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P08648

- ITA5_HUMAN

UniProt

P08648 - ITA5_HUMAN

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Protein
Integrin alpha-5
Gene
ITGA5, FNRA
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 – 28891 Publication
Calcium bindingi334 – 34291 Publication
Calcium bindingi401 – 40991 Publication
Calcium bindingi465 – 47391 Publication

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 junction assembly Source: Ensembl
  7. extracellular matrix organization Source: Reactome
  8. heterophilic cell-cell adhesion Source: Ensembl
  9. integrin-mediated signaling pathway Source: UniProtKB-KW
  10. leukocyte cell-cell adhesion Source: Ensembl
  11. leukocyte migration Source: Reactome
  12. memory Source: Ensembl
  13. negative regulation of anoikis Source: UniProtKB
  14. positive regulation of cell migration Source: Ensembl
  15. positive regulation of cell-substrate adhesion Source: Ensembl
  16. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  17. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  18. viral process Source: UniProtKB-KW
  19. 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 – 995954Extracellular Reviewed prediction
Add
BLAST
Transmembranei996 – 102126Helical; Reviewed prediction
Add
BLAST
Topological domaini1022 – 104928Cytoplasmic Reviewed prediction
Add
BLAST

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
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 Publication
Add
BLAST
Chaini42 – 10491008Integrin alpha-5
PRO_0000016249Add
BLAST
Chaini42 – 894853Integrin alpha-5 heavy chain
PRO_0000016250Add
BLAST
Chaini895 – 1049155Integrin alpha-5 light chain
PRO_0000016251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
Disulfide bondi99 ↔ 1082 Publications
Disulfide bondi156 ↔ 1762 Publications
Glycosylationi182 – 1821N-linked (GlcNAc...)1 Publication
Disulfide bondi192 ↔ 2052 Publications
Glycosylationi297 – 2971N-linked (GlcNAc...)3 Publications
Glycosylationi307 – 3071N-linked (GlcNAc...)3 Publications
Glycosylationi316 – 3161N-linked (GlcNAc...)1 Publication
Disulfide bondi513 ↔ 5222 Publications
Glycosylationi524 – 5241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi528 ↔ 5842 Publications
Glycosylationi530 – 5301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi593 – 5931N-linked (GlcNAc...) Reviewed prediction
Glycosylationi609 – 6091N-linked (GlcNAc...)1 Publication
Disulfide bondi645 ↔ 6512 Publications
Glycosylationi675 – 6751N-linked (GlcNAc...)1 Publication
Glycosylationi712 – 7121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi718 ↔ 7312 Publications
Glycosylationi724 – 7241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi771 – 7711N-linked (GlcNAc...); atypical1 Publication
Glycosylationi773 – 7731N-linked (GlcNAc...)2 Publications
Glycosylationi868 – 8681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi869 ↔ 921Interchain (between heavy and light chains)2 Publications
Disulfide bondi911 ↔ 9162 Publications

Post-translational modificationi

Proteolytic cleavage by PCSK5 mediates activation of the precursor.

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

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.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

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

Sequence similaritiesi

Contains 7 FG-GAP repeats.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261L → V1 Publication
Sequence conflicti26 – 261L → V1 Publication
Sequence conflicti33 – 331L → V1 Publication
Sequence conflicti33 – 331L → V1 Publication

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

« 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: September 3, 2014
This is version 168 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

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