Details for: VIM

Gene ID: 7431

Symbol: VIM

Ensembl ID: ENSG00000026025

Description: vimentin

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: endocardial cell (CL0002350)
    Fold Change: 9.71
    Marker Score: 5490
  • Cell Name: thyroid follicular cell (CL0002258)
    Fold Change: 6.53
    Marker Score: 5113
  • Cell Name: early promyelocyte (CL0002154)
    Fold Change: 5.05
    Marker Score: 4045
  • Cell Name: alveolar capillary type 1 endothelial cell (CL4028002)
    Fold Change: 5.04
    Marker Score: 12816
  • Cell Name: mature T cell (CL0002419)
    Fold Change: 4.96
    Marker Score: 49118
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 4.89
    Marker Score: 166528
  • Cell Name: mesenchymal stem cell (CL0000134)
    Fold Change: 4.75
    Marker Score: 7316
  • Cell Name: theca cell (CL0000503)
    Fold Change: 4.75
    Marker Score: 3402
  • Cell Name: cell of skeletal muscle (CL0000188)
    Fold Change: 4.6
    Marker Score: 3502
  • Cell Name: mesodermal cell (CL0000222)
    Fold Change: 4.58
    Marker Score: 60415
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: 4.55
    Marker Score: 254397
  • Cell Name: alveolar capillary type 2 endothelial cell (CL4028003)
    Fold Change: 4.5
    Marker Score: 6513
  • Cell Name: blood cell (CL0000081)
    Fold Change: 4.25
    Marker Score: 49452
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 4.22
    Marker Score: 37050
  • Cell Name: skeletal muscle satellite cell (CL0000594)
    Fold Change: 4.22
    Marker Score: 2823
  • Cell Name: mature alpha-beta T cell (CL0000791)
    Fold Change: 4.11
    Marker Score: 217168.5
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 4.08
    Marker Score: 4358
  • Cell Name: fibroblast of connective tissue of nonglandular part of prostate (CL1000304)
    Fold Change: 4.07
    Marker Score: 3470
  • Cell Name: T-helper 22 cell (CL0001042)
    Fold Change: 4.07
    Marker Score: 17442
  • Cell Name: supporting cell (CL0000630)
    Fold Change: 4.03
    Marker Score: 7565
  • Cell Name: kidney interstitial cell (CL1000500)
    Fold Change: 4.01
    Marker Score: 2854
  • Cell Name: double negative T regulatory cell (CL0011024)
    Fold Change: 3.99
    Marker Score: 3858
  • Cell Name: myofibroblast cell (CL0000186)
    Fold Change: 3.97
    Marker Score: 4896
  • Cell Name: CD4-positive, alpha-beta memory T cell (CL0000897)
    Fold Change: 3.96
    Marker Score: 2323
  • Cell Name: lung macrophage (CL1001603)
    Fold Change: 3.82
    Marker Score: 4367
  • Cell Name: granulocyte (CL0000094)
    Fold Change: 3.79
    Marker Score: 1700
  • Cell Name: IgA plasma cell (CL0000987)
    Fold Change: 3.78
    Marker Score: 3223
  • Cell Name: pulmonary artery endothelial cell (CL1001568)
    Fold Change: 3.78
    Marker Score: 3256
  • Cell Name: decidual natural killer cell, human (CL0002343)
    Fold Change: 3.77
    Marker Score: 10409
  • Cell Name: interstitial cell of ovary (CL0002094)
    Fold Change: 3.76
    Marker Score: 24477
  • Cell Name: cardiac neuron (CL0010022)
    Fold Change: 3.74
    Marker Score: 4663
  • Cell Name: CD8-positive, alpha-beta memory T cell, CD45RO-positive (CL0001203)
    Fold Change: 3.71
    Marker Score: 10401
  • Cell Name: myeloid leukocyte (CL0000766)
    Fold Change: 3.68
    Marker Score: 4449
  • Cell Name: mature gamma-delta T cell (CL0000800)
    Fold Change: 3.68
    Marker Score: 11616
  • Cell Name: fibroblast (CL0000057)
    Fold Change: 3.68
    Marker Score: 3551
  • Cell Name: activated CD8-positive, alpha-beta T cell (CL0000906)
    Fold Change: 3.64
    Marker Score: 2639
  • Cell Name: myelocyte (CL0002193)
    Fold Change: 3.62
    Marker Score: 1565
  • Cell Name: fibroblast of lung (CL0002553)
    Fold Change: 3.61
    Marker Score: 9464
  • Cell Name: bronchus fibroblast of lung (CL2000093)
    Fold Change: 3.59
    Marker Score: 4937
  • Cell Name: smooth muscle cell (CL0000192)
    Fold Change: 3.57
    Marker Score: 2347
  • Cell Name: type I NK T cell (CL0000921)
    Fold Change: 3.56
    Marker Score: 2796
  • Cell Name: endothelial cell of vascular tree (CL0002139)
    Fold Change: 3.56
    Marker Score: 5168
  • Cell Name: uterine smooth muscle cell (CL0002601)
    Fold Change: 3.56
    Marker Score: 4631
  • Cell Name: hematopoietic cell (CL0000988)
    Fold Change: 3.51
    Marker Score: 2330
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 3.49
    Marker Score: 3330
  • Cell Name: fetal cardiomyocyte (CL0002495)
    Fold Change: 3.48
    Marker Score: 1144
  • Cell Name: endothelial cell of uterus (CL0009095)
    Fold Change: 3.47
    Marker Score: 6924
  • Cell Name: alpha-beta T cell (CL0000789)
    Fold Change: 3.46
    Marker Score: 2624
  • Cell Name: capillary endothelial cell (CL0002144)
    Fold Change: 3.46
    Marker Score: 3720
  • Cell Name: basophil (CL0000767)
    Fold Change: 3.45
    Marker Score: 1640
