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P08648

- ITA5_HUMAN

UniProt

P08648 - ITA5_HUMAN

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Protein

Integrin alpha-5

Gene

ITGA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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. endodermal cell differentiation Source: UniProtKB
  9. extracellular matrix organization Source: Reactome
  10. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: Ensembl
  11. heterotypic cell-cell adhesion Source: UniProtKB
  12. integrin-mediated signaling pathway Source: UniProtKB-KW
  13. leukocyte cell-cell adhesion Source: Ensembl
  14. leukocyte migration Source: Reactome
  15. memory Source: Ensembl
  16. negative regulation of anoikis Source: UniProtKB
  17. positive regulation of cell migration Source: Ensembl
  18. positive regulation of cell-substrate adhesion Source: Ensembl
  19. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  20. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  21. viral process Source: UniProtKB-KW
  22. wound healing, spreading of epidermal cells Source: BHF-UCL
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 995954ExtracellularSequence AnalysisAdd
BLAST
Transmembranei996 – 102126HelicalSequence AnalysisAdd
BLAST
Topological domaini1022 – 104928CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
  2. cell surface Source: UniProtKB
  3. cytoplasm Source: Ensembl
  4. external side of plasma membrane Source: Ensembl
  5. focal adhesion Source: UniProtKB
  6. integrin complex Source: ProtInc
  7. plasma membrane Source: Reactome
  8. ruffle Source: HGNC
  9. synapse Source: Ensembl
Complete GO annotation...

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

BgeeiP08648.
CleanExiHS_ITGA5.
ExpressionAtlasiP08648. baseline and differential.
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. 22 interactions.
DIPiDIP-40037N.
IntActiP08648. 15 interactions.
MINTiMINT-5005934.
STRINGi9606.ENSP00000293379.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VI3X-ray2.90A/C42-664[»]
3VI4X-ray2.90A/C42-664[»]
ProteinModelPortaliP08648.
SMRiP08648. Positions 42-988.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118782.
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

        10         20         30         40         50
MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA
60 70 80 90 100
VLSGPPGSFF GFSVEFYRPG TDGVSVLVGA PKANTSQPGV LQGGAVYLCP
110 120 130 140 150
WGASPTQCTP IEFDSKGSRL LESSLSSSEG EEPVEYKSLQ WFGATVRAHG
160 170 180 190 200
SSILACAPLY SWRTEKEPLS DPVGTCYLST DNFTRILEYA PCRSDFSWAA
210 220 230 240 250
GQGYCQGGFS AEFTKTGRVV LGGPGSYFWQ GQILSATQEQ IAESYYPEYL
260 270 280 290 300
INLVQGQLQT RQASSIYDDS YLGYSVAVGE FSGDDTEDFV AGVPKGNLTY
310 320 330 340 350
GYVTILNGSD IRSLYNFSGE QMASYFGYAV AATDVNGDGL DDLLVGAPLL
360 370 380 390 400
MDRTPDGRPQ EVGRVYVYLQ HPAGIEPTPT LTLTGHDEFG RFGSSLTPLG
410 420 430 440 450
DLDQDGYNDV AIGAPFGGET QQGVVFVFPG GPGGLGSKPS QVLQPLWAAS
460 470 480 490 500
HTPDFFGSAL RGGRDLDGNG YPDLIVGSFG VDKAVVYRGR PIVSASASLT
510 520 530 540 550
IFPAMFNPEE RSCSLEGNPV ACINLSFCLN ASGKHVADSI GFTVELQLDW
560 570 580 590 600
QKQKGGVRRA LFLASRQATL TQTLLIQNGA REDCREMKIY LRNESEFRDK
610 620 630 640 650
LSPIHIALNF SLDPQAPVDS HGLRPALHYQ SKSRIEDKAQ ILLDCGEDNI
660 670 680 690 700
CVPDLQLEVF GEQNHVYLGD KNALNLTFHA QNVGEGGAYE AELRVTAPPE
710 720 730 740 750
AEYSGLVRHP GNFSSLSCDY FAVNQSRLLV CDLGNPMKAG ASLWGGLRFT
760 770 780 790 800
VPHLRDTKKT IQFDFQILSK NLNNSQSDVV SFRLSVEAQA QVTLNGVSKP
810 820 830 840 850
EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI SQGVLELSCP
860 870 880 890 900
QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLHH QQKREAPSRS
910 920 930 940 950
SASSGPQILK CPEAECFRLR CELGPLHQQE SQSLQLHFRV WAKTFLQREH
960 970 980 990 1000
QPFSLQCEAV YKALKMPYRI LPRQLPQKER QVATAVQWTK AEGSYGVPLW
1010 1020 1030 1040
IIILAILFGL LLLGLLIYIL YKLGFFKRSL PYGTAMEKAQ LKPPATSDA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109884. 22 interactions.
DIPi DIP-40037N.
IntActi P08648. 15 interactions.
MINTi MINT-5005934.
STRINGi 9606.ENSP00000293379.

Chemistry

BindingDBi P08648.
ChEMBLi CHEMBL2095226.

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.
GeneTreei ENSGT00760000118782.
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

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

Gene expression databases

Bgeei P08648.
CleanExi HS_ITGA5.
ExpressionAtlasi P08648. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 171 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