoId=Q15723-2; Sequence=VSP_014154, VSP_014155;
CC Name=3 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1b
CC {ECO:0000303|PubMed:8756667};
CC IsoId=Q15723-3; Sequence=VSP_014154;
CC Name=4 {ECO:0000305};
CC IsoId=Q15723-4; Sequence=VSP_014154, VSP_014156;
CC -!- TISSUE SPECIFICITY: Expressed in all fetal and adult tissues examined.
CC Among fetal tissues, highest levels of expression detected in heart,
CC lung, liver and kidney, and lower levels in brain. Among adult tissues,
CC highest levels of expression detected in heart, placenta, lung,
CC skeletal muscle, spleen, thymus, testis and ovary. Moderate expression
CC in prostate, small intestine, kidney, liver and pancreas, and weak
CC expression in colon, brain and peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:8756667}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65025.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U43188; AAB37759.1; -; mRNA.
DR EMBL; U43189; AAB37760.1; -; mRNA.
DR EMBL; U43189; AAB37761.1; -; mRNA.
DR EMBL; AF256222; AAF67195.1; -; mRNA.
DR EMBL; AF256223; AAF67196.1; -; mRNA.
DR EMBL; AC024032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034951; AAH34951.1; -; mRNA.
DR EMBL; BC065025; AAH65025.1; ALT_FRAME; mRNA.
DR CCDS; CCDS3744.1; -. [Q15723-1]
DR CCDS; CCDS3745.1; -. [Q15723-3]
DR CCDS; CCDS64062.1; -. [Q15723-2]
DR CCDS; CCDS64063.1; -. [Q15723-4]
DR CCDS; CCDS82954.1; -. [Q15723-5]
DR PIR; G02318; G02318.
DR RefSeq; NP_001263386.1; NM_001276457.1. [Q15723-4]
DR RefSeq; NP_001263387.1; NM_001276458.1. [Q15723-2]
DR RefSeq; NP_001263388.1; NM_001276459.1.
DR RefSeq; NP_001317965.1; NM_001331036.1. [Q15723-5]
DR RefSeq; NP_006865.1; NM_006874.3. [Q15723-3]
DR RefSeq; NP_973728.1; NM_201999.2. [Q15723-1]
DR RefSeq; XP_005262861.1; XM_005262804.2.
DR AlphaFoldDB; Q15723; -.
DR SMR; Q15723; -.
DR BioGRID; 108313; 138.
DR IntAct; Q15723; 116.
DR MINT; Q15723; -.
DR STRING; 9606.ENSP00000377782; -.
DR GlyGen; Q15723; 23 sites, 2 O-linked glycans (23 sites).
DR iPTMnet; Q15723; -.
DR PhosphoSitePlus; Q15723; -.
DR BioMuta; ELF2; -.
DR DMDM; 68052029; -.
DR EPD; Q15723; -.
DR jPOST; Q15723; -.
DR MassIVE; Q15723; -.
DR MaxQB; Q15723; -.
DR PaxDb; Q15723; -.
DR PeptideAtlas; Q15723; -.
DR PRIDE; Q15723; -.
DR ProteomicsDB; 19535; -.
DR ProteomicsDB; 60718; -. [Q15723-5]
DR ProteomicsDB; 60719; -. [Q15723-1]
DR ProteomicsDB; 60720; -. [Q15723-2]
DR ProteomicsDB; 60721; -. [Q15723-3]
DR ProteomicsDB; 60722; -. [Q15723-4]
DR Antibodypedia; 896; 157 antibodies from 26 providers.
DR DNASU; 1998; -.
DR Ensembl; ENST00000358635.7; ENSP00000351458.2; ENSG00000109381.21. [Q15723-3]
DR Ensembl; ENST00000379549.7; ENSP00000368867.2; ENSG00000109381.21. [Q15723-4]
DR Ensembl; ENST00000379550.5; ENSP00000368868.1; ENSG00000109381.21. [Q15723-5]
DR Ensembl; ENST00000394235.6; ENSP00000377782.1; ENSG00000109381.21. [Q15723-1]
DR Ensembl; ENST00000510408.5; ENSP00000426997.1; ENSG00000109381.21. [Q15723-2]
DR Ensembl; ENST00000686138.1; ENSP00000510098.1; ENSG00000109381.21. [Q15723-5]
DR GeneID; 1998; -.
