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Vimentin

 VIME_MOUSE              Reviewed;         466 AA.
P20152; O08704; Q8CCH1;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 187.
RecName: Full=Vimentin;
Name=Vim;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2744479; DOI=10.1016/0378-1119(89)90020-6;
Wood L., Theriault N., Vogeli G.;
"Vimentin cDNA clones covering the complete intermediate-filament
protein are found in an EHS tumor cDNA library.";
Gene 76:171-175(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Spleen;
Podolin P.L., Prystowsky M.B.;
Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2325630; DOI=10.1007/BF00280364;
Hennekes H., Kuehn S., Traub P.;
"Coding sequence and flanking regions of the mouse vimentin gene.";
Mol. Gen. Genet. 221:33-36(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Smooth muscle;
PubMed=2140597;
Capetanaki Y., Kuisk I., Rothblum K., Starnes S.;
"Mouse vimentin: structural relationship to fos, jun, CREB and tpr.";
Oncogene 5:645-655(1990).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rauscher A.;
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
STRAIN=BALB/cJ;
PubMed=8543176; DOI=10.1016/0378-1119(95)00600-1;
Nakamura N., Shida M., Hirayoshi K., Nagata K.;
"Transcriptional regulation of the vimentin-encoding gene in mouse
myeloid leukemia M1 cells.";
Gene 166:281-286(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-188.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
PROTEIN SEQUENCE OF 5-69, AND PHOSPHORYLATION AT SER-7; SER-9; SER-10;
SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 AND
SER-66.
TISSUE=Smooth muscle;
PubMed=2500966; DOI=10.1021/bi00433a035;
Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.;
"Domain- and sequence-specific phosphorylation of vimentin induces
disassembly of the filament structure.";
Biochemistry 28:2974-2979(1989).
[9]
PROTEIN SEQUENCE OF 72-91.
TISSUE=Fibroblast;
PubMed=7523108; DOI=10.1002/elps.11501501101;
Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
"Separation and sequencing of familiar and novel murine proteins using
preparative two-dimensional gel electrophoresis.";
Electrophoresis 15:735-745(1994).
[10]
PHOSPHORYLATION AT SER-39 AND SER-83.
PubMed=1850997; DOI=10.1016/0006-291X(91)91658-Y;
Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.;
"Evidence that Ser-82 is a unique phosphorylation site on vimentin for
Ca2(+)-calmodulin-dependent protein kinase II.";
Biochem. Biophys. Res. Commun. 175:955-962(1991).
[11]
PHOSPHORYLATION AT SER-39 AND SER-72.
PubMed=9565595; DOI=10.1074/jbc.273.19.11728;
Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M.,
Kaibuchi K., Inagaki M.;
"Phosphorylation of vimentin by Rho-associated kinase at a unique
amino-terminal site that is specifically phosphorylated during
cytokinesis.";
J. Biol. Chem. 273:11728-11736(1998).
[12]
INTERACTION WITH PLEC.
PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x;
Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.;
"Actin-binding domain of mouse plectin. Crystal structure and binding
to vimentin.";
Eur. J. Biochem. 271:1873-1884(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[15]
INTERACTION WITH SYNM.
PubMed=17356066; DOI=10.1242/jcs.03423;
Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M.,
Skalli O.;
"Synemin is expressed in reactive astrocytes in neurotrauma and
interacts differentially with vimentin and GFAP intermediate filament
networks.";
J. Cell Sci. 120:1267-1277(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[18]
INTERACTION WITH LGSN.
PubMed=18178558; DOI=10.1074/jbc.M709144200;
Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.;
"A role for lengsin, a recruited enzyme, in terminal differentiation
in the vertebrate lens.";
J. Biol. Chem. 283:6607-6615(2008).
[19]
INTERACTION WITH TOR1A.
PubMed=18827015; DOI=10.1242/jcs.029454;
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D.,
Li Y., Wiche G., Sonnenberg A., Breakefield X.O.;
"TorsinA binds the KASH domain of nesprins and participates in linkage
between nuclear envelope and cytoskeleton.";
J. Cell Sci. 121:3476-3486(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-214 AND SER-459,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56;
SER-66; SER-420 AND SER-430, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56; SER-83;
SER-325; SER-419; SER-420 AND SER-459, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[23]
TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK;
BFSP1; BFSP2; ANK2; PLEC; PRX AND SPECTRIN, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036;
Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J.,
Rao P.V.;
"Periaxin is required for hexagonal geometry and membrane organization
of mature lens fibers.";
Dev. Biol. 357:179-190(2011).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-129; LYS-139;
LYS-168; LYS-188; LYS-223; LYS-235; LYS-294 AND LYS-373, SUCCINYLATION
[LARGE SCALE ANALYSIS] AT LYS-120; LYS-129; LYS-188; LYS-294 AND
LYS-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Vimentins are class-III intermediate filaments found in
various non-epithelial cells, especially mesenchymal cells.
Vimentin is attached to the nucleus, endoplasmic reticulum, and
mitochondria, either laterally or terminally.
-!- FUNCTION: Involved with LARP6 in the stabilization of type I
collagen mRNAs for CO1A1 and CO1A2. {ECO:0000250}.
-!- SUBUNIT: Interacts with BCAS3 (By similarity). Homopolymer
assembled from elementary dimers. Interacts with HCV core protein.
Interacts with LGSN (PubMed:18178558). Interacts with SYNM
(PubMed:17356066). Interacts (via rod region) with PLEC (via CH 1
domain) (PubMed:15128297). Interacts with SLC6A4. Interacts with
STK33. Interacts with LARP6. Interacts with RAB8B. Interacts with
TOR1A; the interaction associates TOR1A with the cytoskeleton.
Interacts with TOR1AIP1. Interacts with DIAPH1 (By similarity).
Identified in complexes that contain VIM, EZR, AHNAK, BFSP1,
BFSP2, ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts
with EPPK1; interaction is dependent of higher-order structure of
intermediate filament (By similarity).
{ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000,
ECO:0000269|PubMed:15128297, ECO:0000269|PubMed:17356066,
ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:18827015,
ECO:0000269|PubMed:21745462}.
-!- INTERACTION:
P35465:Pak1 (xeno); NbExp=2; IntAct=EBI-299269, EBI-444379;
Q96RG2:PASK (xeno); NbExp=2; IntAct=EBI-299269, EBI-1042651;
Q9R269:Ppl; NbExp=2; IntAct=EBI-299269, EBI-368293;
P17452:toxA (xeno); NbExp=4; IntAct=EBI-299269, EBI-9541048;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein
level). {ECO:0000269|PubMed:21745462}.
-!- DOMAIN: The central alpha-helical coiled-coil IF rod domain
mediates elementary homodimerization. {ECO:0000250}.
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
-!- PTM: Phosphorylation by PKN1 inhibits the formation of filaments.
Filament disassembly during mitosis is promoted by phosphorylation
at Ser-55 as well as by nestin (By similarity). One of the most
prominent phosphoproteins in various cells of mesenchymal origin.
Phosphorylation is enhanced during cell division, at which time
vimentin filaments are significantly reorganized. Phosphorylated
at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm.
Phosphorylated by STK33 (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000250|UniProtKB:P08670}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; M24849; AAA40555.1; -; mRNA.
EMBL; X56397; CAA39807.1; -; mRNA.
EMBL; M26251; AAA40556.1; -; mRNA.
EMBL; Z22526; CAA80251.1; -; Genomic_DNA.
EMBL; X51438; CAA35803.1; -; mRNA.
EMBL; Y07738; CAA69019.1; -; Genomic_DNA.
EMBL; AK033175; BAC28181.1; -; mRNA.
EMBL; D50805; BAA19834.1; -; Genomic_DNA.
CCDS; CCDS15696.1; -.
PIR; A43803; A43803.
RefSeq; NP_035831.2; NM_011701.4.
UniGene; Mm.268000; -.
ProteinModelPortal; P20152; -.
SMR; P20152; -.
BioGrid; 204524; 20.
DIP; DIP-188N; -.
IntAct; P20152; 27.
MINT; MINT-1202726; -.
STRING; 10090.ENSMUSP00000028062; -.
iPTMnet; P20152; -.
PhosphoSitePlus; P20152; -.
SwissPalm; P20152; -.
REPRODUCTION-2DPAGE; IPI00227299; -.
SWISS-2DPAGE; P20152; -.
UCD-2DPAGE; P20152; -.
EPD; P20152; -.
PaxDb; P20152; -.
PeptideAtlas; P20152; -.
PRIDE; P20152; -.
Ensembl; ENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
GeneID; 22352; -.
KEGG; mmu:22352; -.
UCSC; uc008ikb.2; mouse.
CTD; 7431; -.
MGI; MGI:98932; Vim.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
GeneTree; ENSGT00830000128228; -.
HOGENOM; HOG000230977; -.
HOVERGEN; HBG013015; -.
InParanoid; P20152; -.
KO; K07606; -.
OMA; QVINEST; -.
OrthoDB; EOG091G12MK; -.
PhylomeDB; P20152; -.
TreeFam; TF330122; -.
Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-MMU-390522; Striated Muscle Contraction.
ChiTaRS; Vim; mouse.
PRO; PR:P20152; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026728; -.
CleanEx; MM_VIM; -.
ExpressionAtlas; P20152; baseline and differential.
Genevisible; P20152; MM.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045098; C:type III intermediate filament; TAS:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:1990254; F:keratin filament binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:MGI.
GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
GO; GO:0005198; F:structural molecule activity; IMP:MGI.
GO; GO:0014002; P:astrocyte development; IGI:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI.
GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
GO; GO:0045103; P:intermediate filament-based process; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IDA:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
InterPro; IPR001664; IF.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR027699; Vimentin.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Intermediate filament;
Isopeptide bond; Methylation; Nitration; Phosphoprotein;
Reference proteome; S-nitrosylation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08670}.
CHAIN 2 466 Vimentin.
/FTId=PRO_0000063756.
DOMAIN 103 411 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 95 Head.
REGION 96 131 Coil 1A.
REGION 132 153 Linker 1.
REGION 154 245 Coil 1B.
REGION 246 268 Linker 12.
REGION 269 407 Coil 2.
REGION 408 466 Tail.
COILED 96 131
COILED 154 245
COILED 303 407
MOTIF 326 329 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P08670}.
SITE 351 351 Stutter. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 7 7 Phosphoserine; by PKA and PKC; alternate.
{ECO:0000269|PubMed:2500966}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 9 9 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 10 10 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 11 11 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 13 13 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 20 20 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 21 21 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 25 25 Phosphoserine; by PKA and PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 26 26 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 28 28 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 28 28 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P31001}.
MOD_RES 34 34 Phosphoserine; by PKC; alternate.
{ECO:0000269|PubMed:2500966}.
MOD_RES 39 39 Phosphoserine; by CaMK2, PKA, PKC and
ROCK2. {ECO:0000244|PubMed:19131326,
ECO:0000269|PubMed:1850997,
ECO:0000269|PubMed:2500966,
ECO:0000269|PubMed:9565595}.
MOD_RES 42 42 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2500966}.
MOD_RES 47 47 Phosphoserine; by PKA.
{ECO:0000269|PubMed:2500966}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 51 51 Phosphoserine; by PKA and PKC.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:2500966}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:P31000}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 61 61 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 66 66 Phosphoserine; by PKA and PKC.
{ECO:0000244|PubMed:19131326,
ECO:0000269|PubMed:2500966}.
MOD_RES 72 72 Phosphoserine; by AURKB and ROCK2.
{ECO:0000269|PubMed:9565595}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 83 83 Phosphoserine; by CaMK2.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1850997}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 117 117 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 120 120 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 120 120 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 129 129 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 129 129 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 139 139 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 168 168 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 188 188 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 188 188 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 223 223 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 235 235 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 294 294 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 294 294 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 299 299 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 373 373 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 383 383 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P21807}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000250|UniProtKB:P84198}.
MOD_RES 419 419 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 426 426 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 445 445 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 445 445 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 458 458 Phosphothreonine.
{ECO:0000250|UniProtKB:P08670}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 7 7 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 33 33 O-linked (GlcNAc) threonine.
{ECO:0000250}.
CARBOHYD 34 34 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CROSSLNK 104 104 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 129 129 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 139 139 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 223 223 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 262 262 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 373 373 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 439 439 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P08670}.
CONFLICT 70 70 L -> S (in Ref. 6; BAA19834).
{ECO:0000305}.
CONFLICT 110 115 LNDRFA -> ILLAEL (in Ref. 6; BAA19834).
{ECO:0000305}.
CONFLICT 156 157 EL -> DV (in Ref. 4; CAA35803).
{ECO:0000305}.
CONFLICT 164 164 L -> F (in Ref. 2; CAA39807).
{ECO:0000305}.
CONFLICT 338 338 E -> V (in Ref. 4; CAA35803).
{ECO:0000305}.
CONFLICT 374 374 E -> D (in Ref. 1; AAA40555).
{ECO:0000305}.
SEQUENCE 466 AA; 53688 MW; A94EECEA6D70C899 CRC64;
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA
YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPTFSS
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE


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