P05107 (ITB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-2

Alternative name(s):
Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta
Complement receptor C3 subunit beta
CD_antigen=CD18

Gene names

Name:	ITGB2
Synonyms:	CD18, MFI7

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	769 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. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation. Ref.15
Subunit structure	Heterodimer of an alpha and a beta subunit. Beta-2 associates with either alpha-L, alpha-M, alpha-X or alpha-D. Interacts with FGR By similarity. Interacts with COPS5 and RANBP9. Ref.11 Ref.13 Ref.18
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters. Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins. Ref.12
Involvement in disease	Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27
Sequence similarities	Belongs to the integrin beta chain family. Contains 1 VWFA domain.
Sequence caution	The sequence BAD96225.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Disease	Disease mutation
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Metal-binding
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Non-traceable author statement PubMed 12885943. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cell-cell signaling Non-traceable author statement PubMed 12885943. Source: UniProtKB cell-matrix adhesion Inferred from electronic annotation. Source: InterPro inflammatory response Non-traceable author statement PubMed 12885943. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome integrin-mediated signaling pathway Non-traceable author statement PubMed 12885943. Source: UniProtKB leukocyte cell-cell adhesion Inferred from direct assay PubMed 12885943. Source: UniProtKB multicellular organismal development Inferred from electronic annotation. Source: InterPro neutrophil chemotaxis Inferred from direct assay PubMed 12885943. Source: UniProtKB regulation of cell shape Non-traceable author statement PubMed 12885943. Source: UniProtKB regulation of peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 12885943. Source: UniProtKB toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	integrin complex Non-traceable author statement PubMed 12885943. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 769

