Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)

 ITB2_HUMAN              Reviewed;         769 AA.
P05107; B3KTS8; D3DSM1; Q16418; Q53HS5; Q9UD72;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 224.
RecName: Full=Integrin beta-2;
AltName: Full=Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta;
AltName: Full=Complement receptor C3 subunit beta;
AltName: CD_antigen=CD18;
Flags: Precursor;
Name=ITGB2; Synonyms=CD18, MFI7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-354.
PubMed=3028646; DOI=10.1016/0092-8674(87)90246-7;
Kishimoto T.K., O'Connor K., Lee A., Roberts T.M., Springer T.A.;
"Cloning of the beta subunit of the leukocyte adhesion proteins:
homology to an extracellular matrix receptor defines a novel supergene
family.";
Cell 48:681-690(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-354.
PubMed=1683838; DOI=10.1016/0014-5793(91)81351-8;
Weitzman J.B., Wells C.E., Wright A.H., Clark P.A., Law S.K.A.;
"The gene organisation of the human beta 2 integrin subunit (CD18).";
FEBS Lett. 294:97-103(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
TISSUE=Synovial cell;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
TISSUE=Adipose tissue;
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
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.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-354.
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-354.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-769, PARTIAL PROTEIN SEQUENCE,
PYROGLUTAMATE FORMATION AT GLN-23, AND VARIANT HIS-354.
TISSUE=Spleen;
PubMed=2954816;
Law S.K.A., Gagnon J., Hildreth J.E., Wells C.E., Willis A.C.,
Wong A.J.;
"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.";
EMBO J. 6:915-919(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 124-199, AND VARIANT LAD1 LEU-178.
TISSUE=Lymphoblast;
PubMed=7509236; DOI=10.1002/humu.1380020606;
Ohashi Y., Yambe T., Tsuchiya S., Kikuchi H., Konno T.;
"Familial genetic defect in a case of leukocyte adhesion deficiency.";
Hum. Mutat. 2:458-467(1993).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-355, VARIANTS LAD1 SER-351 AND
TRP-586, AND VARIANT HIS-354.
PubMed=1346613;
Nelson C., Rabb H., Arnaout M.A.;
"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.";
J. Biol. Chem. 267:3351-3357(1992).
[11]
INTERACTION WITH COPS5.
PubMed=10766246; DOI=10.1038/35007098;
Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A.,
Rogge L., Pardi R.;
"Integrin LFA-1 interacts with the transcriptional co-activator JAB1
to modulate AP-1 activity.";
Nature 404:617-621(2000).
[12]
PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.
PubMed=11700305; DOI=10.1074/jbc.M106856200;
Fagerholm S., Morrice N., Gahmberg C.G., Cohen P.;
"Phosphorylation of the cytoplasmic domain of the integrin CD18 chain
by protein kinase C isoforms in leukocytes.";
J. Biol. Chem. 277:1728-1738(2002).
[13]
FUNCTION.
PubMed=11812992; DOI=10.1038/ni755;
Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.;
"JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in
transendothelial migration of leukocytes.";
Nat. Immunol. 3:151-158(2002).
[14]
INTERACTION WITH RANBP9.
PubMed=14722085; DOI=10.1074/jbc.M313515200;
Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
Fabbri M., Pardi R., Bianchi E.;
"RanBPM is a phosphoprotein that associates with the plasma membrane
and interacts with the integrin LFA-1.";
J. Biol. Chem. 279:13027-13034(2004).
[15]
FUNCTION.
PubMed=15356110; DOI=10.4049/jimmunol.173.6.3653;
Barber D.F., Faure M., Long E.O.;
"LFA-1 contributes an early signal for NK cell cytotoxicity.";
J. Immunol. 173:3653-3659(2004).
[16]
PHOSPHORYLATION AT THR-758, AND MUTAGENESIS OF THR-758.
PubMed=16301335; DOI=10.1083/jcb.200504016;
Fagerholm S.C., Hilden T.J., Nurmi S.M., Gahmberg C.G.;
"Specific integrin alpha and beta chain phosphorylations regulate LFA-
1 activation through affinity-dependent and -independent mechanisms.";
J. Cell Biol. 171:705-715(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
FUNCTION DURING LUNG INJURY.
PubMed=18587400; DOI=10.1038/ni.1628;
Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.;
"Nonmuscle myosin light-chain kinase mediates neutrophil
transmigration in sepsis-induced lung inflammation by activating beta2
integrins.";
Nat. Immunol. 9:880-886(2008).
[19]
INTERACTION WITH FLNA.
PubMed=19828450; DOI=10.1074/jbc.M109.060954;
Ithychanda S.S., Hsu D., Li H., Yan L., Liu D.D., Liu D., Das M.,
Plow E.F., Qin J.;
"Identification and characterization of multiple similar ligand-
binding repeats in filamin: implication on filamin-mediated receptor
clustering and cross-talk.";
J. Biol. Chem. 284:35113-35121(2009).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-212.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50; ASN-116; ASN-212;
ASN-213 AND ASN-215.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23775590; DOI=10.1007/s10495-013-0873-z;
Kristof E., Zahuczky G., Katona K., Doro Z., Nagy E., Fesues L.;
"Novel role of ICAM3 and LFA-1 in the clearance of apoptotic
neutrophils by human macrophages.";
Apoptosis 18:1235-1251(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
INTERACTION WITH THBD.
PubMed=27055590; DOI=10.1016/j.bbrc.2016.04.007;
Kawamoto E., Okamoto T., Takagi Y., Honda G., Suzuki K., Imai H.,
Shimaoka M.;
"LFA-1 and Mac-1 integrins bind to the serine/threonine-rich domain of
thrombomodulin.";
Biochem. Biophys. Res. Commun. 473:1005-1012(2016).
[25]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 23-699 IN COMPLEX WITH ITGAX,
GLYCOSYLATION AT ASN-116, DISULFIDE BONDS, CALCIUM-BINDING SITES, AND
SUBUNIT.
PubMed=20033057; DOI=10.1038/emboj.2009.367;
Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.;
"Structure of an integrin with an alphaI domain, complement receptor
type 4.";
EMBO J. 29:666-679(2010).
[26]
VARIANTS LAD1 THR-196 AND CYS-593.
PubMed=1968911; DOI=10.1172/JCI114529;
Arnaout M.A., Dana N., Gupta S.K., Tenen D.G., Fathallah D.M.;
"Point mutations impairing cell surface expression of the common beta
subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM)
deficiency.";
J. Clin. Invest. 85:977-981(1990).
[27]
VARIANTS LAD1 PRO-149 AND ARG-169.
PubMed=1694220; DOI=10.1084/jem.172.1.335;
Wardlaw A.J., Hibbs M.L., Stacker S.A., Springer T.A.;
"Distinct mutations in two patients with leukocyte adhesion deficiency
and their functional correlates.";
J. Exp. Med. 172:335-345(1990).
[28]
VARIANT LAD1 ASN-128.
PubMed=1590804; DOI=10.1016/S0006-291X(05)80047-6;
Matsuura S., Kishi F., Tsukahara M., Nunoi H., Matsuda I.,
Kobayashi K., Kajii T.;
"Leukocyte adhesion deficiency: identification of novel mutations in
two Japanese patients with a severe form.";
Biochem. Biophys. Res. Commun. 184:1460-1467(1992).
[29]
VARIANT LAD1 ARG-169.
PubMed=1352501; DOI=10.1002/eji.1830220730;
Corbi A., Vara A., Ursa A., Rodriguez M.C.G., Fontan G.,
Sanchez-Madrid F.;
"Molecular basis for a severe case of leukocyte adhesion deficiency.";
Eur. J. Immunol. 22:1877-1881(1992).
[30]
VARIANT LAD1 LEU-178.
PubMed=1347532;
Back L.L., Kwok W.W., Hickstein D.D.;
"Identification of two molecular defects in a child with leukocyte
adherence deficiency.";
J. Biol. Chem. 267:5482-5487(1992).
[31]
VARIANT LAD1 SER-284.
PubMed=7686755; DOI=10.1006/bbrc.1993.1712;
Back L.A., Kerkering M., Baker D., Bauer T.R., Embree L.J.,
Hickstein D.D.;
"A point mutation associated with leukocyte adhesion deficiency type 1
of moderate severity.";
Biochem. Biophys. Res. Commun. 193:912-918(1993).
[32]
VARIANTS LAD1 PRO-138 AND ARG-273.
PubMed=9884339; DOI=10.1172/JCI3312;
Hogg N., Stewart M.P., Scarth S.L., Newton R., Shaw J.M., Law S.K.A.,
Klein N.;
"A novel leukocyte adhesion deficiency caused by expressed but
nonfunctional beta2 integrins Mac-1 and LFA-1.";
J. Clin. Invest. 103:97-106(1999).
[33]
VARIANT LAD1 VAL-300.
PubMed=20529581;
Li L., Jin Y.Y., Cao R.M., Chen T.X.;
"A novel point mutation in CD18 causing leukocyte adhesion deficiency
in a Chinese patient.";
Chin. Med. J. 123:1278-1282(2010).
[34]
VARIANTS LAD1 TYR-128; THR-239 AND ALA-716.
PubMed=20549317; DOI=10.1007/s10875-010-9433-2;
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.;
"Characterization of 11 new cases of leukocyte adhesion deficiency
type 1 with seven novel mutations in the ITGB2 gene.";
J. Clin. Immunol. 30:756-760(2010).
-!- 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. Contributes to natural
killer cell cytotoxicity (PubMed:15356110). Involved in leukocyte
adhesion and transmigration of leukocytes including T-cells and
neutrophils (PubMed:11812992). Triggers neutrophil transmigration
during lung injury through PTK2B/PYK2-mediated activation
(PubMed:18587400). Integrin alpha-L/beta-2 in association with
ICAM3, contributes to apoptotic neutrophil phagocytosis by
macrophages (PubMed:23775590). {ECO:0000269|PubMed:11812992,
ECO:0000269|PubMed:15356110, ECO:0000269|PubMed:18587400,
ECO:0000269|PubMed:23775590}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit
(PubMed:20033057). Beta-2 associates with either alpha-L, alpha-M,
alpha-X or alpha-D. Interacts with FGR (By similarity). Interacts
with COPS5 and RANBP9 (PubMed:10766246, PubMed:14722085).
Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and
23) (PubMed:19828450). Interacts with THBD (PubMed:27055590).
{ECO:0000250|UniProtKB:P11835, ECO:0000269|PubMed:10766246,
ECO:0000269|PubMed:14722085, ECO:0000269|PubMed:19828450,
ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:27055590}.
-!- INTERACTION:
P00519:ABL1; NbExp=4; IntAct=EBI-300173, EBI-375543;
P20702:ITGAX; NbExp=3; IntAct=EBI-300173, EBI-2568308;
Q7Z3S9:NOTCH2NL; NbExp=8; IntAct=EBI-300173, EBI-945833;
P35241:RDX; NbExp=2; IntAct=EBI-300173, EBI-2514878;
Q9Y4G6:TLN2; NbExp=5; IntAct=EBI-300173, EBI-1220811;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Leukocytes. {ECO:0000269|PubMed:23775590}.
-!- PTM: Both Ser-745 and Ser-756 become phosphorylated when T-cells
are exposed to phorbol esters (PubMed:11700305). Phosphorylation
on Thr-758 (but not on Ser-756) allows interaction with 14-3-3
proteins (PubMed:11700305, PubMed:16301335).
{ECO:0000269|PubMed:11700305, ECO:0000269|PubMed:16301335}.
-!- 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.
{ECO:0000269|PubMed:1346613, ECO:0000269|PubMed:1347532,
ECO:0000269|PubMed:1352501, ECO:0000269|PubMed:1590804,
ECO:0000269|PubMed:1694220, ECO:0000269|PubMed:1968911,
ECO:0000269|PubMed:20529581, ECO:0000269|PubMed:20549317,
ECO:0000269|PubMed:7509236, ECO:0000269|PubMed:7686755,
ECO:0000269|PubMed:9884339}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD96225.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=ITGB2base; Note=ITGB2 mutation db;
URL="http://structure.bmc.lu.se/idbase/ITGB2base/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M15395; AAA59490.1; -; mRNA.
EMBL; X64072; CAA45427.1; -; Genomic_DNA.
EMBL; X64073; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64074; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64075; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64076; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64077; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64078; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64079; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64080; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64081; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64082; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X64083; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X63924; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X63925; CAA45427.1; JOINED; Genomic_DNA.
EMBL; X63926; CAA45427.1; JOINED; Genomic_DNA.
EMBL; AK095992; BAG53190.1; -; mRNA.
EMBL; AK222505; BAD96225.1; ALT_INIT; mRNA.
EMBL; AL163300; CAB90553.1; -; Genomic_DNA.
EMBL; CH471079; EAX09381.1; -; Genomic_DNA.
EMBL; CH471079; EAX09382.1; -; Genomic_DNA.
EMBL; CH471079; EAX09385.1; -; Genomic_DNA.
EMBL; BC005861; AAH05861.1; -; mRNA.
EMBL; Y00057; CAA68266.1; -; mRNA.
EMBL; S81234; AAB21404.1; -; mRNA.
