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P06756 (ITAV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-V
Alternative name(s):
Vitronectin receptor subunit alpha
CD_antigen=CD51
Gene names
Name:ITGAV
Synonyms:MSK8, VNRA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1048 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The alpha-V integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

Subunit structure

Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-V associates with either beta-1, beta-3, beta-5, beta-6 or beta-8 subunit. Interacts with HIV-1 Tat. Alpha-V/beta-6 binds to foot-and-mouth disease virus (FMDV) VP1 protein and acts as a receptor for this virus By similarity. Alpha-V/beta-6 binds to coxsackievirus A9 and coxsackievirus B1 capsid proteins and acts as a receptor for these viruses. Interacts with RAB25. Alpha-V/beta-3 interacts with herpes virus 8/HHV-8 glycoprotein B and acts as a receptor for the virus. Interacts with CIB1. Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20 Ref.25

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Sequence caution

The sequence BAD93131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   Molecular functionHost cell receptor for virus entry
Integrin
Receptor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: BHF-UCL

angiogenesis

Inferred from expression pattern PubMed 11866539. Source: UniProtKB

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

calcium ion transmembrane transport

Inferred from direct assay PubMed 18395422. Source: UniProtKB

cell adhesion

Inferred from direct assay PubMed 10218736. Source: BHF-UCL

cell-matrix adhesion

Non-traceable author statement PubMed 11877390. Source: UniProtKB

entry of symbiont into host cell by promotion of host phagocytosis

Non-traceable author statement PubMed 10570297. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from sequence or structural similarity. Source: BHF-UCL

integrin-mediated signaling pathway

Non-traceable author statement PubMed 11877390. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of entry of bacterium into host cell

Inferred from direct assay PubMed 10570297. Source: BHF-UCL

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 10708943. Source: BHF-UCL

negative regulation of lipid storage

Inferred from mutant phenotype PubMed 15215180. Source: BHF-UCL

negative regulation of lipid transport

Inferred from mutant phenotype PubMed 15215180. Source: BHF-UCL

negative regulation of lipoprotein metabolic process

Inferred from mutant phenotype PubMed 15215180. Source: BHF-UCL

negative regulation of low-density lipoprotein particle receptor biosynthetic process

Inferred from mutant phenotype PubMed 15215180. Source: BHF-UCL

negative regulation of macrophage derived foam cell differentiation

Inferred from mutant phenotype PubMed 15215180. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from direct assay PubMed 10708943. Source: BHF-UCL

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 19578119. Source: BHF-UCL

positive regulation of osteoblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic cell clearance

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of phagocytosis

Inferred from direct assay PubMed 10570297. Source: BHF-UCL

viral entry into host cell

Traceable author statement PubMed 10570297. Source: BHF-UCL

   Cellular_componentalphav-beta3 integrin-IGF-1-IGF1R complex

Inferred from direct assay PubMed 19578119. Source: BHF-UCL

cell surface

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

integral component of plasma membrane

Non-traceable author statement PubMed 11877390. Source: UniProtKB

integrin complex

Non-traceable author statement PubMed 11877390. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

phagocytic vesicle

Traceable author statement. Source: Reactome

plasma membrane

Inferred from direct assay PubMed 21310825. Source: BHF-UCL

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11877390Ref.19Ref.25. Source: UniProtKB

transforming growth factor beta binding

Inferred from sequence or structural similarity. Source: BHF-UCL

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

voltage-gated calcium channel activity

Inferred from direct assay PubMed 18395422. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB3P0510611EBI-298282,EBI-702847
ITGB5P180842EBI-298282,EBI-1223434

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06756-1)

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.
Isoform 2 (identifier: P06756-2)

The sequence of this isoform differs from the canonical sequence as follows:
     175-211: QDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQG → R
Note: No experimental confirmation available.
Isoform 3 (identifier: P06756-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAFPPRRRLR...VDFFVPSASS → MLLGTLLLILYILMLC
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.11
Chain31 – 10481018Integrin alpha-V
PRO_0000016301
Chain31 – 889859Integrin alpha-V heavy chain
PRO_0000016302
Chain891 – 1048158Integrin alpha-V light chain
PRO_0000016303

