P19320 (VCAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	VCAM1
Synonyms:	L1CAM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 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 process	Cell adhesion Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred by curator PubMed 1715889. Source: BHF-UCL acute inflammatory response Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara cellular response to glucose stimulus Inferred from electronic annotation. Source: Compara chorio-allantoic fusion Inferred from electronic annotation. Source: Compara chronic inflammatory response Inferred from electronic annotation. Source: Compara heart development Inferred from electronic annotation. Source: Compara heterophilic cell-cell adhesion Inferred from direct assay PubMed 1715889. Source: BHF-UCL interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome 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 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 hypoxia Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	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 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW microvillus Inferred from direct assay PubMed 12082081. Source: BHF-UCL podosome Inferred from direct assay PubMed 15220135. Source: BHF-UCL sarcolemma Inferred from electronic annotation. Source: Compara
Molecular_function	cell adhesion molecule binding Inferred from direct assay Ref.12. Source: BHF-UCL integrin binding Inferred from direct assay Ref.12PubMed 15220135. Source: BHF-UCL
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.13

Chain

25 – 739

715

Vascular cell adhesion protein 1

PRO_0000014997

Regions

Topological domain

25 – 698

674

Extracellular Potential

Transmembrane

699 – 720

22

Helical; Potential

Topological domain

721 – 739

19

Cytoplasmic Potential

Domain

25 – 105

81

Ig-like C2-type 1

Domain

109 – 212

104

Ig-like C2-type 2

Domain

223 – 309

87

Ig-like C2-type 3

Domain

312 – 399

88

Ig-like C2-type 4

Domain

408 – 506

99

Ig-like C2-type 5

Domain

511 – 595

85

Ig-like C2-type 6

Domain

600 – 684

85

Ig-like C2-type 7

Amino acid modifications

Glycosylation

273

1

N-linked (GlcNAc...) Potential

Glycosylation

365

1

N-linked (GlcNAc...) Potential

Glycosylation

417

1

N-linked (GlcNAc...) Potential

Glycosylation

463

1

N-linked (GlcNAc...) Potential

Glycosylation

531

1

N-linked (GlcNAc...) Potential

Glycosylation

561

1

N-linked (GlcNAc...) Ref.14

Disulfide bond

47 ↔ 95

Disulfide bond

52 ↔ 99

Disulfide bond

137 ↔ 195

Disulfide bond

246 ↔ 291

By similarity

Disulfide bond

335 ↔ 383

By similarity

Disulfide bond

534 ↔ 579

By similarity

Natural variations

Alternative sequence

52 – 113

62

Missing in isoform 3.

VSP_044636

Alternative sequence

310 – 402

93

EKPFT…VELYS → A in isoform 2.

VSP_002580

Natural variant

18

1

M → I.
Corresponds to variant rs34228330 [ dbSNP | Ensembl ].

VAR_049951

Natural variant

318

1

S → F. Ref.5
Corresponds to variant rs3783611 [ dbSNP | Ensembl ].

VAR_014309

Natural variant

384

1

T → A. Ref.5
Corresponds to variant rs3783612 [ dbSNP | Ensembl ].

VAR_014310

Natural variant

413

1

G → A. Ref.5
Corresponds to variant rs3783613 [ dbSNP | Ensembl ].

VAR_014311

Natural variant

421

1

V → I.
Corresponds to variant rs34100871 [ dbSNP | Ensembl ].

VAR_049952

Natural variant

488

1

H → R.
Corresponds to variant rs34199378 [ dbSNP | Ensembl ].

VAR_049953

Natural variant

716

1

I → L. Ref.5
Corresponds to variant rs3783615 [ dbSNP | Ensembl ].

VAR_014312

Experimental info

Sequence conflict

182

1

F → G Ref.12

Sequence conflict

402

1

S → T Ref.11

Sequence conflict

728

1

S → P in BAG59286. Ref.6

Secondary structure

1

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739

Helix Strand Turn

Details...

Beta strand

26 – 38

13

Beta strand

43 – 51

9

Beta strand

56 – 61

6

Beta strand

68 – 74

7

Beta strand

77 – 84

8

Helix

87 – 89

3

Beta strand

91 – 99

9

Beta strand

102 – 114

13

Beta strand

120 – 125

6

Beta strand

133 – 144

12

Helix

145 – 147

3

Beta strand

148 – 154

7

Beta strand

157 – 163

7

Beta strand

169 – 171

3

Beta strand

174 – 182

9

Helix

186 – 188

3

Beta strand

192 – 199

8

Beta strand

209 – 216

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) (VCAM-7D) [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 050E2EBD39AC2FF4	FASTA	739	81,276
	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
	Isoform 2 (Short) (VCAM-6D) [UniParc]. Checksum: 7EA67DB70AC91EF8	FASTA	647	71,255
	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 RKEVELIVQA FPRDPEIEMS GGLVNGSSVT VSCKVPSVYP LDRLEIELLK GETILENIEF 370 380 390 400 410 420 LEDTDMKSLE NKSLEMTFIP TIEDTGKALV CQAKLHIDDM EFEPKQRQST QTLYVNVAPR 430 440 450 460 470 480 DTTVLVSPSS ILEEGSSVNM TCLSQGFPAP KILWSRQLPN GELQPLSENA TLTLISTKME 490 500 510 520 530 540 DSGVYLCEGI NQAGRSRKEV ELIIQVTPKD IKLTAFPSES VKEGDTVIIS CTCGNVPETW 550 560 570 580 590 600 IILKKKAETG DTVLKSIDGA YTIRKAQLKD AGVYECESKN KVGSQLRSLT LDVQGRENNK 610 620 630 640 DYFSPELLVL YFASSLIIPA IGMIIYFARK ANMKGSYSLV EAQKSKV
	Isoform 3 [UniParc]. Checksum: CA0C2F8A7E51EC83	FASTA	677	74,346
	10 20 30 40 50 60 MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GSFPKDPEIH 70 80 90 100 110 120 LSGPLEAGKP ITVKCSVADV YPFDRLEIDL LKGDHLMKSQ EFLEDADRKS LETKSLEVTF 130 140 150 160 170 180 TPVIEDIGKV LVCRAKLHID EMDSVPTVRQ AVKELQVYIS PKNTVISVNP STKLQEGGSV 190 200 210 220 230 240 TMTCSSEGLP APEIFWSKKL DNGNLQHLSG NATLTLIAMR MEDSGIYVCE GVNLIGKNRK 250 260 270 280 290 300 EVELIVQEKP FTVEISPGPR IAAQIGDSVM LTCSVMGCES PSFSWRTQID SPLSGKVRSE 310 320 330 340 350 360 GTNSTLTLSP VSFENEHSYL CTVTCGHKKL EKGIQVELYS FPRDPEIEMS GGLVNGSSVT 370 380 390 400 410 420 VSCKVPSVYP LDRLEIELLK GETILENIEF LEDTDMKSLE NKSLEMTFIP TIEDTGKALV 430 440 450 460 470 480 CQAKLHIDDM EFEPKQRQST QTLYVNVAPR DTTVLVSPSS ILEEGSSVNM TCLSQGFPAP 490 500 510 520 530 540 KILWSRQLPN GELQPLSENA TLTLISTKME DSGVYLCEGI NQAGRSRKEV ELIIQVTPKD 550 560 570 580 590 600 IKLTAFPSES VKEGDTVIIS CTCGNVPETW IILKKKAETG DTVLKSIDGA YTIRKAQLKD 610 620 630 640 650 660 AGVYECESKN KVGSQLRSLT LDVQGRENNK DYFSPELLVL YFASSLIIPA IGMIIYFARK 670 ANMKGSYSLV EAQKSKV

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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.

Web resources

Wikipedia

VCAM1 entry

SeattleSNPs

Functional Glycomics Gateway - Glycan Binding

VCAM-1

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.

IPI

IPI00018136.
IPI00082827.
IPI00643090.

PIR

A41288.
B41288.

RefSeq

NP_001069.1. NM_001078.3.
NP_001186763.1. NM_001199834.1.
NP_542413.1. NM_080682.2.

UniGene

Hs.109225.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P19320.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19320. 630 interactions.

STRING

9606.ENSP00000294728.

PTM databases

PhosphoSite

P19320.

Polymorphism databases

DMDM

137560.

Proteomic databases

PaxDb

P19320.

PRIDE

P19320.

Protocols and materials databases

DNASU

7412.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000294728; ENSP00000294728; ENSG00000162692.
ENST00000347652; ENSP00000304611; ENSG00000162692.
ENST00000370119; ENSP00000359137; ENSG00000162692.

GeneID

7412.

KEGG

hsa:7412.

UCSC

uc001dti.3. human.
uc001dtj.3. human.

Organism-specific databases

CTD

7412.

GeneCards

GC01P101185.

HGNC

HGNC:12663. VCAM1.

HPA

CAB005426.

MIM

192225. gene.

neXtProt

NX_P19320.

PharmGKB

PA37286.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG148090.

HOGENOM

HOG000004820.

HOVERGEN

HBG053965.

InParanoid

P19320.

KO

K06527.

OMA

YPFDRLE.

Enzyme and pathway databases

Pathway_Interaction_DB

anthraxpathway. Cellular roles of Anthrax toxin.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P19320.

Bgee

P19320.

CleanEx

HS_L1CAM.
HS_VCAM1.

Genevestigator

P19320.

GermOnline

ENSG00000162692. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 7 hits.

InterPro

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]

Pfam

PF05790. C2-set. 2 hits.
PF07679. I-set. 3 hits.
PF00047. ig. 1 hit.
[Graphical view]

PRINTS

PR01472. ICAMVCAM1.
PR01474. VCAM1.

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 3 hits.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P19320.

ChEMBL

CHEMBL3735.

ChiTaRS

VCAM1. human.

DrugBank

DB01136. Carvedilol.

EvolutionaryTrace

P19320.

GenomeRNAi

7412.

NextBio

29020.

PMAP-CutDB

P19320.

SOURCE

Search...

Entry information

Entry name

VCAM1_HUMAN

Accession

Primary (citable) accession number: P19320
Secondary accession number(s): A8K6R7 , B4DKS4, E9PDD1, Q6NUP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 173 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.