CCDS; CCDS13716.1; -.
PIR; A25967; IJHULM.
RefSeq; NP_000202.3; NM_000211.4.
RefSeq; NP_001120963.2; NM_001127491.2.
RefSeq; NP_001290167.1; NM_001303238.1.
UniGene; Hs.375957; -.
PDB; 1JX3; Model; -; A=126-364.
PDB; 1L3Y; NMR; -; A=535-574.
PDB; 1YUK; X-ray; 1.80 A; A=23-125, B=365-482.
PDB; 2JF1; X-ray; 2.20 A; T=735-769.
PDB; 2P26; X-ray; 1.75 A; A=23-535.
PDB; 2P28; X-ray; 2.20 A; A=23-122, B=362-574.
PDB; 2V7D; X-ray; 2.50 A; P/Q/R/S=755-764.
PDB; 3K6S; X-ray; 3.50 A; B/D/F/H=23-699.
PDB; 3K71; X-ray; 3.95 A; B/D/F/H=23-699.
PDB; 3K72; X-ray; 3.70 A; B/D=23-699.
PDB; 4NEH; X-ray; 2.75 A; B=23-695.
PDB; 4NEN; X-ray; 2.90 A; B=23-696.
PDB; 5E6R; X-ray; 2.90 A; B=23-482.
PDB; 5E6S; X-ray; 2.15 A; B/D/F=23-482.
PDB; 5E6U; X-ray; 2.50 A; B=23-482.
PDB; 5E6V; X-ray; 1.80 A; A=24-482.
PDB; 5E6W; X-ray; 2.20 A; A=23-118, A=362-574.
PDB; 5E6X; X-ray; 1.75 A; A=23-535.
PDB; 5ES4; X-ray; 3.30 A; B/D/F/H=23-696.
PDBsum; 1JX3; -.
PDBsum; 1L3Y; -.
PDBsum; 1YUK; -.
PDBsum; 2JF1; -.
PDBsum; 2P26; -.
PDBsum; 2P28; -.
PDBsum; 2V7D; -.
PDBsum; 3K6S; -.
PDBsum; 3K71; -.
PDBsum; 3K72; -.
PDBsum; 4NEH; -.
PDBsum; 4NEN; -.
PDBsum; 5E6R; -.
PDBsum; 5E6S; -.
PDBsum; 5E6U; -.
PDBsum; 5E6V; -.
PDBsum; 5E6W; -.
PDBsum; 5E6X; -.
PDBsum; 5ES4; -.
ProteinModelPortal; P05107; -.
SMR; P05107; -.
BioGrid; 109895; 36.
CORUM; P05107; -.
DIP; DIP-478N; -.
ELM; P05107; -.
IntAct; P05107; 24.
MINT; MINT-129139; -.
STRING; 9606.ENSP00000303242; -.
BindingDB; P05107; -.
ChEMBL; CHEMBL3631; -.
DrugBank; DB00641; Simvastatin.
GuidetoPHARMACOLOGY; 2456; -.
iPTMnet; P05107; -.
PhosphoSitePlus; P05107; -.
BioMuta; ITGB2; -.
DMDM; 124056465; -.
EPD; P05107; -.
MaxQB; P05107; -.
PaxDb; P05107; -.
PeptideAtlas; P05107; -.
PRIDE; P05107; -.
DNASU; 3689; -.
Ensembl; ENST00000302347; ENSP00000303242; ENSG00000160255.
Ensembl; ENST00000355153; ENSP00000347279; ENSG00000160255.
Ensembl; ENST00000397850; ENSP00000380948; ENSG00000160255.
Ensembl; ENST00000397852; ENSP00000380950; ENSG00000160255.
Ensembl; ENST00000397857; ENSP00000380955; ENSG00000160255.
GeneID; 3689; -.
KEGG; hsa:3689; -.
UCSC; uc002zgd.4; human.
CTD; 3689; -.
DisGeNET; 3689; -.
EuPathDB; HostDB:ENSG00000160255.16; -.
GeneCards; ITGB2; -.
HGNC; HGNC:6155; ITGB2.
HPA; HPA008877; -.
HPA; HPA016894; -.
MalaCards; ITGB2; -.
MIM; 116920; phenotype.
MIM; 600065; gene.
neXtProt; NX_P05107; -.
Orphanet; 99842; Leukocyte adhesion deficiency type I.
PharmGKB; PA29955; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
HOGENOM; HOG000252936; -.
HOVERGEN; HBG006190; -.
InParanoid; P05107; -.
KO; K06464; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P05107; -.
TreeFam; TF105392; -.
Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P05107; -.
SIGNOR; P05107; -.
ChiTaRS; ITGB2; human.
EvolutionaryTrace; P05107; -.
GeneWiki; CD18; -.
GenomeRNAi; 3689; -.
PMAP-CutDB; P05107; -.
PRO; PR:P05107; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160255; -.
CleanEx; HS_ITGB2; -.
ExpressionAtlas; P05107; baseline and differential.
Genevisible; P05107; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; NAS:ARUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0034687; C:integrin alphaL-beta2 complex; IDA:UniProtKB.
GO; GO:0034688; C:integrin alphaM-beta2 complex; NAS:ARUK-UCL.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
GO; GO:0001851; F:complement component C3b binding; ISS:ARUK-UCL.
GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
GO; GO:0030369; F:ICAM-3 receptor activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; NAS:ARUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; NAS:ARUK-UCL.
GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0045123; P:cellular extravasation; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:1990266; P:neutrophil migration; IMP:UniProtKB.
GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0043315; P:positive regulation of neutrophil degranulation; IGI:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:UniProtKB.
GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; NAS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR015439; Integrin_bsu-2.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF15; PTHR10082:SF15; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Integrin; Membrane; Metal-binding; Phagocytosis;
Phosphoprotein; Pyrrolidone carboxylic acid; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22
CHAIN 23 769 Integrin beta-2.
/FTId=PRO_0000016341.
TOPO_DOM 23 700 Extracellular. {ECO:0000255}.
TRANSMEM 701 723 Helical. {ECO:0000255}.
TOPO_DOM 724 769 Cytoplasmic. {ECO:0000255}.
DOMAIN 124 363 VWFA.
REPEAT 449 496 I.
REPEAT 497 540 II.
REPEAT 541 581 III.
REPEAT 582 617 IV.
REGION 449 617 Cysteine-rich tandem repeats.
MOTIF 397 399 Cell attachment site. {ECO:0000255}.
METAL 138 138 Calcium; via carbonyl oxygen.
METAL 141 141 Calcium.
METAL 142 142 Calcium.
METAL 347 347 Calcium.
MOD_RES 23 23 Pyrrolidone carboxylic acid.
{ECO:0000305|PubMed:2954816}.
MOD_RES 745 745 Phosphoserine; by PKC.
{ECO:0000269|PubMed:11700305}.
MOD_RES 756 756 Phosphoserine.
{ECO:0000269|PubMed:11700305}.
MOD_RES 758 758 Phosphothreonine; by PKC; in vitro.
{ECO:0000269|PubMed:11700305,
ECO:0000269|PubMed:16301335}.
MOD_RES 759 759 Phosphothreonine. {ECO:0000255}.
MOD_RES 760 760 Phosphothreonine; by PKC/PRKCA; in vitro.
{ECO:0000269|PubMed:11700305}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20033057}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 642 642 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 43 {ECO:0000269|PubMed:20033057}.
DISULFID 33 447 {ECO:0000269|PubMed:20033057}.
DISULFID 36 62 {ECO:0000269|PubMed:20033057}.
DISULFID 46 73 {ECO:0000269|PubMed:20033057}.
DISULFID 191 198 {ECO:0000269|PubMed:20033057}.
DISULFID 246 286 {ECO:0000269|PubMed:20033057}.
DISULFID 386 400 {ECO:0000269|PubMed:20033057}.
DISULFID 420 445 {ECO:0000269|PubMed:20033057}.
DISULFID 449 467 {ECO:0000269|PubMed:20033057}.
DISULFID 459 470 {ECO:0000269|PubMed:20033057}.
DISULFID 472 481 {ECO:0000269|PubMed:20033057}.
DISULFID 483 514 {ECO:0000269|PubMed:20033057}.
DISULFID 497 512 {ECO:0000269|PubMed:20033057}.
DISULFID 506 517 {ECO:0000269|PubMed:20033057}.
DISULFID 519 534 {ECO:0000269|PubMed:20033057}.
DISULFID 536 559 {ECO:0000269|PubMed:20033057}.
DISULFID 541 557 {ECO:0000269|PubMed:20033057}.
DISULFID 549 562 {ECO:0000269|PubMed:20033057}.
DISULFID 564 573 {ECO:0000269|PubMed:20033057}.
DISULFID 575 598 {ECO:0000269|PubMed:20033057}.
DISULFID 582 596 {ECO:0000269|PubMed:20033057}.
DISULFID 590 601 {ECO:0000269|PubMed:20033057}.
DISULFID 603 612 {ECO:0000269|PubMed:20033057}.
DISULFID 615 618 {ECO:0000269|PubMed:20033057}.
DISULFID 622 662 {ECO:0000269|PubMed:20033057}.
DISULFID 628 647 {ECO:0000269|PubMed:20033057}.
DISULFID 631 643 {ECO:0000269|PubMed:20033057}.
DISULFID 670 695 {ECO:0000269|PubMed:20033057}.
VARIANT 128 128 D -> N (in LAD1; dbSNP:rs137852615).
{ECO:0000269|PubMed:1590804}.
/FTId=VAR_003984.
VARIANT 128 128 D -> Y (in LAD1; dbSNP:rs137852615).
{ECO:0000269|PubMed:20549317}.
/FTId=VAR_065661.
VARIANT 138 138 S -> P (in LAD1; dbSNP:rs137852617).
{ECO:0000269|PubMed:9884339}.
/FTId=VAR_013402.
VARIANT 149 149 L -> P (in LAD1; dbSNP:rs137852611).
{ECO:0000269|PubMed:1694220}.
/FTId=VAR_003985.
VARIANT 169 169 G -> R (in LAD1; dbSNP:rs137852612).
{ECO:0000269|PubMed:1352501,
ECO:0000269|PubMed:1694220}.
/FTId=VAR_003986.
VARIANT 178 178 P -> L (in LAD1; dbSNP:rs137852614).
{ECO:0000269|PubMed:1347532,
ECO:0000269|PubMed:7509236}.
/FTId=VAR_003987.
VARIANT 196 196 K -> T (in LAD1; dbSNP:rs137852610).
{ECO:0000269|PubMed:1968911}.
/FTId=VAR_003988.
VARIANT 239 239 A -> T (in LAD1; dbSNP:rs179363873).
{ECO:0000269|PubMed:20549317}.
/FTId=VAR_065662.
VARIANT 273 273 G -> R (in LAD1; dbSNP:rs137852618).
{ECO:0000269|PubMed:9884339}.
/FTId=VAR_013403.
VARIANT 284 284 G -> S (in LAD1; dbSNP:rs137852616).
{ECO:0000269|PubMed:7686755}.
/FTId=VAR_003989.
VARIANT 300 300 D -> V (in LAD1; dbSNP:rs179363874).
{ECO:0000269|PubMed:20529581}.
/FTId=VAR_065663.
VARIANT 351 351 N -> S (in LAD1; dbSNP:rs137852613).
{ECO:0000269|PubMed:1346613}.
/FTId=VAR_003990.
VARIANT 354 354 Q -> H (in dbSNP:rs235330).
{ECO:0000269|PubMed:1346613,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1683838,
ECO:0000269|PubMed:2954816,
ECO:0000269|PubMed:3028646,
ECO:0000269|Ref.4, ECO:0000269|Ref.6}.
/FTId=VAR_030035.
VARIANT 586 586 R -> W (in LAD1; dbSNP:rs5030672).
{ECO:0000269|PubMed:1346613}.
/FTId=VAR_003991.
VARIANT 593 593 R -> C (in LAD1; dbSNP:rs137852609).
{ECO:0000269|PubMed:1968911}.
/FTId=VAR_003992.
VARIANT 716 716 G -> A (in LAD1; dbSNP:rs179363872).
{ECO:0000269|PubMed:20549317}.
/FTId=VAR_065664.
MUTAGEN 758 758 T->A: Abolishes phosphorylation. Reduces
COS cell adhesion to ICAM1.
{ECO:0000269|PubMed:16301335}.
CONFLICT 199 199 Q -> P (in Ref. 8; CAA68266).
{ECO:0000305}.
CONFLICT 279 279 L -> P (in Ref. 4; BAD96225).
{ECO:0000305}.
CONFLICT 526 526 G -> C (in Ref. 3; BAG53190).
{ECO:0000305}.
CONFLICT 630 630 E -> K (in Ref. 3; BAG53190).
{ECO:0000305}.
HELIX 33 37 {ECO:0000244|PDB:2P26}.
STRAND 44 46 {ECO:0000244|PDB:2P26}.
HELIX 49 51 {ECO:0000244|PDB:2P28}.
STRAND 54 56 {ECO:0000244|PDB:5E6R}.
HELIX 58 61 {ECO:0000244|PDB:2P26}.
HELIX 65 70 {ECO:0000244|PDB:2P26}.
