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P08648

- ITA5_HUMAN

UniProt

P08648 - ITA5_HUMAN

Protein

Integrin alpha-5

Gene

ITGA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (10 Oct 2002)
      Previous versions | rss
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    Functioni

    Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei262 – 2621Arg of R-G-D substrate
    Binding sitei269 – 2691Arg of R-G-D substrate
    Metal bindingi280 – 2801Calcium 1
    Metal bindingi282 – 2821Calcium 1
    Metal bindingi284 – 2841Calcium 1
    Metal bindingi286 – 2861Calcium 1; via carbonyl oxygen
    Metal bindingi288 – 2881Calcium 1
    Metal bindingi334 – 3341Calcium 2
    Metal bindingi336 – 3361Calcium 2
    Metal bindingi338 – 3381Calcium 2
    Metal bindingi340 – 3401Calcium 2; via carbonyl oxygen
    Metal bindingi342 – 3421Calcium 2
    Metal bindingi401 – 4011Calcium 3
    Metal bindingi403 – 4031Calcium 3
    Metal bindingi405 – 4051Calcium 3
    Metal bindingi407 – 4071Calcium 3; via carbonyl oxygen
    Metal bindingi409 – 4091Calcium 3
    Metal bindingi465 – 4651Calcium 4
    Metal bindingi467 – 4671Calcium 4
    Metal bindingi469 – 4691Calcium 4
    Metal bindingi471 – 4711Calcium 4; via carbonyl oxygen
    Metal bindingi473 – 4731Calcium 4

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi280 – 2889
    Calcium bindingi334 – 3429
    Calcium bindingi401 – 4099
    Calcium bindingi465 – 4739

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. platelet-derived growth factor receptor binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. vascular endothelial growth factor receptor 2 binding Source: BHF-UCL

    GO - Biological processi

    1. angiogenesis Source: BHF-UCL
    2. axon guidance Source: Reactome
    3. blood coagulation Source: Reactome
    4. cell adhesion Source: ProtInc
    5. cell-cell adhesion mediated by integrin Source: Ensembl
    6. cell-substrate adhesion Source: UniProtKB
    7. cell-substrate junction assembly Source: Ensembl
    8. extracellular matrix organization Source: Reactome
    9. heterophilic cell-cell adhesion Source: Ensembl
    10. integrin-mediated signaling pathway Source: UniProtKB-KW
    11. leukocyte cell-cell adhesion Source: Ensembl
    12. leukocyte migration Source: Reactome
    13. memory Source: Ensembl
    14. negative regulation of anoikis Source: UniProtKB
    15. positive regulation of cell migration Source: Ensembl
    16. positive regulation of cell-substrate adhesion Source: Ensembl
    17. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    18. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    19. viral process Source: UniProtKB-KW
    20. wound healing, spreading of epidermal cells Source: BHF-UCL

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_150366. Elastic fibre formation.
    REACT_160131. Fibronectin matrix formation.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP08648.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-5
    Alternative name(s):
    CD49 antigen-like family member E
    Fibronectin receptor subunit alpha
    Integrin alpha-F
    VLA-5
    CD_antigen: CD49e
    Cleaved into the following 2 chains:
    Gene namesi
    Name:ITGA5
    Synonyms:FNRA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6141. ITGA5.

    Subcellular locationi

    GO - Cellular componenti

    1. alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
    2. cytoplasm Source: Ensembl
    3. external side of plasma membrane Source: Ensembl
    4. integrin complex Source: ProtInc
    5. plasma membrane Source: Reactome
    6. ruffle Source: HGNC
    7. synapse Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29941.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 41411 PublicationAdd
    BLAST
    Chaini42 – 10491008Integrin alpha-5PRO_0000016249Add
    BLAST
    Chaini42 – 894853Integrin alpha-5 heavy chainPRO_0000016250Add
    BLAST
    Chaini895 – 1049155Integrin alpha-5 light chainPRO_0000016251Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
    Disulfide bondi99 ↔ 108
    Disulfide bondi156 ↔ 176
    Glycosylationi182 – 1821N-linked (GlcNAc...)1 Publication
    Disulfide bondi192 ↔ 205
    Glycosylationi297 – 2971N-linked (GlcNAc...)3 Publications
    Glycosylationi307 – 3071N-linked (GlcNAc...)3 Publications
    Glycosylationi316 – 3161N-linked (GlcNAc...)1 Publication
    Disulfide bondi513 ↔ 522
    Glycosylationi524 – 5241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi528 ↔ 584
    Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi609 – 6091N-linked (GlcNAc...)1 Publication
    Disulfide bondi645 ↔ 651
    Glycosylationi675 – 6751N-linked (GlcNAc...)1 Publication
    Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi718 ↔ 731
    Glycosylationi724 – 7241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi771 – 7711N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi773 – 7731N-linked (GlcNAc...)2 Publications
    Glycosylationi868 – 8681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi869 ↔ 921Interchain (between heavy and light chains)
    Disulfide bondi911 ↔ 916

    Post-translational modificationi

    Proteolytic cleavage by PCSK5 mediates activation of the precursor.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08648.
    PaxDbiP08648.
    PeptideAtlasiP08648.
    PRIDEiP08648.

    PTM databases

    PhosphoSiteiP08648.
    UniCarbKBiP08648.

    Expressioni

    Gene expression databases

    ArrayExpressiP08648.
    BgeeiP08648.
    CleanExiHS_ITGA5.
    GenevestigatoriP08648.

    Organism-specific databases

    HPAiCAB009008.
    HPA002642.

    Interactioni

    Subunit structurei

    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-5 associates with beta-1. Interacts with HPS5 and NISCH. Interacts with RAB21 and COMP. Interacts with HIV-1 Tat. Interacts with CIB1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ENGP178134EBI-1382311,EBI-2834630
    SHARPINQ9H0F64EBI-1382311,EBI-3942966

    Protein-protein interaction databases

    BioGridi109884. 21 interactions.
    DIPiDIP-40037N.
    IntActiP08648. 16 interactions.
    MINTiMINT-5005934.
    STRINGi9606.ENSP00000293379.

    Structurei

    Secondary structure

    1
    1049
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 534
    Beta strandi62 – 676
    Beta strandi69 – 724
    Beta strandi75 – 806
    Beta strandi95 – 1028
    Beta strandi109 – 1113
    Beta strandi125 – 1295
    Beta strandi133 – 1364
    Beta strandi144 – 1496
    Beta strandi152 – 1576
    Beta strandi165 – 1673
    Beta strandi175 – 1806
    Turni181 – 1844
    Beta strandi185 – 1895
    Beta strandi193 – 1953
    Turni199 – 2046
    Beta strandi209 – 2135
    Beta strandi219 – 2235
    Helixi226 – 2294
    Beta strandi231 – 2366
    Helixi238 – 2447
    Helixi265 – 2673
    Beta strandi274 – 2796
    Beta strandi282 – 2865
    Beta strandi288 – 29710
    Beta strandi300 – 3067
    Beta strandi308 – 3103
    Beta strandi313 – 3186
    Beta strandi328 – 3336
    Beta strandi336 – 3405
    Beta strandi342 – 3476
    Beta strandi351 – 3533
    Beta strandi359 – 3613
    Beta strandi364 – 3685
    Beta strandi380 – 3845
    Helixi392 – 3943
    Beta strandi395 – 40713
    Beta strandi409 – 4146
    Beta strandi424 – 4285
    Beta strandi440 – 4434
    Beta strandi458 – 4647
    Beta strandi467 – 4704
    Beta strandi474 – 4785
    Helixi479 – 4813
    Beta strandi483 – 4875
    Beta strandi492 – 50312
    Beta strandi513 – 5208
    Beta strandi522 – 53211
    Beta strandi534 – 5363
    Beta strandi538 – 54811
    Turni549 – 5557
    Beta strandi560 – 5623
    Turni563 – 5653
    Beta strandi566 – 57712
    Beta strandi583 – 5919
    Beta strandi604 – 6129
    Beta strandi614 – 6163
    Beta strandi620 – 6223
    Beta strandi634 – 6418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VI3X-ray2.90A/C42-664[»]
    3VI4X-ray2.90A/C42-664[»]
    ProteinModelPortaliP08648.
    SMRiP08648. Positions 42-988, 997-1034.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 995954ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1022 – 104928CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei996 – 102126HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati43 – 10866FG-GAP 1Add
    BLAST
    Repeati128 – 18861FG-GAP 2Add
    BLAST
    Repeati192 – 24554FG-GAP 3Add
    BLAST
    Repeati259 – 31557FG-GAP 4Add
    BLAST
    Repeati316 – 37762FG-GAP 5Add
    BLAST
    Repeati378 – 43760FG-GAP 6Add
    BLAST
    Repeati441 – 50464FG-GAP 7Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1021 – 10288Interaction with HPS5

