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Alpha-crystallin B chain (Alpha(B)-crystallin) (Heat shock protein beta-5) (HspB5) (Renal carcinoma antigen NY-REN-27) (Rosenthal fiber component)

 CRYAB_HUMAN             Reviewed;         175 AA.
P02511; B0YIX0; O43416; Q9UC37; Q9UC38; Q9UC39; Q9UC40; Q9UC41;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
20-DEC-2017, entry version 209.
RecName: Full=Alpha-crystallin B chain;
AltName: Full=Alpha(B)-crystallin;
AltName: Full=Heat shock protein beta-5;
Short=HspB5;
AltName: Full=Renal carcinoma antigen NY-REN-27;
AltName: Full=Rosenthal fiber component;
Name=CRYAB; Synonyms=CRYA2, HSPB5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PRELIMINARY PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND ACETYLATION AT
MET-1.
PubMed=838078; DOI=10.1016/0014-5793(77)80757-6;
Kramps J.A., de Man B.M., de Jong W.W.;
"The primary structure of the B2 chain of human alpha-crystallin.";
FEBS Lett. 74:82-84(1977).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=2387586; DOI=10.1016/0888-7543(90)90204-8;
Dubin R.A., Ally A.H., Chung S., Piatigorsky J.;
"Human alpha B-crystallin gene and preferential promoter function in
lens.";
Genomics 7:594-601(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1407707; DOI=10.1016/0304-3940(92)90689-5;
Iwaki A., Iwaki T., Goldman J.E., Ogomori K., Tateishi J., Sakaki Y.;
"Accumulation of alpha B-crystallin in brains of patients with
Alexander's disease is not due to an abnormality of the 5'-flanking
and coding sequence of the genomic DNA.";
Neurosci. Lett. 140:89-92(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Yu W., Sarginson J., Gibbs R.A.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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).
[10]
PROTEIN SEQUENCE OF 2-24; 35-66 AND 118-175, AND ASSOCIATION WITH
HSPB1.
TISSUE=Pectoralis muscle;
PubMed=1560006;
Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.;
"Copurification of small heat shock protein with alpha B crystallin
from human skeletal muscle.";
J. Biol. Chem. 267:7718-7725(1992).
[11]
PROTEIN SEQUENCE OF 57-66.
PubMed=8999933; DOI=10.1074/jbc.272.4.2268;
Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L.,
David L.L.;
"Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes
the identification of the major proteins in young human lens.";
J. Biol. Chem. 272:2268-2275(1997).
[12]
PROTEIN SEQUENCE OF 83-89 AND 164-172.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 107-175.
PubMed=2539261; DOI=10.1016/0092-8674(89)90173-6;
Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E.;
"Alpha B-crystallin is expressed in non-lenticular tissues and
accumulates in Alexander's disease brain.";
Cell 57:71-78(1989).
[14]
RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP, AND ACETYLATION AT MET-1.
PubMed=8142454; DOI=10.1016/0167-4838(94)90003-5;
Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.;
"Simultaneous racemization and isomerization at specific aspartic acid
residues in alpha B-crystallin from the aged human lens.";
Biochim. Biophys. Acta 1204:157-163(1994).
[15]
PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, AND MASS SPECTROMETRY.
PubMed=8175657;
Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L.,
Smith J.B.;
"Post-translational modifications of water-soluble human lens
crystallins from young adults.";
J. Biol. Chem. 269:12494-12502(1994).
[16]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[17]
MASS SPECTROMETRY, SUSCEPTIBILITY TO OXIDATION, AND PHOSPHORYLATION.
PubMed=10930324; DOI=10.1006/exer.2000.0868;
Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.;
"The major in vivo modifications of the human water-insoluble lens
crystallins are disulfide bonds, deamidation, methionine oxidation and
backbone cleavage.";
Exp. Eye Res. 71:195-207(2000).
[18]
INTERACTION WITH HSPBAP1.
PubMed=10751411; DOI=10.1074/jbc.M001981200;
Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
"Identification and characterization of a novel protein from Sertoli
cells, PASS1, that associates with mammalian small stress protein
hsp27.";
J. Biol. Chem. 275:18724-18731(2000).
[19]
INVOLVEMENT IN CTRCT16.