DR KEGG; hsa:1998; -.
DR MANE-Select; ENST00000686138.1; ENSP00000510098.1; NM_001331036.3; NP_001317965.1.
DR UCSC; uc003ihm.3; human. [Q15723-5]
DR CTD; 1998; -.
DR DisGeNET; 1998; -.
DR GeneCards; ELF2; -.
DR HGNC; HGNC:3317; ELF2.
DR HPA; ENSG00000109381; Low tissue specificity.
DR MIM; 619798; gene.
DR neXtProt; NX_Q15723; -.
DR OpenTargets; ENSG00000109381; -.
DR PharmGKB; PA27745; -.
DR VEuPathDB; HostDB:ENSG00000109381; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000154953; -.
DR HOGENOM; CLU_027279_2_0_1; -.
DR InParanoid; Q15723; -.
DR OMA; MKNHEEN; -.
DR OrthoDB; 837296at2759; -.
DR PhylomeDB; Q15723; -.
DR TreeFam; TF318679; -.
DR PathwayCommons; Q15723; -.
DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR SignaLink; Q15723; -.
DR SIGNOR; Q15723; -.
DR BioGRID-ORCS; 1998; 59 hits in 1115 CRISPR screens.
DR ChiTaRS; ELF2; human.
DR GeneWiki; ELF2; -.
DR GenomeRNAi; 1998; -.
DR Pharos; Q15723; Tbio.
DR PRO; PR:Q15723; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q15723; protein.
DR Bgee; ENSG00000109381; Expressed in calcaneal tendon and 193 other tissues.
DR ExpressionAtlas; Q15723; baseline and differential.
DR Genevisible; Q15723; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR022084; TF_Elf_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF12310; Elf-1_N; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..593
FT /note="ETS-related transcription factor Elf-2"
FT /id="PRO_0000204087"
FT DNA_BIND 208..290
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 146..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHC9"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHC9"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 494
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 536
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..79
FT /note="MTSAVVDSGGTILELSSNGVENQEESEKVSEYPAVIVEPVPSARLEQGYAAQ
FT VLVYDDETYMMQDVAEEQEVETENVET -> MATSLHEGPTNQLDLLIRA (in
FT isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8756667, ECO:0000303|Ref.2"
FT /id="VSP_014154"
FT VAR_SEQ 117..129
FT /note="PVEVFVPPCVSTP -> P (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:8756667, ECO:0000303|Ref.2"
FT /id="VSP_014155"
FT VAR_SEQ 175..203
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014156"
SQ SEQUENCE 593 AA; 63967 MW; B67013B453559910 CRC64;
MTSAVVDSGG TILELSSNGV ENQEESEKVS EYPAVIVEPV PSARLEQGYA AQVLVYDDET
YMMQDVAEEQ EVETENVETV EASVHSSNAH CTDKTIEAAE ALLHMESPTC LRDSRSPVEV
FVPPCVSTPE FIHAAMRPDV ITETVVEVST EESEPMDTSP IPTSPDSHEP MKKKKVGRKP
KTQQSPISNG SPELGIKKKP REGKGNTTYL WEFLLDLLQD KNTCPRYIKW TQREKGIFKL
VDSKAVSKLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK DMPKNIVVID
DDKSETCNED LAGTTDEKSL ERVSLSAESL LKAASSVRSG KNSSPINCSR AEKGVARVVN
ITSPGHDASS RSPTTTASVS ATAAPRTVRV AMQVPVVMTS LGQKISTVAV QSVNAGAPLI
TSTSPTTATS PKVVIQTIPT VMPASTENGD KITMQPAKII TIPATQLAQC QLQTKSNLTG
SGSINIVGTP LAVRALTPVS IAHGTPVMRL SMPTQQASGQ TPPRVISAVI KGPEVKSEAV
AKKQEHDVKT LQLVEEKPAD GNKTVTHVVV VSAPSAIALP VTMKTEGLVT CEK
