VIME_RAT
ID VIME_RAT Reviewed; 466 AA.
AC P31000;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Vimentin;
GN Name=Vim;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RX PubMed=1540169; DOI=10.1016/0006-291x(92)91866-o;
RA Bussemakers M.J.G., Verhaegh G.W.C.T., van Bokhoven A., Debruyne F.M.J.,
RA Schalken J.A.;
RT "Differential expression of vimentin in rat prostatic tumors.";
RL Biochem. Biophys. Res. Commun. 182:1254-1259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP PROTEIN SEQUENCE OF 37-50, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4]
RP PROTEIN SEQUENCE OF 51-64; 123-129; 223-235; 295-304; 321-341; 346-364;
RP 391-401 AND 411-424, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-160.
RC TISSUE=Mammary gland;
RA Paine M.L.;
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=2192768; DOI=10.1016/0248-4900(90)90299-i;
RA Katsumoto T., Mitsushima A., Kurimura T.;
RT "The role of the vimentin intermediate filaments in rat 3Y1 cells
RT elucidated by immunoelectron microscopy and computer-graphic
RT reconstruction.";
RL Biol. Cell 68:139-146(1990).
RN [7]
RP INTERACTION WITH RAB8B.
RX PubMed=12639940; DOI=10.1210/en.2002-220893;
RA Lau A.S., Mruk D.D.;
RT "Rab8B GTPase and junction dynamics in the testis.";
RL Endocrinology 144:1549-1563(2003).
RN [8]
RP PHOSPHORYLATION AT SER-55, AND MUTAGENESIS OF SER-55 AND 458-THR-SER-459.
RX PubMed=12686602; DOI=10.1091/mbc.e02-08-0545;
RA Chou Y.-H., Khuon S., Herrmann H., Goldman R.D.;
RT "Nestin promotes the phosphorylation-dependent disassembly of vimentin
RT intermediate filaments during mitosis.";
RL Mol. Biol. Cell 14:1468-1478(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56; SER-83; SER-144;
RP SER-214; SER-412; SER-419; SER-420; SER-430 AND SER-459, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC various non-epithelial cells, especially mesenchymal cells. Vimentin is
CC attached to the nucleus, endoplasmic reticulum, and mitochondria,
CC either laterally or terminally. {ECO:0000269|PubMed:2192768}.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. {ECO:0000250}.
CC -!- SUBUNIT: Homomer assembled from elementary dimers (By similarity).
CC Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2,
CC ANK2, PLEC, PRX and spectrin (By similarity). Interacts with BCAS3 (By
CC similarity). Interacts with LGSN (By similarity). Interacts with SYNM
CC (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain)
CC (By similarity). Interacts with STK33 (By similarity). Interacts with
CC LARP6 (By similarity). Interacts with RAB8B (PubMed:12639940).
CC Interacts with TOR1A; the interaction associates TOR1A with the
CC cytoskeleton. Interacts with TOR1AIP1 (By similarity). Interacts with
CC TOR1AIP1 (By similarity). Interacts with DIAPH1 (By similarity).
CC Interacts with EPPK1; interaction is dependent of higher-order
CC structure of intermediate filament (By similarity). Interacts with the
CC non-receptor tyrosine kinase SRMS; the interaction leads to
CC phosphorylation of VIM (By similarity). Interacts with NOD2 (By
CC similarity). Interacts (via head region) with CORO1C (By similarity).
CC Interacts with HDGF (By similarity). Interacts with PRKCE (via phorbol-
CC ester/DAG-type 2 domain) (By similarity). Interacts with BFSP2 (By
CC similarity). Interacts with PPL (By similarity).
CC {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P20152,
CC ECO:0000269|PubMed:12639940}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix
CC {ECO:0000269|PubMed:16128803}. Cell membrane
CC {ECO:0000250|UniProtKB:P20152}.
