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P19320

- VCAM1_HUMAN

UniProt

P19320 - VCAM1_HUMAN

Protein

Vascular cell adhesion protein 1

Gene

VCAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 187 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. integrin binding Source: BHF-UCL
    3. primary amine oxidase activity Source: UniProtKB

    GO - Biological processi

    1. acute inflammatory response Source: Ensembl
    2. aging Source: Ensembl
    3. amine metabolic process Source: UniProtKB
    4. B cell differentiation Source: BHF-UCL
    5. cell adhesion Source: BHF-UCL
    6. cell chemotaxis Source: Ensembl
    7. cellular response to glucose stimulus Source: Ensembl
    8. cellular response to tumor necrosis factor Source: Ensembl
    9. cellular response to vascular endothelial growth factor stimulus Source: Ensembl
    10. chorio-allantoic fusion Source: Ensembl
    11. chronic inflammatory response Source: Ensembl
    12. cytokine-mediated signaling pathway Source: Reactome
    13. extracellular matrix organization Source: Reactome
    14. heart development Source: Ensembl
    15. heterophilic cell-cell adhesion Source: BHF-UCL
    16. interferon-gamma-mediated signaling pathway Source: Reactome
    17. leukocyte cell-cell adhesion Source: BHF-UCL
    18. leukocyte tethering or rolling Source: BHF-UCL
    19. membrane to membrane docking Source: BHF-UCL
    20. oxidation-reduction process Source: GOC
    21. positive regulation of T cell proliferation Source: BHF-UCL
    22. regulation of immune response Source: Reactome
    23. response to ethanol Source: Ensembl
    24. response to hypoxia Source: Ensembl
    25. response to ionizing radiation Source: Ensembl
    26. response to lipopolysaccharide Source: Ensembl
    27. response to nicotine Source: Ensembl
    28. response to nutrient Source: Ensembl
    29. response to zinc ion Source: Ensembl
    30. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular cell adhesion protein 1
    Short name:
    V-CAM 1
    Short name:
    VCAM-1
    Alternative name(s):
    INCAM-100
    CD_antigen: CD106
    Gene namesi
    Name:VCAM1
    Synonyms:L1CAM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12663. VCAM1.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex Source: BHF-UCL
    2. apical part of cell Source: BHF-UCL
    3. cell surface Source: UniProtKB
    4. early endosome Source: UniProtKB
    5. endoplasmic reticulum Source: UniProtKB
    6. external side of plasma membrane Source: BHF-UCL
    7. extracellular space Source: BHF-UCL
    8. extracellular vesicular exosome Source: UniProt
    9. filopodium Source: BHF-UCL
    10. Golgi apparatus Source: UniProtKB
    11. integral component of membrane Source: UniProtKB-KW
    12. microvillus Source: BHF-UCL
    13. plasma membrane Source: Reactome
    14. podosome Source: BHF-UCL
    15. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37286.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 739715Vascular cell adhesion protein 1PRO_0000014997Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 95
    Disulfide bondi52 ↔ 99
    Disulfide bondi137 ↔ 195
    Disulfide bondi246 ↔ 291PROSITE-ProRule annotation
    Glycosylationi273 – 2731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi335 ↔ 383PROSITE-ProRule annotation
    Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi534 ↔ 579PROSITE-ProRule annotation
    Glycosylationi561 – 5611N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Sialoglycoprotein.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP19320.
    PRIDEiP19320.

    PTM databases

    PhosphoSiteiP19320.

    Miscellaneous databases

    PMAP-CutDBP19320.

    Expressioni

    Tissue specificityi

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

    Inductioni

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

    Gene expression databases

    ArrayExpressiP19320.
    BgeeiP19320.
    CleanExiHS_L1CAM.
    HS_VCAM1.
    GenevestigatoriP19320.

    Organism-specific databases

    HPAiCAB005426.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi113255. 439 interactions.
    IntActiP19320. 630 interactions.
    STRINGi9606.ENSP00000294728.

    Structurei

    Secondary structure

    1
    739
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 3813
    Beta strandi43 – 519
    Beta strandi56 – 616
    Beta strandi68 – 747
    Beta strandi77 – 848
    Helixi87 – 893
    Beta strandi91 – 999
    Beta strandi102 – 11413
    Beta strandi120 – 1256
    Beta strandi133 – 14412
    Helixi145 – 1473
    Beta strandi148 – 1547
    Beta strandi157 – 1637
    Beta strandi169 – 1713
    Beta strandi174 – 1829
    Helixi186 – 1883
    Beta strandi192 – 1998
    Beta strandi209 – 2168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IJ9X-ray3.00A25-220[»]
    1VCAX-ray1.80A/B25-226[»]
    1VSCX-ray1.90A/B25-219[»]
    ProteinModelPortaliP19320.
    SMRiP19320. Positions 25-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19320.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 698674ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini721 – 73919CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei699 – 72022HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 10581Ig-like C2-type 1Add
    BLAST
    Domaini109 – 212104Ig-like C2-type 2Add
    BLAST
    Domaini223 – 30987Ig-like C2-type 3Add
    BLAST
    Domaini312 – 39988Ig-like C2-type 4Add
    BLAST
    Domaini408 – 50699Ig-like C2-type 5Add
    BLAST
    Domaini511 – 59585Ig-like C2-type 6Add
    BLAST
    Domaini600 – 68485Ig-like C2-type 7Add
    BLAST

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG148090.
    HOGENOMiHOG000004820.
    HOVERGENiHBG053965.
    InParanoidiP19320.
    KOiK06527.
    OMAiENEHSYL.
    OrthoDBiEOG7JMGD2.
    PhylomeDBiP19320.
    TreeFamiTF333571.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    InterProiIPR003987. 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]
    PfamiPF05790. C2-set. 2 hits.
    PF07679. I-set. 3 hits.
    PF00047. ig. 1 hit.
    [Graphical view]
    PRINTSiPR01472. ICAMVCAM1.
    PR01474. VCAM1.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 3 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 5 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P19320-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT    50
    GCESPFFSWR TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE 100
    SRKLEKGIQV EIYSFPKDPE IHLSGPLEAG KPITVKCSVA DVYPFDRLEI 150
    DLLKGDHLMK SQEFLEDADR KSLETKSLEV TFTPVIEDIG KVLVCRAKLH 200
    IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG SVTMTCSSEG 250
    LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN 300
    RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ 350
    IDSPLSGKVR SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL 400
    YSFPRDPEIE MSGGLVNGSS VTVSCKVPSV YPLDRLEIEL LKGETILENI 450
    EFLEDTDMKS LENKSLEMTF IPTIEDTGKA LVCQAKLHID DMEFEPKQRQ 500
    STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP APKILWSRQL 550
    PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP 600
    KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID 650
    GAYTIRKAQL KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL 700
    VLYFASSLII PAIGMIIYFA RKANMKGSYS LVEAQKSKV 739

    Note: Major isoform.

    Length:739
    Mass (Da):81,276
    Last modified:November 1, 1990 - v1
    Checksum:i050E2EBD39AC2FF4
    GO
    Isoform 2 (identifier: P19320-2) [UniParc]FASTAAdd to Basket

    Also known as: Short, VCAM-6D

    The sequence of this isoform differs from the canonical sequence as follows:
         310-402: EKPFTVEISP...EKGIQVELYS → A

    Show »
    Length:647
    Mass (Da):71,255
    Checksum:i7EA67DB70AC91EF8
    GO
    Isoform 3 (identifier: P19320-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         52-113: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:677
    Mass (Da):74,346
    Checksum:iCA0C2F8A7E51EC83
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti182 – 1821F → G(PubMed:1377228)Curated
    Sequence conflicti402 – 4021S → T(PubMed:1707234)Curated
    Sequence conflicti728 – 7281S → P in BAG59286. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181M → I.
    Corresponds to variant rs34228330 [ dbSNP | Ensembl ].
    VAR_049951
    Natural varianti318 – 3181S → F.1 Publication
    Corresponds to variant rs3783611 [ dbSNP | Ensembl ].
    VAR_014309
    Natural varianti384 – 3841T → A.1 Publication
    Corresponds to variant rs3783612 [ dbSNP | Ensembl ].
    VAR_014310
    Natural varianti413 – 4131G → A.1 Publication
    Corresponds to variant rs3783613 [ dbSNP | Ensembl ].
    VAR_014311
    Natural varianti421 – 4211V → I.
    Corresponds to variant rs34100871 [ dbSNP | Ensembl ].
    VAR_049952
    Natural varianti488 – 4881H → R.
    Corresponds to variant rs34199378 [ dbSNP | Ensembl ].
    VAR_049953
    Natural varianti716 – 7161I → L.1 Publication
    Corresponds to variant rs3783615 [ dbSNP | Ensembl ].
    VAR_014312

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei52 – 11362Missing in isoform 3. 1 PublicationVSP_044636Add
    BLAST
    Alternative sequencei310 – 40293EKPFT…VELYS → A in isoform 2. 1 PublicationVSP_002580Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS55617.1. [P19320-3]
    CCDS773.1. [P19320-1]
    CCDS774.1. [P19320-2]
    PIRiA41288.
    B41288.
    RefSeqiNP_001069.1. NM_001078.3. [P19320-1]
    NP_001186763.1. NM_001199834.1. [P19320-3]
    NP_542413.1. NM_080682.2. [P19320-2]
    UniGeneiHs.109225.

    Genome annotation databases

    EnsembliENST00000294728; ENSP00000294728; ENSG00000162692. [P19320-1]
    ENST00000347652; ENSP00000304611; ENSG00000162692. [P19320-2]
    ENST00000370119; ENSP00000359137; ENSG00000162692. [P19320-3]
    GeneIDi7412.
    KEGGihsa:7412.
    UCSCiuc001dti.3. human. [P19320-1]
    uc001dtj.3. human. [P19320-2]

    Polymorphism databases

    DMDMi137560.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    VCAM1 entry

    SeattleSNPs
    Functional Glycomics Gateway - Glycan Binding

    VCAM-1

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS55617.1. [P19320-3 ]
    CCDS773.1. [P19320-1 ]
    CCDS774.1. [P19320-2 ]
    PIRi A41288.
    B41288.
    RefSeqi NP_001069.1. NM_001078.3. [P19320-1 ]
    NP_001186763.1. NM_001199834.1. [P19320-3 ]
    NP_542413.1. NM_080682.2. [P19320-2 ]
    UniGenei Hs.109225.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IJ9 X-ray 3.00 A 25-220 [» ]
    1VCA X-ray 1.80 A/B 25-226 [» ]
    1VSC X-ray 1.90 A/B 25-219 [» ]
    ProteinModelPortali P19320.
    SMRi P19320. Positions 25-712.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113255. 439 interactions.
    IntActi P19320. 630 interactions.
    STRINGi 9606.ENSP00000294728.

    Chemistry

    BindingDBi P19320.
    ChEMBLi CHEMBL3735.
    DrugBanki DB01136. Carvedilol.

    PTM databases

    PhosphoSitei P19320.

    Polymorphism databases

    DMDMi 137560.

    Proteomic databases

    PaxDbi P19320.
    PRIDEi P19320.

    Protocols and materials databases

    DNASUi 7412.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294728 ; ENSP00000294728 ; ENSG00000162692 . [P19320-1 ]
    ENST00000347652 ; ENSP00000304611 ; ENSG00000162692 . [P19320-2 ]
    ENST00000370119 ; ENSP00000359137 ; ENSG00000162692 . [P19320-3 ]
    GeneIDi 7412.
    KEGGi hsa:7412.
    UCSCi uc001dti.3. human. [P19320-1 ]
    uc001dtj.3. human. [P19320-2 ]

    Organism-specific databases

    CTDi 7412.
    GeneCardsi GC01P101185.
    HGNCi HGNC:12663. VCAM1.
    HPAi CAB005426.
    MIMi 192225. gene.
    neXtProti NX_P19320.
    PharmGKBi PA37286.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG148090.
    HOGENOMi HOG000004820.
    HOVERGENi HBG053965.
    InParanoidi P19320.
    KOi K06527.
    OMAi ENEHSYL.
    OrthoDBi EOG7JMGD2.
    PhylomeDBi P19320.
    TreeFami TF333571.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    ChiTaRSi VCAM1. human.
    EvolutionaryTracei P19320.
    GeneWikii VCAM-1.
    GenomeRNAii 7412.
    NextBioi 29020.
    PMAP-CutDB P19320.
    PROi P19320.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19320.
    Bgeei P19320.
    CleanExi HS_L1CAM.
    HS_VCAM1.
    Genevestigatori P19320.

    Family and domain databases

    Gene3Di 2.60.40.10. 7 hits.
    InterProi IPR003987. 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 ]
    Pfami PF05790. C2-set. 2 hits.
    PF07679. I-set. 3 hits.
    PF00047. ig. 1 hit.
    [Graphical view ]
    PRINTSi PR01472. ICAMVCAM1.
    PR01474. VCAM1.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 3 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiVCAM1_HUMAN
    AccessioniPrimary (citable) accession number: P19320
    Secondary accession number(s): A8K6R7
    , B4DKS4, E9PDD1, Q6NUP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 187 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3