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CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)

 CD44_HUMAN              Reviewed;         742 AA.
P16070; A5YRN9; B6EAT9; D3DR12; D3DR13; O95370; P22511; Q04858;
Q13419; Q13957; Q13958; Q13959; Q13960; Q13961; Q13967; Q13968;
Q13980; Q15861; Q16064; Q16065; Q16066; Q16208; Q16522; Q86T72;
Q86Z27; Q8N694; Q92493; Q96J24; Q9H5A5; Q9UC28; Q9UC29; Q9UC30;
Q9UCB0; Q9UJ36;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
30-AUG-2017, entry version 211.
RecName: Full=CD44 antigen;
AltName: Full=CDw44;
AltName: Full=Epican;
AltName: Full=Extracellular matrix receptor III;
Short=ECMR-III;
AltName: Full=GP90 lymphocyte homing/adhesion receptor;
AltName: Full=HUTCH-I;
AltName: Full=Heparan sulfate proteoglycan;
AltName: Full=Hermes antigen;
AltName: Full=Hyaluronate receptor;
AltName: Full=Phagocytic glycoprotein 1;
Short=PGP-1;
AltName: Full=Phagocytic glycoprotein I;
Short=PGP-I;
AltName: CD_antigen=CD44;
Flags: Precursor;
Name=CD44; Synonyms=LHR, MDU2, MDU3, MIC4;
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 12).
PubMed=2466575; DOI=10.1016/0092-8674(89)90638-7;
Stamenkovic I., Amiot M., Pesando J.M., Seed B.;
"A lymphocyte molecule implicated in lymph node homing is a member of
the cartilage link protein family.";
Cell 56:1057-1062(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
TISSUE=Reticulocyte;
PubMed=1840487; DOI=10.1016/0006-291X(91)91009-2;
Harn H.-J., Isola N., Cooper D.L.;
"The multispecific cell adhesion molecule CD44 is represented in
reticulocyte cDNA.";
Biochem. Biophys. Res. Commun. 178:1127-1134(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND VARIANT THR-479.
PubMed=1991450;
Stamenkovic I., Aruffo A., Amiot M., Seed B.;
"The hematopoietic and epithelial forms of CD44 are distinct
polypeptides with different adhesion potentials for hyaluronate-
bearing cells.";
EMBO J. 10:343-348(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11), AND VARIANT THR-479.
TISSUE=Myeloid leukemia cell;
PubMed=2056274; DOI=10.1084/jem.174.1.1;
Dougherty G.J., Lansdorp P.M., Cooper D.L., Humphries R.K.;
"Molecular cloning of CD44R1 and CD44R2, two novel isoforms of the
human CD44 lymphocyte 'homing' receptor expressed by hemopoietic
cells.";
J. Exp. Med. 174:1-5(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-479.
TISSUE=Keratinocyte;
PubMed=1281868; DOI=10.1111/1523-1747.ep12614896;
Kugelman L.C., Ganguly S., Haggerty J.G., Weissman S.M.,
Milstone L.M.;
"The core protein of epican, a heparan sulfate proteoglycan on
keratinocytes, is an alternative form of CD44.";
J. Invest. Dermatol. 99:886-891(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS
ARG-417 AND THR-479.
TISSUE=Lymphoblast;
PubMed=1465456; DOI=10.1073/pnas.89.24.12160;
Screaton G.R., Bell M.V., Jackson D.G., Cornelis F.B., Gerth U.,
Bell J.I.;
"Genomic structure of DNA encoding the lymphocyte homing receptor CD44
reveals at least 12 alternatively spliced exons.";
Proc. Natl. Acad. Sci. U.S.A. 89:12160-12164(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-417; THR-479
AND HIS-494.
PubMed=7508842;
Gunthert U.;
"CD44: a multitude of isoforms with diverse functions.";
Curr. Top. Microbiol. Immunol. 184:47-63(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 13 AND 14), AND VARIANT
THR-479.
TISSUE=Mammary carcinoma;
PubMed=8352881; DOI=10.1002/mc.2940070403;
Tanabe K.K., Nishi T., Saya H.;
"Novel variants of CD44 arising from alternative splicing: changes in
the CD44 alternative splicing pattern of MCF-7 breast carcinoma cells
treated with hyaluronidase.";
Mol. Carcinog. 7:212-220(1993).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19).
PubMed=10933060; DOI=10.1038/sj.neo.7900045;
Chiu R.K., Carpenito C., Dougherty S.T., Hayes G.M., Dougherty G.J.;
"Identification and characterization of CD44RC, a novel alternatively
spliced soluble CD44 isoform that can potentiate the hyaluronan
binding activity of cell surface CD44.";
Neoplasia 1:446-452(1999).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
TISSUE=Articular cartilage;
Bosch P.P., Stevens J.W., Buckwalter J.A., Midura R.J.;
"CD44 in normal and neoplastic human cartilage.";
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 12), AND VARIANT THR-479.