Regions

Topological domain31 – 992962Extracellular Potential
Transmembrane993 – 101624Helical; Potential
Topological domain1017 – 104832Cytoplasmic Potential
Repeat32 – 9867FG-GAP 1
Repeat109 – 17062FG-GAP 2
Repeat173 – 22553FG-GAP 3
Repeat237 – 29559FG-GAP 4
Repeat296 – 35762FG-GAP 5
Repeat358 – 41558FG-GAP 6
Repeat419 – 48264FG-GAP 7
Calcium binding260 – 2689 Potential
Calcium binding314 – 3229 Potential
Calcium binding379 – 3879 Potential
Calcium binding443 – 4519 Potential
Motif1019 – 10235GFFKR motif

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Ref.22 Ref.23
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation4881N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Potential
Glycosylation6151N-linked (GlcNAc...) Ref.15 Ref.22
Glycosylation7041N-linked (GlcNAc...) Ref.22
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation8511N-linked (GlcNAc...) Potential
Glycosylation8741N-linked (GlcNAc...) Ref.22 Ref.23
Glycosylation9451N-linked (GlcNAc...) Potential
Glycosylation9731N-linked (GlcNAc...) Potential
Glycosylation9801N-linked (GlcNAc...) Potential
Disulfide bond89 ↔ 97 Ref.16
Disulfide bond138 ↔ 158 Ref.16
Disulfide bond172 ↔ 185 Ref.16
Disulfide bond491 ↔ 502 Ref.16
Disulfide bond508 ↔ 565 Ref.16
Disulfide bond626 ↔ 632 Ref.16
Disulfide bond698 ↔ 711 Ref.16
Disulfide bond852 ↔ 914Interchain (between heavy and light chains) Ref.16
Disulfide bond904 ↔ 909 Ref.16

Natural variations

Alternative sequence1 – 6262MAFPP…PSASS → MLLGTLLLILYILMLC in isoform 3.
VSP_044914
Alternative sequence175 – 21137QDIDA…FYWQG → R in isoform 2.
VSP_024351
Natural variant4051I → V.
Corresponds to variant rs3738918 [ dbSNP | Ensembl ].
VAR_024289
Natural variant5481S → A.
Corresponds to variant rs2230615 [ dbSNP | Ensembl ].
VAR_055970
Natural variant7831V → I. Ref.1 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10
Corresponds to variant rs2230616 [ dbSNP | Ensembl ].
VAR_031547

Experimental info

Sequence conflict4251W → R in AAG03000. Ref.2
Sequence conflict7001F → L in AAI44101. Ref.8
Sequence conflict10391H → R in AAG03000. Ref.2

Secondary structure

.................................................................................................................................................................................................... 1048
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 364EE25C5303A2D7

FASTA1,048116,038
        10         20         30         40         50         60 
MAFPPRRRLR LGPRGLPLLL SGLLLPLCRA FNLDVDSPAE YSGPEGSYFG FAVDFFVPSA 

        70         80         90        100        110        120 
SSRMFLLVGA PKANTTQPGI VEGGQVLKCD WSSTRRCQPI EFDATGNRDY AKDDPLEFKS 

       130        140        150        160        170        180 
HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSQDIDAD 

       190        200        210        220        230        240 
GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IVSKYDPNVY SIKYNNQLAT 

       250        260        270        280        290        300 
RTAQAIFDDS YLGYSVAVGD FNGDGIDDFV SGVPRAARTL GMVYIYDGKN MSSLYNFTGE 

       310        320        330        340        350        360 
QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ RASGDFQTTK 

       370        380        390        400        410        420 
LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GIVYIFNGRS TGLNAVPSQI 

       430        440        450        460        470        480 
LEGQWAARSM PPSFGYSMKG ATDIDKNGYP DLIVGAFGVD RAILYRARPV ITVNAGLEVY 

       490        500        510        520        530        540 
PSILNQDNKT CSLPGTALKV SCFNVRFCLK ADGKGVLPRK LNFQVELLLD KLKQKGAIRR 

       550        560        570        580        590        600 
ALFLYSRSPS HSKNMTISRG GLMQCEELIA YLRDESEFRD KLTPITIFME YRLDYRTAAD 

       610        620        630        640        650        660 
TTGLQPILNQ FTPANISRQA HILLDCGEDN VCKPKLEVSV DSDQKKIYIG DDNPLTLIVK 

       670        680        690        700        710        720 
AQNQGEGAYE AELIVSIPLQ ADFIGVVRNN EALARLSCAF KTENQTRQVV CDLGNPMKAG 

       730        740        750        760        770        780 
TQLLAGLRFS VHQQSEMDTS VKFDLQIQSS NLFDKVSPVV SHKVDLAVLA AVEIRGVSSP 

       790        800        810        820        830        840 
DHVFLPIPNW EHKENPETEE DVGPVVQHIY ELRNNGPSSF SKAMLHLQWP YKYNNNTLLY 

       850        860        870        880        890        900 
ILHYDIDGPM NCTSDMEINP LRIKISSLQT TEKNDTVAGQ GERDHLITKR DLALSEGDIH 

       910        920        930        940        950        960 
TLGCGVAQCL KIVCQVGRLD RGKSAILYVK SLLWTETFMN KENQNHSYSL KSSASFNVIE 

       970        980        990       1000       1010       1020 
FPYKNLPIED ITNSTLVTTN VTWGIQPAPM PVPVWVIILA VLAGLLLLAV LVFVMYRMGF 

      1030       1040 
FKRVRPPQEE QEREQLQPHE NGEGNSET 

« Hide

Isoform 2 [UniParc].

Checksum: 132A3F554FCDE8B6
Show »

FASTA1,012112,258
Isoform 3 [UniParc].

Checksum: D6178F9822C83829
Show »

FASTA1,002111,132

References

« Hide 'large scale' references
[1]"Amino acid sequence of the vitronectin receptor alpha subunit and comparative expression of adhesion receptor mRNAs."
Suzuki S., Argraves W.S., Arai H., Languino L.R., Pierschbacher M.D., Ruoslahti E.
J. Biol. Chem. 262:14080-14085(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-783.
[2]"Cloning and characterisation of ITGAV, the genomic sequence for human cell adhesion protein (vitronectin) receptor alpha subunit, CD51."
Sims M.A., Field S., Barnes M.R., Shaikh N., Ellington K., Murphy K.E., Spurr N.K., Campbell D.A.
Cytogenet. Cell Genet. 89:268-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] (ISOFORM 3), VARIANT ILE-783.
Tissue: Testis.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-783.
Tissue: Aortic endothelium.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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], VARIANT ILE-783.
[7]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-783.
[8]"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] (ISOFORMS 1 AND 2), VARIANT ILE-783.
[9]"The integrin alpha v gene: identification and characterization of the promoter region."
Donahue J.P., Sugg N., Hawiger J.
Biochim. Biophys. Acta 1219:228-232(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
[10]"cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors."
Suzuki S., Argraves W.S., Pytela R., Arai H., Krusius T., Pierschbacher M.D., Ruoslahti E.
Proc. Natl. Acad. Sci. U.S.A. 83:8614-8618(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-1048, VARIANT ILE-783.
[11]"A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells."
Cheresh D.A., Smith J.W., Cooper H.M., Quaranta V.
Cell 57:59-69(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-41.
[12]"Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of human colon cancer cells."
Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.
Virology 239:71-77(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
[13]"The Tat protein of human immunodeficiency virus type-1 promotes vascular cell growth and locomotion by engaging the alpha5beta1 and alphavbeta3 integrins and by mobilizing sequestered basic fibroblast growth factor."
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[14]"The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus."
Jackson T., Sheppard D., Denyer M., Blakemore W., King A.M.
J. Virol. 74:4949-4956(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FMDV VP1.
[15]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-615.
[16]"Mass spectrometric based mapping of the disulfide bonding patterns of integrin alpha chains."
Krokhin O.V., Cheng K., Sousa S.L., Ens W., Standing K.G., Wilkins J.A.
Biochemistry 42:12950-12959(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[17]"Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9."
Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.
J. Virol. 78:6967-6973(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments."
Caswell P.T., Spence H.J., Parsons M., White D.P., Clark K., Cheng K.W., Mills G.B., Humphries M.J., Messent A.J., Anderson K.I., McCaffrey M.W., Ozanne B.W., Norman J.C.
Dev. Cell 13:496-510(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB25.
[20]"Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of Kaposi's sarcoma-associated herpesvirus and functions as an RGD-dependent entry receptor."
Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.
J. Virol. 82:1570-1580(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-8 GLYCOPROTEIN B.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-704 AND ASN-874.
Tissue: Liver.
[23]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-874.
Tissue: Leukemic T-cell.
[24]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity."
Freeman T.C. Jr., Black J.L., Bray H.G., Dagliyan O., Wu Y.I., Tripathy A., Dokholyan N.V., Leisner T.M., Parise L.V.
Biochemistry 52:7082-7090(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIB1.
[26]"Crystal structure of the extracellular segment of integrin alpha Vbeta3."
Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A.
Science 294:339-345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-987.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14648 mRNA. Translation: AAA36808.1.
AF251841 expand/collapse EMBL AC list , AF251818, AF251819, AF251820, AF251821, AF251822, AF251823, AF251824, AF251825, AF251826, AF251827, AF251828, AF251829, AF251830, AF251831, AF251832, AF251833, AF251834, AF251835, AF251836, AF251837, AF251838, AF251839, AF251840 Genomic DNA. Translation: AAG03000.1.
AK302990 mRNA. Translation: BAH13869.1.
AB209894 mRNA. Translation: BAD93131.1. Different initiation.
AC017101 Genomic DNA. Translation: AAY24257.1.
EU332844 Genomic DNA. Translation: ABY87533.1.
CH471058 Genomic DNA. Translation: EAX10934.1.
BC126231 mRNA. Translation: AAI26232.1.
BC136442 mRNA. Translation: AAI36443.1.
BC144100 mRNA. Translation: AAI44101.1.
U07375 Genomic DNA. Translation: AAA61631.1.
CCDSCCDS2292.1. [P06756-1]
CCDS46470.1. [P06756-2]
CCDS46471.1. [P06756-3]
PIRA27421.
RefSeqNP_001138471.1. NM_001144999.2.
NP_001138472.1. NM_001145000.2.
NP_002201.1. NM_002210.4.
UniGeneHs.436873.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JV2X-ray3.10A31-987[»]
1L5GX-ray3.20A31-987[»]
1M1XX-ray3.30A31-987[»]
1U8CX-ray3.10A31-987[»]
3IJEX-ray2.90A31-997[»]
4G1EX-ray3.00A31-989[»]
4G1MX-ray2.90A31-989[»]
4MMXX-ray3.32A31-989[»]
4MMYX-ray3.18A31-989[»]
4MMZX-ray3.10A31-989[»]
4O02X-ray3.60A31-992[»]
ProteinModelPortalP06756.
SMRP06756. Positions 31-989, 992-1031.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109891. 19 interactions.
DIPDIP-31785N.
IntActP06756. 12 interactions.
MINTMINT-209462.
STRING9606.ENSP00000261023.

Chemistry

BindingDBP06756.
ChEMBLCHEMBL2096675.

PTM databases

PhosphoSiteP06756.

Polymorphism databases

DMDM143811408.

Proteomic databases

MaxQBP06756.
PaxDbP06756.
PRIDEP06756.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261023; ENSP00000261023; ENSG00000138448. [P06756-1]
ENST00000374907; ENSP00000364042; ENSG00000138448. [P06756-2]
ENST00000433736; ENSP00000404291; ENSG00000138448. [P06756-3]
GeneID3685.
KEGGhsa:3685.
UCSCuc002upq.4. human. [P06756-1]

Organism-specific databases

CTD3685.
GeneCardsGC02P187418.
HGNCHGNC:6150. ITGAV.
HPACAB002499.
HPA004856.
MIM193210. gene.
neXtProtNX_P06756.
PharmGKBPA37336.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26407.
HOVERGENHBG006186.
KOK06487.
OMADKNGYPD.
OrthoDBEOG7R830R.
PhylomeDBP06756.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP06756.

Gene expression databases

ArrayExpressP06756.
BgeeP06756.
CleanExHS_ITGAV.
GenevestigatorP06756.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]
PfamPF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
[Graphical view]
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGAV. human.
EvolutionaryTraceP06756.
GeneWikiITGAV.
GenomeRNAi3685.
NextBio14423.
PMAP-CutDBB0LPF4.
PROP06756.
SOURCESearch...

Entry information

Entry nameITAV_HUMAN
AccessionPrimary (citable) accession number: P06756
Secondary accession number(s): A0AV67 expand/collapse secondary AC list , B0LPF4, B7Z883, B7ZLX0, D3DPG8, E7EWZ6, Q53SK4, Q59EB7, Q6LD15
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 178 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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