P08648 (ITA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Integrin alpha-5 heavy chain
2. Integrin alpha-5 light chain

Gene names

Name:	ITGA5
Synonyms:	FNRA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1049 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Heterodimer of an alpha and a beta subunit. The alpha subunit is composed of a heavy and a light chain linked by a disulfide bond. Alpha-5 associates with beta-1. Interacts with HPS5 and NISCH. Interacts with RAB21 and COMP. Interacts with HIV-1 Tat. Ref.7 Ref.8 Ref.10 Ref.11 Ref.16
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Proteolytic cleavage by PCSK5 mediates activation of the precursor.
Sequence similarities	Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Integrin Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Traceable author statement PubMed 19267251. Source: BHF-UCL axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell adhesion Traceable author statement PubMed 2454952. Source: ProtInc cell-cell adhesion mediated by integrin Inferred from electronic annotation. Source: Compara cell-substrate junction assembly Inferred from electronic annotation. Source: Compara heterophilic cell-cell adhesion Inferred from electronic annotation. Source: Compara integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW leukocyte cell-cell adhesion Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome memory Inferred from electronic annotation. Source: Compara negative regulation of anoikis Inferred from mutant phenotype PubMed 15006356. Source: UniProtKB positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype PubMed 10022831. Source: BHF-UCL positive regulation of vascular endothelial growth factor receptor signaling pathway Traceable author statement PubMed 19267251. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW wound healing, spreading of epidermal cells Inferred from expression pattern PubMed 14970227. Source: BHF-UCL
Cellular_component	alphav-beta3 integrin-vitronectin complex Traceable author statement PubMed 19267251. Source: BHF-UCL external side of plasma membrane Inferred from electronic annotation. Source: Compara integrin complex Traceable author statement PubMed 2454952. Source: ProtInc ruffle Traceable author statement PubMed 11919189. Source: HGNC synapse Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW platelet-derived growth factor receptor binding Traceable author statement PubMed 19267251. Source: BHF-UCL vascular endothelial growth factor receptor 2 binding Traceable author statement PubMed 19267251. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SHARPIN	Q9H0F6	4	EBI-1382311,EBI-3942966