CC -!- DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates
CC elementary homodimerization. {ECO:0000250}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
CC -!- PTM: One of the most prominent phosphoproteins in various cells of
CC mesenchymal origin (By similarity). Phosphorylation is enhanced during
CC cell division, at which time vimentin filaments are significantly
CC reorganized (By similarity). Phosphorylation by PKN1 inhibits the
CC formation of filaments (By similarity). Filament disassembly during
CC mitosis is promoted by phosphorylation at Ser-55 as well as by nestin
CC (PubMed:12686602). Phosphorylated at Ser-56 by CDK5 during neutrophil
CC secretion in the cytoplasm (By similarity). Phosphorylated by STK33 (By
CC similarity). Phosphorylated on tyrosine residues by SRMS (By
CC similarity). {ECO:0000250|UniProtKB:P08670,
CC ECO:0000269|PubMed:12686602}.
CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the
CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; X62952; CAA44722.1; -; mRNA.
DR EMBL; BC061847; AAH61847.1; -; mRNA.
DR EMBL; M84481; AAA42339.1; -; mRNA.
DR PIR; S22119; S22119.
DR RefSeq; NP_112402.1; NM_031140.1.
DR AlphaFoldDB; P31000; -.
DR SMR; P31000; -.
DR BioGRID; 249676; 11.
DR CORUM; P31000; -.
DR DIP; DIP-31882N; -.
DR IntAct; P31000; 15.
DR MINT; P31000; -.
DR STRING; 10116.ENSRNOP00000024430; -.
DR CarbonylDB; P31000; -.
DR GlyGen; P31000; 3 sites.
DR iPTMnet; P31000; -.
DR PhosphoSitePlus; P31000; -.
DR SwissPalm; P31000; -.
DR jPOST; P31000; -.
DR PaxDb; P31000; -.
DR PRIDE; P31000; -.
DR GeneID; 81818; -.
DR KEGG; rno:81818; -.
DR UCSC; RGD:621646; rat.
DR CTD; 7431; -.
DR RGD; 621646; Vim.
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; P31000; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P31000; -.
DR Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-RNO-9646399; Aggrephagy.
DR PRO; PR:P31000; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0045098; C:type III intermediate filament; TAS:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:1990254; F:keratin filament binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005212; F:structural constituent of eye lens; ISO:RGD.
DR GO; GO:0005198; F:structural molecule activity; TAS:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0046697; P:decidualization; IEP:RGD.
DR GO; GO:0045444; P:fat cell differentiation; IEP:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
DR GO; GO:0045103; P:intermediate filament-based process; ISO:RGD.
DR GO; GO:0070307; P:lens fiber cell development; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:RGD.
DR GO; GO:0043488; P:regulation of mRNA stability; ISO:RGD.
DR GO; GO:1900147; P:regulation of Schwann cell migration; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IEP:RGD.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:RGD.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027699; Vimentin.
DR PANTHER; PTHR45652:SF5; PTHR45652:SF5; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 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 Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CHAIN 2..466
FT /note="Vimentin"
FT /id="PRO_0000063759"
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..95
FT /note="Head"
FT REGION 96..131
FT /note="Coil 1A"
FT REGION 132..153
FT /note="Linker 1"
FT REGION 154..245
FT /note="Coil 1B"
FT REGION 246..268
FT /note="Linker 12"
FT REGION 269..407
FT /note="Coil 2"
FT REGION 408..466
FT /note="Tail"
FT COILED 96..131
FT COILED 154..245
FT COILED 303..407
FT MOTIF 326..329
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT SITE 351
FT /note="Stutter"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 7
FT /note="Phosphoserine; by PKA and PKC; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 10
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 34
FT /note="Phosphoserine; by PKC; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 39
FT /note="Phosphoserine; by CaMK2, PKA, PKC and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 42
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 47
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12686602"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 61
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 66
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 72
FT /note="Phosphoserine; by AURKB and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 117
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 120
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 120
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 139
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 223
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 373
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 445
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 445
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 7
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 33
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 34
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 104
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 223
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MUTAGEN 55
FT /note="S->A: Retains filamentous network during mitosis
FT when transfected alone and when coexpressed with nestin."
FT /evidence="ECO:0000269|PubMed:12686602"
FT MUTAGEN 458..459
FT /note="TS->AA: Induces loss of filamentous network when
FT coexpressed with nestin."
FT /evidence="ECO:0000269|PubMed:12686602"
SQ SEQUENCE 466 AA; 53733 MW; 501CDCD706166829 CRC64;
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA
YVTRSSAVRL RSSMPGVRLL 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 ISLPLPNFSS
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