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1024 – 10285GFFKR motif

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG26407.
    HOGENOMiHOG000231603.
    HOVERGENiHBG006186.
    InParanoidiP08648.
    KOiK06484.
    OMAiERSCSLE.
    OrthoDBiEOG7HQN77.
    PhylomeDBiP08648.
    TreeFamiTF105391.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view]
    PfamiPF01839. FG-GAP. 3 hits.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    [Graphical view]
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08648-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA     50
    VLSGPPGSFF GFSVEFYRPG TDGVSVLVGA PKANTSQPGV LQGGAVYLCP 100
    WGASPTQCTP IEFDSKGSRL LESSLSSSEG EEPVEYKSLQ WFGATVRAHG 150
    SSILACAPLY SWRTEKEPLS DPVGTCYLST DNFTRILEYA PCRSDFSWAA 200
    GQGYCQGGFS AEFTKTGRVV LGGPGSYFWQ GQILSATQEQ IAESYYPEYL 250
    INLVQGQLQT RQASSIYDDS YLGYSVAVGE FSGDDTEDFV AGVPKGNLTY 300
    GYVTILNGSD IRSLYNFSGE QMASYFGYAV AATDVNGDGL DDLLVGAPLL 350
    MDRTPDGRPQ EVGRVYVYLQ HPAGIEPTPT LTLTGHDEFG RFGSSLTPLG 400
    DLDQDGYNDV AIGAPFGGET QQGVVFVFPG GPGGLGSKPS QVLQPLWAAS 450
    HTPDFFGSAL RGGRDLDGNG YPDLIVGSFG VDKAVVYRGR PIVSASASLT 500
    IFPAMFNPEE RSCSLEGNPV ACINLSFCLN ASGKHVADSI GFTVELQLDW 550
    QKQKGGVRRA LFLASRQATL TQTLLIQNGA REDCREMKIY LRNESEFRDK 600
    LSPIHIALNF SLDPQAPVDS HGLRPALHYQ SKSRIEDKAQ ILLDCGEDNI 650
    CVPDLQLEVF GEQNHVYLGD KNALNLTFHA QNVGEGGAYE AELRVTAPPE 700
    AEYSGLVRHP GNFSSLSCDY FAVNQSRLLV CDLGNPMKAG ASLWGGLRFT 750
    VPHLRDTKKT IQFDFQILSK NLNNSQSDVV SFRLSVEAQA QVTLNGVSKP 800
    EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI SQGVLELSCP 850
    QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLHH QQKREAPSRS 900
    SASSGPQILK CPEAECFRLR CELGPLHQQE SQSLQLHFRV WAKTFLQREH 950
    QPFSLQCEAV YKALKMPYRI LPRQLPQKER QVATAVQWTK AEGSYGVPLW 1000
    IIILAILFGL LLLGLLIYIL YKLGFFKRSL PYGTAMEKAQ LKPPATSDA 1049
    Length:1,049
    Mass (Da):114,536
    Last modified:October 10, 2002 - v2
    Checksum:i6B4D558D4F739CBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261L → V(PubMed:2958481)Curated
    Sequence conflicti26 – 261L → V(PubMed:1834647)Curated
    Sequence conflicti33 – 331L → V(PubMed:2958481)Curated
    Sequence conflicti33 – 331L → V(PubMed:1834647)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti585 – 5851R → I.
    Corresponds to variant rs12318746 [ dbSNP | Ensembl ].
    VAR_049631

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06256 mRNA. Translation: CAA29601.1.
    BC008786 mRNA. Translation: AAH08786.1.
    M13918 mRNA. Translation: AAA52467.1. Sequence problems.
    CCDSiCCDS8880.1.
    PIRiA27079.
    RefSeqiNP_002196.2. NM_002205.2.
    UniGeneiHs.505654.

    Genome annotation databases

    EnsembliENST00000293379; ENSP00000293379; ENSG00000161638.
    GeneIDi3678.
    KEGGihsa:3678.
    UCSCiuc001sga.3. human.

    Polymorphism databases

    DMDMi23831237.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06256 mRNA. Translation: CAA29601.1 .
    BC008786 mRNA. Translation: AAH08786.1 .
    M13918 mRNA. Translation: AAA52467.1 . Sequence problems.
    CCDSi CCDS8880.1.
    PIRi A27079.
    RefSeqi NP_002196.2. NM_002205.2.
    UniGenei Hs.505654.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VI3 X-ray 2.90 A/C 42-664 [» ]
    3VI4 X-ray 2.90 A/C 42-664 [» ]
    ProteinModelPortali P08648.
    SMRi P08648. Positions 42-988, 997-1034.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109884. 21 interactions.
    DIPi DIP-40037N.
    IntActi P08648. 16 interactions.
    MINTi MINT-5005934.
    STRINGi 9606.ENSP00000293379.

    Chemistry

    BindingDBi P08648.
    ChEMBLi CHEMBL2111425.

    PTM databases

    PhosphoSitei P08648.
    UniCarbKBi P08648.

    Polymorphism databases

    DMDMi 23831237.

    Proteomic databases

    MaxQBi P08648.
    PaxDbi P08648.
    PeptideAtlasi P08648.
    PRIDEi P08648.

    Protocols and materials databases

    DNASUi 3678.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000293379 ; ENSP00000293379 ; ENSG00000161638 .
    GeneIDi 3678.
    KEGGi hsa:3678.
    UCSCi uc001sga.3. human.

    Organism-specific databases

    CTDi 3678.
    GeneCardsi GC12M054789.
    HGNCi HGNC:6141. ITGA5.
    HPAi CAB009008.
    HPA002642.
    MIMi 135620. gene.
    neXtProti NX_P08648.
    PharmGKBi PA29941.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG26407.
    HOGENOMi HOG000231603.
    HOVERGENi HBG006186.
    InParanoidi P08648.
    KOi K06484.
    OMAi ERSCSLE.
    OrthoDBi EOG7HQN77.
    PhylomeDBi P08648.
    TreeFami TF105391.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_150366. Elastic fibre formation.
    REACT_160131. Fibronectin matrix formation.
    REACT_22272. Signal transduction by L1.
    SignaLinki P08648.

    Miscellaneous databases

    GeneWikii ITGA5.
    GenomeRNAii 3678.
    NextBioi 14395.
    PROi P08648.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08648.
    Bgeei P08648.
    CleanExi HS_ITGA5.
    Genevestigatori P08648.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 3 hits.
    PF08441. Integrin_alpha2. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    [Graphical view ]
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Placenta.
    3. "The alpha 5 beta 1 fibronectin receptor. Characterization of the alpha 5 gene promoter."
      Birkenmeier T.M., McQuillan J.J., Boedeker E.D., Argraves W.S., Ruoslahti E., Dean D.C.
      J. Biol. Chem. 266:20544-20549(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-73.
    4. "Comparison of cDNA-derived protein sequences of the human fibronectin and vitronectin receptor alpha-subunits and platelet glycoprotein IIb."
      Fitzgerald L.A., Poncz M., Steiner B., Rall S.C., Bennett J.S., Phillips D.R.
      Biochemistry 26:8158-8165(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-1049.
    5. "cDNA sequences from the alpha subunit of the fibronectin receptor predict a transmembrane domain and a short cytoplasmic peptide."
      Argraves W.S., Pytela R., Suzuki S., Millan J.L., Pierschbacher M.D., Ruoslahti E.
      J. Biol. Chem. 261:12922-12924(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 821-1049.
    6. "The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis."
      Takada Y., Strominger J.L., Hemler M.E.
      Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 42-55.
    7. "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.
    8. "Insulin receptor substrate 4 associates with the protein IRAS."
      Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
      J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NISCH.
    9. "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.
    10. "Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins."
      Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.
      J. Biol. Chem. 280:32655-32661(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COMP.
    11. "Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins."
      Pellinen T., Arjonen A., Vuoriluoto K., Kallio K., Fransen J.A.M., Ivaska J.
      J. Cell Biol. 173:767-780(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAB21.
    12. "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-297; ASN-307; ASN-675 AND ASN-773.
      Tissue: Liver.
    13. "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-297; ASN-307; ASN-771 AND ASN-773.
      Tissue: Leukemic T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Cleavage of endometrial alpha-integrins into their functional forms is mediated by proprotein convertase 5/6."
      Paule S., Aljofan M., Simon C., Rombauts L.J., Nie G.
      Hum. Reprod. 27:2766-2774(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC CLEAVAGE BY PCSK5.
    16. "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.
    17. "Crystal structure of alpha5beta1 integrin ectodomain: atomic details of the fibronectin receptor."
      Nagae M., Re S., Mihara E., Nogi T., Sugita Y., Takagi J.
      J. Cell Biol. 197:131-140(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 42-664 IN COMPLEX WITH ANTIBODY; ITGB1 AND RGD PEPTIDE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-84; ASN-182; ASN-297; ASN-307; ASN-316 AND ASN-609, SUBSTRATE-BINDING SITES, CALCIUM-BINDING SITES, SUBUNIT.

    Entry informationi

    Entry nameiITA5_HUMAN
    AccessioniPrimary (citable) accession number: P08648
    Secondary accession number(s): Q96HA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 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 12
      Human chromosome 12: 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