P11215 (ITAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin alpha-M

Alternative name(s):
CD11 antigen-like family member B
CR-3 alpha chain
Cell surface glycoprotein MAC-1 subunit alpha
Leukocyte adhesion receptor MO1
Neutrophil adherence receptor
CD_antigen=CD11b

Gene names

Name:	ITGAM
Synonyms:	CD11B, CR3A

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	1152 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-M/beta-2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles. It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin alpha-M/beta-2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain.
Subunit structure	Heterodimer of an alpha and a beta subunit. Alpha-M associates with beta-2. Interacts with JAM3. Ref.10 Ref.11
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Predominantly expressed in monocytes and granulocytes.
Domain	The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.
Involvement in disease	Systemic lupus erythematosus 6 (SLEB6) [MIM:609939]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow. Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.
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	Polymorphism
Disease	Systemic lupus erythematosus
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activated T cell proliferation Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome cell adhesion Traceable author statement Ref.6. Source: ProtInc cellular extravasation 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 microglia development Inferred from electronic annotation. Source: Compara neutrophil chemotaxis Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integrin complex Traceable author statement Ref.6. Source: ProtInc nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	heparin binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.9

Chain

17 – 1152

1136

Integrin alpha-M

PRO_0000016289

Regions

Topological domain

17 – 1104

1088

Extracellular Potential

Transmembrane

1105 – 1128

24

Helical; Potential

Topological domain

1129 – 1152

24

Cytoplasmic Potential

Repeat

18 – 75

58

FG-GAP 1

Repeat

76 – 135

60

FG-GAP 2

Domain

150 – 328

179

VWFA

Repeat

339 – 390

52

FG-GAP 3

Repeat

391 – 444

54

FG-GAP 4

Repeat

445 – 503

59

FG-GAP 5

Repeat

506 – 564

59

FG-GAP 6

Repeat

569 – 629

61

FG-GAP 7

Calcium binding

465 – 473

9

Potential

Calcium binding

529 – 537

9

Potential

Calcium binding

592 – 600

9

Potential

Motif

1131 – 1135

5

GFFKR motif

Amino acid modifications

Glycosylation

86

1

N-linked (GlcNAc...) Potential

Glycosylation

240

1

N-linked (GlcNAc...) Potential

Glycosylation

391

1

N-linked (GlcNAc...) Potential

Glycosylation

469

1

N-linked (GlcNAc...) Potential

Glycosylation

692

1

N-linked (GlcNAc...) Potential

Glycosylation

696

1

N-linked (GlcNAc...) Potential

Glycosylation

734

1

N-linked (GlcNAc...) Potential

Glycosylation

801

1

N-linked (GlcNAc...) Potential

Glycosylation

880

1

N-linked (GlcNAc...) Potential

Glycosylation

900

1

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

Glycosylation

911

1

N-linked (GlcNAc...) Potential

Glycosylation

940

1

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

Glycosylation

946

1

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

Glycosylation

978

1

N-linked (GlcNAc...) Potential

Glycosylation

993

1

N-linked (GlcNAc...) Potential

Glycosylation

1021

1

N-linked (GlcNAc...) Potential

Glycosylation

1044

1

N-linked (GlcNAc...) Potential

Glycosylation

1050

1

N-linked (GlcNAc...) Potential

Glycosylation

1075

1

N-linked (GlcNAc...) Potential

Disulfide bond

66 ↔ 73

By similarity

Disulfide bond

105 ↔ 123

By similarity

Disulfide bond

654 ↔ 711

By similarity

Disulfide bond

770 ↔ 776

By similarity

Disulfide bond

847 ↔ 864

By similarity

Disulfide bond

998 ↔ 1022

By similarity

Disulfide bond

1027 ↔ 1032

By similarity

Natural variations

Natural variant

77

1

R → H Influences susceptibility to SLE. Ref.17
Corresponds to variant rs1143679 [ dbSNP | Ensembl ].

VAR_043870

Natural variant

441

1

M → T. Ref.5
Corresponds to variant rs11861251 [ dbSNP | Ensembl ].

VAR_043871

Natural variant

858

1

A → V.
Corresponds to variant rs1143683 [ dbSNP | Ensembl ].

VAR_043872

Natural variant

1146

1

P → S.
Corresponds to variant rs1143678 [ dbSNP | Ensembl ].

VAR_043873

Experimental info

Sequence conflict

499

1

G → GQ Ref.1

Sequence conflict

499

1

G → GQ Ref.6

Sequence conflict

965

1

L → P Ref.2

Sequence conflict

965

1

L → P Ref.3

Secondary structure

1

.

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.

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1152

Helix Strand Turn

Details...

Beta strand

149 – 156

8

Helix

163 – 180

18

Beta strand

185 – 200

16

Helix

202 – 207

6

Helix

211 – 215

5

Helix

227 – 236

10

Turn

237 – 239

3

Helix

241 – 243

3

Beta strand

249 – 259

11

Helix

268 – 270

3

Helix

272 – 277

6

Beta strand

280 – 288

9

Helix

289 – 291

3

Helix

294 – 303

10

Helix

308 – 311

4

Beta strand

312 – 317

6

Helix

318 – 324

7

Helix

325 – 333

9

Helix

1130 – 1132

3

Helix

1133 – 1143

11

Beta strand

1147 – 1149

3

Sequences

	Sequence		Length	Mass (Da)
	P11215 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: DF77408ED5EE25F9	FASTA	1,152	127,179
	10 20 30 40 50 60 MALRVLLLTA LTLCHGFNLD TENAMTFQEN ARGFGQSVVQ LQGSRVVVGA PQEIVAANQR 70 80 90 100 110 120 GSLYQCDYST GSCEPIRLQV PVEAVNMSLG LSLAATTSPP QLLACGPTVH QTCSENTYVK 130 140 150 160 170 180 GLCFLFGSNL RQQPQKFPEA LRGCPQEDSD IAFLIDGSGS IIPHDFRRMK EFVSTVMEQL 190 200 210 220 230 240 KKSKTLFSLM QYSEEFRIHF TFKEFQNNPN PRSLVKPITQ LLGRTHTATG IRKVVRELFN 250 260 270 280 290 300 ITNGARKNAF KILVVITDGE KFGDPLGYED VIPEADREGV IRYVIGVGDA FRSEKSRQEL 310 320 330 340 350 360 NTIASKPPRD HVFQVNNFEA LKTIQNQLRE KIFAIEGTQT GSSSSFEHEM SQEGFSAAIT 370 380 390 400 410 420 SNGPLLSTVG SYDWAGGVFL YTSKEKSTFI NMTRVDSDMN DAYLGYAAAI ILRNRVQSLV 430 440 450 460 470 480 LGAPRYQHIG LVAMFRQNTG MWESNANVKG TQIGAYFGAS LCSVDVDSNG STDLVLIGAP 490 500 510 520 530 540 HYYEQTRGGQ VSVCPLPRGR ARWQCDAVLY GEQGQPWGRF GAALTVLGDV NGDKLTDVAI 550 560 570 580 590 600 GAPGEEDNRG AVYLFHGTSG SGISPSHSQR IAGSKLSPRL QYFGQSLSGG QDLTMDGLVD 610 620 630 640 650 660 LTVGAQGHVL LLRSQPVLRV KAIMEFNPRE VARNVFECND QVVKGKEAGE VRVCLHVQKS 670 680 690 700 710 720 TRDRLREGQI QSVVTYDLAL DSGRPHSRAV FNETKNSTRR QTQVLGLTQT CETLKLQLPN 730 740 750 760 770 780 CIEDPVSPIV LRLNFSLVGT PLSAFGNLRP VLAEDAQRLF TALFPFEKNC GNDNICQDDL 790 800 810 820 830 840 SITFSFMSLD CLVVGGPREF NVTVTVRNDG EDSYRTQVTF FFPLDLSYRK VSTLQNQRSQ 850 860 870 880 890 900 RSWRLACESA SSTEVSGALK STSCSINHPI FPENSEVTFN ITFDVDSKAS LGNKLLLKAN 910 920 930 940 950 960 VTSENNMPRT NKTEFQLELP VKYAVYMVVT SHGVSTKYLN FTASENTSRV MQHQYQVSNL 970 980 990 1000 1010 1020 GQRSLPISLV FLVPVRLNQT VIWDRPQVTF SENLSSTCHT KERLPSHSDF LAELRKAPVV 1030 1040 1050 1060 1070 1080 NCSIAVCQRI QCDIPFFGIQ EEFNATLKGN LSFDWYIKTS HNHLLIVSTA EILFNDSVFT 1090 1100 1110 1120 1130 1140 LLPGQGAFVR SQTETKVEPF EVPNPLPLIV GSSVGGLLLL ALITAALYKL GFFKRQYKDM 1150 MSEGGPPGAE PQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human leukocyte adhesion glycoprotein Mac-1 (complement receptor type 3, CD11b) alpha subunit. Cloning, primary structure, and relation to the integrins, von Willebrand factor and factor B." Corbi A.L., Kishimoto T.K., Miller L.J., Springer T.A. J. Biol. Chem. 263:12403-12411(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of the alpha subunit of human and guinea pig leukocyte adhesion glycoprotein Mo1: chromosomal localization and homology to the alpha subunits of integrins." Arnaout M.A., Remold-O'Donnell E., Pierce M.W., Harris P., Tenen D.G. Proc. Natl. Acad. Sci. U.S.A. 85:2776-2780(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Amino acid sequence of the alpha subunit of human leukocyte adhesion receptor Mo1 (complement receptor type 3)." Arnaout M.A., Gupta S.K., Pierce M.W., Tenen D.G. J. Cell Biol. 106:2153-2158(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Structural analysis of the CD11b gene and phylogenetic analysis of the alpha-integrin gene family demonstrate remarkable conservation of genomic organization and suggest early diversification during evolution." Fleming J.C., Pahl H.L., Gonzalez D.A., Smith T.F., Tenen D.G. J. Immunol. 150:480-490(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"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], VARIANT THR-441.
[6]	"cDNA sequence for the alpha M subunit of the human neutrophil adherence receptor indicates homology to integrin alpha subunits." Hickstein D.D., Hickey M.J., Ozols J., Baker D.M., Back A.L., Roth G.J. Proc. Natl. Acad. Sci. U.S.A. 86:257-261(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-1152.
[7]	"The promoter of the CD11b gene directs myeloid-specific and developmentally regulated expression." Shelley C.S., Arnaout M.A. Proc. Natl. Acad. Sci. U.S.A. 88:10525-10529(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[8]	"Characterization of the myeloid-specific CD11b promoter." Pahl H.L., Rosmarin A.G., Tenen D.G. Blood 79:865-870(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. Tissue: Blood.
[9]	"N-terminal sequence of human leukocyte glycoprotein Mo1: conservation across species and homology to platelet IIb/IIIa." Pierce M.W., Remold-O'Donnell E., Todd R.F. III, Arnaout M.A. Biochim. Biophys. Acta 874:368-371(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-31.
[10]	"The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1." Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T., Chavakis T. J. Exp. Med. 196:679-691(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JAM3.
[11]	"JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration." Zen K., Babbin B.A., Liu Y., Whelan J.B., Nusrat A., Parkos C.A. Mol. Biol. Cell 15:3926-3937(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JAM3.
[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-900; ASN-940 AND ASN-946, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)." Lee J.O., Rieu P., Arnaout M.A., Liddington R. Cell 80:631-638(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 148-331.
[14]	"Two conformations of the integrin A-domain (I-domain): a pathway for activation?" Lee J.O., Bankston L.A., Arnaout M.A., Liddington R.C. Structure 3:1333-1340(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 148-334.
[15]	"Cation binding to the integrin CD11b I domain and activation model assessment." Baldwin E.T., Sarver R.W., Bryant G.L. Jr., Curry K.A., Fairbanks M.B., Finzel B.C., Garlick R.L., Heinrikson R.L., Horton N.C., Kelley L.L., Mildner A.M., Moon J.B., Mott J.E., Mutchler V.T., Tomich C.S., Watenpaugh K.D., Wiley V.H. Structure 6:923-935(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 148-337.
[16]	"Experimental support for a beta-propeller domain in integrin alpha-subunits and a calcium binding site on its lower surface." Oxvig C., Springer T.A. Proc. Natl. Acad. Sci. U.S.A. 95:4870-4875(1998) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 17-616.
[17]	"A nonsynonymous functional variant in integrin-alpha(M) (encoded by ITGAM) is associated with systemic lupus erythematosus." Nath S.K., Han S., Kim-Howard X., Kelly J.A., Viswanathan P., Gilkeson G.S., Chen W., Zhu C., McEver R.P., Kimberly R.P., Alarcon-Riquelme M.E., Vyse T.J., Li Q.-Z., Wakeland E.K., Merrill J.T., James J.A., Kaufman K.M., Guthridge J.M., Harley J.B. Nat. Genet. 40:152-154(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO SLE, VARIANT HIS-77.
[18]	"Genome-wide association scan in women with systemic lupus erythematosus identifies susceptibility variants in ITGAM, PXK, KIAA1542 and other loci." Harley J.B., Alarcon-Riquelme M.E., Criswell L.A., Jacob C.O., Kimberly R.P., Moser K.L., Tsao B.P., Vyse T.J., Langefeld C.D., Nath S.K., Guthridge J.M., Cobb B.L., Mirel D.B., Marion M.C., Williams A.H., Divers J., Wang W., Frank S.G. , Namjou B., Gabriel S.B., Lee A.T., Gregersen P.K., Behrens T.W., Taylor K.E., Fernando M., Zidovetzki R., Gaffney P.M., Edberg J.C., Rioux J.D., Ojwang J.O., James J.A., Merrill J.T., Gilkeson G.S., Seldin M.F., Yin H., Baechler E.C., Li Q.-Z., Wakeland E.K., Bruner G.R., Kaufman K.M., Kelly J.A. Nat. Genet. 40:204-210(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO SLE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03925 mRNA. Translation: AAA59544.1.
M18044 mRNA. Translation: AAA59491.1.
S52227 , S52152, S52153, S52154, S52155, S52157, S52159, S52161, S52164, S52165, S52167, S52169, S52170, S52173, S52174, S52180, S52181, S52184, S52189, S52191, S52192, S52203, S52212, S52213, S52216, S52219, S52220, S52221, S52222, S52226 Genomic DNA. Translation: AAB24821.1.
BC096346 mRNA. Translation: AAH96346.1.
BC096348 mRNA. Translation: AAH96348.1.
BC099660 mRNA. Translation: AAH99660.1.
J04145 mRNA. Translation: AAA59903.1.
M76724 Genomic DNA. Translation: AAA58410.1.
M84477 Genomic DNA. Translation: AAA51960.1.

IPI

IPI00217987.

PIR

RWHU1B. A31108.

RefSeq

NP_000623.2. NM_000632.3.
NP_001139280.1. NM_001145808.1.

UniGene

Hs.172631.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A8X	model	-	A	17-1152	[»]
1BHO	X-ray	2.70	1/2	149-337	[»]
1BHQ	X-ray	2.70	1/2	149-337	[»]
1IDN	X-ray	2.70	1/2	149-337	[»]
1IDO	X-ray	1.70	A	143-331	[»]
1JLM	X-ray	2.00	A	143-334	[»]
1M1U	X-ray	2.30	A	139-331	[»]
1MF7	X-ray	1.25	A	144-333	[»]
1N9Z	X-ray	2.50	A	145-335	[»]
1NA5	X-ray	1.50	A	144-335	[»]
2LKE	NMR	-	A	1129-1152	[»]
2LKJ	NMR	-	A	1129-1152	[»]
3Q3G	X-ray	2.70	E/G/I/L	148-337	[»]
3QA3	X-ray	3.00	E/G/I/L	148-337	[»]

ProteinModelPortal

P11215.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1489258.

STRING

9606.ENSP00000287497.

PTM databases

PhosphoSite

P11215.

Polymorphism databases

DMDM

1708572.

Proteomic databases

PaxDb

P11215.

PRIDE

P11215.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000287497; ENSP00000287497; ENSG00000169896.
ENST00000544665; ENSP00000441691; ENSG00000169896.

GeneID

3684.

KEGG

hsa:3684.

UCSC

uc002ebq.3. human.

Organism-specific databases

CTD

3684.

GeneCards

GC16P031271.

HGNC

HGNC:6149. ITGAM.

HPA

CAB025091.
HPA002274.

MIM

120980. gene.
609939. phenotype.

neXtProt

NX_P11215.

PharmGKB

PA29949.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG301393.

HOGENOM

HOG000113114.

HOVERGEN

HBG100530.

InParanoid

P11215.

KO

K06461.

OrthoDB

EOG4TQM86.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P11215.

Bgee

P11215.

CleanEx

HS_ITGAM.

Genevestigator

P11215.

GermOnline

ENSG00000169896. 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.
IPR002035. VWF_A.
[Graphical view]

Pfam

PF01839. FG-GAP. 1 hit.
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

PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11215.

ChEMBL

CHEMBL3826.

EvolutionaryTrace

P11215.

GenomeRNAi

3684.

NextBio

14419.

SOURCE

Search...

Entry information

Entry name

ITAM_HUMAN

Accession

Primary (citable) accession number: P11215
Secondary accession number(s): Q4VAK0, Q4VAK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 151 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.