HELIX 75 77 {ECO:0000244|PDB:2P26}.
STRAND 84 88 {ECO:0000244|PDB:2P26}.
STRAND 91 94 {ECO:0000244|PDB:2P26}.
STRAND 96 99 {ECO:0000244|PDB:2P26}.
STRAND 101 107 {ECO:0000244|PDB:2P26}.
STRAND 113 119 {ECO:0000244|PDB:2P26}.
STRAND 121 123 {ECO:0000244|PDB:2P26}.
STRAND 127 134 {ECO:0000244|PDB:5E6S}.
HELIX 137 139 {ECO:0000244|PDB:5E6S}.
HELIX 140 146 {ECO:0000244|PDB:5E6S}.
HELIX 150 160 {ECO:0000244|PDB:5E6S}.
STRAND 161 163 {ECO:0000244|PDB:5E6S}.
STRAND 165 171 {ECO:0000244|PDB:5E6S}.
TURN 177 179 {ECO:0000244|PDB:5E6S}.
HELIX 184 188 {ECO:0000244|PDB:5E6S}.
STRAND 196 198 {ECO:0000244|PDB:4NEH}.
STRAND 203 212 {ECO:0000244|PDB:5E6S}.
HELIX 214 222 {ECO:0000244|PDB:5E6S}.
STRAND 230 234 {ECO:0000244|PDB:5E6S}.
HELIX 236 245 {ECO:0000244|PDB:5E6S}.
HELIX 247 250 {ECO:0000244|PDB:5E6S}.
STRAND 254 265 {ECO:0000244|PDB:5E6S}.
HELIX 272 276 {ECO:0000244|PDB:5E6S}.
STRAND 289 292 {ECO:0000244|PDB:4NEH}.
HELIX 294 297 {ECO:0000244|PDB:5E6S}.
HELIX 304 313 {ECO:0000244|PDB:5E6S}.
STRAND 316 322 {ECO:0000244|PDB:5E6S}.
HELIX 324 326 {ECO:0000244|PDB:5E6S}.
HELIX 327 331 {ECO:0000244|PDB:5E6S}.
HELIX 333 336 {ECO:0000244|PDB:5E6S}.
STRAND 337 339 {ECO:0000244|PDB:5E6S}.
STRAND 341 344 {ECO:0000244|PDB:5E6S}.
HELIX 352 364 {ECO:0000244|PDB:5E6S}.
STRAND 365 371 {ECO:0000244|PDB:2P26}.
STRAND 378 385 {ECO:0000244|PDB:2P26}.
STRAND 387 389 {ECO:0000244|PDB:2P26}.
STRAND 391 402 {ECO:0000244|PDB:2P26}.
STRAND 409 419 {ECO:0000244|PDB:2P26}.
STRAND 424 430 {ECO:0000244|PDB:2P26}.
STRAND 437 443 {ECO:0000244|PDB:2P26}.
STRAND 452 454 {ECO:0000244|PDB:3K6S}.
HELIX 458 461 {ECO:0000244|PDB:2P26}.
STRAND 462 466 {ECO:0000244|PDB:2P26}.
STRAND 469 472 {ECO:0000244|PDB:2P26}.
STRAND 476 478 {ECO:0000244|PDB:2P26}.
STRAND 483 487 {ECO:0000244|PDB:4NEH}.
HELIX 490 495 {ECO:0000244|PDB:2P26}.
STRAND 498 500 {ECO:0000244|PDB:2P28}.
HELIX 505 508 {ECO:0000244|PDB:2P26}.
STRAND 509 513 {ECO:0000244|PDB:2P26}.
STRAND 516 519 {ECO:0000244|PDB:2P26}.
STRAND 528 531 {ECO:0000244|PDB:2P26}.
STRAND 536 539 {ECO:0000244|PDB:2P28}.
STRAND 544 550 {ECO:0000244|PDB:1L3Y}.
TURN 552 554 {ECO:0000244|PDB:2P28}.
STRAND 555 558 {ECO:0000244|PDB:2P28}.
STRAND 561 564 {ECO:0000244|PDB:2P28}.
STRAND 568 570 {ECO:0000244|PDB:2P28}.
STRAND 575 577 {ECO:0000244|PDB:4NEH}.
TURN 580 582 {ECO:0000244|PDB:4NEH}.
TURN 590 592 {ECO:0000244|PDB:5ES4}.
STRAND 593 597 {ECO:0000244|PDB:4NEH}.
STRAND 600 603 {ECO:0000244|PDB:4NEH}.
TURN 609 611 {ECO:0000244|PDB:4NEH}.
STRAND 616 618 {ECO:0000244|PDB:4NEN}.
HELIX 622 624 {ECO:0000244|PDB:4NEH}.
HELIX 626 634 {ECO:0000244|PDB:4NEH}.
HELIX 637 639 {ECO:0000244|PDB:4NEH}.
TURN 640 642 {ECO:0000244|PDB:4NEH}.
HELIX 643 646 {ECO:0000244|PDB:4NEH}.
STRAND 650 655 {ECO:0000244|PDB:4NEH}.
STRAND 658 665 {ECO:0000244|PDB:4NEH}.
STRAND 667 669 {ECO:0000244|PDB:5ES4}.
STRAND 671 679 {ECO:0000244|PDB:4NEH}.
TURN 680 683 {ECO:0000244|PDB:4NEH}.
STRAND 684 689 {ECO:0000244|PDB:4NEH}.
STRAND 754 762 {ECO:0000244|PDB:2JF1}.
SEQUENCE 769 AA; 84782 MW; EB9F3C3DF338B4E1 CRC64;
MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN FTGPGDPDSI
RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP QKVTLYLRPG QAAAFNVTFR
RAKGYPIDLY YLMDLSYSML DDLRNVKKLG GDLLRALNEI TESGRIGFGS FVDKTVLPFV
NTHPDKLRNP CPNKEKECQP PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM
MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD
YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS NVVQLIKNAY
NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC DGVQINVPIT FQVKVTATEC
IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR DQSRDRSLCH GKGFLECGIC RCDTGYIGKN
CECQTQGRSS QELEGSCRKD NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN
CERYNGQVCG GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV
CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL QLSNNPVKGR
TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN IAAIVGGTVA GIVLIGILLL
VIWKALIHLS DLREYRRFEK EKLKSQWNND NPLFKSATTT VMNPKFAES


Related products :

Catalog number Product name Quantity
20-783-72240 RAT ANTI HUMAN CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.1 mg
20-783-72241 RAT ANTI HUMAN CD18 RPE - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 100 TESTS
20-783-72237 RAT ANTI HUMAN CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.2 mg
20-783-72550 MOUSE ANTI RAT CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.1 mg
20-783-70512 MOUSE ANTI RAT CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.25 mg
20-783-70453 RAT ANTI MOUSE CD18 RPE - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.5 ml
20-783-72548 MOUSE ANTI RAT CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.2 mg
20-783-72242 RAT ANTI HUMAN CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.02 mg
20-783-70037 RAT ANTI MOUSE CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.25 mg
20-783-72551 MOUSE ANTI RAT CD18 RPE - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 100 TESTS
20-783-72238 RAT ANTI HUMAN CD18 Biotin - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.1 mg
20-783-70946 MOUSE ANTI CANINE CD18 - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 2 ml
20-783-72549 MOUSE ANTI RAT CD18 FITC - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.1 mg
20-783-70452 RAT ANTI MOUSE CD18 FITC - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.1 mg
20-783-72239 RAT ANTI HUMAN CD18 FITC - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 100 TESTS
20-783-72552 MOUSE ANTI RAT CD18 Azide Free - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 1 mg
20-783-70038 RAT ANTI MOUSE CD18 Azide Free - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 1 mg
20-783-72243 RAT ANTI HUMAN CD18 Azide Free - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 1 mg
15-288-21356 Integrin beta-2 - Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Polyclonal 0.05 mg
15-288-21356 Integrin beta-2 - Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Polyclonal 0.1 mg
20-783-71460 MOUSE ANTI HUMAN CD18 (ACTIVATION EPITOPE) RPE - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 100 TESTS
20-783-71457 MOUSE ANTI HUMAN CD18 (ACTIVATION EPITOPE) - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclonal 0.2 mg
20-783-71459 MOUSE ANTI HUMAN CD18 (ACTIVATION EPITOPE) FITC - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclona 0.1 mg
20-783-71458 MOUSE ANTI HUMAN CD18 (ACTIVATION EPITOPE) Biotin - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Monoclo 0.1 mg
20-783-71461 MOUSE ANTI HUMAN CD18 (ACTIVATION EPITOPE) Azide Free - INTEGRIN BETA 2 CHAIN; Cell surface adhesion glycoproteins LFA-1_CR3_p150.95 subunit beta; Complement receptor C3 subunit beta; CD18 antigen Mon 1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur