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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.
13-FEB-2019, entry version 238.
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 AND ASN-212.
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, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGAM,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=21193407; DOI=10.1074/jbc.M110.171256;
Jerke U., Rolle S., Dittmar G., Bayat B., Santoso S., Sporbert A.,
Luft F., Kettritz R.;
"Complement receptor Mac-1 is an adaptor for NB1 (CD177)-mediated PR3-
ANCA neutrophil activation.";
J. Biol. Chem. 286:7070-7081(2011).
[23]
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).
[24]
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).
[25]
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).
[26]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH CD177 AND ITGAM,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=28807980; DOI=10.1182/blood-2017-03-768507;
Bai M., Grieshaber-Bouyer R., Wang J., Schmider A.B., Wilson Z.S.,
Zeng L., Halyabar O., Godin M.D., Nguyen H.N., Levescot A., Cunin P.,
Lefort C.T., Soberman R.J., Nigrovic P.A.;
"CD177 modulates human neutrophil migration through activation-
mediated integrin and chemoreceptor regulation.";
Blood 130:2092-2100(2017).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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 ITGAL/ITGB2 is a receptor for ICAM1, ICAM2,
ICAM3 and ICAM4. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are
receptors for the iC3b fragment of the third complement component
and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence
G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes
P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2
is also a receptor for factor X. Integrin ITGAD/ITGB2 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, PubMed:28807980). Triggers neutrophil
transmigration during lung injury through PTK2B/PYK2-mediated
activation (PubMed:18587400). Integrin ITGAL/ITGB2 in association
with ICAM3, contributes to apoptotic neutrophil phagocytosis by
macrophages (PubMed:23775590). In association with alpha subunit
ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF
primed neutrophils (PubMed:21193407).
{ECO:0000269|PubMed:11812992, ECO:0000269|PubMed:15356110,
ECO:0000269|PubMed:18587400, ECO:0000269|PubMed:21193407,
ECO:0000269|PubMed:23775590, ECO:0000269|PubMed:28807980}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit
(PubMed:20033057). ITGB2 associates with either ITGAL, ITGAM,
ITGAX or ITGAD. Found in a complex with CD177 and ITGAM/CD11b
(PubMed:21193407, PubMed:28807980). 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:21193407, ECO:0000269|PubMed:27055590,
ECO:0000269|PubMed:28807980}.
-!- INTERACTION:
P00519:ABL1; NbExp=4; IntAct=EBI-300173, EBI-375543;
P20702:ITGAX; NbExp=3; IntAct=EBI-300173, EBI-2568308;
Q7Z3S9:NOTCH2NLA; 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: Cell membrane {ECO:0000269|PubMed:21193407,
ECO:0000269|PubMed:28807980}; Single-pass type I membrane protein
{ECO:0000305}. Membrane raft {ECO:0000269|PubMed:21193407};
Single-pass type I membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Leukocytes (PubMed:23775590). Expressed in
neutrophils (at protein level) (PubMed:21193407, PubMed:28807980).
{ECO:0000269|PubMed:21193407, ECO:0000269|PubMed:23775590,
ECO:0000269|PubMed:28807980}.
-!- 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/";
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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.
PDB; 5XR1; NMR; -; A=752-763.
PDB; 5ZAZ; NMR; -; A=689-739.
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; -.
PDBsum; 5XR1; -.
PDBsum; 5ZAZ; -.
ProteinModelPortal; P05107; -.
SMR; P05107; -.
BioGrid; 109895; 36.
ComplexPortal; CPX-1825; Integrin alphaL-beta2 complex.
ComplexPortal; CPX-1826; Integrin alphaM-beta2 complex.
ComplexPortal; CPX-1827; Integrin alphaX-beta2 complex.
ComplexPortal; CPX-1828; Integrin alphaD-beta2 complex.
CORUM; P05107; -.
DIP; DIP-478N; -.
ELM; P05107; -.
IntAct; P05107; 27.
MINT; P05107; -.
STRING; 9606.ENSP00000303242; -.
BindingDB; P05107; -.
ChEMBL; CHEMBL3631; -.
DrugBank; DB00641; Simvastatin.
GuidetoPHARMACOLOGY; 2456; -.
GlyConnect; 1415; -.
iPTMnet; P05107; -.
PhosphoSitePlus; P05107; -.
BioMuta; ITGB2; -.
DMDM; 124056465; -.
EPD; P05107; -.
jPOST; P05107; -.
MaxQB; P05107; -.
PaxDb; P05107; -.
PeptideAtlas; P05107; -.
PRIDE; P05107; -.
ProteomicsDB; 51793; -.
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; 473040at2759; -.
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 Interleukin-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; Expressed in 187 organ(s), highest expression level in blood.
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; HDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
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; IBA:GO_Central.
GO; GO:0016020; C:membrane; HDA: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:0005178; F:integrin binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0098609; P:cell-cell adhesion; ISS:BHF-UCL.
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:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
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:0001774; P:microglial cell activation; NAS:ARUK-UCL.
GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
GO; GO:0045963; P:negative regulation of dopamine metabolic process; NAS:ARUK-UCL.
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:1903980; P:positive regulation of microglial cell activation; NAS:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; NAS:ARUK-UCL.
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:2000363; P:positive regulation of prostaglandin-E synthase activity; NAS:ARUK-UCL.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; NAS:ARUK-UCL.
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:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
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; 1.20.5.630; -; 1.
Gene3D; 3.40.50.410; -; 1.
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; Cell membrane; 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 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}.
HELIX 702 734 {ECO:0000244|PDB:5ZAZ}.
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


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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP2328: Allograft rejection
WP1045: TGF-beta Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1367: TGF-beta Receptor Signaling Pathway
WP1897: Regulation of beta-cell development
WP258: TGF-beta Receptor Signaling Pathway
WP32: Translation Factors
WP362: TGF-beta Receptor Signaling Pathway
WP566: canonical wnt - zebrafish
WP809: TGF-beta Receptor Signaling Pathway
WP926: TGF-beta Receptor Signaling Pathway
WP1048: TGF Beta Signaling Pathway
WP105: Fatty Acid Beta Oxidation 2
WP1058: Senescence and Autophagy
WP1061: Fatty Acid Beta Oxidation
WP1069: Integrin-mediated cell adhesion
WP1106: Keap1-Nrf2
WP1107: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP113: TGF Beta Signaling Pathway
WP1164: TGF Beta Signaling Pathway
WP1177: Fatty Acid Beta Oxidation
WP1185: Integrin-mediated cell adhesion

Related Genes :
[ITGB2 CD18 MFI7] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[Itgb2] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGB2 CD18] Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)
[ITGAM CD11B CR3A] Integrin alpha-M (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)
[C3 CPAMD1] Complement C3 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; C3-beta-c (C3bc); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[TIF4631 YGR162W] Eukaryotic initiation factor 4F subunit p150 (eIF-4F p150) (eIF4F p150) (eIF4G1) (mRNA cap-binding protein complex subunit p150)
[C3] Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]
[Inpp5d 7a33 Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship)
[c3] Complement C3 [Cleaved into: Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (Fragment)
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[ITGAL CD11A] Integrin alpha-L (CD11 antigen-like family member A) (Leukocyte adhesion glycoprotein LFA-1 alpha chain) (LFA-1A) (Leukocyte function-associated molecule 1 alpha chain) (CD antigen CD11a)
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[] Non-structural polyprotein p200 (p200) [Cleaved into: Protease/methyltransferase p150 (p150) (EC 3.4.22.-); RNA-directed RNA polymerase p90 (p90) (EC 2.7.7.48) (EC 3.6.1.15) (EC 3.6.4.13)]
[C4B CO4 CPAMD3; C4B_2] Complement C4-B (Basic complement C4) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3) [Cleaved into: Complement C4 beta chain; Complement C4-B alpha chain; C4a anaphylatoxin; C4b-B; C4d-B; Complement C4 gamma chain]
[CR2 C3DR] Complement receptor type 2 (Cr2) (Complement C3d receptor) (Epstein-Barr virus receptor) (EBV receptor) (CD antigen CD21)
[nnrD nnrE CR3_1523] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]

Bibliography :