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 41

41

Ref.6

Chain

42 – 1049

1008

Integrin alpha-5

PRO_0000016249

Chain

42 – 894

853

Integrin alpha-5 heavy chain

PRO_0000016250

Chain

895 – 1049

155

Integrin alpha-5 light chain

PRO_0000016251

Regions

Topological domain

42 – 995

954

Extracellular Potential

Transmembrane

996 – 1021

26

Helical; Potential

Topological domain

1022 – 1049

28

Cytoplasmic Potential

Repeat

43 – 108

66

FG-GAP 1

Repeat

128 – 188

61

FG-GAP 2

Repeat

192 – 245

54

FG-GAP 3

Repeat

259 – 315

57

FG-GAP 4

Repeat

316 – 377

62

FG-GAP 5

Repeat

378 – 437

60

FG-GAP 6

Repeat

441 – 504

64

FG-GAP 7

Calcium binding

280 – 288

9

Ref.16

Calcium binding

334 – 342

9

Ref.16

Calcium binding

401 – 409

9

Ref.16

Calcium binding

465 – 473

9

Ref.16

Region

1021 – 1028

8

Interaction with HPS5

Motif

1024 – 1028

5

GFFKR motif

Sites

Metal binding

280

1

Calcium 1

Metal binding

282

1

Calcium 1

Metal binding

284

1

Calcium 1

Metal binding

286

1

Calcium 1; via carbonyl oxygen

Metal binding

288

1

Calcium 1

Metal binding

334

1

Calcium 2

Metal binding

336

1

Calcium 2

Metal binding

338

1

Calcium 2

Metal binding

340

1

Calcium 2; via carbonyl oxygen

Metal binding

342

1

Calcium 2

Metal binding

401

1

Calcium 3

Metal binding

403

1

Calcium 3

Metal binding

405

1

Calcium 3

Metal binding

407

1

Calcium 3; via carbonyl oxygen

Metal binding

409

1

Calcium 3

Metal binding

465

1

Calcium 4

Metal binding

467

1

Calcium 4

Metal binding

469

1

Calcium 4

Metal binding

471

1

Calcium 4; via carbonyl oxygen

Metal binding

473

1

Calcium 4

Binding site

262

1

Arg of R-G-D substrate

Binding site

269

1

Arg of R-G-D substrate

Amino acid modifications

Glycosylation

84

1

N-linked (GlcNAc...) Ref.16

Glycosylation

182

1

N-linked (GlcNAc...) Ref.16

Glycosylation

297

1

N-linked (GlcNAc...) Ref.12 Ref.13 Ref.16

Glycosylation

307

1

N-linked (GlcNAc...) Ref.12 Ref.13 Ref.16

Glycosylation

316

1

N-linked (GlcNAc...) Ref.16

Glycosylation

524

1

N-linked (GlcNAc...) Potential

Glycosylation

530

1

N-linked (GlcNAc...) Potential

Glycosylation

593

1

N-linked (GlcNAc...) Potential

Glycosylation

609

1

N-linked (GlcNAc...) Ref.16

Glycosylation

675

1

N-linked (GlcNAc...) Ref.12

Glycosylation

712

1

N-linked (GlcNAc...) Potential

Glycosylation

724

1

N-linked (GlcNAc...) Potential

Glycosylation

771

1

N-linked (GlcNAc...) Ref.13

Glycosylation

773

1

N-linked (GlcNAc...) Ref.12 Ref.13

Glycosylation

868

1

N-linked (GlcNAc...) Potential

Disulfide bond

99 ↔ 108

Ref.9 Ref.16

Disulfide bond

156 ↔ 176

Ref.9 Ref.16

Disulfide bond

192 ↔ 205

Ref.9 Ref.16

Disulfide bond

513 ↔ 522

Ref.9 Ref.16

Disulfide bond

528 ↔ 584

Ref.9 Ref.16

Disulfide bond

645 ↔ 651

Ref.9 Ref.16

Disulfide bond

718 ↔ 731

Ref.9 Ref.16

Disulfide bond

869 ↔ 921

Interchain (between heavy and light chains) Ref.9 Ref.16

Disulfide bond

911 ↔ 916

Ref.9 Ref.16

Natural variations

Natural variant

585

1

R → I.
Corresponds to variant rs12318746 [ dbSNP | Ensembl ].

VAR_049631

Experimental info

Sequence conflict

26

1

L → V Ref.1

Sequence conflict

26

1

L → V Ref.3

Sequence conflict

33

1

L → V Ref.1

Sequence conflict

33

1

L → V Ref.3

Secondary structure

1

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1049

Helix Strand Turn

Details...

