Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P48616 (VIME_BOVIN)

Entry version 160 (25 May 2022)
Sequence version 3 (01 May 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Vimentin

Gene

VIM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.

Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei351StutterBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-BTA-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-BTA-390522, Striated Muscle Contraction

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vimentin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VIM
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSBTAG00000018463

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:36796, VIM

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Intermediate filament, Membrane, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000637512 – 466VimentinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei5PhosphoserineBy similarity1
Modified residuei7Phosphoserine; by PKA and PKC; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi7O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei9Phosphoserine; by PKCBy similarity1
Modified residuei10Phosphoserine; by PKCBy similarity1
Modified residuei20PhosphothreonineBy similarity1
Modified residuei25Phosphoserine; by PKA and PKCBy similarity1
Modified residuei26Phosphoserine; by PKCBy similarity1
Glycosylationi33O-linked (GlcNAc) threonineBy similarity1
Modified residuei34Phosphoserine; by PKC; alternateBy similarity1
Glycosylationi34O-linked (GlcNAc) serine; alternateBy similarity1
Modified residuei39Phosphoserine; by CaMK2, PKA, PKC and ROCK2By similarity1
Modified residuei42Phosphoserine; by PKCBy similarity1
Modified residuei49PhosphoserineBy similarity1
Modified residuei53PhosphotyrosineBy similarity1
Modified residuei55PhosphoserineBy similarity1
Modified residuei56Phosphoserine; by CDK5 and CDK1By similarity1
Modified residuei61PhosphotyrosineBy similarity1
Modified residuei66Phosphoserine; by PKA and PKCBy similarity1
Modified residuei72Phosphoserine; by AURKB and ROCK2By similarity1
Modified residuei83Phosphoserine; by CaMK2By similarity1
Modified residuei87PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei117PhosphotyrosineBy similarity1
Modified residuei120N6-acetyllysine; alternateBy similarity1
Modified residuei120N6-succinyllysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei129N6-acetyllysine; alternateBy similarity1
Modified residuei129N6-succinyllysine; alternateBy similarity1
Cross-linki129Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei139N6-acetyllysine; alternateBy similarity1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei144PhosphoserineBy similarity1
Modified residuei168N6-acetyllysineBy similarity1
Modified residuei188N6-acetyllysine; alternateBy similarity1
Modified residuei188N6-succinyllysine; alternateBy similarity1
Modified residuei214PhosphoserineBy similarity1
Modified residuei223N6-acetyllysine; alternateBy similarity1
Cross-linki223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei226PhosphoserineBy similarity1
Modified residuei235N6-acetyllysineBy similarity1
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei294N6-acetyllysine; alternateBy similarity1
Modified residuei294N6-succinyllysine; alternateBy similarity1
Cross-linki294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei299PhosphoserineBy similarity1
Cross-linki313Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei373N6-acetyllysine; alternateBy similarity1
Cross-linki373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei409PhosphoserineBy similarity1
Modified residuei412PhosphoserineBy similarity1
Modified residuei419PhosphoserineBy similarity1
Modified residuei420PhosphoserineBy similarity1
Modified residuei426PhosphothreonineBy similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei438PhosphoserineBy similarity1
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei445N6-acetyllysine; alternateBy similarity1
Modified residuei445N6-succinyllysine; alternateBy similarity1
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei446PhosphothreonineBy similarity1
Modified residuei458PhosphothreonineBy similarity1
Modified residuei459PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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. Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS.By similarity
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P48616

PeptideAtlas

More...PeptideAtlasi		P48616

PRoteomics IDEntifications database

More...PRIDEi		P48616

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P48616

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000018463, Expressed in subcutaneous adipose tissue and 96 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homomer assembled from elementary dimers (By similarity). Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).

Interacts with BCAS3 (By similarity).

Interacts with LGSN (By similarity).

Interacts with SYNM (By similarity).

Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity).

Interacts with STK33 (By similarity).

Interacts with LARP6 (By similarity).

Interacts with RAB8B (By similarity).

Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton.

Interacts with TOR1AIP1 (By similarity).

Interacts with TOR1AIP1 (By similarity).

Interacts with DIAPH1 (By similarity).

Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament (By similarity).

Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (By similarity).

Interacts with NOD2 (By similarity).

Interacts (via head region) with CORO1C (By similarity).

Interacts with HDGF (By similarity).

Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain) (By similarity).

Interacts with BFSP2 (By similarity).

Interacts with PPL (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P48616, 3 interactors

Molecular INTeraction database

More...MINTi		P48616

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000024572

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P48616

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P48616

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini103 – 411IF rodPROSITE-ProRule annotationAdd BLAST309

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 31DisorderedSequence analysisAdd BLAST31
Regioni2 – 95HeadAdd BLAST94
Regioni96 – 131Coil 1AAdd BLAST36
Regioni132 – 153Linker 1Add BLAST22
Regioni154 – 245Coil 1BAdd BLAST92
Regioni246 – 268Linker 12Add BLAST23
Regioni269 – 407Coil 2Add BLAST139
Regioni408 – 466TailAdd BLAST59

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili96 – 131Add BLAST36
Coiled coili154 – 245Add BLAST92
Coiled coili303 – 407Add BLAST105

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi326 – 329[IL]-x-C-x-x-[DE] motifBy similarity4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.By similarity
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.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the intermediate filament family.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0977, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156146

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012560_7_4_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P48616

Identification of Orthologs from Complete Genome Data

More...OMAi		PPMRLHD

Database of Orthologous Groups

More...OrthoDBi		655109at2759

TreeFam database of animal gene trees

More...TreeFami		TF330122

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR018039, IF_conserved
IPR039008, IF_rod_dom
IPR006821, Intermed_filament_DNA-bd
IPR027699, Vimentin

The PANTHER Classification System

More...PANTHERi		PTHR45652:SF5, PTHR45652:SF5, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00038, Filament, 1 hit
PF04732, Filament_head, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01391, Filament, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00226, IF_ROD_1, 1 hit
PS51842, IF_ROD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P48616-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTRSVSSSS YRRMFGGPGT ASRPSSTRSY VTTSTRTYSL GSALRPTTSR 
        60         70         80         90        100
TLYTSSPGGV YATRSSAVRL RSGVPGVRLL QDSVDFSLAD AINTEFKNTR 
       110        120        130        140        150
TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY 
       160        170        180        190        200
EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE 
       210        220        230        240        250
STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ 
       260        270        280        290        300
EQHVQIDMDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 
       310        320        330        340        350
AANRNNDALR QAKQESNEYR RQVQTLTCEV DALKGTNESL ERQMREMEEN 
       360        370        380        390        400
FSVEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY 
       410        420        430        440        450
RKLLEGEESR ISLPLPNFSS LNLRETNLDS LPLVDTHSKR TLLIKTVETR 
       460 
DGQVINETSQ HHDDLE
Length:466
Mass (Da):53,728
Last modified:May 1, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8722F645FED23BDC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti148D → Q in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti171V → A in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti176D → H in AAA53661 (PubMed:8144034).Curated1
Sequence conflicti240E → A in AAA53661 (PubMed:8144034).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L13263 mRNA Translation: AAA53661.1
BC118269 mRNA Translation: AAI18270.1

NCBI Reference Sequences

More...RefSeqi		NP_776394.2, NM_173969.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463

Database of genes from NCBI RefSeq genomes

More...GeneIDi		280955

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:280955

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13263 mRNA Translation: AAA53661.1
BC118269 mRNA Translation: AAI18270.1
RefSeqiNP_776394.2, NM_173969.3

3D structure databases

AlphaFoldDBiP48616
SMRiP48616
ModBaseiSearch...

Protein-protein interaction databases

IntActiP48616, 3 interactors
MINTiP48616
STRINGi9913.ENSBTAP00000024572

PTM databases

iPTMnetiP48616

Proteomic databases

PaxDbiP48616
PeptideAtlasiP48616
PRIDEiP48616

Genome annotation databases

EnsembliENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463
GeneIDi280955
KEGGibta:280955

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7431
VEuPathDBiHostDB:ENSBTAG00000018463
VGNCiVGNC:36796, VIM

Phylogenomic databases

eggNOGiKOG0977, Eukaryota
GeneTreeiENSGT00940000156146
HOGENOMiCLU_012560_7_4_1
InParanoidiP48616
OMAiPPMRLHD
OrthoDBi655109at2759
TreeFamiTF330122

Enzyme and pathway databases

ReactomeiR-BTA-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-BTA-390522, Striated Muscle Contraction

Gene expression databases

BgeeiENSBTAG00000018463, Expressed in subcutaneous adipose tissue and 96 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR018039, IF_conserved
IPR039008, IF_rod_dom
IPR006821, Intermed_filament_DNA-bd
IPR027699, Vimentin
PANTHERiPTHR45652:SF5, PTHR45652:SF5, 1 hit
PfamiView protein in Pfam
PF00038, Filament, 1 hit
PF04732, Filament_head, 1 hit
SMARTiView protein in SMART
SM01391, Filament, 1 hit
PROSITEiView protein in PROSITE
PS00226, IF_ROD_1, 1 hit
PS51842, IF_ROD_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVIME_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P48616
Secondary accession number(s): Q17QM7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 1, 2007
Last modified: May 25, 2022
This is version 160 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again