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Protein

Integrin alpha-5

Gene

ITGA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881).4 Publications
(Microbial infection) Integrin ITGA5:ITGB1 acts as a receptor for human metapneumovirus (PubMed:12907437). Integrin ITGA2:ITGB1 acts as a receptor for human parvovirus B19 (PubMed:24478423). In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions (PubMed:10397733).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei262Arg of R-G-D substrate1
Binding sitei269Arg of R-G-D substrate1
Metal bindingi280Calcium 11
Metal bindingi282Calcium 11
Metal bindingi284Calcium 11
Metal bindingi286Calcium 1; via carbonyl oxygen1
Metal bindingi288Calcium 11
Metal bindingi334Calcium 21
Metal bindingi336Calcium 21
Metal bindingi338Calcium 21
Metal bindingi340Calcium 2; via carbonyl oxygen1
Metal bindingi342Calcium 21
Metal bindingi401Calcium 31
Metal bindingi403Calcium 31
Metal bindingi405Calcium 31
Metal bindingi407Calcium 3; via carbonyl oxygen1
Metal bindingi409Calcium 31
Metal bindingi465Calcium 41
Metal bindingi467Calcium 41
Metal bindingi469Calcium 41
Metal bindingi471Calcium 4; via carbonyl oxygen1
Metal bindingi473Calcium 41

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi280 – 2889
Calcium bindingi334 – 3429
Calcium bindingi401 – 4099
Calcium bindingi465 – 4739

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • angiogenesis Source: BHF-UCL
  • cell adhesion Source: ProtInc
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell-cell adhesion mediated by integrin Source: Ensembl
  • cell-substrate adhesion Source: UniProtKB
  • cell-substrate junction assembly Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: Ensembl
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • leukocyte cell-cell adhesion Source: Ensembl
  • leukocyte migration Source: Reactome
  • memory Source: Ensembl
  • negative regulation of anoikis Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell-substrate adhesion Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of sprouting angiogenesis Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • wound healing, spreading of epidermal cells Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000161638-MONOMER.
ReactomeiR-HSA-1566948. Elastic fibre formation.
R-HSA-1566977. Fibronectin matrix formation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-445144. Signal transduction by L1.
SignaLinkiP08648.
SIGNORiP08648.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6141. ITGA5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini42 – 995ExtracellularSequence analysisAdd BLAST954
Transmembranei996 – 1021HelicalSequence analysisAdd BLAST26
Topological domaini1022 – 1049CytoplasmicSequence analysisAdd BLAST28

GO - Cellular componenti

  • alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
  • cell surface Source: UniProtKB
  • cytoplasmic vesicle Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • external side of plasma membrane Source: Ensembl
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • integrin complex Source: ProtInc
  • plasma membrane Source: Reactome
  • ruffle Source: HGNC
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3678.
OpenTargetsiENSG00000161638.
PharmGKBiPA29941.

Chemistry databases

ChEMBLiCHEMBL3955.

Polymorphism and mutation databases

BioMutaiITGA5.
DMDMi23831237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 411 PublicationAdd BLAST41
ChainiPRO_000001624942 – 1049Integrin alpha-5Add BLAST1008
ChainiPRO_000001625042 – 894Integrin alpha-5 heavy chainAdd BLAST853
ChainiPRO_0000016251895 – 1049Integrin alpha-5 light chainAdd BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi84N-linked (GlcNAc...)1 Publication1
Disulfide bondi99 ↔ 108
Modified residuei127PhosphoserineCombined sources1
Disulfide bondi156 ↔ 176
Glycosylationi182N-linked (GlcNAc...)1 Publication1
Disulfide bondi192 ↔ 205
Glycosylationi297N-linked (GlcNAc...)3 Publications1
Glycosylationi307N-linked (GlcNAc...)3 Publications1
Glycosylationi316N-linked (GlcNAc...)1 Publication1
Disulfide bondi513 ↔ 522
Glycosylationi524N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi528 ↔ 584
Glycosylationi530N-linked (GlcNAc...)Sequence analysis1
Glycosylationi593N-linked (GlcNAc...)Sequence analysis1
Glycosylationi609N-linked (GlcNAc...)1 Publication1
Disulfide bondi645 ↔ 651
Glycosylationi675N-linked (GlcNAc...)1 Publication1
Glycosylationi712N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi718 ↔ 731
Glycosylationi724N-linked (GlcNAc...)Sequence analysis1
Glycosylationi771N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi773N-linked (GlcNAc...)2 Publications1
Glycosylationi868N-linked (GlcNAc...)Sequence analysis1
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, Phosphoprotein

Proteomic databases

EPDiP08648.
MaxQBiP08648.
PaxDbiP08648.
PeptideAtlasiP08648.
PRIDEiP08648.
TopDownProteomicsiP08648.