PubMed=11577372; DOI=10.1086/324158;
Berry V., Francis P., Reddy M.A., Collyer D., Vithana E., MacKay I.,
Dawson G., Carey A.H., Moore A., Bhattacharya S.S., Quinlan R.A.;
"Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital
posterior polar cataract in humans.";
Am. J. Hum. Genet. 69:1141-1145(2001).
[20]
PHOSPHORYLATION AT SER-45 AND SER-59.
PubMed=11158243; DOI=10.1046/j.1471-4159.2001.00038.x;
Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N.,
Ohta H., Kishikawa M.;
"Ser-59 is the major phosphorylation site in alphaB-crystallin
accumulated in the brains of patients with Alexander's disease.";
J. Neurochem. 76:730-736(2001).
[21]
ACETYLATION AT LYS-92.
PubMed=11369851; DOI=10.1110/ps.40901;
Lapko V.N., Smith D.L., Smith J.B.;
"In vivo carbamylation and acetylation of water-soluble human lens
alphaB-crystallin lysine 92.";
Protein Sci. 10:1130-1136(2001).
[22]
INVOLVEMENT IN MFM2.
PubMed=14681890; DOI=10.1002/ana.10767;
Selcen D., Engel A.G.;
"Myofibrillar myopathy caused by novel dominant negative alpha B-
crystallin mutations.";
Ann. Neurol. 54:804-810(2003).
[23]
INTERACTION WITH TTN.
PubMed=14676215; DOI=10.1074/jbc.M307473200;
Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M.,
Labeit D., Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.;
"Association of the chaperone alphaB-crystallin with titin in heart
muscle.";
J. Biol. Chem. 279:7917-7924(2004).
[24]
SUBCELLULAR LOCATION.
PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005;
Vos M.J., Kanon B., Kampinga H.H.;
"HSPB7 is a SC35 speckle resident small heat shock protein.";
Biochim. Biophys. Acta 1793:1343-1353(2009).
[25]
SUBUNIT.
PubMed=20836128; DOI=10.1002/iub.373;
Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.;
"Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA
to alphaB ratio: stability, aggregation, and modifications.";
IUBMB Life 62:693-702(2010).
[26]
INVOLVEMENT IN MFMFIH-CRYAB.
PubMed=21337604; DOI=10.1002/ana.22331;
Del Bigio M.R., Chudley A.E., Sarnat H.B., Campbell C., Goobie S.,
Chodirker B.N., Selcen D.;
"Infantile muscular dystrophy in Canadian aboriginals is an alphaB-
crystallinopathy.";
Ann. Neurol. 69:866-871(2011).
[27]
ACETYLATION AT LYS-92 AND LYS-166.
PubMed=22120592; DOI=10.1016/j.bbadis.2011.11.011;
Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M.,
Padmanabha S., Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K.,
Biswas A.;
"Acetylation of alphaA-crystallin in the human lens: effects on
structure and chaperone function.";
Biochim. Biophys. Acta 1822:120-129(2012).
[28]
SUBUNIT, AND ZINC-BINDING SITES.
PubMed=22890888; DOI=10.1007/s10930-012-9439-0;
Karmakar S., Das K.P.;
"Identification of histidine residues involved in Zn(2+) binding to
alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF
mass spectrometry.";
Protein J. 31:623-640(2012).
[29]
INTERACTION WITH TMEM109.
PubMed=23542032; DOI=10.1016/j.febslet.2013.03.024;
Yamashita A., Taniwaki T., Kaikoi Y., Yamazaki T.;
"Protective role of the endoplasmic reticulum protein mitsugumin23
against ultraviolet C-induced cell death.";
FEBS Lett. 587:1299-1303(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND 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).
[31]
INTERACTION WITH DES.
PubMed=28470624; DOI=10.1007/s12192-017-0788-7;
Sharma S., Conover G.M., Elliott J.L., Der Perng M., Herrmann H.,
Quinlan R.A.;
"alphaB-crystallin is a sensor for assembly intermediates and for the
subunit topology of desmin intermediate filaments.";
Cell Stress Chaperones 22:613-626(2017).
[32]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN RESTRICTIVE
CARDIOMYOPATHY, VARIANT GLY-109, AND CHARACTERIZATION OF VARIANT
GLY-109 AND GLY-120.
PubMed=28493373; DOI=10.1002/humu.23248;
Brodehl A., Gaertner-Rommel A., Klauke B., Grewe S.A., Schirmer I.,
Peterschroeder A., Faber L., Vorgerd M., Gummert J., Anselmetti D.,
Schulz U., Paluszkiewicz L., Milting H.;
"The novel alphaB-crystallin (CRYAB) mutation p.D109G causes
restrictive cardiomyopathy.";
Hum. Mutat. 38:947-952(2017).
[33]
VARIANT MFM2 GLY-120.
PubMed=9731540; DOI=10.1038/1765;
Vicart P., Caron A., Guicheney P., Li Z., Prevost M.-C., Faure A.,
Chateau D., Chapon F., Tome F., Dupret J.-M., Paulin D., Fardeau M.;
"A missense mutation in the alphaB-crystallin chaperone gene causes a
desmin-related myopathy.";
Nat. Genet. 20:92-95(1998).
[34]
CHARACTERIZATION OF VARIANTS MFM2 GLY-120.
PubMed=12601044; DOI=10.1167/iovs.02-0950;
Fu L., Liang J.J.-N.;
"Alteration of protein-protein interactions of congenital cataract
crystallin mutants.";
Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003).
[35]
X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, AND
HOMODIMERIZATION.
PubMed=19646995; DOI=10.1016/j.jmb.2009.07.069;
Bagneris C., Bateman O.A., Naylor C.E., Cronin N., Boelens W.C.,
Keep N.H., Slingsby C.;
"Crystal structures of alpha-crystallin domain dimers of alphaB-
crystallin and Hsp20.";
J. Mol. Biol. 392:1242-1252(2009).
[36]
VARIANT CMD1II HIS-157.
PubMed=16483541; DOI=10.1016/j.bbrc.2006.01.154;
Inagaki N., Hayashi T., Arimura T., Koga Y., Takahashi M., Shibata H.,
Teraoka K., Chikamori T., Yamashina A., Kimura A.;
"Alpha B-crystallin mutation in dilated cardiomyopathy.";
Biochem. Biophys. Res. Commun. 342:379-386(2006).
[37]
VARIANT CMD1II SER-154.
PubMed=16793013; DOI=10.1016/j.bbrc.2006.05.203;
Pilotto A., Marziliano N., Pasotti M., Grasso M., Costante A.M.,
Arbustini E.;
"alphaB-crystallin mutation in dilated cardiomyopathies: low
prevalence in a consecutive series of 200 unrelated probands.";
Biochem. Biophys. Res. Commun. 346:1115-1117(2006).
[38]
VARIANT MFM2 HIS-109.
PubMed=21920752; DOI=10.1016/j.nmd.2011.07.004;
Sacconi S., Feasson L., Antoine J.C., Pecheux C., Bernard R.,
Cobo A.M., Casarin A., Salviati L., Desnuelle C., Urtizberea A.;
"A novel CRYAB mutation resulting in multisystemic disease.";
Neuromuscul. Disord. 22:66-72(2012).
-!- FUNCTION: May contribute to the transparency and refractive index
of the lens. Has chaperone-like activity, preventing aggregation
of various proteins under a wide range of stress conditions.
-!- SUBUNIT: Heteropolymer composed of three CRYAA and one CRYAB
subunits (PubMed:20836128). Aggregates with homologous proteins,
including the small heat shock protein HSPB1, to form large
heteromeric complexes (PubMed:10751411). Inter-subunit bridging
via zinc ions enhances stability, which is crucial as there is no
protein turn over in the lens (PubMed:22890888). Interacts with
HSPBAP1 and TTN/titin (PubMed:14676215). Interacts with TMEM109
(PubMed:23542032). Interacts with DES; binds rapidly during early
stages of DES filament assembly and a reduced binding seen in the
later stages (PubMed:28470624). {ECO:0000269|PubMed:10751411,
ECO:0000269|PubMed:14676215, ECO:0000269|PubMed:20836128,
ECO:0000269|PubMed:22890888, ECO:0000269|PubMed:23542032,
ECO:0000269|PubMed:28470624}.
-!- INTERACTION:
Self; NbExp=27; IntAct=EBI-739060, EBI-739060;
P02489:CRYAA; NbExp=19; IntAct=EBI-739060, EBI-6875961;
P05813:CRYBA1; NbExp=2; IntAct=EBI-739060, EBI-7043337;
P07315:CRYGC; NbExp=3; IntAct=EBI-739060, EBI-6875941;
P22914:CRYGS; NbExp=2; IntAct=EBI-739060, EBI-11308647;
P04792:HSPB1; NbExp=5; IntAct=EBI-739060, EBI-352682;
Q16082:HSPB2; NbExp=3; IntAct=EBI-739060, EBI-739395;
O14558:HSPB6; NbExp=4; IntAct=EBI-739060, EBI-739095;
Q9UJY1:HSPB8; NbExp=2; IntAct=EBI-739060, EBI-739074;
Q3UBX0:Tmem109 (xeno); NbExp=2; IntAct=EBI-739060, EBI-2366300;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326,
ECO:0000269|PubMed:28493373}. Nucleus
{ECO:0000269|PubMed:19464326}. Note=Translocates to the nucleus
during heat shock and resides in sub-nuclear structures known as
SC35 speckles or nuclear splicing speckles (PubMed:19464326).
Localizes at the Z-bands and the intercalated disk in
cardiomyocytes (PubMed:28493373). {ECO:0000269|PubMed:19464326,
ECO:0000269|PubMed:28493373}.
-!- TISSUE SPECIFICITY: Lens as well as other tissues (PubMed:838078,
PubMed:2387586). Expressed in myocardial tissue (PubMed:28493373).
{ECO:0000269|PubMed:2387586, ECO:0000269|PubMed:28493373,
ECO:0000269|PubMed:838078}.
-!- MASS SPECTROMETRY: Mass=20201; Method=Electrospray; Range=1-175;
Evidence={ECO:0000269|PubMed:10930324,
ECO:0000269|PubMed:8175657};
-!- MASS SPECTROMETRY: Mass=20281; Method=Electrospray; Range=1-175;
Note=With 1 phosphate group.;
Evidence={ECO:0000269|PubMed:10930324,
ECO:0000269|PubMed:8175657};
-!- MASS SPECTROMETRY: Mass=20360; Method=Electrospray; Range=1-175;
Note=With 2 phosphate groups.;
Evidence={ECO:0000269|PubMed:8175657};
-!- MASS SPECTROMETRY: Mass=20199; Method=Electrospray; Range=1-175;
Evidence={ECO:0000269|PubMed:10930324,
ECO:0000269|PubMed:8175657};
-!- MASS SPECTROMETRY: Mass=20278; Method=Electrospray; Range=1-175;
Note=With 1 phosphate group.;
Evidence={ECO:0000269|PubMed:10930324,
ECO:0000269|PubMed:8175657};
-!- DISEASE: Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A form of
myofibrillar myopathy, a group of chronic neuromuscular disorders
characterized at ultrastructural level by disintegration of the
sarcomeric Z disc and myofibrils, and replacement of the normal
myofibrillar markings by small dense granules, or larger hyaline
masses, or amorphous material. MFM2 is characterized by weakness
of the proximal and distal limb muscles, weakness of the neck,
velopharynx and trunk muscles, hypertrophic cardiomyopathy, and
cataract in a subset of patients. {ECO:0000269|PubMed:12601044,
ECO:0000269|PubMed:14681890, ECO:0000269|PubMed:21920752,
ECO:0000269|PubMed:9731540}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cataract 16, multiple types (CTRCT16) [MIM:613763]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. In general, the more posteriorly located
and dense an opacity, the greater the impact on visual function.
CTRCT16 includes posterior polar cataract, among others. Posterior
polar cataract is a subcapsular opacity, usually disk-shaped,
located at the back of the lens. {ECO:0000269|PubMed:11577372}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=CRYAB mutations may be involved in restrictive
cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM
is characterized by restrictive ventricular-filling physiology in
the presence of normal or reduced diastolic and/or systolic
volumes (of 1 or both ventricles), biatrial enlargement, and
normal ventricular wall thickness. {ECO:0000269|PubMed:28493373}.
-!- DISEASE: Myopathy, myofibrillar, fatal infantile hypertonic,
alpha-B crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A form of
myofibrillar myopathy, a group of chronic neuromuscular disorders
characterized at ultrastructural level by disintegration of the
sarcomeric Z disc and myofibrils, and replacement of the normal
myofibrillar markings by small dense granules, or larger hyaline
masses, or amorphous material. MFMFIH-CRYAB has onset in the first
weeks of life after a normal neonatal period. Affected infants
show rapidly progressive muscular rigidity of the trunk and limbs
associated with increasing respiratory difficulty resulting in
death before age 3 years. {ECO:0000269|PubMed:21337604}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:16483541, ECO:0000269|PubMed:16793013}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
family. {ECO:0000255|PROSITE-ProRule:PRU00285}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CRYABID40156ch11q23.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M28638; AAA52104.1; -; Genomic_DNA.
EMBL; S45630; AAB23453.1; -; mRNA.
EMBL; AF007162; AAC19161.1; -; mRNA.
EMBL; AK314029; BAG36739.1; -; mRNA.
EMBL; BT006770; AAP35416.1; -; mRNA.
EMBL; EF444955; ACA05949.1; -; Genomic_DNA.
EMBL; CH471065; EAW67162.1; -; Genomic_DNA.
EMBL; BC007008; AAH07008.1; -; mRNA.
EMBL; M24906; AAA60267.1; -; mRNA.
CCDS; CCDS8351.1; -.
PIR; A35332; CYHUAB.
RefSeq; NP_001276736.1; NM_001289807.1.
RefSeq; NP_001276737.1; NM_001289808.1.
RefSeq; NP_001876.1; NM_001885.2.
RefSeq; XP_011540910.1; XM_011542608.1.
UniGene; Hs.53454; -.
UniGene; Hs.703770; -.
PDB; 2KLR; NMR; -; A/B=1-175.
PDB; 2N0K; NMR; -; A/B=64-152.
PDB; 2WJ7; X-ray; 2.63 A; A/B/C/D/E=67-157.
PDB; 2Y1Y; X-ray; 2.00 A; A=71-157.
PDB; 2Y1Z; X-ray; 2.50 A; A/B=67-157.
PDB; 2Y22; X-ray; 3.70 A; A/B/C/D/E/F=67-157.
PDB; 2YGD; EM; 9.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175.
PDB; 3J07; Other; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175.
PDB; 3L1G; X-ray; 3.32 A; A=68-162.
PDB; 3SGM; X-ray; 1.70 A; A/B/C/D=90-100.
PDB; 3SGN; X-ray; 2.81 A; A/B=90-100.
PDB; 3SGO; X-ray; 2.56 A; A=90-100.
PDB; 3SGP; X-ray; 1.40 A; A/B/C/D=90-100.
PDB; 3SGR; X-ray; 2.17 A; A/B/C/D/E/F=90-100.
PDB; 3SGS; X-ray; 1.70 A; A=95-100.
PDB; 4M5S; X-ray; 1.37 A; A=68-153, B=156-164.
PDB; 4M5T; X-ray; 2.00 A; A/C/E/G=68-153, B/D/F/H=156-164.
PDB; 5VVV; X-ray; 2.80 A; B/D=38-50.
PDBsum; 2KLR; -.
PDBsum; 2N0K; -.
PDBsum; 2WJ7; -.
PDBsum; 2Y1Y; -.
PDBsum; 2Y1Z; -.
PDBsum; 2Y22; -.
PDBsum; 2YGD; -.
PDBsum; 3J07; -.
PDBsum; 3L1G; -.
PDBsum; 3SGM; -.
PDBsum; 3SGN; -.
PDBsum; 3SGO; -.
PDBsum; 3SGP; -.
PDBsum; 3SGR; -.
PDBsum; 3SGS; -.
PDBsum; 4M5S; -.
PDBsum; 4M5T; -.
PDBsum; 5VVV; -.
DisProt; DP00445; -.
ProteinModelPortal; P02511; -.
SMR; P02511; -.
BioGrid; 107800; 111.
CORUM; P02511; -.
DIP; DIP-35017N; -.
IntAct; P02511; 25.
MINT; MINT-221013; -.
STRING; 9606.ENSP00000227251; -.
ChEMBL; CHEMBL3621022; -.
iPTMnet; P02511; -.
PhosphoSitePlus; P02511; -.
UniCarbKB; P02511; -.
BioMuta; CRYAB; -.
DMDM; 117385; -.
REPRODUCTION-2DPAGE; IPI00021369; -.
SWISS-2DPAGE; P02511; -.
UCD-2DPAGE; P02511; -.
EPD; P02511; -.
PaxDb; P02511; -.
PeptideAtlas; P02511; -.
PRIDE; P02511; -.
DNASU; 1410; -.
Ensembl; ENST00000227251; ENSP00000227251; ENSG00000109846.
Ensembl; ENST00000526180; ENSP00000436051; ENSG00000109846.
Ensembl; ENST00000527950; ENSP00000437149; ENSG00000109846.
Ensembl; ENST00000531198; ENSP00000434247; ENSG00000109846.
Ensembl; ENST00000533475; ENSP00000433560; ENSG00000109846.
Ensembl; ENST00000616970; ENSP00000483554; ENSG00000109846.
GeneID; 1410; -.
KEGG; hsa:1410; -.
CTD; 1410; -.
DisGeNET; 1410; -.
EuPathDB; HostDB:ENSG00000109846.7; -.
GeneCards; CRYAB; -.
GeneReviews; CRYAB; -.
HGNC; HGNC:2389; CRYAB.
HPA; CAB002053; -.
HPA; CAB040560; -.
HPA; HPA057100; -.
MalaCards; CRYAB; -.
MIM; 123590; gene.
MIM; 608810; phenotype.
MIM; 613763; phenotype.
MIM; 613869; phenotype.
MIM; 615184; phenotype.
neXtProt; NX_P02511; -.
OpenTargets; ENSG00000109846; -.
Orphanet; 399058; Alpha-B crystallin-related late-onset distal myopathy.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 280553; Fatal infantile hypertonic myofibrillar myopathy.
Orphanet; 98993; Posterior polar cataract.
Orphanet; 98995; Zonular cataract.
PharmGKB; PA26907; -.
eggNOG; KOG3591; Eukaryota.
eggNOG; ENOG410YERS; LUCA.
GeneTree; ENSGT00760000119238; -.
HOVERGEN; HBG054766; -.
InParanoid; P02511; -.
KO; K09542; -.
OMA; TAPMKKL; -.
OrthoDB; EOG091G0USC; -.
PhylomeDB; P02511; -.
TreeFam; TF105049; -.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
SIGNOR; P02511; -.
ChiTaRS; CRYAB; human.
EvolutionaryTrace; P02511; -.
GeneWiki; CRYAB; -.
GenomeRNAi; 1410; -.
PMAP-CutDB; P02511; -.
PRO; PR:P02511; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000109846; -.
CleanEx; HS_CRYAB; -.
ExpressionAtlas; P02511; baseline and differential.
Genevisible; P02511; HS.
GO; GO:0032432; C:actin filament bundle; IEA:Ensembl.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0097512; C:cardiac myofibril; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0031430; C:M band; IEA:Ensembl.
GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IPI:ARUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
GO; GO:0051082; F:unfolded protein binding; IPI:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
GO; GO:0031109; P:microtubule polymerization or depolymerization; IEA:Ensembl.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:ARUK-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0032387; P:negative regulation of intracellular transport; IDA:HGNC.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IDA:ARUK-UCL.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0006457; P:protein folding; NAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:0010941; P:regulation of cell death; IMP:MGI.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl.
GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR002068; A-crystallin/Hsp20_dom.
InterPro; IPR001436; Alpha-crystallin/HSP.
InterPro; IPR003090; Alpha-crystallin_N.
InterPro; IPR031107; HSP20.
InterPro; IPR008978; HSP20-like_chaperone.
PANTHER; PTHR11527; PTHR11527; 1.
Pfam; PF00525; Crystallin; 1.
Pfam; PF00011; HSP20; 1.
PIRSF; PIRSF036514; Sm_HSP_B1; 1.
PRINTS; PR00299; ACRYSTALLIN.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS01031; SHSP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cardiomyopathy; Cataract; Chaperone;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Eye lens protein; Glycoprotein; Metal-binding;
Myofibrillar myopathy; Nucleus; Oxidation; Phosphoprotein;
Polymorphism; Reference proteome; Zinc.
CHAIN 1 175 Alpha-crystallin B chain.
/FTId=PRO_0000125907.
DOMAIN 56 164 sHSP. {ECO:0000255|PROSITE-
ProRule:PRU00285}.
METAL 83 83 Zinc 1. {ECO:0000250}.
METAL 104 104 Zinc 2. {ECO:0000305}.
METAL 106 106 Zinc 2. {ECO:0000250}.
METAL 111 111 Zinc 1. {ECO:0000305}.
METAL 119 119 Zinc 1. {ECO:0000305}.
SITE 48 48 Susceptible to oxidation.
SITE 60 60 Susceptible to oxidation.
SITE 68 68 Susceptible to oxidation.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:8142454,
ECO:0000269|PubMed:838078}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000269|PubMed:8175657}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000269|PubMed:11158243,
ECO:0000269|PubMed:8175657}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11158243,
ECO:0000269|PubMed:8175657}.
MOD_RES 92 92 N6-acetyllysine; partial.
{ECO:0000269|PubMed:11369851,
ECO:0000269|PubMed:22120592}.
MOD_RES 166 166 N6-acetyllysine.
{ECO:0000269|PubMed:22120592}.
CARBOHYD 170 170 O-linked (GlcNAc) threonine.
{ECO:0000250}.
VARIANT 41 41 S -> Y (in dbSNP:rs2234703).
/FTId=VAR_014607.
VARIANT 51 51 P -> L (in dbSNP:rs2234704).
/FTId=VAR_014608.
VARIANT 109 109 D -> G (probable disease-associated
mutation found in patients with
restrictive cardiomyopathy; reduces CRYAB
and DES localization at the Z-bands and
the intercalated disk in the myocardium;
cytoplasmic aggregations of CRYAB and
DES). {ECO:0000269|PubMed:28493373}.
/FTId=VAR_079841.
VARIANT 109 109 D -> H (in MFM2; dbSNP:rs387907339).
{ECO:0000269|PubMed:21920752}.
/FTId=VAR_069528.
VARIANT 120 120 R -> G (in MFM2; decreased interactions
with wild-type CRYAA and CRYAB but
increased interactions with wild-type
CRYBB2 and CRYGC; cytoplasmic
aggregation; dbSNP:rs104894201).
{ECO:0000269|PubMed:12601044,
ECO:0000269|PubMed:28493373,
ECO:0000269|PubMed:9731540}.
/FTId=VAR_007899.
VARIANT 154 154 G -> S (in CMD1II; dbSNP:rs150516929).
{ECO:0000269|PubMed:16793013}.
/FTId=VAR_070035.
VARIANT 157 157 R -> H (in CMD1II; dbSNP:rs141638421).
{ECO:0000269|PubMed:16483541}.
/FTId=VAR_070036.
CONFLICT 165 165 E -> K (in Ref. 4; AAC19161).
{ECO:0000305}.
CONFLICT 175 175 K -> KKMPFLELHFLKQESFPTSE (in Ref. 4;
AAC19161). {ECO:0000305}.
STRAND 68 70 {ECO:0000244|PDB:4M5S}.
STRAND 72 80 {ECO:0000244|PDB:4M5S}.
STRAND 82 84 {ECO:0000244|PDB:2N0K}.
HELIX 86 88 {ECO:0000244|PDB:4M5S}.
STRAND 89 94 {ECO:0000244|PDB:4M5S}.
STRAND 97 109 {ECO:0000244|PDB:4M5S}.
STRAND 112 123 {ECO:0000244|PDB:4M5S}.
TURN 125 127 {ECO:0000244|PDB:2KLR}.
HELIX 130 132 {ECO:0000244|PDB:4M5S}.
STRAND 134 137 {ECO:0000244|PDB:4M5S}.
STRAND 141 148 {ECO:0000244|PDB:4M5S}.
STRAND 157 159 {ECO:0000244|PDB:4M5T}.
STRAND 161 163 {ECO:0000244|PDB:4M5T}.
SEQUENCE 175 AA; 20159 MW; AE08BED46B7849CB CRC64;
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW
FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK


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