747

Integrin beta-2

PRO_0000016341

Regions

Topological domain

23 – 700

678

Extracellular Potential

Transmembrane

701 – 723

23

Helical; Potential

Topological domain

724 – 769

46

Cytoplasmic Potential

Domain

124 – 363

240

VWFA

Repeat

449 – 496

48

I

Repeat

497 – 540

44

II

Repeat

541 – 581

41

III

Repeat

582 – 617

36

IV

Region

449 – 617

169

Cysteine-rich tandem repeats

Motif

397 – 399

3

Cell attachment site Potential

Sites

Metal binding

138

1

Calcium; via carbonyl oxygen

Metal binding

141

1

Calcium

Metal binding

142

1

Calcium

Metal binding

347

1

Calcium

Amino acid modifications

Modified residue

23

1

Pyrrolidone carboxylic acid

Modified residue

745

1

Phosphoserine; by PKC Ref.12

Modified residue

756

1

Phosphoserine Ref.12

Modified residue

758

1

Phosphothreonine; by PKC; in vitro Ref.12

Modified residue

759

1

Phosphothreonine Potential

Modified residue

760

1

Phosphothreonine; by PKC/PRKCA; in vitro Ref.12

Glycosylation

50

1

N-linked (GlcNAc...) Ref.16 Ref.17

Glycosylation

116

1

N-linked (GlcNAc...) Ref.17 Ref.18

Glycosylation

212

1

N-linked (GlcNAc...) Ref.14 Ref.16 Ref.17

Glycosylation

213

1

N-linked (GlcNAc...) Ref.17

Glycosylation

215

1

N-linked (GlcNAc...) Ref.17

Glycosylation

254

1

N-linked (GlcNAc...) Potential

Glycosylation

501

1

N-linked (GlcNAc...) Potential

Glycosylation

642

1

N-linked (GlcNAc...) Potential

Disulfide bond

25 ↔ 43

Ref.18

Disulfide bond

33 ↔ 447

Ref.18

Disulfide bond

36 ↔ 62

Ref.18

Disulfide bond

46 ↔ 73

Ref.18

Disulfide bond

191 ↔ 198

Ref.18

Disulfide bond

246 ↔ 286

Ref.18

Disulfide bond

386 ↔ 400

Ref.18

Disulfide bond

420 ↔ 445

Ref.18

Disulfide bond

449 ↔ 467

Ref.18

Disulfide bond

459 ↔ 470

Ref.18

Disulfide bond

472 ↔ 481

Ref.18

Disulfide bond

483 ↔ 514

Ref.18

Disulfide bond

497 ↔ 512

Ref.18

Disulfide bond

506 ↔ 517

Ref.18

Disulfide bond

519 ↔ 534

Ref.18

Disulfide bond

536 ↔ 559

Ref.18

Disulfide bond

541 ↔ 557

Ref.18

Disulfide bond

549 ↔ 562

Ref.18

Disulfide bond

564 ↔ 573

Ref.18

Disulfide bond

575 ↔ 598

Ref.18

Disulfide bond

582 ↔ 596

Ref.18

Disulfide bond

590 ↔ 601

Ref.18

Disulfide bond

603 ↔ 612

Ref.18

Disulfide bond

615 ↔ 618

Ref.18

Disulfide bond

622 ↔ 662

Ref.18

Disulfide bond

628 ↔ 647

Ref.18

Disulfide bond

631 ↔ 643

Ref.18

Disulfide bond

670 ↔ 695

Ref.18

Natural variations

Natural variant

128

1

D → N in LAD1. Ref.21
Corresponds to variant rs137852615 [ dbSNP | Ensembl ].

VAR_003984

Natural variant

128

1

D → Y in LAD1.
Corresponds to variant rs137852615 [ dbSNP | Ensembl ].

VAR_065661

Natural variant

138

1

S → P in LAD1. Ref.25
Corresponds to variant rs137852617 [ dbSNP | Ensembl ].

VAR_013402

Natural variant

149

1

L → P in LAD1. Ref.20
Corresponds to variant rs137852611 [ dbSNP | Ensembl ].

VAR_003985

Natural variant

169

1

G → R in LAD1. Ref.20 Ref.22
Corresponds to variant rs137852612 [ dbSNP | Ensembl ].

VAR_003986

Natural variant

178

1

P → L in LAD1. Ref.9 Ref.23
Corresponds to variant rs137852614 [ dbSNP | Ensembl ].

VAR_003987

Natural variant

196

1

K → T in LAD1. Ref.19
Corresponds to variant rs137852610 [ dbSNP | Ensembl ].

VAR_003988

Natural variant

239

1

A → T in LAD1. Ref.27
Corresponds to variant rs179363873 [ dbSNP | Ensembl ].

VAR_065662

Natural variant

273

1

G → R in LAD1. Ref.25
Corresponds to variant rs137852618 [ dbSNP | Ensembl ].

VAR_013403

Natural variant

284

1

G → S in LAD1. Ref.24
Corresponds to variant rs137852616 [ dbSNP | Ensembl ].

VAR_003989

Natural variant

300

1

D → V in LAD1. Ref.26
Corresponds to variant rs179363874 [ dbSNP | Ensembl ].

VAR_065663

Natural variant

351

1

N → S in LAD1. Ref.10
Corresponds to variant rs137852613 [ dbSNP | Ensembl ].

VAR_003990

Natural variant

354

1

Q → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10
Corresponds to variant rs235330 [ dbSNP | Ensembl ].

VAR_030035

Natural variant

586

1

R → W in LAD1. Ref.10
Corresponds to variant rs5030672 [ dbSNP | Ensembl ].

VAR_003991

Natural variant

593

1

R → C in LAD1. Ref.19
Corresponds to variant rs137852609 [ dbSNP | Ensembl ].

VAR_003992

Natural variant

716

1

G → A in LAD1. Ref.27
Corresponds to variant rs179363872 [ dbSNP | Ensembl ].

VAR_065664

Experimental info

Sequence conflict

199

1

Q → P in CAA68266. Ref.8

Sequence conflict

279

1

L → P in BAD96225. Ref.4

Sequence conflict

526

1

G → C in BAG53190. Ref.3

Sequence conflict

630

1

E → K in BAG53190. Ref.3

Secondary structure

1

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769

Helix Strand Turn

Details...

Helix

33 – 37

5

Beta strand

44 – 46

3

Helix

58 – 61

4

Helix

65 – 70

6

Helix

75 – 77

3

Beta strand

84 – 88

5

Beta strand

91 – 94

4

Beta strand

96 – 99

4

Beta strand

101 – 107

7

Beta strand

113 – 119

7

Beta strand

128 – 134

7

Helix

140 – 144

5

Turn

145 – 148

4

Helix

153 – 158

6

Beta strand

165 – 171

7

Turn

185 – 188

4

Beta strand

205 – 212

8

Helix

215 – 222

8

Beta strand

230 – 233

4

Helix

236 – 243

8

Helix

247 – 250

4

Beta strand

258 – 262

5

Helix

272 – 276

5

Beta strand

289 – 292

4

Helix

296 – 298

3

Helix

304 – 306

3

Helix

307 – 313

7

Beta strand

320 – 322

3

Helix

324 – 326

3

Helix

327 – 336

10

Beta strand

337 – 339

3

Beta strand

342 – 344

3

Helix

353 – 355

3

Turn

356 – 358

3

Helix

359 – 363

5

Beta strand

365 – 371

7

Beta strand

378 – 385

8

Beta strand

387 – 389

3

Beta strand

391 – 402

12

Beta strand

409 – 419

11

Beta strand

424 – 430

7

Beta strand

437 – 443

7

Beta strand

452 – 454

3

Helix

458 – 461

4

Beta strand

462 – 466

5

Beta strand

469 – 472

4

Beta strand

476 – 478

3

Beta strand

483 – 487

5

Helix

490 – 495

6

Beta strand

498 – 500

3

Helix

505 – 508

4

Beta strand

509 – 513

5

Beta strand

516 – 519

4

Beta strand

528 – 531

4

Beta strand

536 – 539

4

Beta strand

544 – 550

7

Helix

551 – 554

4

Beta strand

555 – 558

4

Beta strand

561 – 564

4

Turn

570 – 573

4

Beta strand

591 – 593

3

Turn

609 – 612

4

Turn

623 – 625

3

Helix

626 – 629

4

Turn

630 – 633

4

Beta strand

643 – 646

4

Beta strand

662 – 665

4

Beta strand

667 – 669

3

Beta strand

671 – 676

6

Beta strand

686 – 689

4

Beta strand

754 – 762

9

Sequences

	Sequence		Length	Mass (Da)
	P05107 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: EB9F3C3DF338B4E1	FASTA	769	84,782
	10 20 30 40 50 60 MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN FTGPGDPDSI 70 80 90 100 110 120 RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP QKVTLYLRPG QAAAFNVTFR 130 140 150 160 170 180 RAKGYPIDLY YLMDLSYSML DDLRNVKKLG GDLLRALNEI TESGRIGFGS FVDKTVLPFV 190 200 210 220 230 240 NTHPDKLRNP CPNKEKECQP PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM 250 260 270 280 290 300 MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD 310 320 330 340 350 360 YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS NVVQLIKNAY 370 380 390 400 410 420 NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC DGVQINVPIT FQVKVTATEC 430 440 450 460 470 480 IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR DQSRDRSLCH GKGFLECGIC RCDTGYIGKN 490 500 510 520 530 540 CECQTQGRSS QELEGSCRKD NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN 550 560 570 580 590 600 CERYNGQVCG GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV 610 620 630 640 650 660 CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL QLSNNPVKGR 670 680 690 700 710 720 TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN IAAIVGGTVA GIVLIGILLL 730 740 750 760 VIWKALIHLS DLREYRRFEK EKLKSQWNND NPLFKSATTT VMNPKFAES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the beta subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family." Kishimoto T.K., O'Connor K., Lee A., Roberts T.M., Springer T.A. Cell 48:681-690(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-354.
[2]	"The gene organisation of the human beta 2 integrin subunit (CD18)." Weitzman J.B., Wells C.E., Wright A.H., Clark P.A., Law S.K.A. FEBS Lett. 294:97-103(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-354.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-354. Tissue: Synovial cell.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-354. Tissue: Adipose tissue.
[5]	"The DNA sequence of human chromosome 21." Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-354.
[7]	"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 HIS-354. Tissue: Muscle.
[8]	"The primary structure of the beta-subunit of the cell surface adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to the fibronectin receptor." Law S.K.A., Gagnon J., Hildreth J.E., Wells C.E., Willis A.C., Wong A.J. EMBO J. 6:915-919(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-769, PARTIAL PROTEIN SEQUENCE, VARIANT HIS-354. Tissue: Spleen.
[9]	"Familial genetic defect in a case of leukocyte adhesion deficiency." Ohashi Y., Yambe T., Tsuchiya S., Kikuchi H., Konno T. Hum. Mutat. 2:458-467(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-199, VARIANT LAD1 LEU-178. Tissue: Lymphoblast.
[10]	"Genetic cause of leukocyte adhesion molecule deficiency. Abnormal splicing and a missense mutation in a conserved region of CD18 impair cell surface expression of beta 2 integrins." Nelson C., Rabb H., Arnaout M.A. J. Biol. Chem. 267:3351-3357(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-355, VARIANTS LAD1 SER-351 AND TRP-586, VARIANT HIS-354.
[11]	"Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity." Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A., Rogge L., Pardi R. Nature 404:617-621(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COPS5.
[12]	"Phosphorylation of the cytoplasmic domain of the integrin CD18 chain by protein kinase C isoforms in leukocytes." Fagerholm S., Morrice N., Gahmberg C.G., Cohen P. J. Biol. Chem. 277:1728-1738(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.
[13]	"RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1." Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E. J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RANBP9.
[14]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins." Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B. Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION DURING LUNG INJURY.
[16]	"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-50 AND ASN-212, MASS SPECTROMETRY. Tissue: Liver.
[17]	"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-50; ASN-116; ASN-212; ASN-213 AND ASN-215, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Structure of an integrin with an alphaI domain, complement receptor type 4." Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A. EMBO J. 29:666-679(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 23-699 IN COMPLEX WITH ITGAX, GLYCOSYLATION AT ASN-116, DISULFIDE BONDS, CALCIUM-BINDING SITES, SUBUNIT.
[19]	"Point mutations impairing cell surface expression of the common beta subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM) deficiency." Arnaout M.A., Dana N., Gupta S.K., Tenen D.G., Fathallah D.M. J. Clin. Invest. 85:977-981(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LAD1 THR-196 AND CYS-593.
[20]	"Distinct mutations in two patients with leukocyte adhesion deficiency and their functional correlates." Wardlaw A.J., Hibbs M.L., Stacker S.A., Springer T.A. J. Exp. Med. 172:335-345(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LAD1 PRO-149 AND ARG-169.
[21]	"Leukocyte adhesion deficiency: identification of novel mutations in two Japanese patients with a severe form." Matsuura S., Kishi F., Tsukahara M., Nunoi H., Matsuda I., Kobayashi K., Kajii T. Biochem. Biophys. Res. Commun. 184:1460-1467(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LAD1 ASN-128.
[22]	"Molecular basis for a severe case of leukocyte adhesion deficiency." Corbi A., Vara A., Ursa A., Rodriguez M.C.G., Fontan G., Sanchez-Madrid F. Eur. J. Immunol. 22:1877-1881(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LAD1 ARG-169.
[23]	"Identification of two molecular defects in a child with leukocyte adherence deficiency." Back L.L., Kwok W.W., Hickstein D.D. J. Biol. Chem. 267:5482-5487(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LAD1 LEU-178.
[24]	"A point mutation associated with leukocyte adhesion deficiency type 1 of moderate severity." Back L.A., Kerkering M., Baker D., Bauer T.R., Embree L.J., Hickstein D.D. Biochem. Biophys. Res. Commun. 193:912-918(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LAD1 SER-284.
[25]	"A novel leukocyte adhesion deficiency caused by expressed but nonfunctional beta2 integrins Mac-1 and LFA-1." Hogg N., Stewart M.P., Scarth S.L., Newton R., Shaw J.M., Law S.K.A., Klein N. J. Clin. Invest. 103:97-106(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LAD1 PRO-138 AND ARG-273.
[26]	"A novel point mutation in CD18 causing leukocyte adhesion deficiency in a Chinese patient." Li L., Jin Y.Y., Cao R.M., Chen T.X. Chin. Med. J. 123:1278-1282(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LAD1 VAL-300.
[27]	"Characterization of 11 new cases of leukocyte adhesion deficiency type 1 with seven novel mutations in the ITGB2 gene." Parvaneh N., Mamishi S., Rezaei A., Rezaei N., Tamizifar B., Parvaneh L., Sherkat R., Ghalehbaghi B., Kashef S., Chavoshzadeh Z., Isaeian A., Ashrafi F., Aghamohammadi A. J. Clin. Immunol. 30:756-760(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LAD1 TYR-128; THR-239 AND ALA-716.
+	Additional computationally mapped references.

Web resources

ITGB2base

ITGB2 mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15395 mRNA. Translation: AAA59490.1.
X64072 , X64073, X64074, X64075, X64076, X64077, X64078, X64079, X64080, X64081, X64082, X64083, X63924, X63925, X63926 Genomic DNA. Translation: CAA45427.1.
AK095992 mRNA. Translation: BAG53190.1.
AK222505 mRNA. Translation: BAD96225.1. Different initiation.
AL163300 Genomic DNA. Translation: CAB90553.1.
CH471079 Genomic DNA. Translation: EAX09381.1.
CH471079 Genomic DNA. Translation: EAX09382.1.
CH471079 Genomic DNA. Translation: EAX09385.1.
BC005861 mRNA. Translation: AAH05861.1.
Y00057 mRNA. Translation: CAA68266.1.
S81234 mRNA. Translation: AAB21404.1.

IPI

IPI00291792.

PIR

IJHULM. A25967.

RefSeq

NP_000202.2. NM_000211.3.
NP_001120963.1. NM_001127491.1.

UniGene

Hs.375957.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JX3	model	-	A	126-364	[»]
1L3Y	NMR	-	A	535-574	[»]
1YUK	X-ray	1.80	A	23-125	[»]
			B	365-482	[»]
2JF1	X-ray	2.20	T	735-769	[»]
2P26	X-ray	1.75	A	23-535	[»]
2P28	X-ray	2.20	A	23-122	[»]
			B	362-574	[»]
2V7D	X-ray	2.50	P/Q/R/S	755-764	[»]
3K6S	X-ray	3.50	B/D/F/H	23-699	[»]
3K71	X-ray	3.95	B/D/F/H	23-699	[»]
3K72	X-ray	3.70	B/D	23-699	[»]

ProteinModelPortal

P05107.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-478N.

IntAct

P05107. 7 interactions.

MINT

MINT-129139.

STRING

9606.ENSP00000303242.

PTM databases

PhosphoSite

P05107.

Polymorphism databases

DMDM

124056465.

Proteomic databases

PaxDb

P05107.

PRIDE

P05107.

Protocols and materials databases

DNASU

3689.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302347; ENSP00000303242; ENSG00000160255.
ENST00000355153; ENSP00000347279; ENSG00000160255.
ENST00000397850; ENSP00000380948; ENSG00000160255.
ENST00000397852; ENSP00000380950; ENSG00000160255.
ENST00000397857; ENSP00000380955; ENSG00000160255.

GeneID

3689.

KEGG

hsa:3689.

UCSC

uc002zgd.2. human.

Organism-specific databases

CTD

3689.

GeneCards

GC21M046305.

HGNC

HGNC:6155. ITGB2.

HPA

HPA008877.
HPA016894.

MIM

116920. phenotype.
600065. gene.

neXtProt

NX_P05107.

Orphanet

99842. Leukocyte adhesion deficiency type I.

PharmGKB

PA29955.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG287997.

HOGENOM

HOG000252936.

HOVERGEN

HBG006190.

InParanoid

P05107.

KO

K06464.

OMA

RGRCRCN.

OrthoDB

EOG4V6ZG0.

PhylomeDB

P05107.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.

Reactome

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

SignaLink

P05107.

Gene expression databases

ArrayExpress

P05107.

Bgee

P05107.

CleanEx

HS_ITGB2.

Genevestigator

P05107.

GermOnline

ENSG00000160255. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR015812. Integrin_bsu.
IPR015439. Integrin_bsu-2.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR003659. Plexin-like.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]

PANTHER

PTHR10082. PTHR10082. 1 hit.
PTHR10082:SF15. PTHR10082:SF15. 1 hit.

Pfam

PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]

PIRSF

PIRSF002512. Integrin_B. 1 hit.

PRINTS

PR01186. INTEGRINB.

SMART

SM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF69687. Integrin_bsu_tail. 1 hit.
SSF103575. Plexin-like_fold. 1 hit.

PROSITE

PS00022. EGF_1. 2 hits. Uncertain.
PS01186. EGF_2. 3 hits. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05107.

ChEMBL

CHEMBL3631.

ChiTaRS

ITGB2. human.

DrugBank

DB00641. Simvastatin.

EvolutionaryTrace

P05107.

GenomeRNAi

3689.

NextBio

14449.

PMAP-CutDB

P05107.

SOURCE

Search...

Entry information

Entry name

ITB2_HUMAN

Accession

Primary (citable) accession number: P05107
Secondary accession number(s): B3KTS8 , D3DSM1, Q16418, Q53HS5, Q9UD72

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 178 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.