PTM databases

iPTMnetiP08648.
PhosphoSitePlusiP08648.
SwissPalmiP08648.
UniCarbKBiP08648.

Expressioni

Gene expression databases

BgeeiENSG00000161638.
CleanExiHS_ITGA5.
ExpressionAtlasiP08648. baseline and differential.
GenevisibleiP08648. HS.

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 CIB1. ITGA5:ITGB1 interacts with NOV. ITGA5:ITGB1 interacts with FBN1 (PubMed:12807887, PubMed:17158881).8 Publications
(Microbial infection) Integrin ITGA5:ITGB1 interacts with human metapneumovirus fusion protein.1 Publication
(Microbial infection) Integrin ITGA2:ITGB1 interacts with human parvovirus B19 capsid proteins.1 Publication
(Microbial infection) Interacts with HIV-1 Tat.1 Publication

Binary interactionsi

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

GO - Molecular functioni

  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109884. 31 interactors.
DIPiDIP-40037N.
IntActiP08648. 17 interactors.
MINTiMINT-5005934.
STRINGi9606.ENSP00000293379.

Chemistry databases

BindingDBiP08648.

Structurei

Secondary structure

11049
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi50 – 53Combined sources4
Turni56 – 61Combined sources6
Beta strandi62 – 67Combined sources6
Beta strandi69 – 71Combined sources3
Beta strandi75 – 80Combined sources6
Beta strandi95 – 101Combined sources7
Beta strandi102 – 104Combined sources3
Beta strandi109 – 111Combined sources3
Helixi122 – 124Combined sources3
Beta strandi125 – 130Combined sources6
Beta strandi133 – 136Combined sources4
Beta strandi144 – 149Combined sources6
Beta strandi152 – 157Combined sources6
Beta strandi165 – 167Combined sources3
Beta strandi175 – 180Combined sources6
Turni181 – 184Combined sources4
Beta strandi185 – 189Combined sources5
Beta strandi193 – 196Combined sources4
Turni198 – 204Combined sources7
Beta strandi209 – 213Combined sources5
Beta strandi219 – 223Combined sources5
Helixi226 – 229Combined sources4
Beta strandi231 – 236Combined sources6
Helixi238 – 243Combined sources6
Beta strandi249 – 251Combined sources3
Helixi265 – 267Combined sources3
Beta strandi274 – 279Combined sources6
Beta strandi282 – 286Combined sources5
Beta strandi288 – 293Combined sources6
Turni294 – 300Combined sources7
Beta strandi302 – 306Combined sources5
Turni308 – 310Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi328 – 333Combined sources6
Beta strandi335 – 339Combined sources5
Beta strandi342 – 347Combined sources6
Beta strandi351 – 353Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi364 – 368Combined sources5
Beta strandi380 – 384Combined sources5
Helixi392 – 394Combined sources3
Beta strandi396 – 400Combined sources5
Beta strandi405 – 407Combined sources3
Beta strandi409 – 414Combined sources6
Beta strandi424 – 428Combined sources5
Beta strandi440 – 443Combined sources4
Beta strandi458 – 464Combined sources7
Beta strandi466 – 471Combined sources6
Beta strandi473 – 478Combined sources6
Helixi479 – 481Combined sources3
Beta strandi483 – 487Combined sources5
Beta strandi492 – 503Combined sources12
Beta strandi513 – 520Combined sources8
Beta strandi522 – 532Combined sources11
Beta strandi534 – 536Combined sources3
Beta strandi538 – 548Combined sources11
Turni549 – 555Combined sources7
Beta strandi560 – 562Combined sources3
Turni563 – 565Combined sources3
Beta strandi566 – 577Combined sources12
Beta strandi583 – 591Combined sources9
Beta strandi604 – 612Combined sources9
Beta strandi614 – 616Combined sources3
Beta strandi620 – 622Combined sources3
Beta strandi634 – 641Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VI3X-ray2.90A/C42-664[»]
3VI4X-ray2.90A/C42-664[»]
4WJKX-ray1.85A42-491[»]
4WK0X-ray1.78A42-491[»]
4WK2X-ray2.50A42-491[»]
4WK4X-ray2.50A42-491[»]
ProteinModelPortaliP08648.
SMRiP08648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati43 – 108FG-GAP 1PROSITE-ProRule annotationAdd BLAST66
Repeati128 – 188FG-GAP 2PROSITE-ProRule annotationAdd BLAST61
Repeati192 – 245FG-GAP 3PROSITE-ProRule annotationAdd BLAST54
Repeati259 – 311FG-GAP 4PROSITE-ProRule annotationAdd BLAST53
Repeati312 – 377FG-GAP 5PROSITE-ProRule annotationAdd BLAST66
Repeati378 – 437FG-GAP 6PROSITE-ProRule annotationAdd BLAST60
Repeati441 – 504FG-GAP 7PROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1021 – 1028Interaction with HPS58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1024 – 1028GFFKR motif5

