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P20701 (ITAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin alpha-L
Alternative name(s):
CD11 antigen-like family member A
Leukocyte adhesion glycoprotein LFA-1 alpha chain
Short name=LFA-1A
Leukocyte function-associated molecule 1 alpha chain
CD_antigen=CD11a
Gene names
Name:ITGAL
Synonyms:CD11A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1170 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.

Subunit structure

Heterodimer of an alpha and a beta subunit. Alpha-L associates with beta-2.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Leukocytes.

Domain

The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

Sequence similarities

Belongs to the integrin alpha chain family.

Contains 7 FG-GAP repeats.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Magnesium
Metal-binding
   Molecular functionIntegrin
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell

Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL

activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Non-traceable author statement Ref.8. Source: UniProtKB

cellular component movement

Traceable author statement PubMed 10477596. Source: ProtInc

extracellular matrix organization

Traceable author statement. Source: Reactome

heterophilic cell-cell adhesion

Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL

inflammatory response

Non-traceable author statement Ref.8. Source: UniProtKB

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

leukocyte cell-cell adhesion

Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL

leukocyte migration

Traceable author statement. Source: Reactome

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Traceable author statement. Source: Reactome

signal transduction

Non-traceable author statement Ref.8. Source: UniProtKB

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

immunological synapse

Inferred from electronic annotation. Source: Ensembl

integrin complex

Non-traceable author statement Ref.8. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncell adhesion molecule binding

Inferred from physical interaction PubMed 1448173. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 15946252PubMed 18985028. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9WMX22EBI-961214,EBI-6863748From a different organism.
PTPRCP085752EBI-961214,EBI-1341

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P20701-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P20701-2)

The sequence of this isoform differs from the canonical sequence as follows:
     954-954: Q → QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGVSEAFRDNIRAGPCR
Note: No experimental confirmation available.
Isoform 3 (identifier: P20701-3)

The sequence of this isoform differs from the canonical sequence as follows:
     110-192: Missing.
     746-746: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 11701145Integrin alpha-L
PRO_0000016292

Regions

Topological domain26 – 10901065Extracellular Potential
Transmembrane1091 – 111121Helical; Potential
Topological domain1112 – 117059Cytoplasmic Potential
Repeat31 – 8252FG-GAP 1
Repeat83 – 14159FG-GAP 2
Domain156 – 327172VWFA
Repeat338 – 38952FG-GAP 3
Repeat390 – 44556FG-GAP 4
Repeat446 – 50661FG-GAP 5
Repeat507 – 56357FG-GAP 6
Repeat567 – 62761FG-GAP 7
Calcium binding468 – 4769 Potential
Calcium binding530 – 5389 Potential
Calcium binding590 – 5989 Potential
Motif1115 – 11195GFFKR motif

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Ref.10
Glycosylation6491N-linked (GlcNAc...) Potential
Glycosylation6701N-linked (GlcNAc...) Potential
Glycosylation7261N-linked (GlcNAc...) Potential
Glycosylation7301N-linked (GlcNAc...) Potential
Glycosylation8621N-linked (GlcNAc...) Potential
Glycosylation8851N-linked (GlcNAc...) Potential
Glycosylation8971N-linked (GlcNAc...) Potential
Glycosylation10601N-linked (GlcNAc...) Potential
Glycosylation10711N-linked (GlcNAc...) Potential
Disulfide bond73 ↔ 80 By similarity
Disulfide bond111 ↔ 129 By similarity
Disulfide bond653 ↔ 707 By similarity
Disulfide bond771 ↔ 777 By similarity
Disulfide bond845 ↔ 861 By similarity
Disulfide bond998 ↔ 1013 By similarity
Disulfide bond1021 ↔ 1052 By similarity

Natural variations

Alternative sequence110 – 19283Missing in isoform 3.
VSP_042842
Alternative sequence7461Missing in isoform 3.
VSP_042843
Alternative sequence9541Q → QGVHGLVEMQTSKQILCRPA GDAEHTVGAQEGELPCPWGV SEAFRDNIRAGPCR in isoform 2.
VSP_002738
Natural variant1441R → H. Ref.2
Corresponds to variant rs34166708 [ dbSNP | Ensembl ].
VAR_025235
Natural variant2141R → W. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1064524 [ dbSNP | Ensembl ].
VAR_025236
Natural variant7461Q → K. Ref.2
Corresponds to variant rs34838942 [ dbSNP | Ensembl ].
VAR_025237
Natural variant7911R → T. Ref.2
Corresponds to variant rs2230433 [ dbSNP | Ensembl ].
VAR_025238