TISSUE=Colon adenocarcinoma, and Retinal pigment epithelium;
Wiebe G.J., Freund D., Corbeil D.;
"Sequence analysis of the human CD44 antigen.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
Xiang Q., Wang J., Fan C., He X., Huang L., Zhu H., Qiu X., Luo W.;
"Sequence analysis of a novel human CD44 variant.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
Fang X., Xu W., Zhang X.;
"Construction of human CD44 eukaryotic vector and its expression in
mammary carcinoma cells MCF-7.";
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
TISSUE=Spinal cord;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 12), AND
VARIANTS ARG-417 AND THR-479.
TISSUE=Pancreas, and Retinal pigment epithelium;
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).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
TISSUE=Lymphoblast;
PubMed=1922057; DOI=10.1128/MCB.11.11.5446;
Shtivelman E., Bishop J.M.;
"Expression of CD44 is repressed in neuroblastoma cells.";
Mol. Cell. Biol. 11:5446-5453(1991).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-742 (ISOFORM 15).
PubMed=2466576; DOI=10.1016/0092-8674(89)90639-9;
Goldstein L.A., Zhou D.F.H., Picker L.J., Minty C.N., Bargatze R.F.,
Ding J.F., Butcher E.C.;
"A human lymphocyte homing receptor, the hermes antigen, is related to
cartilage proteoglycan core and link proteins.";
Cell 56:1063-1072(1989).
[20]
PROTEIN SEQUENCE OF 55-108.
TISSUE=Glial tumor;
PubMed=7527301; DOI=10.1007/BF01519984;
Okada H., Yoshida J., Seo H., Wakabayashi T., Sugita K., Hagiwara M.;
"Anti-(glioma surface antigen) monoclonal antibody G-22 recognizes
overexpressed CD44 in glioma cells.";
Cancer Immunol. Immunother. 39:313-317(1994).
[21]
PROTEIN SEQUENCE OF 67-89.
TISSUE=Peripheral blood;
PubMed=7508992;
Shepley M.P., Racaniello V.R.;
"A monoclonal antibody that blocks poliovirus attachment recognizes
the lymphocyte homing receptor CD44.";
J. Virol. 68:1301-1308(1994).
[22]
NUCLEOTIDE SEQUENCE [MRNA] OF 184-625 (ISOFORM 10), AND VARIANT
THR-479.
TISSUE=Foreskin;
PubMed=2007624; DOI=10.1083/jcb.113.1.207;
Brown T.A., Bouchard T., St John T., Wayner E., Carter W.G.;
"Human keratinocytes express a new CD44 core protein (CD44E) as a
heparan-sulfate intrinsic membrane proteoglycan with additional
exons.";
J. Cell Biol. 113:207-221(1991).
[23]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-267.
PubMed=8148709; DOI=10.1136/bmj.308.6929.619;
Matsumura Y., Hanbury D., Smith J., Tarin D.;
"Non-invasive detection of malignancy by identification of unusual
CD44 gene activity in exfoliated cancer cells.";
BMJ 308:619-624(1994).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 267-603 (ISOFORM 1), AND VARIANT
ARG-417.
TISSUE=Lung;
PubMed=1717145;
Hofmann M., Rudy W., Zoeller M., Toelg C., Ponta H., Herrlich P.,
Guenthert U.;
"CD44 splice variants confer metastatic behavior in rats: homologous
sequences are expressed in human tumor cell lines.";
Cancer Res. 51:5292-5297(1991).
[25]
REVIEW ON FUNCTION, AND POST-TRANSLATIONAL MODIFICATIONS.
PubMed=12511867; DOI=10.1038/nrm1004;
Ponta H., Sherman L., Herrlich P.A.;
"CD44: from adhesion molecules to signalling regulators.";
Nat. Rev. Mol. Cell Biol. 4:33-45(2003).
[26]
PHOSPHORYLATION AT SER-706.
PubMed=9580567;
Peck D., Isacke C.M.;
"Hyaluronan-dependent cell migration can be blocked by a CD44
cytoplasmic domain peptide containing a phosphoserine at position
325.";
J. Cell Sci. 111:1595-1601(1998).
[27]
PHOSPHORYLATION AT SER-672.
PubMed=12032545; DOI=10.1038/ncb797;
Legg J.W., Lewis C.A., Parsons M., Ng T., Isacke C.M.;
"A novel PKC-regulated mechanism controls CD44 ezrin association and
directional cell motility.";
Nat. Cell Biol. 4:399-407(2002).
[28]
GLYCOSYLATION, AND PROTEOLYTIC PROCESSING.
PubMed=12883358; DOI=10.1097/00008390-200308000-00001;
Bartolazzi A.;
"CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage
are regulated at post-translational level in cells of melanocytic
lineage.";
Melanoma Res. 13:325-337(2003).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57.
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[31]
FUNCTION.
PubMed=16541107; DOI=10.1038/sj.emboj.7601039;
Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M.,
Christiansen J., Nielsen F.C.;
"RNA-binding IMPs promote cell adhesion and invadopodia formation.";
EMBO J. 25:1456-1468(2006).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND 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).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[35]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-110.
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).
[36]
INTERACTION WITH UNC119.
PubMed=19381274; DOI=10.1371/journal.pone.0005211;
Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
"Unc119 protects from Shigella infection by inhibiting the Abl family
kinases.";
PLoS ONE 4:E5211-E5211(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[39]
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).
[40]
GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, 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).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
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).
[45]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-178, STRUCTURE BY NMR OF
20-178, AND INTERACTION WITH HA.
PubMed=14992719; DOI=10.1016/S1097-2765(04)00080-2;
Teriete P., Banerji S., Noble M., Blundell C.D., Wright A.J.,
Pickford A.R., Lowe E., Mahoney D.J., Tammi M.I., Kahmann J.D.,
Campbell I.D., Day A.J., Jackson D.G.;
"Structure of the regulatory hyaluronan binding domain in the
inflammatory leukocyte homing receptor CD44.";
Mol. Cell 13:483-496(2004).
[46]
STRUCTURE BY NMR OF 20-178 IN COMPLEX WITH HA.
PubMed=17085435; DOI=10.1074/jbc.M608425200;
Takeda M., Ogino S., Umemoto R., Sakakura M., Kajiwara M.,
Sugahara K.N., Hayasaka H., Miyasaka M., Terasawa H., Shimada I.;
"Ligand-induced structural changes of the CD44 hyaluronan-binding
domain revealed by NMR.";
J. Biol. Chem. 281:40089-40095(2006).
[47]
VARIANT BLOOD GROUP INDIAN PRO-46.
PubMed=8636151; DOI=10.1074/jbc.271.12.7147;
Telen M.J., Udani M., Washington M.K., Levesque M.C., Lloyd E.,
Rao N.;
"A blood group-related polymorphism of CD44 abolishes a hyaluronan-
binding consensus sequence without preventing hyaluronan binding.";
J. Biol. Chem. 271:7147-7153(1996).
-!- FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell
and cell-matrix interactions through its affinity for HA, and
possibly also through its affinity for other ligands such as
osteopontin, collagens, and matrix metalloproteinases (MMPs).
Adhesion with HA plays an important role in cell migration, tumor
growth and progression. In cancer cells, may play an important
role in invadopodia formation. Also involved in lymphocyte
activation, recirculation and homing, and in hematopoiesis.
Altered expression or dysfunction causes numerous pathogenic
phenotypes. Great protein heterogeneity due to numerous
alternative splicing and post-translational modification events.
Receptor for LGALS9; the interaction enhances binding of SMAD3 to
the FOXP3 promoter, leading to up-regulation of FOXP3 expression
and increased induced regulatory T (iTreg) cell stability and
suppressive function (By similarity).
{ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:16541107}.
-!- SUBUNIT: Interacts with PKN2 (By similarity). Interacts with TIAM1
and TIAM2 (By similarity). Interacts with HA, as well as other
glycosaminoglycans, collagen, laminin, and fibronectin via its N-
terminal segment (PubMed:14992719, PubMed:17085435). Interacts
with ANK, the ERM proteins (VIL2, RDX and MSN), and NF2 via its C-
terminal segment. Interacts with UNC119 (PubMed:19381274).
{ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:14992719,
ECO:0000269|PubMed:17085435, ECO:0000269|PubMed:19381274}.
-!- INTERACTION:
P18011:ipaB (xeno); NbExp=4; IntAct=EBI-490245, EBI-490239;
P26038:MSN; NbExp=6; IntAct=EBI-490245, EBI-528768;
Q9UPY5:SLC7A11; NbExp=4; IntAct=EBI-490245, EBI-3843348;
P10451:SPP1; NbExp=4; IntAct=EBI-490245, EBI-723648;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P15379}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P15379}. Note=Colocalizes with
actin in membrane protrusions at wounding edges.
{ECO:0000250|UniProtKB:P15379}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=19;
Comment=Additional isoforms seem to exist. Additional isoforms
are produced by alternative splicing of 10 out of 19 exons
within the extracellular domain. Additional diversity is
generated through the utilization of internal splice donor and
acceptor sites within 2 of the exons. A variation in the
cytoplasmic domain was shown to result from the alternative
splicing of 2 exons. Isoform CD44 is expected to be expressed in
normal cells. Splice variants have been found in many tumor cell
lines. Exons 5, 6, 7, 8, 9, 10, 11, 13, 14 and 19 are
alternatively spliced. Experimental confirmation may be lacking
for some isoforms. {ECO:0000269|PubMed:1465456};
Name=1; Synonyms=CD44;
IsoId=P16070-1; Sequence=Displayed;
Note=Corresponds to the largest isoform.;
Name=2; Synonyms=CD44SP;
IsoId=P16070-2; Sequence=VSP_005303, VSP_005304;
Name=3;
IsoId=P16070-3; Sequence=VSP_005305, VSP_005306;
Note=Alternative splice donor/acceptor on exon 5.;
Name=4; Synonyms=Epidermal;
IsoId=P16070-4; Sequence=VSP_005307, VSP_005308;
Note=Lacks exon 6.;
Name=5;
IsoId=P16070-5; Sequence=VSP_005313;
Note=Alternative splice donor/acceptor on exon 7.;
Name=6;
IsoId=P16070-6; Sequence=VSP_005314, VSP_005315;
Note=Lacks exon 10.;
Name=7;
IsoId=P16070-7; Sequence=VSP_005316, VSP_005317;
Note=Lacks exon 13.;
Name=8;
IsoId=P16070-8; Sequence=VSP_005318, VSP_005319;
Note=Lacks exon 14.;
Name=9;
IsoId=P16070-9; Sequence=VSP_005320, VSP_005321;
Note=Lacks exon 19.;
Name=10; Synonyms=CD44E, CD44R1, Epithelial, Keratinocyte;
IsoId=P16070-10; Sequence=VSP_005309, VSP_005310;
Note=Lacks exons 6-11.;
Name=11; Synonyms=CD44R2;
IsoId=P16070-11; Sequence=VSP_022797;
Note=Lacks exons 6-13.;
Name=12; Synonyms=CDw44, Reticulocyte;
IsoId=P16070-12; Sequence=VSP_005311, VSP_005312;
Note=Lacks exons 6-14.;
Name=13; Synonyms=CD44R4;
IsoId=P16070-13; Sequence=VSP_005309, VSP_005310, VSP_005318,
VSP_005319;
Note=Lacks exons 6-11 and exon 14.;
Name=14; Synonyms=CD44R5;
IsoId=P16070-14; Sequence=VSP_005309, VSP_005310, VSP_005316,
VSP_005317, VSP_005318, VSP_005319;
Note=Lacks exons 6-11, exon 13 and exon 14.;
Name=15; Synonyms=Hermes;
IsoId=P16070-15; Sequence=VSP_005311, VSP_005312, VSP_005320,
VSP_005321;
Note=Lacks exons 6-14 and exon 19.;
Name=16;
IsoId=P16070-16; Sequence=VSP_005305, VSP_005306, VSP_005314,
VSP_005315;
Note=Alternative splice donor/acceptor on exon 5 and lacks exon
10.;
Name=17;
IsoId=P16070-17; Sequence=VSP_005313, VSP_005314, VSP_005315;
Note=Alternative splice donor/acceptor on exon 7 and lacks exon
10.;
Name=18;
IsoId=P16070-18; Sequence=VSP_005311, VSP_005312, VSP_043575;
Note=No experimental confirmation available.;
Name=19; Synonyms=CD44RC;
IsoId=P16070-19; Sequence=VSP_043870, VSP_043871;
Note=Soluble isoform, has enhanced hyaluronan binding.;
-!- TISSUE SPECIFICITY: Isoform 10 (epithelial isoform) is expressed
by cells of epithelium and highly expressed by carcinomas.
Expression is repressed in neuroblastoma cells.
-!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
binding. {ECO:0000250}.
-!- PTM: Proteolytically cleaved in the extracellular matrix by
specific proteinases (possibly MMPs) in several cell lines and
tumors. {ECO:0000269|PubMed:12883358}.
-!- PTM: N- and O-glycosylated. O-glycosylation contains more-or-less-
sulfated chondroitin sulfate glycans, whose number may affect the
accessibility of specific proteinases to their cleavage site(s).
It is uncertain if O-glycosylation occurs on Thr-637 or Thr-638.
{ECO:0000269|PubMed:12883358, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.
-!- PTM: Phosphorylated; activation of PKC results in the
dephosphorylation of Ser-706 (constitutive phosphorylation site),
and the phosphorylation of Ser-672. {ECO:0000269|PubMed:12032545,
ECO:0000269|PubMed:9580567}.
-!- POLYMORPHISM: CD44 is responsible for the Indian blood group
system. The molecular basis of the In(A)=In1/In(B)=In2 blood group
antigens is a single variation in position 46; In(B), the most
frequent allele, has Arg-46. {ECO:0000269|PubMed:8636151}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=indian";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD44 entry;
URL="https://en.wikipedia.org/wiki/CD44";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CD44ID980CH11p13.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M24915; AAA35674.1; -; mRNA.
EMBL; M59040; AAA51950.1; -; mRNA.
EMBL; X55150; CAA38951.1; -; mRNA.
EMBL; X56794; CAA40133.1; -; mRNA.
EMBL; X66733; CAA47271.1; -; mRNA.
EMBL; L05423; AAB13622.1; -; Genomic_DNA.
EMBL; L05407; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05409; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13622.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13622.1; JOINED; Genomic_DNA.
EMBL; L05423; AAB13623.1; -; Genomic_DNA.
EMBL; L05407; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05411; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05412; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05414; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05415; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05416; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05417; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05418; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05419; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13623.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13623.1; JOINED; Genomic_DNA.
EMBL; L05424; AAB13624.1; -; Genomic_DNA.
EMBL; L05407; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13624.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13624.1; JOINED; Genomic_DNA.
EMBL; L05424; AAB13625.1; -; Genomic_DNA.
EMBL; L05407; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05411; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05412; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05414; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05416; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05417; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05418; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05419; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13625.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13625.1; JOINED; Genomic_DNA.
EMBL; L05424; AAB13626.1; -; Genomic_DNA.
EMBL; L05407; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05411; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05412; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05414; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05416; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05417; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05418; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05419; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13626.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13626.1; JOINED; Genomic_DNA.
EMBL; L05424; AAB13627.1; -; Genomic_DNA.
EMBL; L05407; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05417; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05418; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13627.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13627.1; JOINED; Genomic_DNA.
EMBL; L05424; AAB13628.1; -; Genomic_DNA.
EMBL; L05407; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05408; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05410; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05411; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05412; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05414; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05415; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05416; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05417; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05418; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05419; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05420; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05421; AAB13628.1; JOINED; Genomic_DNA.
EMBL; L05422; AAB13628.1; JOINED; Genomic_DNA.
EMBL; M69215; AAB13628.1; JOINED; Genomic_DNA.
EMBL; AJ251595; CAB61878.1; -; mRNA.
EMBL; S66400; AAB27917.1; -; mRNA.
EMBL; S66400; AAB27918.2; -; mRNA.
EMBL; S66400; AAB27919.1; -; mRNA.
EMBL; AF098641; AAC70782.1; -; mRNA.
EMBL; U40373; AAA82949.1; -; mRNA.
EMBL; AY101192; AAM50040.1; -; mRNA.
EMBL; AY101193; AAM50041.1; -; mRNA.
EMBL; EF581837; ABQ59315.1; -; mRNA.
EMBL; FJ216964; ACI46596.1; -; mRNA.
EMBL; AL832642; CAD89965.1; -; mRNA.
EMBL; AL133330; CAC10347.1; -; Genomic_DNA.
EMBL; AL136989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68147.1; -; Genomic_DNA.
EMBL; CH471064; EAW68148.1; -; Genomic_DNA.
EMBL; CH471064; EAW68149.1; -; Genomic_DNA.
EMBL; CH471064; EAW68151.1; -; Genomic_DNA.
EMBL; CH471064; EAW68152.1; -; Genomic_DNA.
EMBL; BC004372; AAH04372.1; -; mRNA.
EMBL; BC067348; AAH67348.1; -; mRNA.
EMBL; M25078; AAA36138.1; -; mRNA.
EMBL; X55938; CAA39404.1; -; mRNA.
EMBL; S72928; AAB30429.1; -; Genomic_DNA.
EMBL; X62739; CAA44602.1; -; mRNA.
CCDS; CCDS31455.1; -. [P16070-4]
CCDS; CCDS31456.1; -. [P16070-10]
CCDS; CCDS31457.1; -. [P16070-12]
CCDS; CCDS31458.1; -. [P16070-19]
CCDS; CCDS55754.1; -. [P16070-11]
CCDS; CCDS55755.1; -. [P16070-18]
CCDS; CCDS7897.1; -. [P16070-1]
PIR; A47195; A47195.
PIR; I37369; I37369.
PIR; I77371; I77371.
PIR; I77372; I77372.
PIR; JH0417; JH0417.
PIR; JH0518; JH0518.
PIR; S13530; S13530.
PIR; S24222; S24222.
RefSeq; NP_000601.3; NM_000610.3. [P16070-1]
RefSeq; NP_001001389.1; NM_001001389.1. [P16070-4]
RefSeq; NP_001001390.1; NM_001001390.1. [P16070-10]
RefSeq; NP_001001391.1; NM_001001391.1. [P16070-12]
RefSeq; NP_001001392.1; NM_001001392.1. [P16070-19]
RefSeq; NP_001189484.1; NM_001202555.1. [P16070-11]
RefSeq; NP_001189485.1; NM_001202556.1. [P16070-18]
RefSeq; NP_001189486.1; NM_001202557.1. [P16070-15]
RefSeq; XP_011518790.1; XM_011520488.1. [P16070-13]
UniGene; Hs.502328; -.
PDB; 1POZ; NMR; -; A=20-178.
PDB; 1UUH; X-ray; 2.20 A; A/B=20-178.
PDB; 2I83; NMR; -; A=21-178.
PDB; 4PZ3; X-ray; 1.08 A; A/B=18-170.
PDB; 4PZ4; X-ray; 1.60 A; A/B=18-171.
PDBsum; 1POZ; -.
PDBsum; 1UUH; -.
PDBsum; 2I83; -.
PDBsum; 4PZ3; -.
PDBsum; 4PZ4; -.
ProteinModelPortal; P16070; -.
SMR; P16070; -.
BioGrid; 107398; 107.
DIP; DIP-1121N; -.
ELM; P16070; -.
IntAct; P16070; 53.
MINT; MINT-5000740; -.
STRING; 9606.ENSP00000398632; -.
BindingDB; P16070; -.
ChEMBL; CHEMBL3232692; -.
DrugBank; DB08818; Hyaluronic acid.
iPTMnet; P16070; -.
PhosphoSitePlus; P16070; -.
SwissPalm; P16070; -.
UniCarbKB; P16070; -.
BioMuta; CD44; -.
DMDM; 308153615; -.
SWISS-2DPAGE; P16070; -.
EPD; P16070; -.
MaxQB; P16070; -.
PaxDb; P16070; -.
PeptideAtlas; P16070; -.
PRIDE; P16070; -.
TopDownProteomics; P16070-12; -. [P16070-12]
TopDownProteomics; P16070-14; -. [P16070-14]
TopDownProteomics; P16070-18; -. [P16070-18]
TopDownProteomics; P16070-4; -. [P16070-4]
TopDownProteomics; P16070-7; -. [P16070-7]
DNASU; 960; -.
Ensembl; ENST00000263398; ENSP00000263398; ENSG00000026508. [P16070-12]
Ensembl; ENST00000278386; ENSP00000278386; ENSG00000026508. [P16070-19]
Ensembl; ENST00000352818; ENSP00000309732; ENSG00000026508. [P16070-18]
Ensembl; ENST00000415148; ENSP00000389830; ENSG00000026508. [P16070-4]
Ensembl; ENST00000428726; ENSP00000398632; ENSG00000026508. [P16070-1]
Ensembl; ENST00000433892; ENSP00000392331; ENSG00000026508. [P16070-10]
Ensembl; ENST00000434472; ENSP00000404447; ENSG00000026508. [P16070-11]
GeneID; 960; -.
KEGG; hsa:960; -.
UCSC; uc001mvu.4; human. [P16070-1]
CTD; 960; -.
DisGeNET; 960; -.
GeneCards; CD44; -.
HGNC; HGNC:1681; CD44.
HPA; CAB000112; -.
HPA; CAB000316; -.
HPA; HPA005785; -.
MIM; 107269; gene.
MIM; 172290; gene.
MIM; 609027; phenotype.
neXtProt; NX_P16070; -.
OpenTargets; ENSG00000026508; -.
PharmGKB; PA26221; -.
eggNOG; ENOG410IZCP; Eukaryota.
eggNOG; ENOG4111S6T; LUCA.
GeneTree; ENSGT00530000063822; -.
HOGENOM; HOG000115236; -.
HOVERGEN; HBG003850; -.
InParanoid; P16070; -.
KO; K06256; -.
OMA; SHPMGRG; -.
OrthoDB; EOG091G0F98; -.
PhylomeDB; P16070; -.
TreeFam; TF334173; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-877300; Interferon gamma signaling.
SIGNOR; P16070; -.
ChiTaRS; CD44; human.
EvolutionaryTrace; P16070; -.
GeneWiki; CD44; -.
GenomeRNAi; 960; -.
PRO; PR:P16070; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000026508; -.
ExpressionAtlas; P16070; baseline and differential.
Genevisible; P16070; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0042995; C:cell projection; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0005518; F:collagen binding; NAS:UniProtKB.
GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
GO; GO:0051216; P:cartilage development; IEP:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0070487; P:monocyte aggregation; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:1900625; P:positive regulation of monocyte aggregation; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:2000392; P:regulation of lamellipodium morphogenesis; IMP:UniProtKB.
GO; GO:0016337; P:single organismal cell-cell adhesion; NAS:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR001231; CD44_antigen.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000538; Link_dom.
PANTHER; PTHR10225:SF8; PTHR10225:SF8; 1.
Pfam; PF00193; Xlink; 1.
PRINTS; PR00658; CD44.
PRINTS; PR01265; LINKMODULE.
SMART; SM00445; LINK; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood group antigen;
Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Proteoglycan;
Pyrrolidone carboxylic acid; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 742 CD44 antigen.
/FTId=PRO_0000026687.
TOPO_DOM 21 649 Extracellular. {ECO:0000255}.
TRANSMEM 650 670 Helical. {ECO:0000255}.
TOPO_DOM 671 742 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 120 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 224 649 Stem.
COMPBIAS 150 158 Arg/Lys-rich (basic).
BINDING 41 41 Hyaluronan. {ECO:0000250}.
BINDING 78 78 Hyaluronan. {ECO:0000250}.
BINDING 79 79 Hyaluronan. {ECO:0000250}.
BINDING 105 105 Hyaluronan. {ECO:0000250}.
MOD_RES 21 21 Pyrrolidone carboxylic acid.
{ECO:0000305}.
MOD_RES 672 672 Phosphoserine; by PKC.
{ECO:0000269|PubMed:12032545}.
MOD_RES 686 686 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:9580567}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 599 599 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 129 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 53 118 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 77 97 {ECO:0000255|PROSITE-ProRule:PRU00323}.
VAR_SEQ 23 29 DLNITCR -> GVGRRKS (in isoform 2).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005303.
VAR_SEQ 30 742 Missing (in isoform 2).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005304.
VAR_SEQ 78 139 RYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYC
FNASAPPEEDCTSVTDLPNAF -> SLHCSQQSKKVWAEEK
ASDQQWQWSCGGQKAKWTQRRGQQVSGNGAFGEQGVVRNSR
PVYDS (in isoform 19).
{ECO:0000303|PubMed:10933060}.
/FTId=VSP_043870.
VAR_SEQ 140 742 Missing (in isoform 19).
{ECO:0000303|PubMed:10933060}.
/FTId=VSP_043871.
VAR_SEQ 192 192 G -> A (in isoform 3 and isoform 16).
{ECO:0000305}.
/FTId=VSP_005305.
VAR_SEQ 193 223 Missing (in isoform 3 and isoform 16).
{ECO:0000305}.
/FTId=VSP_005306.
VAR_SEQ 223 535 Missing (in isoform 11).
{ECO:0000303|PubMed:2056274,
ECO:0000303|Ref.12}.
/FTId=VSP_022797.
VAR_SEQ 223 223 T -> N (in isoform 10, isoform 13 and
isoform 14). {ECO:0000303|PubMed:1991450,
ECO:0000303|PubMed:2007624,
ECO:0000303|PubMed:2056274,
ECO:0000303|PubMed:8352881,
ECO:0000303|Ref.11}.
/FTId=VSP_005309.
VAR_SEQ 223 223 T -> R (in isoform 12, isoform 15 and
isoform 18).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:1840487,
ECO:0000303|PubMed:2466575,
ECO:0000303|PubMed:2466576,
ECO:0000303|Ref.10, ECO:0000303|Ref.11,
ECO:0000303|Ref.13}.
/FTId=VSP_005311.
VAR_SEQ 223 223 T -> S (in isoform 4).
{ECO:0000303|PubMed:1281868,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005307.
VAR_SEQ 224 604 Missing (in isoform 12, isoform 15 and
isoform 18).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:1840487,
ECO:0000303|PubMed:2466575,
ECO:0000303|PubMed:2466576,
ECO:0000303|Ref.10, ECO:0000303|Ref.11,
ECO:0000303|Ref.13}.
/FTId=VSP_005312.
VAR_SEQ 224 472 Missing (in isoform 10, isoform 13 and
isoform 14). {ECO:0000303|PubMed:1991450,
ECO:0000303|PubMed:2007624,
ECO:0000303|PubMed:2056274,
ECO:0000303|PubMed:8352881,
ECO:0000303|Ref.11}.
/FTId=VSP_005310.
VAR_SEQ 224 266 Missing (in isoform 4).
{ECO:0000303|PubMed:1281868,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005308.
VAR_SEQ 266 273 Missing (in isoform 5 and isoform 17).
{ECO:0000305}.
/FTId=VSP_005313.
VAR_SEQ 385 385 I -> T (in isoform 6, isoform 16 and
isoform 17). {ECO:0000305}.
/FTId=VSP_005314.
VAR_SEQ 386 428 Missing (in isoform 6, isoform 16 and
isoform 17). {ECO:0000305}.
/FTId=VSP_005315.
VAR_SEQ 506 506 Q -> R (in isoform 7 and isoform 14).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005316.
VAR_SEQ 507 535 Missing (in isoform 7 and isoform 14).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005317.
VAR_SEQ 536 536 N -> R (in isoform 8, isoform 13 and
isoform 14).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005318.
VAR_SEQ 537 604 Missing (in isoform 8, isoform 13 and
isoform 14).
{ECO:0000303|PubMed:8352881}.
/FTId=VSP_005319.
VAR_SEQ 605 625 Missing (in isoform 18).
{ECO:0000303|Ref.13}.
/FTId=VSP_043575.
VAR_SEQ 675 675 R -> S (in isoform 9 and isoform 15).
{ECO:0000303|PubMed:2466576}.
/FTId=VSP_005320.
VAR_SEQ 676 742 Missing (in isoform 9 and isoform 15).
{ECO:0000303|PubMed:2466576}.
/FTId=VSP_005321.
VARIANT 46 46 R -> P (in In(A) antigen;
dbSNP:rs369473842).
{ECO:0000269|PubMed:8636151}.
/FTId=VAR_006490.
VARIANT 393 393 T -> M (in dbSNP:rs11607491).
/FTId=VAR_030325.
VARIANT 417 417 K -> R (in dbSNP:rs9666607).
{ECO:0000269|PubMed:1465456,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1717145,
ECO:0000269|PubMed:7508842}.
/FTId=VAR_021147.
VARIANT 479 479 I -> T (in dbSNP:rs1467558).
{ECO:0000269|PubMed:1281868,
ECO:0000269|PubMed:1465456,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1991450,
ECO:0000269|PubMed:2007624,
ECO:0000269|PubMed:2056274,
ECO:0000269|PubMed:7508842,
ECO:0000269|PubMed:8352881,
ECO:0000269|Ref.11}.
/FTId=VAR_030326.
VARIANT 494 494 D -> H (in dbSNP:rs12273397).
{ECO:0000269|PubMed:7508842}.
/FTId=VAR_030327.
CONFLICT 26 26 I -> M (in Ref. 10; AAA82949).
{ECO:0000305}.
CONFLICT 109 109 S -> Y (in Ref. 1; AAA35674, 2; AAA51950,
3; CAA38951 and 7; CAB61878).
{ECO:0000305}.
CONFLICT 221 221 A -> R (in Ref. 3; CAA38951).
{ECO:0000305}.
CONFLICT 241 241 T -> A (in Ref. 7; CAB61878).
{ECO:0000305}.
CONFLICT 410 410 E -> V (in Ref. 5; CAA47271).
{ECO:0000305}.
CONFLICT 494 494 D -> N (in Ref. 7; CAB61878).
{ECO:0000305}.
CONFLICT 555 555 T -> H (in Ref. 3; CAA38951).
{ECO:0000305}.
CONFLICT 620 620 G -> E (in Ref. 1; AAA35674).
{ECO:0000305}.
CONFLICT 697 697 S -> I (in Ref. 11; AAM50041 and 16;
AAH67348). {ECO:0000305}.
STRAND 21 26 {ECO:0000244|PDB:4PZ3}.
STRAND 33 38 {ECO:0000244|PDB:4PZ3}.
HELIX 46 55 {ECO:0000244|PDB:4PZ3}.
STRAND 57 59 {ECO:0000244|PDB:1POZ}.
HELIX 63 71 {ECO:0000244|PDB:4PZ3}.
STRAND 80 82 {ECO:0000244|PDB:4PZ3}.
STRAND 85 92 {ECO:0000244|PDB:4PZ3}.
HELIX 98 100 {ECO:0000244|PDB:4PZ3}.
STRAND 103 106 {ECO:0000244|PDB:4PZ3}.
STRAND 109 111 {ECO:0000244|PDB:1POZ}.
STRAND 114 119 {ECO:0000244|PDB:4PZ3}.
STRAND 121 123 {ECO:0000244|PDB:2I83}.
STRAND 125 128 {ECO:0000244|PDB:4PZ3}.
STRAND 130 132 {ECO:0000244|PDB:2I83}.
STRAND 139 148 {ECO:0000244|PDB:4PZ3}.
TURN 150 152 {ECO:0000244|PDB:1POZ}.
STRAND 154 160 {ECO:0000244|PDB:4PZ3}.
HELIX 165 168 {ECO:0000244|PDB:4PZ3}.
SEQUENCE 742 AA; 81538 MW; BB9B66B19B970349 CRC64;
MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL
PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS
GSSSERSSTS GGYIFYTFST VHPIPDEDSP WITDSTDRIP ATTLMSTSAT ATETATKRQE
TWDWFSWLFL PSESKNHLHT TTQMAGTSSN TISAGWEPNE ENEDERDRHL SFSGSGIDDD
EDFISSTIST TPRAFDHTKQ NQDWTQWNPS HSNPEVLLQT TTRMTDVDRN GTTAYEGNWN
PEAHPPLIHH EHHEEEETPH STSTIQATPS STTEETATQK EQWFGNRWHE GYRQTPKEDS
HSTTGTAAAS AHTSHPMQGR TTPSPEDSSW TDFFNPISHP MGRGHQAGRR MDMDSSHSIT
LQPTANPNTG LVEDLDRTGP LSMTTQQSNS QSFSTSHEGL EEDKDHPTTS TLTSSNRNDV
TGGRRDPNHS EGSTTLLEGY TSHYPHTKES RTFIPVTSAK TGSFGVTAVT VGDSNSNVNR
SLSGDQDTFH PSGGSHTTHG SESDGHSHGS QEGGANTTSG PIRTPQIPEW LIILASLLAL
ALILAVCIAV NSRRRCGQKK KLVINSGNGA VEDRKPSGLN GEASKSQEMV HLVNKESSET
PDQFMTADET RNLQNVDMKI GV


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