COBL_HUMAN
ID COBL_HUMAN Reviewed; 1261 AA.
AC O75128; A4D257; A7E2B0; B7ZLW9; B9EGF8; Q2T9J3; Q504Y4; Q86XA7; Q8N304;
AC Q8TCM1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein cordon-bleu;
GN Name=COBL; Synonyms=KIAA0633;
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 6), AND VARIANTS LEU-526;
RP ALA-577; ILE-607 AND GLN-919.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ALA-577 AND
RP ILE-607.
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4; 5 AND 7),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-1261 (ISOFORM 2), AND
RP VARIANTS ALA-577; ILE-607; ASN-927 AND PRO-1015.
RC TISSUE=Brain, Cervix, Muscle, Placenta, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741 AND SER-815, 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 FUNCTION.
RX PubMed=21816349; DOI=10.1016/j.molcel.2011.07.010;
RA Husson C., Renault L., Didry D., Pantaloni D., Carlier M.F.;
RT "Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
RT filament assembly.";
RL Mol. Cell 43:464-477(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-324; SER-347;
RP SER-574; SER-741; SER-815; SER-962 AND SER-1227, AND IDENTIFICATION BY MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269; SER-578; SER-815 AND
RP SER-1192, VARIANT [LARGE SCALE ANALYSIS] ALA-577, 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).
CC -!- FUNCTION: Plays an important role in the reorganization of the actin
CC cytoskeleton. Regulates neuron morphogenesis and increases branching of
CC axons and dendrites. Regulates dendrite branching in Purkinje cells (By
CC similarity). Binds to and sequesters actin monomers (G actin).
CC Nucleates actin polymerization by assembling three actin monomers in
CC cross-filament orientation and thereby promotes growth of actin
CC filaments at the barbed end. Can also mediate actin depolymerization at
CC barbed ends and severing of actin filaments. Promotes formation of cell
CC ruffles. {ECO:0000250, ECO:0000269|PubMed:21816349}.
CC -!- SUBUNIT: Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X. Interacts (via WH2 domains) with actin monomers. Interacts with
CC both PACSIN1 and DBNL. Identified in a complex composed of COBL,
CC PACSIN1 and WASL. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O75128; P13196: ALAS1; NbExp=3; IntAct=EBI-3446582, EBI-3905054;
CC O75128; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-3446582, EBI-721769;
CC O75128; Q9UNF0: PACSIN2; NbExp=3; IntAct=EBI-3446582, EBI-742503;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Note=Recruited to the cell membrane via
CC interaction with PACSIN1. Colocalizes with the actin cytoskeleton.
CC Detected throughout the neuron cell body, as well as in axons and
CC dendrites (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O75128-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75128-2; Sequence=VSP_021607, VSP_021608;
CC Name=3;
CC IsoId=O75128-3; Sequence=VSP_021613;
CC Name=4;
CC IsoId=O75128-4; Sequence=VSP_021609, VSP_021612;
CC Name=5;
CC IsoId=O75128-5; Sequence=VSP_021610, VSP_021611;
CC Name=6;
CC IsoId=O75128-6; Sequence=VSP_040711, VSP_040712;
CC Name=7;
CC IsoId=O75128-7; Sequence=VSP_021608, VSP_021613;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31608.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014533; BAA31608.1; ALT_INIT; mRNA.
DR EMBL; AL713786; CAD28543.1; -; mRNA.
DR EMBL; AC005535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236955; EAL23896.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW60962.1; -; Genomic_DNA.
DR EMBL; BC029275; AAH29275.1; -; mRNA.
DR EMBL; BC045771; AAH45771.1; -; mRNA.
DR EMBL; BC094695; AAH94695.1; -; mRNA.
DR EMBL; BC111496; AAI11497.1; -; mRNA.
DR EMBL; BC136441; AAI36442.1; -; mRNA.
DR EMBL; BC144099; AAI44100.1; -; mRNA.
DR EMBL; BC150263; AAI50264.1; -; mRNA.
DR CCDS; CCDS34637.1; -. [O75128-1]
DR CCDS; CCDS75601.1; -. [O75128-5]
DR CCDS; CCDS75602.1; -. [O75128-7]
DR CCDS; CCDS87505.1; -. [O75128-4]
DR PIR; T00381; T00381.
DR RefSeq; NP_001274365.1; NM_001287436.2. [O75128-7]
DR RefSeq; NP_001274367.1; NM_001287438.2. [O75128-5]
DR RefSeq; NP_001333370.1; NM_001346441.1.
DR RefSeq; NP_001333371.1; NM_001346442.1. [O75128-3]
DR RefSeq; NP_001333372.1; NM_001346443.1.
DR RefSeq; NP_001333373.1; NM_001346444.1. [O75128-4]
DR RefSeq; NP_056013.2; NM_015198.4. [O75128-1]
DR RefSeq; XP_011513537.1; XM_011515235.1. [O75128-2]
DR PDB; 4PL8; X-ray; 2.00 A; H=1095-1106.
DR PDBsum; 4PL8; -.
DR AlphaFoldDB; O75128; -.
DR SMR; O75128; -.
DR BioGRID; 116846; 77.
DR IntAct; O75128; 52.
DR MINT; O75128; -.
DR STRING; 9606.ENSP00000378912; -.
DR iPTMnet; O75128; -.
DR PhosphoSitePlus; O75128; -.
DR BioMuta; COBL; -.
DR EPD; O75128; -.
DR jPOST; O75128; -.
DR MassIVE; O75128; -.
DR MaxQB; O75128; -.
DR PaxDb; O75128; -.
DR PeptideAtlas; O75128; -.
DR PRIDE; O75128; -.
DR ProteomicsDB; 49781; -. [O75128-1]
DR ProteomicsDB; 49782; -. [O75128-2]
DR ProteomicsDB; 49783; -. [O75128-3]
DR ProteomicsDB; 49784; -. [O75128-4]
DR ProteomicsDB; 49785; -. [O75128-5]
DR ProteomicsDB; 49786; -. [O75128-6]
DR ProteomicsDB; 49787; -. [O75128-7]
DR Antibodypedia; 13730; 120 antibodies from 16 providers.
DR DNASU; 23242; -.
DR Ensembl; ENST00000265136.12; ENSP00000265136.7; ENSG00000106078.19. [O75128-1]
DR Ensembl; ENST00000395540.6; ENSP00000378910.2; ENSG00000106078.19. [O75128-4]
DR Ensembl; ENST00000395542.6; ENSP00000378912.3; ENSG00000106078.19. [O75128-7]
DR Ensembl; ENST00000441453.5; ENSP00000399500.1; ENSG00000106078.19. [O75128-5]
DR GeneID; 23242; -.
DR KEGG; hsa:23242; -.
DR MANE-Select; ENST00000265136.12; ENSP00000265136.7; NM_015198.5; NP_056013.2.
DR UCSC; uc003tpr.5; human. [O75128-1]
DR CTD; 23242; -.
DR DisGeNET; 23242; -.
DR GeneCards; COBL; -.
DR HGNC; HGNC:22199; COBL.
DR HPA; ENSG00000106078; Tissue enhanced (brain, skeletal muscle, tongue).
DR MIM; 610317; gene.
DR neXtProt; NX_O75128; -.
DR OpenTargets; ENSG00000106078; -.
DR PharmGKB; PA134869580; -.
DR VEuPathDB; HostDB:ENSG00000106078; -.
DR eggNOG; ENOG502QTAY; Eukaryota.
DR GeneTree; ENSGT00530000063608; -.
DR HOGENOM; CLU_006259_0_0_1; -.
DR InParanoid; O75128; -.
DR OMA; DSQHDSV; -.
DR OrthoDB; 986623at2759; -.
DR PhylomeDB; O75128; -.
DR TreeFam; TF333490; -.
DR PathwayCommons; O75128; -.
DR SignaLink; O75128; -.
DR BioGRID-ORCS; 23242; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; COBL; human.
DR GenomeRNAi; 23242; -.
DR Pharos; O75128; Tbio.
DR PRO; PR:O75128; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O75128; protein.
DR Bgee; ENSG00000106078; Expressed in inferior vagus X ganglion and 179 other tissues.
DR ExpressionAtlas; O75128; baseline and differential.
DR Genevisible; O75128; HS.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0030424; C:axon; ISS:BHF-UCL.
DR GO; GO:0044295; C:axonal growth cone; ISS:BHF-UCL.
DR GO; GO:0005938; C:cell cortex; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0044294; C:dendritic growth cone; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; ISS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0001726; C:ruffle; ISS:BHF-UCL.
DR GO; GO:1990357; C:terminal web; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; ISS:BHF-UCL.
DR GO; GO:0051639; P:actin filament network formation; ISS:BHF-UCL.
DR GO; GO:0030041; P:actin filament polymerization; ISS:BHF-UCL.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:BHF-UCL.
DR GO; GO:0048565; P:digestive tract development; ISS:BHF-UCL.
DR GO; GO:0000578; P:embryonic axis specification; ISS:BHF-UCL.
DR GO; GO:0033504; P:floor plate development; ISS:BHF-UCL.
DR GO; GO:0001889; P:liver development; ISS:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
DR GO; GO:0030903; P:notochord development; ISS:BHF-UCL.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:BHF-UCL.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0001757; P:somite specification; ISS:BHF-UCL.
DR InterPro; IPR039895; COBL-like.
DR InterPro; IPR019025; Cordon-bleu_ubiquitin_domain.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR47008; PTHR47008; 2.
DR Pfam; PF09469; Cobl; 1.
DR Pfam; PF02205; WH2; 3.
DR SMART; SM00246; WH2; 3.
DR PROSITE; PS51082; WH2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1261
FT /note="Protein cordon-bleu"
FT /id="PRO_0000260491"
FT DOMAIN 1109..1129
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1149..1169
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 1237..1257
FT /note="WH2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1196..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 298..303
FT /note="KKRRAP 1"
FT MOTIF 331..336
FT /note="KKRRAP 2"
FT COMPBIAS 259..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5NBX1"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUI5"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5NBX1"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..458
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040711"
FT VAR_SEQ 261
FT /note="K -> KAEQLVLSGADSDEDTSRAAPGRGLN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021607"
FT VAR_SEQ 366
FT /note="V -> GGGRQVPQKPPRGTARGPPQLVLPPPPPYPPPDTDVVEPLSFPGEGA
FT GSEASDPIPKL (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021608"
FT VAR_SEQ 367..469
FT /note="SLPLGSGSHCSPDGAPQVLSEAEETVSVGSCFASEDTTEDSGVMSSPSDIVS
FT LDSQQDSMKYKDKWATDQEDCSDQDLAGTPDLGPQKSPLWEKNGSENSHLR -> YGAA
FT EAVIRLLSLLLNTTAPGTAKPRTLWMSEGRSSLHNPEIKCSCFSSSSPFPQSLLSLLLG
FT LSSICECMCTLRHTHAHTHNPSCVLPTSEILAFGRQSLIS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021609"
FT VAR_SEQ 367..379
FT /note="SLPLGSGSHCSPD -> YCCASFPTQAKRF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021610"
FT VAR_SEQ 380..1261
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021611"
FT VAR_SEQ 459..468
FT /note="EKNGSENSHL -> MSAPFSLVFP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_040712"
FT VAR_SEQ 470..1261
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021612"
FT VAR_SEQ 1169..1215
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021613"
FT VARIANT 526
FT /note="P -> L (in dbSNP:rs17656599)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_050894"
FT VARIANT 577
FT /note="D -> A (in dbSNP:rs10230120)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4,
FT ECO:0007744|PubMed:24275569"
FT /id="VAR_029043"
FT VARIANT 607
FT /note="V -> I (in dbSNP:rs2240090)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4"
FT /id="VAR_029044"
FT VARIANT 919
FT /note="H -> Q (in dbSNP:rs2240089)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_050895"
FT VARIANT 927
FT /note="D -> N (in dbSNP:rs17134128)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029045"
FT VARIANT 1015
FT /note="A -> P (in dbSNP:rs17134127)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029046"
FT CONFLICT 481
FT /note="Missing (in Ref. 5; AAH29275)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="H -> Y (in Ref. 5; AAH45771)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="V -> A (in Ref. 5; AAI44100)"
FT /evidence="ECO:0000305"
FT HELIX 1114..1118
FT /evidence="ECO:0007829|PDB:4PL8"
FT HELIX 1123..1125
FT /evidence="ECO:0007829|PDB:4PL8"
SQ SEQUENCE 1261 AA; 135617 MW; 2DA7113EFD343AB3 CRC64;
MDAPRASAAK PPTGRKMKAR APPPPGKAAT LHVHSDQKPP HDGALGSQQN LVRMKEALRA
STMDVTVVLP SGLEKRSVLN GSHAMMDLLV ELCLQNHLNP SHHALEIRSS ETQQPLSFKP
NTLIGTLNVH TVFLKEKVPE EKVKPGPPKV PEKSVRLVVN YLRTQKAVVR VSPEVPLQNI
LPVICAKCEV SPEHVVLLRD NIAGEELELS KSLNELGIKE LYAWDNRRET FRKSSLGNDE
TDKEKKKFLG FFKVNKRSNS KGCLTTPNSP SMHSRSLTLG PSLSLGSISG VSVKSEMKKR
RAPPPPGSGP PVQDKASEKV SLGSQIDLQK KKRRAPAPPP PQPPPPSPLI PNRTEDKEEN
RKSTMVSLPL GSGSHCSPDG APQVLSEAEE TVSVGSCFAS EDTTEDSGVM SSPSDIVSLD
SQQDSMKYKD KWATDQEDCS DQDLAGTPDL GPQKSPLWEK NGSENSHLRT EKAVTASNDE
EDLLIAGEFR KTLAELDEDL EEMEDSYETD TSSLTSSIHG ASNHCPQDAM IPHGDTDAIP
VTFIGEVSDD PVDSGLFSNR NNNAGSFDSE GVASRRDSLA PLQAEHSQPH EKAREEVPAL
HPASHDVGKG IRVALSNISK DGNLMETAPR VTSFASNLHT DNLNAKVKDK VYGCADGERT
QATERVNSQP VNEKDSNDKN AALAPTSWHQ RGQNPGKSYR LKHGLTTYKI IPPKSEMRCY
DRDVSLSTGA IKIDELGNLV SPHATGIRII SLSSSVPEAE SQPIGKVREF WRCNSVEKHL
GRPSESSARG PPSTPVPTQT QNPESRLQAD PKPISPQQKS AHHEGRNPLG EGRNQPPTMG
MGHVRVPAAH TTEVTFLKPQ RRTSSQYVAS AIAKRIGAPK VHADVVRPHG YAEKGYAGKA
PVLAAPPVTV KDDRTSSPHS ETQGWKDGAQ WPCVTPPNNH GEDLAVGAPP RGEVIGPHRK
LSTQDRPAAI HRSSCFSLVQ SSQRDRVSVG QSCGFSGKQS TSSQEASSAS EPRRAPDGTD
PPPPHTSDTQ ACSRELVNGS VRAPGHGEPS HPPGGSGTES HILLEREEKP SVFSTDGNET
DSIWPPSIFG PKKKFKPVVQ RPVPKDTSLH SALMEAIHSA GGKDRLRKTA EHTGEGRPAK
LSYTEAEGER SALLAAIRGH SGTCSLRKVA SSASEELQSF RDAALSAQGS ESPLLEDLGL
LSPPAIPPPP PPPSQALSAP RTASRFSTGT LSNTADARQA LMDAIRSGTG AARLRKVPLL
V