Experimental info

Sequence conflict6601I → Y in CAA68747. Ref.1

Secondary structure

............................................. 1170
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 7, 2006. Version 3.
Checksum: 22A7AF92EF286876

FASTA1,170128,770
        10         20         30         40         50         60 
MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA 

        70         80         90        100        110        120 
PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILA CDPGLSRTCD 

       130        140        150        160        170        180 
QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC IKGNVDLVFL FDGSMSLQPD EFQKILDFMK 

       190        200        210        220        230        240 
DVMKKLSNTS YQFAAVQFST SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV 

       250        260        270        280        290        300 
ATEVFREELG ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH 

       310        320        330        340        350        360 
KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS SSGISADLSR 

       370        380        390        400        410        420 
GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR AGYLGYTVTW LPSRQKTSLL 

       430        440        450        460        470        480 
ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT IHGTQIGSYF GGELCGVDVD QDGETELLLI 

       490        500        510        520        530        540 
GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA 

       550        560        570        580        590        600 
VGAPLEEQGA VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA 

       610        620        630        640        650        660 
VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI TICFQIKSLI 

       670        680        690        700        710        720 
PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA VTTSMSCTDF SFHFPVCVQD 

       730        740        750        760        770        780 
LISPINVSLN FSLWEEEGTP RDQRAQGKDI PPILRPSLHS ETWEIPFEKN CGEDKKCEAN 

       790        800        810        820        830        840 
LRVSFSPARS RALRLTAFAS LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ 

       850        860        870        880        890        900 
IPVSCEELPE ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC 

       910        920        930        940        950        960 
NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK HMYQVRIQPS 

       970        980        990       1000       1010       1020 
IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY EDLERLPDAA EPCLPGALFR 

      1030       1040       1050       1060       1070       1080 
CPVVFRQEIL VQVIGTLELV GEIEASSMFS LCSSLSISFN SSKHFHLYGS NASLAQVVMK 

      1090       1100       1110       1120       1130       1140 
VDVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS 

      1150       1160       1170 
EQLASGQEAG DPGCLKPLHE KDSESGGGKD 

« Hide

Isoform 2 [UniParc].

Checksum: AF2302FAC076924D
Show »

FASTA1,223134,427
Isoform 3 [UniParc].

Checksum: F6FF2546E8C632F9
Show »

FASTA1,086119,224

References

« Hide 'large scale' references
[1]"Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily."
Larson R.S., Corbi A.L., Berman L., Springer T.
J. Cell Biol. 108:703-712(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT TRP-214.
[2]NIEHS SNPs program
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-144; TRP-214; LYS-746 AND THR-791.
[3]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), VARIANT TRP-214.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 3).
Tissue: Lymph.
[7]"Identification of cell-specific and developmentally regulated nuclear factors that direct myeloid and lymphoid expression of the CD11a gene."
Shelley C.S., Farokhzad O.C., Arnaout M.A.
Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[8]"Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene promoter."
Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.
J. Biol. Chem. 268:19305-19311(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[9]"Description of the leukocyte function-associated antigen 1 (LFA-1 or CD11a) promoter."
Cornwell R.D., Gollahon K.A., Hickstein D.D.
Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[10]"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-188.
Tissue: Leukemic T-cell.
[11]"Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin."
Qu A., Leahy D.J.
Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, SEQUENCE REVISION TO 214.
[12]"The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin."
Qu A., Leahy D.J.
Structure 4:931-942(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
[13]"Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain."
Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G., Cottens S., Weitz-Schmidt G., Hommel U.
J. Mol. Biol. 292:1-9(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
[14]"Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation."
Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.
Cell 112:99-111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00796 mRNA. Translation: CAA68747.1.
DQ131904 Genomic DNA. Translation: AAZ38713.1.
AC002310 Genomic DNA. Translation: AAC31672.1.
AC116348 Genomic DNA. No translation available.
CH471192 Genomic DNA. Translation: EAW52243.1.
BC008777 mRNA. Translation: AAH08777.1.
M95609 Genomic DNA. Translation: AAA16474.2.
Z22804 Genomic DNA. Translation: CAA80461.1.
M87662 Genomic DNA. No translation available.
CCDSCCDS32433.1. [P20701-1]
CCDS45461.1. [P20701-3]
PIRS03308.
RefSeqNP_001107852.1. NM_001114380.1. [P20701-3]
NP_002200.2. NM_002209.2. [P20701-1]
UniGeneHs.174103.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CQPX-ray2.60A/B153-334[»]
1DGQNMR-A152-336[»]
1IJ4model-L153-333[»]
1LFAX-ray1.80A/B150-336[»]
1MJNX-ray1.30A153-331[»]
1MQ8X-ray3.30B/D155-331[»]
1MQ9X-ray2.00A153-331[»]
1MQAX-ray2.50A153-331[»]
1RD4X-ray2.40A/B/C/D150-336[»]
1T0PX-ray1.66A153-326[»]
1XDDX-ray2.20A/B152-336[»]
1XDGX-ray2.10A/B152-336[»]
1XUOX-ray1.80A/B152-336[»]
1ZONX-ray2.00A150-336[»]
1ZOOX-ray3.00A/B150-336[»]
1ZOPX-ray2.00A/B150-336[»]
2ICAX-ray1.56A154-332[»]
2K8ONMR-A1113-1170[»]
2M3ENMR-A1082-1128[»]
2O7NX-ray1.75A154-332[»]
3BN3X-ray2.10A154-332[»]
3BQMX-ray1.95B/C153-334[»]
3BQNX-ray1.80B/C153-334[»]
3E2MX-ray2.00A/B152-334[»]
3EOAX-ray2.80I/J153-333[»]
3EOBX-ray3.60I/J153-333[»]
3F74X-ray1.70A/B/C153-332[»]
3F78X-ray1.60A/B/C153-332[»]
3HI6X-ray2.30A/B153-332[»]
3M6FX-ray1.85A154-332[»]
3TCXX-ray3.60B/D/F/H/J/L/N/P/R/T/V/X/Z/b154-332[»]
4IXDX-ray1.80A152-336[»]
ProteinModelPortalP20701.
SMRP20701. Positions 26-1072, 1082-1170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109889. 6 interactions.
IntActP20701. 7 interactions.
MINTMINT-1130696.
STRING9606.ENSP00000349252.

Chemistry

BindingDBP20701.
ChEMBLCHEMBL2096661.
DrugBankDB00095. Efalizumab.

PTM databases

PhosphoSiteP20701.

Polymorphism databases

DMDM88911345.

Proteomic databases

MaxQBP20701.
PaxDbP20701.
PRIDEP20701.

Protocols and materials databases

DNASU3683.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356798; ENSP00000349252; ENSG00000005844. [P20701-1]
ENST00000358164; ENSP00000350886; ENSG00000005844. [P20701-3]
GeneID3683.
KEGGhsa:3683.
UCSCuc002dyi.4. human. [P20701-1]
uc002dyj.4. human. [P20701-3]

Organism-specific databases

CTD3683.
GeneCardsGC16P030483.
H-InvDBHIX0012960.
HIX0026987.
HGNCHGNC:6148. ITGAL.
HPACAB025011.
MIM153370. gene.
neXtProtNX_P20701.
PharmGKBPA29948.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296688.
HOGENOMHOG000113114.
HOVERGENHBG006188.
InParanoidP20701.
KOK05718.
OMAGEDKKCE.
OrthoDBEOG74XS5V.
PhylomeDBP20701.
TreeFamTF105391.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP20701.

Gene expression databases

ArrayExpressP20701.
BgeeP20701.
CleanExHS_ITGAL.
GenevestigatorP20701.

Family and domain databases

InterProIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PRINTSPR01185. INTEGRINA.
SMARTSM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
PROSITEPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20701.
GeneWikiCD11a.
GenomeRNAi3683.
NextBio14415.
PROP20701.
SOURCESearch...

Entry information

Entry nameITAL_HUMAN
AccessionPrimary (citable) accession number: P20701
Secondary accession number(s): O43746 expand/collapse secondary AC list , Q45H73, Q96HB1, Q9UBC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 7, 2006
Last modified: July 9, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries