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P19320 (VCAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vascular cell adhesion protein 1

Short name=V-CAM 1
Short name=VCAM-1
Alternative name(s):
INCAM-100
CD_antigen=CD106
Gene names
Name:VCAM1
Synonyms:L1CAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation.

Subunit structure

Binds to ECMV-D capsid proteins and acts as a receptor for this virus By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on inflammed vascular endothelium, as well as on macrophage-like and dendritic cell types in both normal and inflammed tissue.

Induction

By cytokines (e.g. IL-1, TNF-alpha).

Domain

Either the first or the fourth Ig-like C2-type domain is required for VLA4-dependent cell adhesion. Ref.12

Post-translational modification

Sialoglycoprotein.

Sequence similarities

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred by curator PubMed 1715889. Source: BHF-UCL

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

amine metabolic process

Inferred from direct assay PubMed 23474851. Source: UniProtKB

cell adhesion

Inferred from direct assay PubMed 16809613. Source: BHF-UCL

cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

cellular response to vascular endothelial growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

chorio-allantoic fusion

Inferred from electronic annotation. Source: Ensembl

chronic inflammatory response

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

heart development

Inferred from electronic annotation. Source: Ensembl

heterophilic cell-cell adhesion

Inferred from direct assay PubMed 1715889. Source: BHF-UCL

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

leukocyte cell-cell adhesion

Inferred from direct assay PubMed 1381355PubMed 1715889Ref.1. Source: BHF-UCL

leukocyte tethering or rolling

Inferred from expression pattern Ref.1. Source: BHF-UCL

membrane to membrane docking

Inferred from expression pattern PubMed 12082081. Source: BHF-UCL

oxidation-reduction process

Inferred from direct assay PubMed 23474851. Source: GOC

positive regulation of T cell proliferation

Inferred from direct assay PubMed 1381355. Source: BHF-UCL

regulation of immune response

Traceable author statement. Source: Reactome

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 23474851. Source: UniProtKB

alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex

Inferred from direct assay PubMed 15220135. Source: BHF-UCL

apical part of cell

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

cell surface

Inferred from direct assay PubMed 23474851. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 23474851. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 23474851. Source: UniProtKB

external side of plasma membrane

Inferred from direct assay Ref.12. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 9290466. Source: BHF-UCL

filopodium

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microvillus

Inferred from direct assay PubMed 12082081. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

podosome

Inferred from direct assay PubMed 15220135. Source: BHF-UCL

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncell adhesion molecule binding

Inferred from direct assay Ref.12. Source: BHF-UCL

integrin binding

Inferred from direct assay Ref.12PubMed 15220135. Source: BHF-UCL

primary amine oxidase activity

Inferred from direct assay PubMed 23474851. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P19320-1)

Also known as: Long; VCAM-7D;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.
Isoform 2 (identifier: P19320-2)

Also known as: Short; VCAM-6D;

The sequence of this isoform differs from the canonical sequence as follows:
     310-402: EKPFTVEISP...EKGIQVELYS → A
Isoform 3 (identifier: P19320-3)

The sequence of this isoform differs from the canonical sequence as follows:
     52-113: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.13
Chain25 – 739715Vascular cell adhesion protein 1
PRO_0000014997

Regions

Topological domain25 – 698674Extracellular Potential
Transmembrane699 – 72022Helical; Potential
Topological domain721 – 73919Cytoplasmic Potential
Domain25 – 10581Ig-like C2-type 1
Domain109 – 212104Ig-like C2-type 2
Domain223 – 30987Ig-like C2-type 3
Domain312 – 39988Ig-like C2-type 4
Domain408 – 50699Ig-like C2-type 5
Domain511 – 59585Ig-like C2-type 6
Domain600 – 68485Ig-like C2-type 7

Amino acid modifications

Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3651N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5611N-linked (GlcNAc...) Ref.14
Disulfide bond47 ↔ 95
Disulfide bond52 ↔ 99
Disulfide bond137 ↔ 195
Disulfide bond246 ↔ 291 By similarity
Disulfide bond335 ↔ 383 By similarity
Disulfide bond534 ↔ 579 By similarity