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08648.
KOiK06484.
OMAiLHYQSKS.
OrthoDBiEOG091G05Z4.
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.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti26L → V (PubMed:2958481).Curated1
Sequence conflicti26L → V (PubMed:1834647).Curated1
Sequence conflicti33L → V (PubMed:2958481).Curated1
Sequence conflicti33L → V (PubMed:1834647).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049631585R → I.Corresponds to variant rs12318746dbSNPEnsembl.1

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_002196.4. NM_002205.4.
UniGeneiHs.505654.

Genome annotation databases

EnsembliENST00000293379; ENSP00000293379; ENSG00000161638.
GeneIDi3678.
KEGGihsa:3678.
UCSCiuc001sga.4. human.

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.
CCDSiCCDS8880.1.
PIRiA27079.
RefSeqiNP_002196.4. NM_002205.4.
UniGeneiHs.505654.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VI3X-ray2.90A/C42-664[»]
3VI4X-ray2.90A/C42-664[»]
4WJKX-ray1.85A42-491[»]
4WK0X-ray1.78A42-491[»]
4WK2X-ray2.50A42-491[»]
4WK4X-ray2.50A42-491[»]
ProteinModelPortaliP08648.
SMRiP08648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109884. 31 interactors.
DIPiDIP-40037N.
IntActiP08648. 17 interactors.
MINTiMINT-5005934.
STRINGi9606.ENSP00000293379.

Chemistry databases

BindingDBiP08648.
ChEMBLiCHEMBL3955.

PTM databases

iPTMnetiP08648.
PhosphoSitePlusiP08648.
SwissPalmiP08648.
UniCarbKBiP08648.

Polymorphism and mutation databases

BioMutaiITGA5.
DMDMi23831237.

Proteomic databases

EPDiP08648.
MaxQBiP08648.
PaxDbiP08648.
PeptideAtlasiP08648.
PRIDEiP08648.
TopDownProteomicsiP08648.

Protocols and materials databases

DNASUi3678.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293379; ENSP00000293379; ENSG00000161638.
GeneIDi3678.
KEGGihsa:3678.
UCSCiuc001sga.4. human.

Organism-specific databases

CTDi3678.
DisGeNETi3678.
GeneCardsiITGA5.
HGNCiHGNC:6141. ITGA5.
HPAiCAB009008.
HPA002642.
MIMi135620. gene.
neXtProtiNX_P08648.
OpenTargetsiENSG00000161638.
PharmGKBiPA29941.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3637. Eukaryota.
ENOG410XPVZ. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000231603.
HOVERGENiHBG006186.
InParanoidiP08648.
KOiK06484.
OMAiLHYQSKS.
OrthoDBiEOG091G05Z4.
PhylomeDBiP08648.
TreeFamiTF105391.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000161638-MONOMER.
ReactomeiR-HSA-1566948. Elastic fibre formation.
R-HSA-1566977. Fibronectin matrix formation.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-445144. Signal transduction by L1.
SignaLinkiP08648.
SIGNORiP08648.

Miscellaneous databases

ChiTaRSiITGA5. human.
GeneWikiiITGA5.
GenomeRNAii3678.
PROiP08648.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000161638.
CleanExiHS_ITGA5.
ExpressionAtlasiP08648. baseline and differential.
GenevisibleiP08648. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.