Beta strand

50 – 53

4

Beta strand

62 – 67

6

Beta strand

69 – 72

4

Beta strand

75 – 80

6

Beta strand

95 – 102

8

Beta strand

109 – 111

3

Beta strand

125 – 129

5

Beta strand

133 – 136

4

Beta strand

144 – 149

6

Beta strand

152 – 157

6

Beta strand

165 – 167

3

Beta strand

175 – 180

6

Turn

181 – 184

4

Beta strand

185 – 189

5

Beta strand

193 – 195

3

Turn

199 – 204

6

Beta strand

209 – 213

5

Beta strand

219 – 223

5

Helix

226 – 229

4

Beta strand

231 – 236

6

Helix

238 – 244

7

Helix

265 – 267

3

Beta strand

274 – 279

6

Beta strand

282 – 286

5

Beta strand

288 – 297

10

Beta strand

300 – 306

7

Beta strand

308 – 310

3

Beta strand

313 – 318

6

Beta strand

328 – 333

6

Beta strand

336 – 340

5

Beta strand

342 – 347

6

Beta strand

351 – 353

3

Beta strand

359 – 361

3

Beta strand

364 – 368

5

Beta strand

380 – 384

5

Helix

392 – 394

3

Beta strand

395 – 407

13

Beta strand

409 – 414

6

Beta strand

424 – 428

5

Beta strand

440 – 443

4

Beta strand

458 – 464

7

Beta strand

467 – 470

4

Beta strand

474 – 478

5

Helix

479 – 481

3

Beta strand

483 – 487

5

Beta strand

492 – 503

12

Beta strand

513 – 520

8

Beta strand

522 – 532

11

Beta strand

534 – 536

3

Beta strand

538 – 548

11

Turn

549 – 555

7

Beta strand

560 – 562

3

Turn

563 – 565

3

Beta strand

566 – 577

12

Beta strand

583 – 591

9

Beta strand

604 – 612

9

Beta strand

614 – 616

3

Beta strand

620 – 622

3

Beta strand

634 – 641

8

Sequences

	Sequence		Length	Mass (Da)
	P08648 [UniParc]. Last modified October 10, 2002. Version 2. Checksum: 6B4D558D4F739CBA	FASTA	1,049	114,536
	10 20 30 40 50 60 MGSRTPESPL HAVQLRWGPR RRPPLLPLLL LLLPPPPRVG GFNLDAEAPA VLSGPPGSFF 70 80 90 100 110 120 GFSVEFYRPG TDGVSVLVGA PKANTSQPGV LQGGAVYLCP WGASPTQCTP IEFDSKGSRL 130 140 150 160 170 180 LESSLSSSEG EEPVEYKSLQ WFGATVRAHG SSILACAPLY SWRTEKEPLS DPVGTCYLST 190 200 210 220 230 240 DNFTRILEYA PCRSDFSWAA GQGYCQGGFS AEFTKTGRVV LGGPGSYFWQ GQILSATQEQ 250 260 270 280 290 300 IAESYYPEYL INLVQGQLQT RQASSIYDDS YLGYSVAVGE FSGDDTEDFV AGVPKGNLTY 310 320 330 340 350 360 GYVTILNGSD IRSLYNFSGE QMASYFGYAV AATDVNGDGL DDLLVGAPLL MDRTPDGRPQ 370 380 390 400 410 420 EVGRVYVYLQ HPAGIEPTPT LTLTGHDEFG RFGSSLTPLG DLDQDGYNDV AIGAPFGGET 430 440 450 460 470 480 QQGVVFVFPG GPGGLGSKPS QVLQPLWAAS HTPDFFGSAL RGGRDLDGNG YPDLIVGSFG 490 500 510 520 530 540 VDKAVVYRGR PIVSASASLT IFPAMFNPEE RSCSLEGNPV ACINLSFCLN ASGKHVADSI 550 560 570 580 590 600 GFTVELQLDW QKQKGGVRRA LFLASRQATL TQTLLIQNGA REDCREMKIY LRNESEFRDK 610 620 630 640 650 660 LSPIHIALNF SLDPQAPVDS HGLRPALHYQ SKSRIEDKAQ ILLDCGEDNI CVPDLQLEVF 670 680 690 700 710 720 GEQNHVYLGD KNALNLTFHA QNVGEGGAYE AELRVTAPPE AEYSGLVRHP GNFSSLSCDY 730 740 750 760 770 780 FAVNQSRLLV CDLGNPMKAG ASLWGGLRFT VPHLRDTKKT IQFDFQILSK NLNNSQSDVV 790 800 810 820 830 840 SFRLSVEAQA QVTLNGVSKP EAVLFPVSDW HPRDQPQKEE DLGPAVHHVY ELINQGPSSI 850 860 870 880 890 900 SQGVLELSCP QALEGQQLLY VTRVTGLNCT TNHPINPKGL ELDPEGSLHH QQKREAPSRS 910 920 930 940 950 960 SASSGPQILK CPEAECFRLR CELGPLHQQE SQSLQLHFRV WAKTFLQREH QPFSLQCEAV 970 980 990 1000 1010 1020 YKALKMPYRI LPRQLPQKER QVATAVQWTK AEGSYGVPLW IIILAILFGL LLLGLLIYIL 1030 1040 YKLGFFKRSL PYGTAMEKAQ LKPPATSDA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of the human fibronectin receptor." Argraves W.S., Suzuki S., Arai H., Thompson K., Pierschbacher M.D., Ruoslahti E. J. Cell Biol. 105:1183-1190(1987) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06256 mRNA. Translation: CAA29601.1.
BC008786 mRNA. Translation: AAH08786.1.
M13918 mRNA. Translation: AAA52467.1. Sequence problems.

IPI

IPI00306604.

PIR

A27079.

RefSeq

NP_002196.2. NM_002205.2.

UniGene

Hs.505654.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P08648.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40037N.

IntAct

P08648. 10 interactions.

MINT

MINT-5005934.

STRING

9606.ENSP00000293379.

PTM databases

GlycoSuiteDB

P08648.

PhosphoSite

P08648.

Polymorphism databases

DMDM

23831237.

Proteomic databases

PaxDb

P08648.

PeptideAtlas

P08648.

PRIDE

P08648.

Protocols and materials databases

DNASU

3678.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000293379; ENSP00000293379; ENSG00000161638.

GeneID

3678.

KEGG

hsa:3678.

UCSC

uc001sga.3. human.

Organism-specific databases

CTD

3678.

GeneCards

GC12M054789.

HGNC

HGNC:6141. ITGA5.

HPA

CAB009008.
HPA002642.

MIM

135620. gene.

neXtProt

NX_P08648.

PharmGKB

PA29941.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG26407.

HOGENOM

HOG000231603.

HOVERGEN

HBG006186.

InParanoid

P08648.

KO

K06484.

OMA

ERSCSLE.

OrthoDB

EOG43JC3X.

PhylomeDB

P08648.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P08648.

Bgee

P08648.

CleanEx

HS_ITGA5.

Genevestigator

P08648.

GermOnline

ENSG00000161638. Homo sapiens.

Family and domain databases

InterPro

IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
[Graphical view]

Pfam

PF01839. FG-GAP. 3 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
[Graphical view]

PROSITE

PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08648.

ChEMBL

CHEMBL3955.

GenomeRNAi

3678.

NextBio

14395.

SOURCE

Search...

Entry information

Entry name

ITA5_HUMAN

Accession

Primary (citable) accession number: P08648
Secondary accession number(s): Q96HA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	October 10, 2002
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.