Natural variations

Alternative sequence52 – 11362Missing in isoform 3.
VSP_044636
Alternative sequence310 – 40293EKPFT…VELYS → A in isoform 2.
VSP_002580
Natural variant181M → I.
Corresponds to variant rs34228330 [ dbSNP | Ensembl ].
VAR_049951
Natural variant3181S → F. Ref.5
Corresponds to variant rs3783611 [ dbSNP | Ensembl ].
VAR_014309
Natural variant3841T → A. Ref.5
Corresponds to variant rs3783612 [ dbSNP | Ensembl ].
VAR_014310
Natural variant4131G → A. Ref.5
Corresponds to variant rs3783613 [ dbSNP | Ensembl ].
VAR_014311
Natural variant4211V → I.
Corresponds to variant rs34100871 [ dbSNP | Ensembl ].
VAR_049952
Natural variant4881H → R.
Corresponds to variant rs34199378 [ dbSNP | Ensembl ].
VAR_049953
Natural variant7161I → L. Ref.5
Corresponds to variant rs3783615 [ dbSNP | Ensembl ].
VAR_014312

Experimental info

Sequence conflict1821F → G Ref.12
Sequence conflict4021S → T Ref.11
Sequence conflict7281S → P in BAG59286. Ref.6

Secondary structure

................................... 739
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (VCAM-7D) [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 050E2EBD39AC2FF4

FASTA73981,276
        10         20         30         40         50         60 
MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GCESPFFSWR 

        70         80         90        100        110        120 
TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE SRKLEKGIQV EIYSFPKDPE 

       130        140        150        160        170        180 
IHLSGPLEAG KPITVKCSVA DVYPFDRLEI DLLKGDHLMK SQEFLEDADR KSLETKSLEV 

       190        200        210        220        230        240 
TFTPVIEDIG KVLVCRAKLH IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG 

       250        260        270        280        290        300 
SVTMTCSSEG LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN 

       310        320        330        340        350        360 
RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ IDSPLSGKVR 

       370        380        390        400        410        420 
SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE MSGGLVNGSS 

       430        440        450        460        470        480 
VTVSCKVPSV YPLDRLEIEL LKGETILENI EFLEDTDMKS LENKSLEMTF IPTIEDTGKA 

       490        500        510        520        530        540 
LVCQAKLHID DMEFEPKQRQ STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP 

       550        560        570        580        590        600 
APKILWSRQL PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP 

       610        620        630        640        650        660 
KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL 

       670        680        690        700        710        720 
KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL VLYFASSLII PAIGMIIYFA 

       730 
RKANMKGSYS LVEAQKSKV 

« Hide

Isoform 2 (Short) (VCAM-6D) [UniParc].

Checksum: 7EA67DB70AC91EF8
Show »

FASTA64771,255
Isoform 3 [UniParc].

Checksum: CA0C2F8A7E51EC83
Show »

FASTA67774,346

References

« Hide 'large scale' references
[1]"Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes."
Osborn L., Hession C., Tizard R., Vassallo C., Luhowskyj S., Chi-Rosso G., Lobb R.
Cell 59:1203-1211(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Full length vascular cell adhesion molecule 1 (VCAM-1)."
Polte T., Newman W., Gopal T.V.
Nucleic Acids Res. 18:5901-5901(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Umbilical vein.
[3]"Cloning of an alternate form of vascular cell adhesion molecule-1 (VCAM1)."
Hession C., Tizard R., Vassallo C., Schiffer S.B., Goff D., Moy P., Chi-Rosso G., Luhowskyj S., Lobb R., Osborn L.
J. Biol. Chem. 266:6682-6685(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Gene structure, chromosomal location, and basis for alternative mRNA splicing of the human VCAM1 gene."
Cybulsky M.I., Fries J.W.U., Williams A.J., Sultan P., Eddy R., Byers M., Shows T., Gimbrone M.A. Jr., Collins T.
Proc. Natl. Acad. Sci. U.S.A. 88:7859-7863(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), ALTERNATIVE SPLICING.
[5]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-318; ALA-384; ALA-413 AND LEU-716.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Placenta and Tongue.
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Retinal pigment epithelium.
[10]"Characterization of the promoter for vascular cell adhesion molecule-1 (VCAM-1)."
Iademarco M.F., McQuillan J.J., Rosen G.D., Dean D.C.
J. Biol. Chem. 267:16323-16329(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
[11]"Alternative splicing of human VCAM-1 in activated vascular endothelium."
Cybulsky M.I., Fries J.W., Williams A.J., Sultan P., Davis V.M., Gimbrone M.A. Jr., Collins T.
Am. J. Pathol. 138:815-820(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 25-686 (ISOFORMS 1 AND 2).
Tissue: Umbilical vein endothelial cell.
[12]"Activated endothelium binds lymphocytes through a novel binding site in the alternately spliced domain of vascular cell adhesion molecule-1."
Osborn L., Vassallo C., Benjamin C.D.
J. Exp. Med. 176:99-107(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 25-402 (ISOFORMS 1 AND 2), CELL ADHESION DOMAIN.
Tissue: Endothelial cell.
[13]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-39.
[14]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-561.
Tissue: Plasma.
[15]"Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8-A resolution."
Jones E.Y., Harlos K., Bottomley M.J., Robinson R.C., Driscoll P.C., Edwards R.M., Clements J.M., Dudgeon T.J., Stuart D.I.
Nature 373:539-544(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-226.
[16]"The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction."
Wang J.-H., Pepinsky R.B., Stehle T., Liu J.-H., Karpusas M., Browning B., Osborn L.
Proc. Natl. Acad. Sci. U.S.A. 92:5714-5718(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220.
[17]"Structure of a functional fragment of VCAM-1 refined at 1.9-A resolution."
Wang J.-H., Stehle T., Pepinsky R.B., Liu J.-H., Karpusas M., Osborn L.
Acta Crystallogr. D 52:369-379(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30257 mRNA. Translation: AAA51917.1.
X53051 mRNA. Translation: CAA37218.1.
M60335 mRNA. Translation: AAA61269.1.
M73255 Genomic DNA. Translation: AAA61270.1.
AF536818 Genomic DNA. Translation: AAM96190.1.
AK291732 mRNA. Translation: BAF84421.1.
AK296692 mRNA. Translation: BAG59286.1.
AC093428 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW72950.1.
BC017276 mRNA. Translation: AAH17276.3.
BC068490 mRNA. Translation: AAH68490.2.
BC085003 mRNA. Translation: AAH85003.1.
M92431 Genomic DNA. No translation available.
CCDSCCDS55617.1. [P19320-3]
CCDS773.1. [P19320-1]
CCDS774.1. [P19320-2]
PIRA41288.
B41288.
RefSeqNP_001069.1. NM_001078.3. [P19320-1]
NP_001186763.1. NM_001199834.1. [P19320-3]
NP_542413.1. NM_080682.2. [P19320-2]
UniGeneHs.109225.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IJ9X-ray3.00A25-220[»]
1VCAX-ray1.80A/B25-226[»]
1VSCX-ray1.90A/B25-219[»]
ProteinModelPortalP19320.
SMRP19320. Positions 25-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113255. 439 interactions.
IntActP19320. 630 interactions.
STRING9606.ENSP00000294728.

Chemistry

BindingDBP19320.
ChEMBLCHEMBL3735.
DrugBankDB01136. Carvedilol.

PTM databases

PhosphoSiteP19320.

Polymorphism databases

DMDM137560.

Proteomic databases

PaxDbP19320.
PRIDEP19320.

Protocols and materials databases

DNASU7412.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294728; ENSP00000294728; ENSG00000162692. [P19320-1]
ENST00000347652; ENSP00000304611; ENSG00000162692. [P19320-2]
ENST00000370119; ENSP00000359137; ENSG00000162692. [P19320-3]
GeneID7412.
KEGGhsa:7412.
UCSCuc001dti.3. human. [P19320-1]
uc001dtj.3. human. [P19320-2]

Organism-specific databases

CTD7412.
GeneCardsGC01P101185.
HGNCHGNC:12663. VCAM1.
HPACAB005426.
MIM192225. gene.
neXtProtNX_P19320.
PharmGKBPA37286.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148090.
HOGENOMHOG000004820.
HOVERGENHBG053965.
InParanoidP19320.
KOK06527.
OMAENEHSYL.
OrthoDBEOG7JMGD2.
PhylomeDBP19320.
TreeFamTF333571.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP19320.
BgeeP19320.
CleanExHS_L1CAM.
HS_VCAM1.
GenevestigatorP19320.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR003989. VCAM-1.
[Graphical view]
PfamPF05790. C2-set. 2 hits.
PF07679. I-set. 3 hits.
PF00047. ig. 1 hit.
[Graphical view]
PRINTSPR01472. ICAMVCAM1.
PR01474. VCAM1.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 3 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVCAM1. human.
EvolutionaryTraceP19320.
GeneWikiVCAM-1.
GenomeRNAi7412.
NextBio29020.
PMAP-CutDBP19320.
PROP19320.
SOURCESearch...

Entry information

Entry nameVCAM1_HUMAN
AccessionPrimary (citable) accession number: P19320
Secondary accession number(s): A8K6R7 expand/collapse secondary AC list , B4DKS4, E9PDD1, Q6NUP8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 9, 2014
This is version 185 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries