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Integrin beta-4 (GP150) (CD antigen CD104)

 ITB4_HUMAN              Reviewed;        1822 AA.
P16144; A0AVL6; O14690; O14691; O15339; O15340; O15341; Q0VF97;
Q9UIQ4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 5.
27-SEP-2017, entry version 221.
RecName: Full=Integrin beta-4;
AltName: Full=GP150;
AltName: CD_antigen=CD104;
Flags: Precursor;
Name=ITGB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4A), AND VARIANT PRO-1779.
PubMed=2311577;
Suzuki S., Naitoh Y.;
"Amino acid sequence of a novel integrin beta 4 subunit and primary
expression of the mRNA in epithelial cells.";
EMBO J. 9:757-763(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4B), AND VARIANT PRO-1779.
PubMed=2311578;
Hogervorst F., Kuikman I., von Dem Borne A.E.G.K., Sonnenberg A.;
"Cloning and sequence analysis of beta-4 cDNA: an integrin subunit
that contains a unique 118 kd cytoplasmic domain.";
EMBO J. 9:765-770(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4C).
TISSUE=Pancreas;
PubMed=1976638; DOI=10.1083/jcb.111.4.1593;
Tamura R.N., Rozzo C., Starr L., Chambers J., Reichardt L.F.,
Cooper H.M., Quaranta V.;
"Epithelial integrin alpha 6 beta 4: complete primary structure of
alpha 6 and variant forms of beta 4.";
J. Cell Biol. 111:1593-1604(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-4A; BETA-4B
AND BETA-4C), AND VARIANTS SER-1764 AND PRO-1779.
PubMed=9194858;
Pulkkinen L., Kurtz K.S., Xu Y., Bruckner-Tuderman L., Uitto J.;
"Genomic organization of the integrin beta 4 gene (ITGB4): a
homozygous splice-site mutation in a patient with junctional
epidermolysis bullosa associated with pyloric atresia.";
Lab. Invest. 76:823-833(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BETA-4A; BETA-4B AND
BETA-4C), AND VARIANTS SER-1764 AND PRO-1779.
TISSUE=Lung;
PubMed=9166594; DOI=10.1007/s003359900467;
Iacovacci S., Gagnoux-Palacios L., Zambruno G., Meneguzzi G.,
D'Alessio M.;
"Genomic organization of the human integrin beta 4 gene.";
Mamm. Genome 8:448-450(1997).
[6]
SEQUENCE REVISION.
D'Alessio M.;
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM BETA-4E), AND
VARIANT PRO-1779.
PubMed=9207246; DOI=10.1006/bbrc.1997.6892;
van Leusden M.R., Kuikman I., Sonnenberg A.;
"The unique cytoplasmic domain of the human integrin variant beta4E is
produced by partial retention of intronic sequences.";
Biochem. Biophys. Res. Commun. 235:826-830(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-4A), AND VARIANT
PRO-1779.
TISSUE=Cerebellum;
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).
[11]
PROTEIN SEQUENCE OF 28-46.
PubMed=2542022;
Kajiji S., Tamura R.N., Quaranta V.;
"A novel integrin (alpha E beta 4) from human epithelial cells
suggests a fourth family of integrin adhesion receptors.";
EMBO J. 8:673-680(1989).
[12]
ALTERNATIVE SPLICING (ISOFORM BETA-4D).
PubMed=7982032;
Clarke A.S., Lotz M.M., Mercurio A.M.;
"A novel structural variant of the human beta 4 integrin cDNA.";
Cell Adhes. Commun. 2:1-6(1994).
[13]
INTERACTION WITH DSP.
PubMed=10637308; DOI=10.1091/mbc.11.1.277;
Hopkinson S.B., Jones J.C.;
"The N terminus of the transmembrane protein BP180 interacts with the
N-terminal domain of BP230, thereby mediating keratin cytoskeleton
anchorage to the cell surface at the site of the hemidesmosome.";
Mol. Biol. Cell 11:277-286(2000).
[14]
INTERACTION WITH DST.
PubMed=11375975; DOI=10.1074/jbc.M011005200;
Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F.,
Saurat J.-H., Sonnenberg A., Borradori L.;
"The hemidesmosomal protein bullous pemphigoid antigen 1 and the
integrin beta 4 subunit bind to ERBIN. Molecular cloning of multiple
alternative splice variants of ERBIN and analysis of their tissue
expression.";
J. Biol. Chem. 276:32427-32436(2001).
[15]
FUNCTION, INTERACTION WITH COL17A1 AND DST, CHARACTERIZATION OF
VARIANT TRP-1281, AND SUBCELLULAR LOCATION.
PubMed=12482924; DOI=10.1242/jcs.00241;
Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.;
"Analysis of the interactions between BP180, BP230, plectin and the
integrin alpha6beta4 important for hemidesmosome assembly.";
J. Cell Sci. 116:387-399(2003).
[16]
PALMITOYLATION.
PubMed=15611341; DOI=10.1083/jcb.200404100;
Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.;
"Palmitoylation supports assembly and function of integrin-tetraspanin
complexes.";
J. Cell Biol. 167:1231-1240(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-695.
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1530, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
FUNCTION, INTERACTION WITH RAC1, AND SUBCELLULAR LOCATION.
PubMed=19403692; DOI=10.1091/mbc.E09-01-0051;
Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.;
"BPAG1e maintains keratinocyte polarity through beta4 integrin-
mediated modulation of Rac1 and cofilin activities.";
Mol. Biol. Cell 20:2954-2962(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[22]
FUNCTION, BINDING TO NRG1, IDENTIFICATION IN A COMPLEX WITH NRG1 AND
ERBB3, AND NRG1-BINDING REGION.
PubMed=20682778; DOI=10.1074/jbc.M110.113878;
Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
Wang B., Takada Y.K., Takada Y.;
"Direct binding of the EGF-like domain of neuregulin-1 to integrins
({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
signaling.";
J. Biol. Chem. 285:31388-31398(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PALMITOYLATION BY DHHC3, AND SUBCELLULAR LOCATION.
PubMed=22314500; DOI=10.1007/s00018-012-0924-6;
Sharma C., Rabinovitz I., Hemler M.E.;
"Palmitoylation by DHHC3 is critical for the function, expression, and
stability of integrin alpha6beta4.";
Cell. Mol. Life Sci. 69:2233-2244(2012).
[25]
FUNCTION, BINDING TO IGF1, IDENTIFICATION IN A COMPLEX WITH IGF1 AND
IGF1R, AND IGF1-BINDING REGION.
PubMed=22351760; DOI=10.1074/jbc.M111.304170;
Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y.,
Sekiguchi K., Takada Y.K., Takada Y.;
"Cross-talk between integrin alpha6beta4 and insulin-like growth
factor-1 receptor (IGF1R) through direct alpha6beta4 binding to IGF1
and subsequent alpha6beta4-IGF1-IGF1R ternary complex formation in
anchorage-independent conditions.";
J. Biol. Chem. 287:12491-12500(2012).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1069; SER-1454;
SER-1457; SER-1474; THR-1487 AND THR-1530, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1126-1320.
PubMed=10428948; DOI=10.1093/emboj/18.15.4087;
de Pereda J.M., Wiche G., Liddington R.C.;
"Crystal structure of a tandem pair of fibronectin type III domains
from the cytoplasmic tail of integrin alpha6beta4.";
EMBO J. 18:4087-4095(1999).
[28]
STRUCTURE BY NMR OF 1515-1622.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the fibronectin type III domain of human
integrin beta-4.";
Submitted (APR-2008) to the PDB data bank.
[29]
VARIANTS EB-PA TYR-61; CYS-252; ARG-562 AND TRP-1281.
PubMed=9792864; DOI=10.1086/302116;
Pulkkinen L., Rouan F., Bruckner-Tuderman L., Wallerstein R.,
Garzon M., Brown T., Smith L., Carter W.G., Uitto J.;
"Novel ITGB4 mutations in lethal and nonlethal variants of
epidermolysis bullosa with pyloric atresia: missense versus
nonsense.";
Am. J. Hum. Genet. 63:1376-1387(1998).
[30]
VARIANT EB-PA GLY-245.
PubMed=9422533;
Pulkkinen L., Kim D.U., Uitto J.;
"Epidermolysis bullosa with pyloric atresia: novel mutations in the
beta-4 integrin gene (ITGB4).";
Am. J. Pathol. 152:157-166(1998).
[31]
VARIANT EB-PA PRO-156.
PubMed=9546354;
Pulkkinen L., Bruckner-Tuderman L., August C., Uitto J.;
"Compound heterozygosity for missense (L156P) and nonsense (R554X)
mutations in the beta-4 integrin gene (ITGB4) underlies mild,
nonlethal phenotype of epidermolysis bullosa with pyloric atresia.";
Am. J. Pathol. 152:935-941(1998).
[32]
VARIANT EB-PA ARG-38.
PubMed=9892956; DOI=10.1046/j.1365-2133.1998.02515.x;
Mellerio J.E., Pulkkinen L., McMillan J.R., Lake B.D., Horn H.M.,
Tidman M.J., Harper J.I., McGrath J.A., Uitto J., Eady R.A.J.;
"Pyloric atresia-junctional epidermolysis bullosa syndrome: mutations
in the integrin beta4 gene (ITGB4) in two unrelated patients with mild
disease.";
Br. J. Dermatol. 139:862-871(1998).
[33]
VARIANT EB-PA TRP-1281.
PubMed=10873890; DOI=10.1053/ajkd.2000.8293;
Kambham N., Tanji N., Seigle R.L., Markowitz G.S., Pulkkinen L.,
Uitto J., D'Agati V.D.;
"Congenital focal segmental glomerulosclerosis associated with beta4
integrin mutation and epidermolysis bullosa.";
Am. J. Kidney Dis. 36:190-196(2000).
[34]
VARIANT GABEB ASP-931.
PubMed=10792571; DOI=10.1046/j.1523-1747.2000.00960-3.x;
Inoue M., Tamai K., Shimizu H., Owaribe K., Nakama T., Hashimoto T.,
McGrath J.A.;
"A homozygous missense mutation in the cytoplasmic tail of beta4
integrin, G931D, that disrupts hemidesmosome assembly and underlies
non-Herlitz junctional epidermolysis bullosa without pyloric
atresia?";
J. Invest. Dermatol. 114:1061-1064(2000).
[35]
VARIANTS EB-PA.
PubMed=11251584; DOI=10.1046/j.1365-2133.2001.04038.x;
Ashton G.H.S., Sorelli P., Mellerio J.E., Keane F.M., Eady R.A.J.,
McGrath J.A.;
"Alpha 6 beta 4 integrin abnormalities in junctional epidermolysis
bullosa with pyloric atresia.";
Br. J. Dermatol. 144:408-414(2001).
[36]
VARIANTS HIS-98 AND LEU-844.
PubMed=11289717; DOI=10.1007/s100380170122;
Hirano A., Nagai H., Harada H., Terada Y., Haga S., Kajiwara T.,
Emi M.;
"Nine novel single-nucleotide polymorphisms in the integrin beta4
(ITGB4) gene in the Japanese population.";
J. Hum. Genet. 46:35-37(2001).
[37]
VARIANTS EB-PA TYR-131; CYS-252; ASP-273; CYS-283; ASP-325; PRO-336
AND HIS-1225, AND VARIANT GLN-1216.
PubMed=11328943; DOI=10.1203/00006450-200105000-00003;
Nakano A., Pulkkinen L., Murrell D., Rico J., Lucky A.W., Garzon M.,
Stevens C.A., Robertson S., Pfendner E., Uitto J.;
"Epidermolysis bullosa with congenital pyloric atresia: novel
mutations in the beta 4 integrin gene (ITGB4) and genotype/phenotype
correlations.";
Pediatr. Res. 49:618-626(2001).
-!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. Plays
a critical structural role in the hemidesmosome of epithelial
cells. Is required for the regulation of keratinocyte polarity and
motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this
binding is essential for NRG1-ERBB signaling (PubMed:20682778).
ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1
signaling (PubMed:22351760). {ECO:0000269|PubMed:12482924,
ECO:0000269|PubMed:19403692, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:22351760}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4
associates with alpha-6. Interacts (via cytoplasmic region) with
COL17A1 (via cytoplasmic region). Interacts (via cytoplasmic
region) with DST isoform 3 (via N-terminus). Isoform beta-4a
interacts (via cytoplasmic domain) with DST (via N-terminus).
Interacts with RAC1. ITGA6:ITGB4 is found in a ternary complex
with NRG1 and ERBB3 (PubMed:20682778). ITGA6:ITGB4 is found in a
ternary complex with IGF1 and IGF1R (PubMed:22351760).
{ECO:0000269|PubMed:10637308, ECO:0000269|PubMed:11375975,
ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692,
ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760}.
-!- INTERACTION:
Q96B67:ARRDC3; NbExp=3; IntAct=EBI-948678, EBI-2875665;
Q8R5M8-2:Cadm1 (xeno); NbExp=3; IntAct=EBI-948678, EBI-5651941;
P23229:ITGA6; NbExp=3; IntAct=EBI-948678, EBI-2436548;
Q9BYR5:KRTAP4-2; NbExp=4; IntAct=EBI-11051601, EBI-10172511;
Q15149:PLEC; NbExp=7; IntAct=EBI-948678, EBI-297903;
Q05397:PTK2; NbExp=7; IntAct=EBI-948678, EBI-702142;
O95136:S1PR2; NbExp=2; IntAct=EBI-948678, EBI-10634606;
Q99500:S1PR3; NbExp=3; IntAct=EBI-948678, EBI-10634734;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell membrane; Lipid-anchor. Cell junction,
hemidesmosome. Note=Colocalizes with DST at the leading edge of
migrating keratinocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Beta-4C;
IsoId=P16144-1; Sequence=Displayed;
Name=Beta-4A;
IsoId=P16144-2; Sequence=VSP_002749;
Name=Beta-4B;
IsoId=P16144-3; Sequence=VSP_002749, VSP_002750;
Name=Beta-4D;
IsoId=P16144-4; Sequence=VSP_002749, VSP_002751;
Name=Beta-4E;
IsoId=P16144-5; Sequence=VSP_002747, VSP_002748;
-!- TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly
expressed by epithelia. Isoform beta-4D is also expressed in colon
and placenta. Isoform beta-4E is also expressed in epidermis,
lung, duodenum, heart, spleen and stomach.
-!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and
plectin and probably also recruit BP230.
-!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-
proximal region, enhancing stability and cell surface expression.
Palmitoylation also promotes secundary association with
tertaspanins. {ECO:0000269|PubMed:15611341,
ECO:0000269|PubMed:22314500}.
-!- DISEASE: Epidermolysis bullosa letalis, with pyloric atresia (EB-
PA) [MIM:226730]: An autosomal recessive, frequently lethal,
epidermolysis bullosa with variable involvement of skin, nails,
mucosa, and with variable effects on the digestive system. It is
characterized by mucocutaneous fragility, aplasia cutis congenita,
and gastrointestinal atresia, which most commonly affects the
pylorus. Pyloric atresia is a primary manifestation rather than a
scarring process secondary to epidermolysis bullosa.
{ECO:0000269|PubMed:10873890, ECO:0000269|PubMed:11251584,
ECO:0000269|PubMed:11328943, ECO:0000269|PubMed:9422533,
ECO:0000269|PubMed:9546354, ECO:0000269|PubMed:9792864,
ECO:0000269|PubMed:9892956}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Generalized atrophic benign epidermolysis bullosa (GABEB)
[MIM:226650]: A non-lethal, adult form of junctional epidermolysis
bullosa characterized by life-long blistering of the skin,
associated with hair and tooth abnormalities.
{ECO:0000269|PubMed:10792571}. 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=CAA37656.1; Type=Frameshift; Positions=1413, 1429; Evidence={ECO:0000305};
Sequence=CAA37656.1; Type=Frameshift; Positions=1414, 1429; Evidence={ECO:0000305};
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EMBL; X51841; CAA36134.1; -; mRNA.
EMBL; X52186; CAA36433.1; -; mRNA.
EMBL; X53587; CAA37656.1; ALT_FRAME; mRNA.
EMBL; U66541; AAC51634.1; -; Genomic_DNA.
EMBL; U66530; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66531; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66532; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66533; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66534; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66535; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66536; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66537; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66538; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66539; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66540; AAC51634.1; JOINED; Genomic_DNA.
EMBL; U66541; AAC51633.1; -; Genomic_DNA.
EMBL; U66530; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66531; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66532; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66533; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66534; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66535; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66536; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66537; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66538; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66539; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66540; AAC51633.1; JOINED; Genomic_DNA.
EMBL; U66541; AAC51632.1; -; Genomic_DNA.
EMBL; U66530; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66531; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66532; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66533; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66534; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66535; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66536; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66537; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66538; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66539; AAC51632.1; JOINED; Genomic_DNA.
EMBL; U66540; AAC51632.1; JOINED; Genomic_DNA.
EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89305.1; -; Genomic_DNA.
EMBL; BC118916; AAI18917.1; -; mRNA.
EMBL; BC126411; AAI26412.1; -; mRNA.
EMBL; AJ251004; CAB61345.1; -; Genomic_DNA.
EMBL; Y11107; CAB61345.1; JOINED; Genomic_DNA.
EMBL; AF011375; AAB65421.1; -; mRNA.
EMBL; AF011376; AAB65422.1; -; Genomic_DNA.
CCDS; CCDS11727.1; -. [P16144-1]
CCDS; CCDS32736.1; -. [P16144-3]
CCDS; CCDS58599.1; -. [P16144-2]
PIR; JC5545; JC5545.
PIR; S12380; A36429.
RefSeq; NP_000204.3; NM_000213.4. [P16144-1]
RefSeq; NP_001005619.1; NM_001005619.1. [P16144-3]
RefSeq; NP_001005731.1; NM_001005731.2. [P16144-2]
RefSeq; NP_001308052.1; NM_001321123.1. [P16144-2]
UniGene; Hs.632226; -.
PDB; 1QG3; X-ray; 2.15 A; A/B=1126-1320.
PDB; 2YRZ; NMR; -; A=1518-1622.
PDB; 3F7P; X-ray; 2.75 A; C/D/E=1126-1369.
PDB; 3F7Q; X-ray; 1.75 A; A/B=1126-1355.
PDB; 3F7R; X-ray; 2.04 A; A=1126-1369.
PDB; 3FQ4; X-ray; 1.49 A; A/B=989-1107.
PDB; 3FSO; X-ray; 1.41 A; A/B=989-1107.
PDB; 3H6A; X-ray; 1.61 A; A/B=989-1107.
PDB; 4Q58; X-ray; 4.00 A; C/D=1126-1320.
PDB; 4WTW; X-ray; 1.61 A; A/B=1527-1618.
PDB; 4WTX; X-ray; 1.50 A; A=1642-1736.
PDBsum; 1QG3; -.
PDBsum; 2YRZ; -.
PDBsum; 3F7P; -.
PDBsum; 3F7Q; -.
PDBsum; 3F7R; -.
PDBsum; 3FQ4; -.
PDBsum; 3FSO; -.
PDBsum; 3H6A; -.
PDBsum; 4Q58; -.
PDBsum; 4WTW; -.
PDBsum; 4WTX; -.
ProteinModelPortal; P16144; -.
SMR; P16144; -.
BioGrid; 109897; 34.
CORUM; P16144; -.
DIP; DIP-40182N; -.
ELM; P16144; -.
IntAct; P16144; 71.
MINT; MINT-5004072; -.
STRING; 9606.ENSP00000200181; -.
DrugBank; DB05122; R1295.
iPTMnet; P16144; -.
PhosphoSitePlus; P16144; -.
SwissPalm; P16144; -.
BioMuta; ITGB4; -.
DMDM; 317373584; -.
EPD; P16144; -.
MaxQB; P16144; -.
PaxDb; P16144; -.
PeptideAtlas; P16144; -.
PRIDE; P16144; -.
Ensembl; ENST00000200181; ENSP00000200181; ENSG00000132470. [P16144-1]
Ensembl; ENST00000449880; ENSP00000400217; ENSG00000132470. [P16144-3]
Ensembl; ENST00000450894; ENSP00000405536; ENSG00000132470. [P16144-2]
Ensembl; ENST00000579662; ENSP00000463651; ENSG00000132470. [P16144-2]
GeneID; 3691; -.
KEGG; hsa:3691; -.
UCSC; uc002jpg.3; human. [P16144-1]
CTD; 3691; -.
DisGeNET; 3691; -.
EuPathDB; HostDB:ENSG00000132470.13; -.
GeneCards; ITGB4; -.
GeneReviews; ITGB4; -.
H-InvDB; HIX0039036; -.
HGNC; HGNC:6158; ITGB4.
HPA; CAB002422; -.
HPA; CAB005258; -.
HPA; HPA036348; -.
HPA; HPA036349; -.
MalaCards; ITGB4; -.
MIM; 147557; gene.
MIM; 226650; phenotype.
MIM; 226730; phenotype.
neXtProt; NX_P16144; -.
OpenTargets; ENSG00000132470; -.
Orphanet; 158684; Epidermolysis bullosa simplex with pyloric atresia.
Orphanet; 79402; Generalized junctional epidermolysis bullosa, non-Herlitz type.
Orphanet; 79403; Junctional epidermolysis bullosa - pyloric atresia.
Orphanet; 251393; Localized junctional epidermolysis bullosa, non-Herlitz type.
PharmGKB; PA29957; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOGENOM; HOG000231105; -.
HOVERGEN; HBG006189; -.
InParanoid; P16144; -.
KO; K06525; -.
OMA; EDDDCTY; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P16144; -.
TreeFam; TF105392; -.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
SignaLink; P16144; -.
SIGNOR; P16144; -.
ChiTaRS; ITGB4; human.
EvolutionaryTrace; P16144; -.
GeneWiki; ITGB4; -.
GenomeRNAi; 3691; -.
PRO; PR:P16144; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132470; -.
CleanEx; HS_ITGB4; -.
ExpressionAtlas; P16144; baseline and differential.
Genevisible; P16144; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0097186; P:amelogenesis; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0048870; P:cell motility; IMP:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
GO; GO:0035878; P:nail development; IMP:UniProtKB.
GO; GO:0072001; P:renal system development; IMP:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
GO; GO:0043588; P:skin development; IMP:UniProtKB.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 4.
Gene3D; 3.30.70.960; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR003644; Calx_beta.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR012013; Integrin_bsu-4.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR016201; PSI.
InterPro; IPR000082; SEA_dom.
InterPro; IPR002035; VWF_A.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF51; PTHR10082:SF51; 1.
Pfam; PF03160; Calx-beta; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF00041; fn3; 4.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002513; Integrin_B4; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00237; Calx_beta; 1.
SMART; SM00060; FN3; 4.
SMART; SM00187; INB; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS00243; INTEGRIN_BETA; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Epidermolysis bullosa; Glycoprotein;
Integrin; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000269|PubMed:2542022}.
CHAIN 28 1822 Integrin beta-4.
/FTId=PRO_0000016346.
TOPO_DOM 28 710 Extracellular. {ECO:0000255}.
TRANSMEM 711 733 Helical. {ECO:0000255}.
TOPO_DOM 734 1822 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 73 PSI.
DOMAIN 131 329 VWFA.
REPEAT 456 502 I.
REPEAT 503 542 II.
REPEAT 543 581 III.
REPEAT 582 619 IV.
DOMAIN 979 1084 Calx-beta.
DOMAIN 1129 1218 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1222 1321 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1530 1625 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1643 1739 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 194 199 Involved in NRG1- and IGF1-binding.
{ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:22351760}.
REGION 456 619 Cysteine-rich tandem repeats.
REGION 732 749 Palmitoylated on several cysteines.
MOD_RES 771 771 Phosphoserine.
{ECO:0000250|UniProtKB:Q64632}.
MOD_RES 1069 1069 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1119 1119 Phosphoserine.
{ECO:0000250|UniProtKB:Q64632}.
MOD_RES 1454 1454 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1457 1457 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1474 1474 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1487 1487 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1494 1494 Phosphoserine.
{ECO:0000250|UniProtKB:Q64632}.
MOD_RES 1530 1530 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:23186163}.
MOD_RES 1791 1791 Phosphoserine.
{ECO:0000250|UniProtKB:Q64632}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 579 579 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 617 617 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 695 695 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 30 455 {ECO:0000250}.
DISULFID 38 48 {ECO:0000250}.
DISULFID 41 72 {ECO:0000250}.
DISULFID 51 61 {ECO:0000250}.
DISULFID 245 288 {ECO:0000250}.
DISULFID 424 671 {ECO:0000250}.
DISULFID 452 457 {ECO:0000250}.
DISULFID 468 479 {ECO:0000250}.
DISULFID 476 512 {ECO:0000250}.
DISULFID 481 490 {ECO:0000250}.
DISULFID 492 503 {ECO:0000250}.
DISULFID 518 523 {ECO:0000250}.
DISULFID 520 551 {ECO:0000250}.
DISULFID 525 536 {ECO:0000250}.
DISULFID 557 562 {ECO:0000250}.
DISULFID 564 573 {ECO:0000250}.
DISULFID 575 582 {ECO:0000250}.
DISULFID 596 601 {ECO:0000250}.
DISULFID 598 648 {ECO:0000250}.
DISULFID 603 614 {ECO:0000250}.
DISULFID 626 635 {ECO:0000250}.
DISULFID 632 706 {ECO:0000250}.
DISULFID 651 680 {ECO:0000250}.
VAR_SEQ 851 964 LNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAP
RSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGM
VEFQEGVELVDVRVPLFIRPEDDDEKQLLVEA -> VRTQE
LGLAGDVAERGLQADLRCTQAPADQVPAAAQCREKARPHHC
GHSADGAPLGQAGPAEAYREAGGTEGLPRPQGGPRLLHPHC
RPGRPGHGGVPGGRGAGGRTGAPLYPA (in isoform
Beta-4E). {ECO:0000303|PubMed:9207246}.
/FTId=VSP_002747.
VAR_SEQ 965 1822 Missing (in isoform Beta-4E).
{ECO:0000303|PubMed:9207246}.
/FTId=VSP_002748.
VAR_SEQ 1370 1439 Missing (in isoform Beta-4A, isoform
Beta-4B and isoform Beta-4D).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2311577,
ECO:0000303|PubMed:2311578,
ECO:0000303|PubMed:9194858}.
/FTId=VSP_002749.
VAR_SEQ 1519 1519 H -> HGLPPIWEHGRSRLPLSWALGSRSRAQMKGFPPSRG
PRDSIILAGRPAAPSWGP (in isoform Beta-4B).
{ECO:0000303|PubMed:2311578,
ECO:0000303|PubMed:9194858}.
/FTId=VSP_002750.
VAR_SEQ 1678 1685 CEMAQGGG -> W (in isoform Beta-4D).
{ECO:0000305}.
/FTId=VSP_002751.
VARIANT 38 38 C -> R (in EB-PA; mild form;
dbSNP:rs121912465).
{ECO:0000269|PubMed:9892956}.
/FTId=VAR_010652.
VARIANT 61 61 C -> Y (in EB-PA; lethal form;
dbSNP:rs80338755).
{ECO:0000269|PubMed:9792864}.
/FTId=VAR_004006.
VARIANT 98 98 R -> H (in dbSNP:rs143114124).
{ECO:0000269|PubMed:11289717}.
/FTId=VAR_011292.
VARIANT 131 131 D -> Y (in EB-PA; lethal form).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011293.
VARIANT 156 156 L -> P (in EB-PA; mild form;
dbSNP:rs121912461).
{ECO:0000269|PubMed:9546354}.
/FTId=VAR_004007.
VARIANT 245 245 C -> G (in EB-PA; lethal form).
{ECO:0000269|PubMed:9422533}.
/FTId=VAR_004008.
VARIANT 252 252 R -> C (in EB-PA; mild form;
dbSNP:rs201494421).
{ECO:0000269|PubMed:11328943,
ECO:0000269|PubMed:9792864}.
/FTId=VAR_004009.
VARIANT 273 273 G -> D (in EB-PA; lethal form).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011294.
VARIANT 283 283 R -> C (in EB-PA).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011295.
VARIANT 325 325 V -> D (in EB-PA).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011296.
VARIANT 336 336 L -> P (in EB-PA; mild form).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011297.
VARIANT 478 478 Q -> H (in dbSNP:rs8079267).
/FTId=VAR_027803.
VARIANT 562 562 C -> R (in EB-PA; mild form;
dbSNP:rs121912463).
{ECO:0000269|PubMed:9792864}.
/FTId=VAR_004010.
VARIANT 844 844 R -> L (in dbSNP:rs140819116).
{ECO:0000269|PubMed:11289717}.
/FTId=VAR_011298.
VARIANT 931 931 G -> D (in GABEB; dbSNP:rs121912466).
{ECO:0000269|PubMed:10792571}.
/FTId=VAR_011299.
VARIANT 1216 1216 H -> Q (in dbSNP:rs149284152).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011300.
VARIANT 1225 1225 R -> H (in EB-PA; mild form;
dbSNP:rs121912468).
{ECO:0000269|PubMed:11328943}.
/FTId=VAR_011301.
VARIANT 1281 1281 R -> W (in EB-PA; mild form; abolishes
interaction with PLEC and reduces
interaction with COL17A1;
dbSNP:rs121912467).
{ECO:0000269|PubMed:10873890,
ECO:0000269|PubMed:12482924,
ECO:0000269|PubMed:9792864}.
/FTId=VAR_004011.
VARIANT 1764 1764 T -> S (in dbSNP:rs1051486).
{ECO:0000269|PubMed:9166594,
ECO:0000269|PubMed:9194858}.
/FTId=VAR_055971.
VARIANT 1779 1779 L -> P (in dbSNP:rs871443).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2311577,
ECO:0000269|PubMed:2311578,
ECO:0000269|PubMed:9166594,
ECO:0000269|PubMed:9194858,
ECO:0000269|PubMed:9207246}.
/FTId=VAR_027804.
CONFLICT 27 27 Missing (in Ref. 5; CAB61345).
{ECO:0000305}.
CONFLICT 43 43 R -> Y (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 K -> P (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 621 704 IHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDEL
KRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHK
KK -> STRASARTYAPACSARRGAPARRRGARVRNATSRS
RWWTSLREARRWWCAAPSGTRMTTAPTATPWKVTAPLGPTA
LSWCTRRR (in Ref. 5; CAB61345).
{ECO:0000305}.
CONFLICT 802 804 GFA -> WLC (in Ref. 8; AAB65422).
{ECO:0000305}.
CONFLICT 1414 1429 HGPPDDGGAGGKGGSL -> TAPRTTAARAGRAAAV (in
Ref. 3; CAA37656). {ECO:0000305}.
CONFLICT 1755 1755 P -> L (in Ref. 10; AAI18917).
{ECO:0000305}.
CONFLICT 1777 1777 Missing (in Ref. 5; CAB61345).
{ECO:0000305}.
STRAND 990 995 {ECO:0000244|PDB:3FSO}.
STRAND 997 1002 {ECO:0000244|PDB:3FSO}.
HELIX 1003 1005 {ECO:0000244|PDB:3FSO}.
STRAND 1006 1016 {ECO:0000244|PDB:3FSO}.
STRAND 1022 1033 {ECO:0000244|PDB:3FSO}.
TURN 1035 1037 {ECO:0000244|PDB:3FSO}.
STRAND 1043 1048 {ECO:0000244|PDB:3FSO}.
STRAND 1054 1061 {ECO:0000244|PDB:3FSO}.
TURN 1070 1073 {ECO:0000244|PDB:3FQ4}.
STRAND 1076 1087 {ECO:0000244|PDB:3FSO}.
STRAND 1096 1103 {ECO:0000244|PDB:3FSO}.
STRAND 1131 1137 {ECO:0000244|PDB:3F7Q}.
STRAND 1139 1141 {ECO:0000244|PDB:3F7Q}.
STRAND 1143 1148 {ECO:0000244|PDB:3F7Q}.
STRAND 1156 1163 {ECO:0000244|PDB:3F7Q}.
HELIX 1168 1170 {ECO:0000244|PDB:3F7Q}.
STRAND 1172 1183 {ECO:0000244|PDB:3F7Q}.
STRAND 1191 1200 {ECO:0000244|PDB:3F7Q}.
STRAND 1203 1207 {ECO:0000244|PDB:3F7P}.
STRAND 1211 1214 {ECO:0000244|PDB:3F7Q}.
STRAND 1227 1230 {ECO:0000244|PDB:3F7Q}.
STRAND 1232 1234 {ECO:0000244|PDB:3F7Q}.
STRAND 1236 1239 {ECO:0000244|PDB:3F7Q}.
STRAND 1252 1260 {ECO:0000244|PDB:3F7Q}.
STRAND 1262 1264 {ECO:0000244|PDB:3F7R}.
STRAND 1266 1268 {ECO:0000244|PDB:3F7Q}.
STRAND 1271 1275 {ECO:0000244|PDB:1QG3}.
STRAND 1282 1286 {ECO:0000244|PDB:3F7Q}.
STRAND 1294 1302 {ECO:0000244|PDB:3F7Q}.
STRAND 1310 1314 {ECO:0000244|PDB:3F7Q}.
HELIX 1316 1318 {ECO:0000244|PDB:3F7Q}.
STRAND 1334 1336 {ECO:0000244|PDB:3F7Q}.
STRAND 1344 1348 {ECO:0000244|PDB:3F7P}.
STRAND 1522 1524 {ECO:0000244|PDB:2YRZ}.
STRAND 1535 1538 {ECO:0000244|PDB:4WTW}.
STRAND 1544 1547 {ECO:0000244|PDB:4WTW}.
STRAND 1557 1566 {ECO:0000244|PDB:4WTW}.
STRAND 1573 1577 {ECO:0000244|PDB:4WTW}.
STRAND 1584 1587 {ECO:0000244|PDB:4WTW}.
STRAND 1595 1604 {ECO:0000244|PDB:4WTW}.
STRAND 1612 1617 {ECO:0000244|PDB:4WTW}.
STRAND 1648 1653 {ECO:0000244|PDB:4WTX}.
STRAND 1656 1662 {ECO:0000244|PDB:4WTX}.
STRAND 1671 1680 {ECO:0000244|PDB:4WTX}.
STRAND 1683 1685 {ECO:0000244|PDB:4WTX}.
STRAND 1688 1694 {ECO:0000244|PDB:4WTX}.
STRAND 1697 1703 {ECO:0000244|PDB:4WTX}.
STRAND 1712 1722 {ECO:0000244|PDB:4WTX}.
STRAND 1724 1732 {ECO:0000244|PDB:4WTX}.
SEQUENCE 1822 AA; 202167 MW; 09710FFBBD719469 CRC64;
MAGPRPSPWA RLLLAALISV SLSGTLANRC KKAPVKSCTE CVRVDKDCAY CTDEMFRDRR
CNTQAELLAA GCQRESIVVM ESSFQITEET QIDTTLRRSQ MSPQGLRVRL RPGEERHFEL
EVFEPLESPV DLYILMDFSN SMSDDLDNLK KMGQNLARVL SQLTSDYTIG FGKFVDKVSV
PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVDEFRNKL QGERISGNLD APEGGFDAIL
QTAVCTRDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MSRNDERCHL DTTGTYTQYR
TQDYPSVPTL VRLLAKHNII PIFAVTNYSY SYYEKLHTYF PVSSLGVLQE DSSNIVELLE
EAFNRIRSNL DIRALDSPRG LRTEVTSKMF QKTRTGSFHI RRGEVGIYQV QLRALEHVDG
THVCQLPEDQ KGNIHLKPSF SDGLKMDAGI ICDVCTCELQ KEVRSARCSF NGDFVCGQCV
CSEGWSGQTC NCSTGSLSDI QPCLREGEDK PCSGRGECQC GHCVCYGEGR YEGQFCEYDN
FQCPRTSGFL CNDRGRCSMG QCVCEPGWTG PSCDCPLSNA TCIDSNGGIC NGRGHCECGR
CHCHQQSLYT DTICEINYSA IHPGLCEDLR SCVQCQAWGT GEKKGRTCEE CNFKVKMVDE
LKRAEEVVVR CSFRDEDDDC TYSYTMEGDG APGPNSTVLV HKKKDCPPGS FWWLIPLLLL
LLPLLALLLL LCWKYCACCK ACLALLPCCN RGHMVGFKED HYMLRENLMA SDHLDTPMLR
SGNLKGRDVV RWKVTNNMQR PGFATHAASI NPTELVPYGL SLRLARLCTE NLLKPDTREC
AQLRQEVEEN LNEVYRQISG VHKLQQTKFR QQPNAGKKQD HTIVDTVLMA PRSAKPALLK
LTEKQVEQRA FHDLKVAPGY YTLTADQDAR GMVEFQEGVE LVDVRVPLFI RPEDDDEKQL
LVEAIDVPAG TATLGRRLVN ITIIKEQARD VVSFEQPEFS VSRGDQVARI PVIRRVLDGG
KSQVSYRTQD GTAQGNRDYI PVEGELLFQP GEAWKELQVK LLELQEVDSL LRGRQVRRFH
VQLSNPKFGA HLGQPHSTTI IIRDPDELDR SFTSQMLSSQ PPPHGDLGAP QNPNAKAAGS
RKIHFNWLPP SGKPMGYRVK YWIQGDSESE AHLLDSKVPS VELTNLYPYC DYEMKVCAYG
AQGEGPYSSL VSCRTHQEVP SEPGRLAFNV VSSTVTQLSW AEPAETNGEI TAYEVCYGLV
NDDNRPIGPM KKVLVDNPKN RMLLIENLRE SQPYRYTVKA RNGAGWGPER EAIINLATQP
KRPMSIPIIP DIPIVDAQSG EDYDSFLMYS DDVLRSPSGS QRPSVSDDTG CGWKFEPLLG
EELDLRRVTW RLPPELIPRL SASSGRSSDA EAPHGPPDDG GAGGKGGSLP RSATPGPPGE
HLVNGRMDFA FPGSTNSLHR MTTTSAAAYG THLSPHVPHR VLSTSSTLTR DYNSLTRSEH
SHSTTLPRDY STLTSVSSHD SRLTAGVPDT PTRLVFSALG PTSLRVSWQE PRCERPLQGY
SVEYQLLNGG ELHRLNIPNP AQTSVVVEDL LPNHSYVFRV RAQSQEGWGR EREGVITIES
QVHPQSPLCP LPGSAFTLST PSAPGPLVFT ALSPDSLQLS WERPRRPNGD IVGYLVTCEM
AQGGGPATAF RVDGDSPESR LTVPGLSENV PYKFKVQART TEGFGPEREG IITIESQDGG
PFPQLGSRAG LFQHPLQSEY SSITTTHTSA TEPFLVDGLT LGAQHLEAGG SLTRHVTQEF
VSRTLTTSGT LSTHMDQQFF QT


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