SYNEM_HUMAN
ID SYNEM_HUMAN Reviewed; 1565 AA.
AC O15061; A7E2Y2; Q2TBJ4; Q5NJJ9; Q8TE61; Q8TE62;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Synemin {ECO:0000305};
DE AltName: Full=Desmuslin;
GN Name=SYNM {ECO:0000312|HGNC:HGNC:24466}; Synonyms=DMN, KIAA0353, SYN;
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] (ISOFORMS 1 AND 2), SUBUNIT, TISSUE SPECIFICITY,
RP AND VARIANTS TRP-355 AND LEU-567.
RC TISSUE=Placenta, and Skeletal muscle;
RX PubMed=11737198; DOI=10.1046/j.0014-2956.2001.02594.x;
RA Titeux M., Brocheriou V., Xue Z., Gao J., Pellissier J.-F., Guicheney P.,
RA Paulin D., Li Z.;
RT "Human synemin gene generates splice variants encoding two distinct
RT intermediate filament proteins.";
RL Eur. J. Biochem. 268:6435-6449(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH DES AND
RP DTNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT ALA-272.
RC TISSUE=Skeletal muscle;
RX PubMed=11353857; DOI=10.1073/pnas.111153298;
RA Mizuno Y., Thompson T.G., Guyon J.R., Lidov H.G.W., Brosius M., Imamura M.,
RA Ozawa E., Watkins S.C., Kunkel L.M.;
RT "Desmuslin, an intermediate filament protein that interacts with alpha-
RT dystrobrevin and desmin.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6156-6161(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Xue Z., Izmiryan A., Paulin D., Li Z.;
RT "Synemin gene generates different spliced isoforms expressed selectively in
RT either astrocytes or neurons.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS TRP-355
RP AND SER-462.
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS TRP-355;
RP SER-462 AND GLY-1386.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-1565 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=14552890; DOI=10.1016/s0014-4886(03)00240-1;
RA Tawk M., Titeux M., Fallet C., Li Z., Daumas-Duport C., Cavalcante L.A.,
RA Paulin D., Moura-Neto V.;
RT "Synemin expression in developing normal and pathological human retina and
RT lens.";
RL Exp. Neurol. 183:499-507(2003).
RN [9]
RP FUNCTION, AND INTERACTION WITH DMD AND UTRN.
RX PubMed=16777071; DOI=10.1016/j.bbrc.2006.05.192;
RA Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.;
RT "Interactions of intermediate filament protein synemin with dystrophin and
RT utrophin.";
RL Biochem. Biophys. Res. Commun. 346:768-777(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP FUNCTION, AND INTERACTION WITH VCL.
RX PubMed=18028034; DOI=10.1042/bj20071188;
RA Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.;
RT "Human alpha-synemin interacts directly with vinculin and metavinculin.";
RL Biochem. J. 409:657-667(2008).
RN [12]
RP INTERACTION WITH TLN1, AND SUBCELLULAR LOCATION.
RX PubMed=18342854; DOI=10.1016/j.yexcr.2008.01.034;
RA Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.;
RT "Identification of a repeated domain within mammalian alpha-synemin that
RT interacts directly with talin.";
RL Exp. Cell Res. 314:1839-1849(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044; SER-1049 AND SER-1435,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-598 AND SER-1181,
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; THR-598; THR-651;
RP SER-653; SER-1044; SER-1049; SER-1181 AND SER-1435, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-1044 AND SER-1049,
RP AND 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 [18]
RP VARIANTS ILE-330; TRP-338; LEU-567; ALA-612; LEU-761; TRP-946; ARG-976;
RP LEU-1059; PRO-1067 AND LEU-1077.
RX PubMed=11454237; DOI=10.1186/1471-2156-2-8;
RA Mizuno Y., Puca A.A., O'Brien K.F., Beggs A.H., Kunkel L.M.;
RT "Genomic organization and single-nucleotide polymorphism map of desmuslin,
RT a novel intermediate filament protein on chromosome 15q26.3.";
RL BMC Genet. 2:8-8(2001).
CC -!- FUNCTION: Type-VI intermediate filament (IF) which plays an important
CC cytoskeletal role within the muscle cell cytoskeleton. It forms
CC heteromeric IFs with desmin and/or vimentin, and via its interaction
CC with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1,
CC utrophin and vinculin, is able to link these heteromeric IFs to
CC adherens-type junctions, such as to the costameres, neuromuscular
CC junctions, and myotendinous junctions within striated muscle cells.
CC {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:16777071,
CC ECO:0000269|PubMed:18028034}.
CC -!- SUBUNIT: Interacts with GFAP and VIM (By similarity). Isoform 1
CC interacts with TLN1 and VCL. Isoform 2 interacts with DES and DTNA.
CC Isoform 1 and isoform 2 interact with DMD and UTRN. {ECO:0000250,
CC ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:11737198,
CC ECO:0000269|PubMed:16777071, ECO:0000269|PubMed:18028034,
CC ECO:0000269|PubMed:18342854}.
CC -!- INTERACTION:
CC O15061; Q8WZ42: TTN; NbExp=3; IntAct=EBI-7843148, EBI-681210;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens
CC junction. Note=There are at least two distinct SYNM subpopulations, one
CC in which SYMN interacts with DES within the Z-lines, and another in
CC which it interacts with both DTNA and DES at the costamere.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=O15061-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=O15061-2; Sequence=VSP_002465;
CC Name=3;
CC IsoId=O15061-3; Sequence=VSP_036478, VSP_036479;
CC -!- TISSUE SPECIFICITY: Isoform 2 is strongly detected in adult heart,
CC fetal skeletal muscles and fetal heart. Isoform 1 is weakly detected in
CC fetal heart and also in fetal skeletal muscle. Isoform 1 and isoform 2
CC are detected in adult bladder (at protein level). The mRNA is
CC predominantly expressed in heart and muscle with some expression in
CC brain which may be due to tissue-specific isoforms.
CC {ECO:0000269|PubMed:11353857, ECO:0000269|PubMed:11737198}.
CC -!- DEVELOPMENTAL STAGE: In lens, first detected at 16 weeks when
CC expression is weakly and uniformly distributed. Subsequently,
CC expression becomes much stronger in the epithelium of the anterior part
CC at 25 weeks and later. In retina, weakly expressed at 15 weeks in the
CC nerve fiber and ganglion cell layers (NFL and GCL). From 25 weeks
CC onwards, much stronger expression is observed in the endfeet of Mueller
CC cells, the NFL, and GCL, and much lower expression is observed in a
CC minor subpopulation of cells in the inner cell layer (INL). At 30 and
CC 36 weeks, expression remains in the neural retina, and subsequently
CC becomes stronger in the NFL, GCL, and INL and is decreased in Mueller
CC cells. At 36 weeks, also expressed at the external border of the outer
CC nuclear layer (ONL) (at protein level). {ECO:0000269|PubMed:14552890}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI10067.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA20810.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ310521; CAC83858.1; -; mRNA.
DR EMBL; AJ310522; CAC83859.1; -; mRNA.
DR EMBL; AF359284; AAK57487.1; -; mRNA.
DR EMBL; AJ697971; CAG27071.1; -; mRNA.
DR EMBL; AB002351; BAA20810.2; ALT_INIT; mRNA.
DR EMBL; AC036108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC223423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110066; AAI10067.1; ALT_INIT; mRNA.
DR EMBL; BC151243; AAI51244.1; -; mRNA.
DR CCDS; CCDS73786.1; -. [O15061-2]
DR CCDS; CCDS73787.1; -. [O15061-1]
DR RefSeq; NP_056101.5; NM_015286.5.
DR RefSeq; NP_663780.2; NM_145728.2.
DR PDB; 6EWO; X-ray; 2.30 A; C/G=426-434.
DR PDBsum; 6EWO; -.
DR AlphaFoldDB; O15061; -.
DR BioGRID; 116923; 47.
DR IntAct; O15061; 22.
DR MINT; O15061; -.
DR STRING; 9606.ENSP00000336775; -.
DR GlyGen; O15061; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15061; -.
DR PhosphoSitePlus; O15061; -.
DR BioMuta; SYNM; -.
DR EPD; O15061; -.
DR jPOST; O15061; -.
DR MassIVE; O15061; -.
DR MaxQB; O15061; -.
DR PaxDb; O15061; -.
DR PeptideAtlas; O15061; -.
DR PRIDE; O15061; -.
DR ProteomicsDB; 48411; -. [O15061-1]
DR ProteomicsDB; 48412; -. [O15061-2]
DR ProteomicsDB; 48413; -. [O15061-3]
DR Antibodypedia; 29140; 175 antibodies from 20 providers.
DR DNASU; 23336; -.
DR Ensembl; ENST00000328642.11; ENSP00000330469.8; ENSG00000182253.15. [O15061-3]
DR Ensembl; ENST00000336292.11; ENSP00000336775.7; ENSG00000182253.15. [O15061-1]
DR Ensembl; ENST00000594047.2; ENSP00000472953.1; ENSG00000182253.15. [O15061-2]
DR GeneID; 23336; -.
DR KEGG; hsa:23336; -.
DR MANE-Select; ENST00000336292.11; ENSP00000336775.7; NM_145728.3; NP_663780.2.
DR UCSC; uc032crv.2; human. [O15061-1]
DR CTD; 23336; -.
DR DisGeNET; 23336; -.
DR GeneCards; SYNM; -.
DR HGNC; HGNC:24466; SYNM.
DR HPA; ENSG00000182253; Tissue enhanced (intestine, skeletal muscle, urinary bladder).
DR MIM; 606087; gene.
DR neXtProt; NX_O15061; -.
DR OpenTargets; ENSG00000182253; -.
DR PharmGKB; PA164726408; -.
DR VEuPathDB; HostDB:ENSG00000182253; -.
DR eggNOG; ENOG502QTUH; Eukaryota.
DR GeneTree; ENSGT00940000159268; -.
DR InParanoid; O15061; -.
DR OrthoDB; 104920at2759; -.
DR PhylomeDB; O15061; -.
DR PathwayCommons; O15061; -.
DR SignaLink; O15061; -.
DR BioGRID-ORCS; 23336; 7 hits in 285 CRISPR screens.
DR ChiTaRS; SYNM; human.
DR GenomeRNAi; 23336; -.
DR Pharos; O15061; Tbio.
DR PRO; PR:O15061; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O15061; protein.
DR Bgee; ENSG00000182253; Expressed in seminal vesicle and 206 other tissues.
DR ExpressionAtlas; O15061; baseline and differential.
DR Genevisible; O15061; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043034; C:costamere; IDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0060053; C:neurofilament cytoskeleton; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; IDA:UniProtKB.
DR GO; GO:0017166; F:vinculin binding; IDA:UniProtKB.
DR GO; GO:0031443; P:fast-twitch skeletal muscle fiber contraction; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; TAS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR030634; SYNM.
DR PANTHER; PTHR47136; PTHR47136; 1.
DR Pfam; PF00038; Filament; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Intermediate filament; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1565
FT /note="Synemin"
FT /id="PRO_0000063778"
FT DOMAIN 11..322
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..10
FT /note="Head"
FT REGION 11..320
FT /note="Interaction with DMD and UTRN"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 11..49
FT /note="Coil 1A"
FT REGION 50..58
FT /note="Linker 1"
FT REGION 59..163
FT /note="Coil 1B"
FT REGION 164..186
FT /note="Linker 12"
FT REGION 187..300
FT /note="Coil 2"
FT REGION 301..1565
FT /note="Tail"
FT REGION 401..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1463
FT /note="Interaction with TLN1 and VCL"
FT /evidence="ECO:0000269|PubMed:18028034,
FT ECO:0000269|PubMed:18342854"
FT REGION 1198..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1563
FT /note="Interaction with DMD and UTRN"
FT /evidence="ECO:0000269|PubMed:16777071"
FT REGION 1332..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1505..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 651
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70IV5"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70IV5"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70IV5"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1487
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q70IV5"
FT VAR_SEQ 336..339
FT /note="EFRN -> DGCE (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036478"
FT VAR_SEQ 340..1565
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036479"
FT VAR_SEQ 1152..1463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11353857,
FT ECO:0000303|PubMed:11737198"
FT /id="VSP_002465"
FT VARIANT 272
FT /note="V -> A (in dbSNP:rs2305445)"
FT /evidence="ECO:0000269|PubMed:11353857"
FT /id="VAR_012295"
FT VARIANT 330
FT /note="V -> I (in dbSNP:rs5030691)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012296"
FT VARIANT 338
FT /note="R -> W"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012297"
FT VARIANT 355
FT /note="R -> W (in dbSNP:rs3743242)"
FT /evidence="ECO:0000269|PubMed:11737198,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_059378"
FT VARIANT 462
FT /note="G -> S (in dbSNP:rs3134595)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_059379"
FT VARIANT 567
FT /note="P -> L (in dbSNP:rs3743244)"
FT /evidence="ECO:0000269|PubMed:11454237,
FT ECO:0000269|PubMed:11737198"
FT /id="VAR_012298"
FT VARIANT 612
FT /note="E -> A (in dbSNP:rs5030692)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012299"
FT VARIANT 761
FT /note="P -> L (in dbSNP:rs3743247)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012300"
FT VARIANT 946
FT /note="R -> W (in dbSNP:rs5030694)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012301"
FT VARIANT 976
FT /note="Q -> R (in dbSNP:rs5030695)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012302"
FT VARIANT 1059
FT /note="P -> L (in dbSNP:rs5030697)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012303"
FT VARIANT 1067
FT /note="R -> P (in dbSNP:rs5030698)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012304"
FT VARIANT 1077
FT /note="S -> L (in dbSNP:rs5030699)"
FT /evidence="ECO:0000269|PubMed:11454237"
FT /id="VAR_012305"
FT VARIANT 1130
FT /note="G -> S (in dbSNP:rs9920074)"
FT /id="VAR_059380"
FT VARIANT 1345
FT /note="G -> A (in dbSNP:rs7167599)"
FT /id="VAR_059381"
FT VARIANT 1386
FT /note="E -> G (in dbSNP:rs2292288)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_012306"
FT VARIANT 1462
FT /note="F -> C (in dbSNP:rs2292287)"
FT /id="VAR_012307"
FT CONFLICT 4
FT /note="W -> L (in Ref. 1; CAC83858/CAC83859 and 3;
FT CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="Missing (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="Missing (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> G (in Ref. 3; CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="A -> T (in Ref. 3; CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="D -> G (in Ref. 3; CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="E -> G (in Ref. 3; CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="E -> Q (in Ref. 1; CAC83858/CAC83859 and 3;
FT CAG27071)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="A -> V (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="Q -> H (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="K -> N (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="E -> Q (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="T -> A (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="V -> L (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="K -> N (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="D -> N (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="E -> Q (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 874
FT /note="R -> P (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="R -> K (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1004
FT /note="N -> D (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1019
FT /note="L -> V (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1039
FT /note="L -> M (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="P -> L (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="E -> G (in Ref. 1; CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1292
FT /note="I -> T (in Ref. 1; CAC83859)"
FT /evidence="ECO:0000305"
FT CONFLICT 1493
FT /note="A -> R (in Ref. 6; AAI10067)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509
FT /note="A -> V (in Ref. 1; CAC83858/CAC83859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1565 AA; 172868 MW; C76056C65127C1C8 CRC64;
MLSWRLQTGP EKAELQELNA RLYDYVCRVR ELERENLLLE EELRGRRGRE GLWAEGQARC
AEEARSLRQQ LDELSWATAL AEGERDALRR ELRELQRLDA EERAARGRLD AELGAQQREL
QEALGARAAL EALLGRLQAE RRGLDAAHER DVRELRARAA SLTMHFRARA TGPAAPPPRL
REVHDSYALL VAESWRETVQ LYEDEVRELE EALRRGQESR LQAEEETRLC AQEAEALRRE
ALGLEQLRAR LEDALLRMRE EYGIQAEERQ RVIDCLEDEK ATLTLAMADW LRDYQDLLQV
KTGLSLEVAT YRALLEGESN PEIVIWAEHV ENMPSEFRNK SYHYTDSLLQ RENERNLFSR
QKAPLASFNH SSALYSNLSG HRGSQTGTSI GGDARRGFLG SGYSSSATTQ QENSYGKAVS
SQTNVRTFSP TYGLLRNTEA QVKTFPDRPK AGDTREVPVY IGEDSTIARE SYRDRRDKVA
AGASESTRSN ERTVILGKKT EVKATREQER NRPETIRTKP EEKMFDSKEK ASEERNLRWE
ELTKLDKEAR QRESQQMKEK AKEKDSPKEK SVREREVPIS LEVSQDRRAE VSPKGLQTPV
KDAGGGTGRE AEARELRFRL GTSDATGSLQ GDSMTETVAE NIVTSILKQF TQSPETEASA
DSFPDTKVTY VDRKELPGER KTKTEIVVES KLTEDVDVSD EAGLDYLLSK DIKEVGLKGK
SAEQMIGDII NLGLKGREGR AKVVNVEIVE EPVSYVSGEK PEEFSVPFKV EEVEDVSPGP
WGLVKEEEGY GESDVTFSVN QHRRTKQPQE NTTHVEEVTE AGDSEGEQSY FVSTPDEHPG
GHDRDDGSVY GQIHIEEEST IRYSWQDEIV QGTRRRTQKD GAVGEKVVKP LDVPAPSLEG
DLGSTHWKEQ ARSGEFHAEP TVIEKEIKIP HEFHTSMKGI SSKEPRQQLV EVIGQLEETL
PERMREELSA LTREGQGGPG SVSVDVKKVQ GAGGSSVTLV AEVNVSQTVD ADRLDLEELS
KDEASEMEKA VESVVRESLS RQRSPAPGSP DEEGGAEAPA AGIRFRRWAT RELYIPSGES
EVAGGASHSS GQRTPQGPVS ATVEVSSPTG FAQSQVLEDV SQAARHIKLG PSEVWRTERM
SYEGPTAEVV EVSAGGDLSQ AASPTGASRS VRHVTLGPGQ SPLSREVIFL GPAPACPEAW
GSPEPGPAES SADMDGSGRH STFGCRQFHA EKEIIFQGPI SAAGKVGDYF ATEESVGTQT
SVRQLQLGPK EGFSGQIQFT APLSDKVELG VIGDSVHMEG LPGSSTSIRH ISIGPQRHQT
TQQIVYHGLV PQLGESGDSE STVHGEGSAD VHQATHSHTS GRQTVMTEKS TFQSVVSESP
QEDSAEDTSG AEMTSGVSRS FRHIRLGPTE TETSEHIAIR GPVSRTFVLA GSADSPELGK
LADSSRTLRH IAPGPKETSF TFQMDVSNVE AIRSRTQEAG ALGVSDRGSW RDADSRNDQA
VGVSFKASAG EGDQAHREQG KEQAMFDKKV QLQRMVDQRS VISDEKKVAL LYLDNEEEEN
DGHWF
