Reviewed, UniProtKB/Swiss-Prot P20701 (ITAL_HUMAN)

Names and origin

Protein names

Recommended name:
    Integrin alpha-L
Alternative name(s):
    Leukocyte adhesion glycoprotein LFA-1 alpha chain
      Short name=LFA-1A
    Leukocyte function-associated molecule 1 alpha chain
    CD11 antigen-like family member A
    CD_antigen=CD11a

Gene names

Name:	ITGAL
Synonyms:	CD11A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1170 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-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 process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane
Ligand	Calcium Magnesium
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Inferred from mutant phenotype. Source: UniProtKB cell motion Traceable author statement. Source: ProtInc heterophilic cell adhesion Inferred from mutant phenotype. Source: UniProtKB inflammatory response Ref.5 Non-traceable author statement. Source: UniProtKB integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW leukocyte adhesion Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integrin complex Ref.1 Ref.5 Non-traceable author statement. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion molecule binding Inferred from physical interaction. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ICAM3	P32942	1	EBI-961214,EBI-725421
Rassf5	Q5EBH1	1	EBI-961214,EBI-960530	From a different organism.

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Chain

26 – 1170

1145

Integrin alpha-L

PRO_0000016292

Regions

Topological domain

26 – 1090

1065

Extracellular Potential

Transmembrane

1091 – 1111

21

Potential

Topological domain

1112 – 1170

59

Cytoplasmic Potential

Repeat

42 – 91

50

FG-GAP 1

Repeat

92 – 149

58

FG-GAP 2

Domain

156 – 327

172

VWFA

Repeat

350 – 400

51

FG-GAP 3

Repeat

401 – 455

55

FG-GAP 4

Repeat

457 – 516

60

FG-GAP 5

Repeat

518 – 575

58

FG-GAP 6

Repeat

578 – 630

53

FG-GAP 7

Calcium binding

468 – 476

9

Potential

Calcium binding

530 – 538

9

Potential

Calcium binding

590 – 598

9

Potential

Motif

1115 – 1119

5

GFFKR motif

Amino acid modifications

Glycosylation

65

1

N-linked (GlcNAc...) Potential

Glycosylation

89

1

N-linked (GlcNAc...) Potential

Glycosylation

188

1

N-linked (GlcNAc...) Ref.7

Glycosylation

649

1

N-linked (GlcNAc...) Potential

Glycosylation

670

1

N-linked (GlcNAc...) Potential

Glycosylation

726

1

N-linked (GlcNAc...) Potential

Glycosylation

730

1

N-linked (GlcNAc...) Potential

Glycosylation

862

1

N-linked (GlcNAc...) Potential

Glycosylation

885

1

N-linked (GlcNAc...) Potential

Glycosylation

897

1

N-linked (GlcNAc...) Potential

Glycosylation

1060

1

N-linked (GlcNAc...) Potential

Glycosylation

1071

1

N-linked (GlcNAc...) Potential

Disulfide bond

73 ↔ 80

By similarity

Disulfide bond

111 ↔ 129

By similarity

Disulfide bond

653 ↔ 707

By similarity

Disulfide bond

771 ↔ 777

By similarity

Disulfide bond

845 ↔ 861

By similarity

Disulfide bond

998 ↔ 1013

By similarity

Disulfide bond

1021 ↔ 1052

By similarity

Natural variations

Alternative sequence

954

1

Q → QGVHGLVEMQTSKQILCRPA GDAEHTVGAQEGELPCPWGV SEAFRDNIRAGPCR in isoform 2.

VSP_002738

Natural variant

144

1

R → H: dbSNP rs34166708. Ref.3

VAR_025235

Natural variant

214

1

R → W: dbSNP rs1064524. Ref.3 Ref.1 Ref.2

VAR_025236

Natural variant

746

1

Q → K: dbSNP rs34838942. Ref.3

VAR_025237

Natural variant

791

1

R → T: dbSNP rs2230433. Ref.3

VAR_025238

Experimental info

Sequence conflict

660

1

I → Y in CAA68747. Ref.1

Secondary structure

1

.

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.

.

.

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.

.

.

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.

1170

Helix Strand Turn

Details...

Beta strand

155 – 162

8

Helix

169 – 185

17

Turn

186 – 188

3

Beta strand

189 – 206

18

Helix

208 – 213

6

Helix

217 – 221

5

Helix

233 – 243

11

Helix

247 – 249

3

Beta strand

255 – 265

11

Helix

274 – 276

3

Beta strand

279 – 287

9

Helix

288 – 290

3

Helix

293 – 297

5

Helix

298 – 302

5

Helix

307 – 310

4

Beta strand

311 – 317

7

Helix

319 – 328

10

Beta strand

331 – 333

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 7, 2006. Version 3. Checksum: 22A7AF92EF286876	FASTA	1,170	128,770
	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
	Isoform 2. Checksum: AF2302FAC076924D	FASTA	1,223	134,427
	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 HMYQGVHGLV 970 980 990 1000 1010 1020 EMQTSKQILC RPAGDAEHTV GAQEGELPCP WGVSEAFRDN IRAGPCRVRI QPSIHDHNIP 1030 1040 1050 1060 1070 1080 TLEAVVGVPQ PPSEGPITHQ WSVQMEPPVP CHYEDLERLP DAAEPCLPGA LFRCPVVFRQ 1090 1100 1110 1120 1130 1140 EILVQVIGTL ELVGEIEASS MFSLCSSLSI SFNSSKHFHL YGSNASLAQV VMKVDVVYEK 1150 1160 1170 1180 1190 1200 QMLYLYVLSG IGGLLLLLLI FIVLYKVGFF KRNLKEKMEA GRGVPNGIPA EDSEQLASGQ 1210 1220 EAGDPGCLKP LHEKDSESGG GKD

References

	« Hide 'large scale' referencesShow '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: 2537322] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT TRP-214.
[2]	"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: 10493829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), VARIANT TRP-214.
[3]	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.
[4]	"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: 8099450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[5]	"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: 8103515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[6]	"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: 8097887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[7]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188, MASS SPECTROMETRY.
[8]	"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: 7479767] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, SEQUENCE REVISION TO 214.
[9]	"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: 8805579] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
[10]	"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: 10493852] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
[11]	"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: 12526797] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00796 mRNA. Translation: CAA68747.1.
AC002310 Genomic DNA. Translation: AAC31672.1.
DQ131904 Genomic DNA. Translation: AAZ38713.1.
M95609 Genomic DNA. Translation: AAA16474.2.
Z22804 Genomic DNA. Translation: CAA80461.1.
M87662 Genomic DNA. No translation available.

IPI

IPI00025380.
IPI00219896.

PIR

S03308.

RefSeq

NP_002200.2.

UniGene

Hs.174103

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CQP	X-ray	2.60	A/B	153-334	[»]
1DGQ	NMR	-	A	152-336	[»]
1IJ4	model	-	L	153-333	[»]
1LFA	X-ray	1.80	A/B	150-336	[»]
1MJN	X-ray	1.30	A	153-331	[»]
1MQ8	X-ray	3.30	B/D	155-331	[»]
1MQ9	X-ray	2.00	A	153-331	[»]
1MQA	X-ray	2.50	A	153-331	[»]
1RD4	X-ray	2.40	A/B/C/D	150-336	[»]
1T0P	X-ray	1.66	A	153-326	[»]
1XDD	X-ray	2.20	A/B	152-336	[»]
1XDG	X-ray	2.10	A/B	152-336	[»]
1XUO	X-ray	1.80	A/B	152-336	[»]
1ZON	X-ray	2.00	A	150-336	[»]
1ZOO	X-ray	3.00	A/B	150-336	[»]
1ZOP	X-ray	2.00	A/B	150-336	[»]
2ICA	X-ray	1.56	A	154-332	[»]
2K8O	NMR	-	A	1113-1170	[»]
2O7N	X-ray	1.75	A	154-332	[»]
3BN3	X-ray	2.10	A	154-332	[»]
3BQM	X-ray	1.95	B/C	153-334	[»]
3BQN	X-ray	1.80	B/C	153-334	[»]
3E2M	X-ray	2.00	A/B	152-334	[»]
3EOA	X-ray	2.80	I/J	153-333	[»]
3EOB	X-ray	3.60	I/J	153-333	[»]
3F74	X-ray	1.70	A/B/C	153-332	[»]
3F78	X-ray	1.60	A/B/C	153-332	[»]
3HI6	X-ray	2.30	A/B	153-332	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P20701. 4 interactions.

STRING

P20701.

PTM databases

PhosphoSite

P20701.

Proteomic databases

PRIDE

P20701.

Genome annotation databases

Ensembl

ENST00000315171; ENSP00000321989; ENSG00000005844; Homo sapiens. [Genome view]
ENST00000356798; ENSP00000349252; ENSG00000005844; Homo sapiens. [Genome view]
ENST00000358164; ENSP00000350886; ENSG00000005844; Homo sapiens. [Genome view]
ENST00000433423; ENSP00000409377; ENSG00000005844; Homo sapiens. [Genome view]
ENST00000454514; ENSP00000408615; ENSG00000005844; Homo sapiens. [Genome view]

GeneID

3683.

UCSC

uc002dyi.2. human.

Organism-specific databases

CTD

3683.

GeneCards

GC16P030391.

HGNC

HGNC:6148. ITGAL.

HPA

CAB025011.

MIM

153370. gene.

PharmGKB

PA29948.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P20701.

HOVERGEN

P20701.

OMA

LSFRKVE.

Enzyme and pathway databases

Pathway_Interaction_DB

a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpress

P20701.

Bgee

P20701.

CleanEx

HS_ITGAL.

Genevestigator

P20701.

GermOnline

ENSG00000005844. Homo sapiens.

Family and domain databases

InterPro

IPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR013513. Integrin_alpha_C.
IPR018184. Integrin_alpha_C_CS.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF01839. FG-GAP. 2 hits.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]

PROSITE

PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00095. Efalizumab.

NextBio

14415.

SOURCE

Search...

Entry information

Entry name

ITAL_HUMAN

Accession

Primary (citable) accession number: P20701
Secondary accession number(s): O43746, Q45H73, Q9UBC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 7, 2006
Last modified:	November 3, 2009
This is version 114 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.