  • Cell Name: effector CD8-positive, alpha-beta T cell (CL0001050)
    Fold Change: 3.44
    Marker Score: 2893
  • Cell Name: naive thymus-derived CD4-positive, alpha-beta T cell (CL0000895)
    Fold Change: 3.43
    Marker Score: 5885
  • Cell Name: chondrocyte (CL0000138)
    Fold Change: 3.43
    Marker Score: 1542
  • Cell Name: natural T-regulatory cell (CL0000903)
    Fold Change: 3.41
    Marker Score: 1752
  • Cell Name: naive T cell (CL0000898)
    Fold Change: 3.4
    Marker Score: 2191
  • Cell Name: chromaffin cell (CL0000166)
    Fold Change: 3.38
    Marker Score: 4756
  • Cell Name: fibroblast of connective tissue of glandular part of prostate (CL1000305)
    Fold Change: 3.37
    Marker Score: 1405
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 3.36
    Marker Score: 2211
  • Cell Name: effector memory CD8-positive, alpha-beta T cell, terminally differentiated (CL0001062)
    Fold Change: 3.36
    Marker Score: 4943
  • Cell Name: Sertoli cell (CL0000216)
    Fold Change: 3.33
    Marker Score: 19757.5
  • Cell Name: mucosal invariant T cell (CL0000940)
    Fold Change: 3.31
    Marker Score: 2948
  • Cell Name: vascular lymphangioblast (CL0005022)
    Fold Change: 3.31
    Marker Score: 5594
  • Cell Name: inflammatory cell (CL0009002)
    Fold Change: 3.29
    Marker Score: 1415
  • Cell Name: late promyelocyte (CL0002151)
    Fold Change: 3.28
    Marker Score: 822
  • Cell Name: effector CD4-positive, alpha-beta T cell (CL0001044)
    Fold Change: 3.27
    Marker Score: 3063
  • Cell Name: non-classical monocyte (CL0000875)
    Fold Change: 3.27
    Marker Score: 7894
  • Cell Name: double negative thymocyte (CL0002489)
    Fold Change: 3.25
    Marker Score: 4485
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 3.25
    Marker Score: 2909
  • Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
    Fold Change: 3.23
    Marker Score: 6295
  • Cell Name: neuroblast (sensu Vertebrata) (CL0000031)
    Fold Change: 3.21
    Marker Score: 2017
  • Cell Name: DN3 thymocyte (CL0000807)
    Fold Change: 3.2
    Marker Score: 1597
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: 3.18
    Marker Score: 7922
  • Cell Name: mesothelial cell of epicardium (CL0011019)
    Fold Change: 3.17
    Marker Score: 1016
  • Cell Name: reticular cell (CL0000432)
    Fold Change: 3.16
    Marker Score: 1155
  • Cell Name: effector memory CD8-positive, alpha-beta T cell (CL0000913)
    Fold Change: 3.15
    Marker Score: 1935
  • Cell Name: effector memory CD4-positive, alpha-beta T cell (CL0000905)
    Fold Change: 3.13
    Marker Score: 2296
  • Cell Name: CD1c-positive myeloid dendritic cell (CL0002399)
    Fold Change: 3.13
    Marker Score: 8113.5
  • Cell Name: memory T cell (CL0000813)
    Fold Change: 3.11
    Marker Score: 1338
  • Cell Name: cord blood hematopoietic stem cell (CL2000095)
    Fold Change: 3.08
    Marker Score: 2324
  • Cell Name: pericyte (CL0000669)
    Fold Change: 3.08
    Marker Score: 1797
  • Cell Name: double-positive, alpha-beta thymocyte (CL0000809)
    Fold Change: 3.06
    Marker Score: 5987
  • Cell Name: memory regulatory T cell (CL0002678)
    Fold Change: 3.05
    Marker Score: 1064
  • Cell Name: alveolar macrophage (CL0000583)
    Fold Change: 3.05
    Marker Score: 77994
  • Cell Name: endothelial cell of lymphatic vessel (CL0002138)
    Fold Change: 3.04
    Marker Score: 1895
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 3.03
    Marker Score: 34178
  • Cell Name: Schwann cell (CL0002573)
    Fold Change: 3.02
    Marker Score: 1048
  • Cell Name: unswitched memory B cell (CL0000970)
    Fold Change: 3
    Marker Score: 1759
  • Cell Name: fibroblast of breast (CL4006000)
    Fold Change: 2.98
    Marker Score: 1701
  • Cell Name: intraepithelial lymphocyte (CL0002496)
    Fold Change: 2.97
    Marker Score: 3304
  • Cell Name: CD8-alpha-alpha-positive, alpha-beta intraepithelial T cell (CL0000915)
    Fold Change: 2.97
    Marker Score: 4207
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 2.95
    Marker Score: 29884
  • Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
    Fold Change: 2.95
    Marker Score: 18843
  • Cell Name: smooth muscle cell of large intestine (CL1000279)
    Fold Change: 2.92
    Marker Score: 1104
  • Cell Name: DN1 thymic pro-T cell (CL0000894)
    Fold Change: 2.92
    Marker Score: 904
  • Cell Name: class switched memory B cell (CL0000972)
    Fold Change: 2.9
    Marker Score: 2724
  • Cell Name: neutrophil (CL0000775)
    Fold Change: 2.89
    Marker Score: 1760
  • Cell Name: decidual cell (CL2000002)
    Fold Change: 2.89
    Marker Score: 12445
  • Cell Name: migratory enteric neural crest cell (CL0002607)
    Fold Change: 2.86
    Marker Score: 2689
  • Cell Name: alternatively activated macrophage (CL0000890)
    Fold Change: 2.86
    Marker Score: 1191
  • Cell Name: IgG memory B cell (CL0000979)
    Fold Change: 2.82
    Marker Score: 1701

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Other Information

**Key Characteristics:** 1. **Intermediate Filament Protein:** Vimentin is a type of intermediate filament protein that forms a network of filaments within the cytoskeleton of cells. This network provides mechanical support and protection to cells against environmental stressors. 2. **High Expression in Mesenchymal Cells:** Vimentin is predominantly expressed in mesenchymal cells, including fibroblasts, endothelial cells, and mesenchymal stem cells. This suggests a critical role in the development and maintenance of mesenchymal tissue. 3. **Diverse Cellular Functions:** Vimentin is involved in various cellular processes, including cell migration, differentiation, and survival. It also plays a role in the regulation of gene expression and protein stability. 4. **Involvement in Disease:** Vimentin has been implicated in several diseases, including cancer, where it is often overexpressed and associated with poor prognosis. **Pathways and Functions:** 1. **Cytoskeletal Organization:** Vimentin forms a network of filaments that provides mechanical support and stability to cells. 2. **Cell Migration and Differentiation:** Vimentin plays a crucial role in cell migration and differentiation, particularly in mesenchymal cells. 3. **Signaling Pathways:** Vimentin interacts with various signaling molecules, including Rho GTPases and microtubule-associated proteins, to regulate cellular processes. 4. **Autophagy and Aggrephagy:** Vimentin has been implicated in autophagy and aggrephagy, processes that are essential for maintaining cellular homeostasis. 5. **Apoptosis and Programmed Cell Death:** Vimentin has been shown to regulate apoptosis and programmed cell death, particularly in cancer cells. **Clinical Significance:** 1. **Cancer:** Vimentin overexpression has been associated with poor prognosis in various types of cancer, including breast, lung, and prostate cancer. 2. **Autoimmune Diseases:** Vimentin has been implicated in autoimmune diseases, such as multiple sclerosis, where it is thought to contribute to the development of demyelination. 3. **Muscle Diseases:** Vimentin mutations have been associated with muscle diseases, including muscular dystrophy. 4. **Thyroid Disease:** Vimentin has been implicated in thyroid disease, particularly in the development of thyroid cancer. 5. **Regenerative Medicine:** Vimentin has been explored as a potential therapeutic target for regenerative medicine, particularly in the development of tissue-engineered scaffolds. In conclusion, vimentin is a multifaceted intermediate filament protein that plays a critical role in maintaining cellular processes and tissue homeostasis. Its involvement in various diseases underscores the need for further research into the molecular mechanisms underlying its functions and the development of therapeutic strategies to target vimentin in disease.

Genular Protein ID: 2534927467

Symbol: VIME_HUMAN

Name: Vimentin

UniProtKB Accession Codes:

P08670 B0YJC2 D3DRU4 Q15867 Q15868 Q15869 Q548L2 Q6LER9 Q8N850 Q96ML2 Q9NTM3

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CORUM 1 CPTAC 6 CTD 1 CarbonylDB 1 ChEMBL 1 ChiTaRS 1 DIP 1 DMDM 1 DNASU 1 DOSAC-COBS-2DPAGE 1 DisGeNET 1 DisProt 1 DrugBank 2 EMBL 28 EPD 1 Ensembl 2 EvolutionaryTrace 1 ExpressionAtlas 1 GO 37 Gene3D 3 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HPA 1 InParanoid 1 IntAct 1 InterPro 3 KEGG 1 MANE-Select 1 MIM 3 MINT 1 MalaCards 1 MassIVE 1 MetOSite 1 MoonDB 1 NCBI Taxonomy 1 OGP 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 28 PDBsum 23 PIR 1 PRIDE 1 PRO 1 PROSITE 2 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 2 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 REPRODUCTION-2DPAGE 2 RNAct 1 Reactome 7 RefSeq 2 SAM 1 SIGNOR 1 SMART 1 SMR 1 STRING 1 SUPFAM 1 SWISS-2DPAGE 1 SignaLink 1 SwissPalm 1 TopDownProteomics 1 TreeFam 1 UCD-2DPAGE 1 UniProtKB 5 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 3467175

Title: Coding sequence and growth regulation of the human vimentin gene.

PubMed ID: 3467175

DOI: 10.1128/mcb.6.11.3614-3620.1986

PubMed ID: 2251132

Title: Nucleotide sequence of cDNA covering the complete coding part of the human vimentin gene.

PubMed ID: 2251132

DOI: 10.1093/nar/18.22.6692

PubMed ID: 14996095

Title: SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.

PubMed ID: 14996095

DOI: 10.1111/j.1365-2133.2004.05651.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15164054

Title: The DNA sequence and comparative analysis of human chromosome 10.

PubMed ID: 15164054

DOI: 10.1038/nature02462

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2472876

Title: Vimentin rather than keratin expression in some hormone-independent breast cancer cell lines and in oncogene-transformed mammary epithelial cells.

PubMed ID: 2472876

PubMed ID: 9150946

Title: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2.

PubMed ID: 9150946

DOI: 10.1002/elps.1150180342

PubMed ID: 3371665

Title: Nucleotide sequence of the human vimentin gene and regulation of its transcription in tissues and cultured cells.

PubMed ID: 3371665

DOI: 10.1016/0378-1119(88)90575-6

PubMed ID: 2323579

Title: Isolation of a human vimentin cDNA with a long 3'-noncoding region from a human osteosarcoma cell line (MG-63).

PubMed ID: 2323579

DOI: 10.1016/0378-1119(90)90295-3

PubMed ID: 9175763

Title: Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN.

PubMed ID: 9175763

DOI: 10.1006/bbrc.1997.6669

PubMed ID: 10852826

Title: Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis.

PubMed ID: 10852826

DOI: 10.1242/jcs.113.13.2471

PubMed ID: 12458200

Title: Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process.

PubMed ID: 12458200

DOI: 10.1074/jbc.m210892200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 14762106

Title: Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments.

PubMed ID: 14762106

DOI: 10.1242/jcs.00906

PubMed ID: 15592455

Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.

PubMed ID: 15592455

DOI: 10.1038/nbt1046

PubMed ID: 15846844

Title: Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein.

PubMed ID: 15846844

DOI: 10.1002/pmic.200401093

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16923132

Title: Interactions between epiplakin and intermediate filaments.

PubMed ID: 16923132

DOI: 10.1111/j.1346-8138.2006.00127.x

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 16361107

Title: Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics.

PubMed ID: 16361107

DOI: 10.1016/j.nbd.2005.10.012

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 17505058

Title: Estrogen induces expression of BCAS3, a novel estrogen receptor-alpha coactivator, through proline-, glutamic acid-, and leucine-rich protein-1 (PELP1).

PubMed ID: 17505058

DOI: 10.1210/me.2006-0514

PubMed ID: 18811945

Title: The serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin.

PubMed ID: 18811945

DOI: 10.1186/1471-2091-9-25

PubMed ID: 18408015

Title: Protein kinase Cepsilon binds peripherin and induces its aggregation, which is accompanied by apoptosis of neuroblastoma cells.

PubMed ID: 18408015

DOI: 10.1074/jbc.m710436200

PubMed ID: 18827015

Title: TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton.

PubMed ID: 18827015

DOI: 10.1242/jcs.029454

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19270731

Title: The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network.

PubMed ID: 19270731

DOI: 10.1371/journal.pone.0004730

PubMed ID: 30707744

Title: Retraction: The Cellular Distribution of Serotonin Transporter Is Impeded on Serotonin-Altered Vimentin Network.

PubMed ID: 30707744

DOI: 10.1371/journal.pone.0211966

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068230

Title: Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.

PubMed ID: 20068230

DOI: 10.1126/scisignal.2000526

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21746880

Title: A novel role of vimentin filaments: binding and stabilization of collagen mRNAs.

PubMed ID: 21746880

DOI: 10.1128/mcb.05263-11

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 21465480

Title: Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced secretion by neutrophils.

PubMed ID: 21465480

DOI: 10.1002/jcp.22782

PubMed ID: 22905912

Title: Resveratrol-induced changes of the human adipocyte secretion profile.

PubMed ID: 22905912

DOI: 10.1021/pr300539b

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23325789

Title: cAMP-stimulated phosphorylation of diaphanous 1 regulates protein stability and interaction with binding partners in adrenocortical cells.

PubMed ID: 23325789

DOI: 10.1091/mbc.e12-08-0597

PubMed ID: 25417112

Title: Target-selective protein S-nitrosylation by sequence motif recognition.

PubMed ID: 25417112

DOI: 10.1016/j.cell.2014.09.032

PubMed ID: 24940650

Title: Interaction of plectin with keratins 5 and 14: dependence on several plectin domains and keratin quaternary structure.

PubMed ID: 24940650

DOI: 10.1038/jid.2014.255

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 26845719

Title: Two new isoforms of the human hepatoma-derived growth factor interact with components of the cytoskeleton.

PubMed ID: 26845719

DOI: 10.1515/hsz-2015-0273

PubMed ID: 26694549

Title: Sporadic and familial congenital cataracts: mutational spectrum and new diagnoses using next-generation sequencing.

PubMed ID: 26694549

DOI: 10.1002/humu.22948

PubMed ID: 27812135

Title: Characterization and Genetic Analyses of New Genes Coding for NOD2 Interacting Proteins.

PubMed ID: 27812135

DOI: 10.1371/journal.pone.0165420

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 29496907

Title: Phosphoproteomics analysis identifies novel candidate substrates of the non-receptor tyrosine kinase, SRMS.

PubMed ID: 29496907

DOI: 10.1074/mcp.ra118.000643

PubMed ID: 11243787

Title: Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments.

PubMed ID: 11243787

DOI: 10.1006/jmbi.2001.4442

PubMed ID: 11889032

Title: Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly.

PubMed ID: 11889032

DOI: 10.1093/emboj/21.6.1255

PubMed ID: 20176112

Title: Atomic structure of vimentin coil 2.

PubMed ID: 20176112

DOI: 10.1016/j.jsb.2010.02.012

PubMed ID: 22119849

Title: Stabilization of vimentin coil2 fragment via an engineered disulfide.

PubMed ID: 22119849

DOI: 10.1016/j.jsb.2011.11.014

PubMed ID: 19126778

Title: Dominant cataract formation in association with a vimentin assembly disrupting mutation.

PubMed ID: 19126778

DOI: 10.1093/hmg/ddn440

PubMed ID: 28450710

Title: Targeted exome sequencing of congenital cataracts related genes: broadening the mutation spectrum and genotype-phenotype correlations in 27 Chinese Han families.

PubMed ID: 28450710

DOI: 10.1038/s41598-017-01182-9

Sequence Information:

  • Length: 466
  • Mass: 53652
  • Checksum: BAB54026665B015A
  • Sequence:
    • MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV 
YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 
DIMRLREKLQ EEMLQREEAE NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE 
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD 
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS 
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.