VCAM1
Vascular cell adhesion protein 1
Also known as: CD106, VCAM1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P19320
- Gene
- VCAM1
- Ensembl
- ENSG00000162692
- Chromosome
- 1
- Canonical length
- 739 aa
- Protein class
- Cancer-related genes, CD markers, Plasma proteins, Predicted membrane proteins
- Subcellular location
- Cell Junctions
- Secretome location
- Secreted to blood
OverviewNCBI Gene
This gene is a member of the Ig superfamily and encodes a cell surface sialoglycoprotein expressed by cytokine-activated endothelium. This type I membrane protein mediates leukocyte-endothelial cell adhesion and signal transduction, and may play a role in the development of artherosclerosis and rheumatoid arthritis. Three alternatively spliced transcripts encoding different isoforms have been described for this gene. [provided by RefSeq, Dec 2010]
Canonical amino-acid sequenceUniProt
739 residues, UniProt reviewed canonical sequence.
>P19320|VCAM1
1 MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GCESPFFSWR
61 TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE SRKLEKGIQV EIYSFPKDPE
121 IHLSGPLEAG KPITVKCSVA DVYPFDRLEI DLLKGDHLMK SQEFLEDADR KSLETKSLEV
181 TFTPVIEDIG KVLVCRAKLH IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG
241 SVTMTCSSEG LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN
301 RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ IDSPLSGKVR
361 SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE MSGGLVNGSS
421 VTVSCKVPSV YPLDRLEIEL LKGETILENI EFLEDTDMKS LENKSLEMTF IPTIEDTGKA
481 LVCQAKLHID DMEFEPKQRQ STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP
541 APKILWSRQL PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP
601 KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL
661 KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL VLYFASSLII PAIGMIIYFA
721 RKANMKGSYS LVEAQKSKVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against VCAM1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.34
- Highest tissue expression
- 367 nTPM
Expression across tissuesHPA
Tissue
- spleen: 367 nTPM
- lymph node: 90 nTPM
- tonsil: 71 nTPM
- urinary bladder: 68 nTPM
- kidney: 61 nTPM
- ovary: 50 nTPM
Single-cell type
- kupffer cells: 1,798 nCPM
- pancreatic duct cells: 641 nCPM
- macrophages: 135 nCPM
- vascular endothelial cells: 117 nCPM
- decidual stromal cells: 116 nCPM
- proximal tubule cells: 90 nCPM
Immune cell
- memory CD8 T-cell: 0.6 nTPM
- gdT-cell: 0.3 nTPM
- naive CD8 T-cell: 0.1 nTPM
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
Brain region
- thalamus: 25 nTPM
- hypothalamus: 15 nTPM
- medulla oblongata: 14 nTPM
- midbrain: 12 nTPM
- spinal cord: 11 nTPM
- choroid plexus: 10 nTPM
ReferencesPubMed · IEDB
Publications for VCAM1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
5 publications
- Thrombogenic effects of antiphospholipid antibodies are mediated by intercellular cell adhesion molecule-1, vascular cell adhesion molecule-1, and P-selectin.
2001 · Circ Res · RCR 3.7 · 145 citations - Fluorescent nanocarriers targeting VCAM-1 for early detection of senescent endothelial cells.
2021 · Nanomedicine · RCR 1.7 · 26 citations - Probing antiphospholipid-mediated thrombosis: the interplay between anticardiolipin antibodies and endothelial cells.
2003 · Lupus · RCR 1.1 · 43 citations - Cardiac troponin I exacerbates myocardial ischaemia/reperfusion injury by inducing the adhesion of monocytes to vascular endothelial cells via a TLR4/NF-κB-dependent pathway.
2016 · Clin Sci (Lond) · RCR 0.5 · 15 citations - Differential effects of antibodies to vascular cell adhesion molecule-1 and distinct epitopes of the alpha4 integrin in HgCl2-induced nephritis in Brown Norway rats.
1998 · J Am Soc Nephrol · RCR 0.3 · 13 citations
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.39
- gnomAD pLI
- 0.8
- gnomAD missense Z
- 1.21
- DepMap mean gene effect
- -0.02
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- amine metabolic process
- B cell differentiation
- cell adhesion
- cell chemotaxis
- cell-cell adhesion mediated by integrin
- cell-matrix adhesion
- cellular response to amyloid-beta
- cellular response to tumor necrosis factor
- cellular response to vascular endothelial growth factor stimulus
- chronic inflammatory response
- heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
- heterotypic cell-cell adhesion
- inflammatory response
- innervation
- leukocyte cell-cell adhesion
- leukocyte tethering or rolling
- membrane to membrane docking
- positive regulation of T cell proliferation
- response to ethanol
- response to hypoxia
- response to ionizing radiation
- response to lipopolysaccharide
- response to nicotine
- response to nutrient
- response to zinc ion
- cardiac neuron differentiation
Molecular functions
- cell adhesion mediator activity
- cell adhesion molecule binding
- integrin binding
- primary methylamine oxidase activity
Cellular components
- apical part of cell
- cell surface
- early endosome
- endoplasmic reticulum
- external side of plasma membrane
- extracellular exosome
- extracellular space
- filopodium
- Golgi apparatus
- microvillus
- plasma membrane
- podosome
- sarcolemma
- alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex
Protein domainsUniProt · Pfam · InterPro
- Immunoglobulin subtype 2
- Immunoglobulin domain subtype
- Intercellular adhesion molecule/vascular cell adhesion molecule, N-terminal
- Immunoglobulin-like domain
- Immunoglobulin C2-set
- Immunoglobulin I-set
- Immunoglobulin V-set domain
- Immunoglobulin-like beta-sandwich domain
- Immunoglobulin-like fold
- Immunoglobulin-like domain superfamily
- Intercellular adhesion molecule/vascular cell adhesion molecule
- Immunoglobulin domain
- Immunoglobulin C2-set domain
- Immunoglobulin I-set domain
- Immunoglobulin domain
- Vascular cell adhesion molecule-1
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of VCAM1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads VCAM1 as an antibody target. Whether an autoantibody or antibody against VCAM1 could matter depends on whether native VCAM1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
VCAM1 is annotated at the cell surface, where native VCAM1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label VCAM1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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