VINC_MOUSE
ID VINC_MOUSE Reviewed; 1066 AA.
AC Q64727; Q8BP32; Q8BS46; Q922C5; Q922D9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Vinculin;
DE AltName: Full=Metavinculin;
GN Name=Vcl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=129/SvJ; TISSUE=Embryo;
RX PubMed=7568093; DOI=10.1073/pnas.92.20.9161;
RA Coll J.-L., Ben-Ze'ev A., Ezzell R.M., Rodriguez Fernandez J.L.,
RA Baribault H., Oshima R.G., Adamson E.D.;
RT "Targeted disruption of vinculin genes in F9 and embryonic stem cells
RT changes cell morphology, adhesion, and locomotion.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9161-9165(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9280281; DOI=10.1016/s0014-5793(97)00901-0;
RA Alatortsev V.E., Kramerova I.A., Frolov M.V., Lavrov S.A., Westphal E.D.;
RT "Vinculin gene is non-essential in Drosophila melanogaster.";
RL FEBS Lett. 413:197-201(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Forelimb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
RP PROTEIN SEQUENCE OF 286-300; 656-666 AND 916-924, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP INTERACTION WITH SORBS1.
RX PubMed=10085297; DOI=10.1083/jcb.144.5.1001;
RA Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H.,
RA Mizoguchi A., Takai Y.;
RT "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at
RT cell-cell and cell-matrix adherens junctions.";
RL J. Cell Biol. 144:1001-1017(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP REGION INVOLVED IN PHOSPHOLIPID MEMBRANE INSERTION.
RX PubMed=20599708; DOI=10.1016/j.bbrc.2010.06.094;
RA Wirth V.F., List F., Diez G., Goldmann W.H.;
RT "Vinculin's C-terminal region facilitates phospholipid membrane
RT insertion.";
RL Biochem. Biophys. Res. Commun. 398:433-437(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-290; SER-346;
RP SER-579; SER-600; SER-721; SER-809 AND TYR-822, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH TLN1.
RX PubMed=20610383; DOI=10.1074/jbc.m109.095455;
RA Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
RA Barsukov I.L., Roberts G.C., Critchley D.R.;
RT "Central region of talin has a unique fold that binds vinculin and actin.";
RL J. Biol. Chem. 285:29577-29587(2010).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=26359501; DOI=10.1074/jbc.m115.678433;
RA Cattin M.E., Wang J., Weldrick J.J., Roeske C.L., Mak E., Thorn S.L.,
RA DaSilva J.N., Wang Y., Lusis A.J., Burgon P.G.;
RT "Deletion of MLIP (muscle-enriched A-type lamin-interacting protein) leads
RT to cardiac hyperactivation of Akt/mammalian target of rapamycin (mTOR) and
RT impaired cardiac adaptation.";
RL J. Biol. Chem. 290:26699-26714(2015).
CC -!- FUNCTION: Actin filament (F-actin)-binding protein involved in cell-
CC matrix adhesion and cell-cell adhesion. Regulates cell-surface E-
CC cadherin expression and potentiates mechanosensing by the E-cadherin
CC complex. May also play important roles in cell morphology and
CC locomotion (By similarity). {ECO:0000250|UniProtKB:P18206,
CC ECO:0000269|PubMed:7568093}.
CC -!- SUBUNIT: Exhibits self-association properties. Part of a complex
CC composed of THSD1, PTK2/FAK1, TLN1 and VCL (By similarity). Interacts
CC with APBB1IP, NRAP and TLN1. Interacts with SYNM. Interacts with CTNNB1
CC and this interaction is necessary for its localization to the cell-cell
CC junctions and for its function in regulating cell surface expression of
CC E-cadherin (By similarity). Interacts with SORBS1 (PubMed:10085297).
CC Interacts with SYNM (By similarity). Interacts with CTNNA1 (By
CC similarity). Binds to ACTN4; this interaction triggers conformational
CC changes (By similarity). {ECO:0000250|UniProtKB:P12003,
CC ECO:0000250|UniProtKB:P18206, ECO:0000269|PubMed:10085297,
CC ECO:0000269|PubMed:20610383}.
CC -!- INTERACTION:
CC Q64727; Q61210: Arhgef1; NbExp=3; IntAct=EBI-432047, EBI-641821;
CC Q64727; Q8VI36: Pxn; NbExp=3; IntAct=EBI-432047, EBI-983394;
CC Q64727; P39447: Tjp1; NbExp=8; IntAct=EBI-432047, EBI-79508;
CC Q64727; P26039: Tln1; NbExp=2; IntAct=EBI-432047, EBI-1039593;
CC Q64727; P49024: PXN; Xeno; NbExp=4; IntAct=EBI-432047, EBI-2896280;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12003};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:26359501}; Peripheral membrane protein
CC {ECO:0000269|PubMed:26359501}; Cytoplasmic side
CC {ECO:0000269|PubMed:26359501}. Note=Recruitment to cell-cell junctions
CC occurs in a myosin II-dependent manner. Interaction with CTNNB1 is
CC necessary for its localization to the cell-cell junctions.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC 'inactive' conformation, extensive interactions between the head and
CC tail domains prevent detectable binding to most of its ligands. It
CC takes on an 'active' conformation after cooperative and simultaneous
CC binding of two different ligands. This activation involves displacement
CC of the head-tail interactions and leads to a significant accumulation
CC of ternary complexes. The active form then binds a number of proteins
CC that have both signaling and structural roles that are essential for
CC cell adhesion. {ECO:0000250|UniProtKB:P18206}.
CC -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-
CC D4. The C-terminal tail (Vt) binds F-actin and cross-links actin
CC filaments into bundles. An intramolecular interaction between Vh and Vt
CC masks the F-actin-binding domain located in Vt. The binding of talin
CC and alpha-actinin to the D1 subdomain of vinculin induces a helical
CC bundle conversion of this subdomain, leading to the disruption of the
CC intramolecular interaction and the exposure of the cryptic F-actin-
CC binding domain of Vt. Vt inhibits actin filament barbed end elongation
CC without affecting the critical concentration of actin assembly.
CC {ECO:0000250|UniProtKB:P18206}.
CC -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC Phosphorylation on Tyr-1065 in activated platelets affects head-tail
CC interactions and cell spreading but has no effect on actin binding nor
CC on localization to focal adhesion plaques (By similarity).
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- PTM: Acetylated; mainly by myristic acid but also by a small amount of
CC palmitic acid. {ECO:0000250|UniProtKB:P12003}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; L13300; AAA40557.1; -; Genomic_DNA.
DR EMBL; L13299; AAA40557.1; JOINED; Genomic_DNA.
DR EMBL; L18880; AAB96843.1; -; mRNA.
DR EMBL; AK035184; BAC28973.1; -; mRNA.
DR EMBL; AK077850; BAC37033.1; -; mRNA.
DR EMBL; BC008520; AAH08520.1; -; mRNA.
DR EMBL; BC008554; AAH08554.1; -; mRNA.
DR CCDS; CCDS26860.1; -.
DR PIR; A60965; A60965.
DR PIR; T10108; T10108.
DR RefSeq; NP_033528.3; NM_009502.4.
DR PDB; 5Y04; X-ray; 2.85 A; A=1-250.
DR PDBsum; 5Y04; -.
DR AlphaFoldDB; Q64727; -.
DR BMRB; Q64727; -.
DR SMR; Q64727; -.
DR BioGRID; 204506; 44.
DR CORUM; Q64727; -.
DR IntAct; Q64727; 16.
DR MINT; Q64727; -.
DR STRING; 10090.ENSMUSP00000022369; -.
DR iPTMnet; Q64727; -.
DR PhosphoSitePlus; Q64727; -.
DR REPRODUCTION-2DPAGE; Q64727; -.
DR CPTAC; non-CPTAC-3755; -.
DR EPD; Q64727; -.
DR jPOST; Q64727; -.
DR MaxQB; Q64727; -.
DR PaxDb; Q64727; -.
DR PeptideAtlas; Q64727; -.
DR PRIDE; Q64727; -.
DR ProteomicsDB; 298282; -.
DR Antibodypedia; 884; 930 antibodies from 45 providers.
DR DNASU; 22330; -.
DR Ensembl; ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
DR GeneID; 22330; -.
DR KEGG; mmu:22330; -.
DR UCSC; uc007skz.1; mouse.
DR CTD; 7414; -.
DR MGI; MGI:98927; Vcl.
DR VEuPathDB; HostDB:ENSMUSG00000021823; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_012338_0_0_1; -.
DR InParanoid; Q64727; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 270073at2759; -.
DR PhylomeDB; Q64727; -.
DR TreeFam; TF313686; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 22330; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Vcl; mouse.
DR PRO; PR:Q64727; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q64727; protein.
DR Bgee; ENSMUSG00000021823; Expressed in aorta tunica media and 255 other tissues.
DR ExpressionAtlas; Q64727; baseline and differential.
DR Genevisible; Q64727; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005903; C:brush border; ISS:AgBase.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0043034; C:costamere; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0002102; C:podosome; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR GO; GO:0002162; F:dystroglycan binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0034333; P:adherens junction assembly; ISO:MGI.
DR GO; GO:0043297; P:apical junction assembly; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IGI:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISO:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:1904702; P:regulation of protein localization to adherens junction; ISO:MGI.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR46180; PTHR46180; 1.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 6.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell adhesion; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1066
FT /note="Vinculin"
FT /id="PRO_0000064253"
FT REPEAT 259..369
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 370..479
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 480..589
FT /note="3"
FT /evidence="ECO:0000255"
FT REGION 1..835
FT /note="N-terminal globular head"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 168..208
FT /note="Talin-interaction"
FT /evidence="ECO:0000250|UniProtKB:P12003"
FT REGION 259..589
FT /note="3 X 112 AA tandem repeats"
FT /evidence="ECO:0000255"
FT REGION 741..764
FT /note="Interaction with ACTN4"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 836..878
FT /note="Linker (Pro-rich)"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 857..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..1066
FT /note="C-terminal tail"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 935..978
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000269|PubMed:20599708"
FT REGION 1052..1066
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000269|PubMed:20599708"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 496
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 537
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 604
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 672
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 822
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1065
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT CONFLICT 16
FT /note="V -> E (in Ref. 1; AAB96843)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="T -> S (in Ref. 1; AAB96843)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> V (in Ref. 1; AAB96843)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="Q -> K (in Ref. 3; BAC37033)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="Q -> R (in Ref. 1; AAB96843)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="M -> K (in Ref. 3; BAC37033)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="G -> D (in Ref. 1; AAB96843)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="A -> T (in Ref. 3; BAC37033)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 7..29
FT /evidence="ECO:0007829|PDB:5Y04"
FT TURN 30..34
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 41..64
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 68..97
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 104..146
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 185..210
FT /evidence="ECO:0007829|PDB:5Y04"
FT HELIX 225..249
FT /evidence="ECO:0007829|PDB:5Y04"
SQ SEQUENCE 1066 AA; 116717 MW; 067F1B16A5285859 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE
LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GTANKSTVEG
IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ
