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Keratin, type II cytoskeletal 5 (58 kDa cytokeratin) (Cytokeratin-5) (CK-5) (Keratin-5) (K5) (Type-II keratin Kb5)

 K2C5_HUMAN              Reviewed;         590 AA.
P13647; Q6PI71; Q6UBJ0; Q8TA91;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 3.
25-OCT-2017, entry version 205.
RecName: Full=Keratin, type II cytoskeletal 5;
AltName: Full=58 kDa cytokeratin;
AltName: Full=Cytokeratin-5;
Short=CK-5;
AltName: Full=Keratin-5;
Short=K5;
AltName: Full=Type-II keratin Kb5;
Name=KRT5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-79 AND THR-387.
PubMed=2456903; DOI=10.1089/dna.1.1988.7.337;
Eckert R.L., Rorke E.A.;
"The sequence of the human epidermal 58-kD (#5) type II keratin
reveals an absence of 5' upstream sequence conservation between
coexpressed epidermal keratins.";
DNA 7:337-345(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-197.
PubMed=2476664; DOI=10.1128/MCB.9.9.3685;
Lersch R., Stellmach V., Stocks X., Giudice G., Fuchs E.;
"Isolation, sequence, and expression of a human keratin K5 gene:
transcriptional regulation of keratins and insights into pairwise
control.";
Mol. Cell. Biol. 9:3685-3697(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-79 AND THR-387.
PubMed=10903910; DOI=10.1006/bbrc.2000.3110;
Whittock N.V., Eady R.A.J., McGrath J.A.;
"Genomic organization and amplification of the human epidermal type II
keratin genes K1 and K5.";
Biochem. Biophys. Res. Commun. 274:149-152(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-528 AND
SER-543.
TISSUE=Brain, and Pancreas;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 83-590, AND VARIANT GLU-197.
PubMed=2447486; DOI=10.1128/MCB.8.1.486;
Lersch R., Fuchs E.;
"Sequence and expression of a type II keratin, K5, in human epidermal
cells.";
Mol. Cell. Biol. 8:486-493(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 186-256, AND VARIANT WC-EBS THR-199.
PubMed=14723728; DOI=10.1111/j.1365-2230.2004.01434.x;
Xu Z., Dong H., Sun X., Zhu X., Yang Y.;
"A new keratin 5 mutation (K199T) in a family with Weber-Cockayne
epidermolysis bullosa simplex.";
Clin. Exp. Dermatol. 29:74-76(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 348-590, AND VARIANT SER-543.
PubMed=2455002; DOI=10.1111/1523-1747.ep12463286;
Galup C., Darmon M.Y.;
"Isolation and characterization of a cDNA clone coding for human
epidermal keratin K5. Sequence of the carboxyterminal half of this
keratin.";
J. Invest. Dermatol. 91:39-42(1988).
[8]
INTERACTION WITH TCHP.
PubMed=15731013; DOI=10.1242/jcs.01667;
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
Usukura J., Inagaki M.;
"Identification of trichoplein, a novel keratin filament-binding
protein.";
J. Cell Sci. 118:1081-1090(2005).
[9]
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).
[10]
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).
[11]
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).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 350-477 IN COMPLEX WITH
KRT14.
PubMed=22705788; DOI=10.1038/nsmb.2330;
Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.;
"Structural basis for heteromeric assembly and perinuclear
organization of keratin filaments.";
Nat. Struct. Mol. Biol. 19:707-715(2012).
[13]
VARIANT DM-EBS GLY-475.
PubMed=1372711; DOI=10.1038/356244a0;
Lane E.B., Rugg E.L., Navsaria H.A., Leigh I.M., Heagerty A.H.M.,
Ishida-Yamamoto A., Eady R.A.J.;
"A mutation in the conserved helix termination peptide of keratin 5 in
hereditary skin blistering.";
Nature 356:244-246(1992).
[14]
VARIANT K-EBS PRO-463.
PubMed=7686424; DOI=10.1002/humu.1380020206;
Dong W., Ryynaenen M., Uitto J.;
"Identification of a leucine-to-proline mutation in the keratin 5 gene
in a family with the generalized Kobner type of epidermolysis bullosa
simplex.";
Hum. Mutat. 2:94-102(1993).
[15]
VARIANT GLU-138.
PubMed=7684424; DOI=10.1111/1523-1747.ep12475671;
Wanner R., Foerster H.-H., Tilmans I., Mischke D.;
"Allelic variations of human keratins K4 and K5 provide polymorphic
markers within the type II keratin gene cluster on chromosome 12.";
J. Invest. Dermatol. 100:735-741(1993).
[16]
VARIANT DM-EBS LYS-193.
Smith F.J.D., Morley S.M., Rugg E.L., Navsaria H.A., Leigh I.M.,
Eady R.A.J., Tidman M.J., Lane E.B.;
"Clustering of epidermolysis bullosa simplex mutations in relation to
disease phenotype: data from Weber-Cockayne EBS.";
J. Invest. Dermatol. 101:481A-481A(1993).
[17]
VARIANT WC-EBS CYS-331.
PubMed=7506097; DOI=10.1038/ng1193-294;
Rugg E.L., Morley S.M., Smith F.J.D., Boxer M., Tidman M.J.,
Navsaria H.A., Leigh I.M., Lane E.B.;
"Missing links: Weber-Cockayne keratin mutations implicate the L12
linker domain in effective cytoskeleton function.";
Nat. Genet. 5:294-300(1993).
[18]
VARIANT WC-EBS SER-161.
PubMed=7688477; DOI=10.1073/pnas.90.15.7414;
Chan Y.-M., Yu Q.-C., Fine J.-D., Fuchs E.;
"The genetic basis of Weber-Cockayne epidermolysis bullosa simplex.";
Proc. Natl. Acad. Sci. U.S.A. 90:7414-7418(1993).
[19]
VARIANTS WC-EBS THR-327 AND LYS-329.
PubMed=7520042;
Chan Y.-M., Yu Q.-C., LeBlanc-Straceski J., Christiano A.,
Pulkkinen L., Kucherlapati R.S., Uitto J., Fuchs E.;
"Mutations in the non-helical linker segment L1-2 of keratin 5 in
patients with Weber-Cockayne epidermolysis bullosa simplex.";
J. Cell Sci. 107:765-774(1994).
[20]
VARIANT K-EBS ASN-173.
PubMed=7534039;
Stephens K., Zlotogorski A., Smith L., Ehrlich P., Wijsman E.M.,
Livingston R.J., Sybert V.P.;
"Epidermolysis bullosa simplex: a keratin 5 mutation is a fully
dominant allele in epidermal cytoskeleton function.";
Am. J. Hum. Genet. 56:577-585(1995).
[21]
VARIANT WC-EBS VAL-328.
PubMed=8595431; DOI=10.1093/hmg/4.10.1999;
Matsuki M., Hashimoto K., Yoshikawa K., Yasuno H., Yamanishi K.;
"Epidermolysis bullosa simplex (Weber-Cockayne) associated with a
novel missense mutation of Asp328 to Val in linker 12 domain of
keratin 5.";
Hum. Mol. Genet. 4:1999-2000(1995).
[22]
VARIANTS WC-EBS LYS-193 AND THR-327.
PubMed=8807337;
DOI=10.1002/(SICI)1098-1004(1996)8:1<57::AID-HUMU8>3.0.CO;2-M;
Humphries M.M., Mansergh F.C., Kiang A.-S., Jordan S.A., Sheils D.M.,
Martin M.J., Farrar G.J., Kenna P.F., Young M.M., Humphries P.;
"Three keratin gene mutations account for the majority of dominant
simplex epidermolysis bullosa cases within the population of
Ireland.";
Hum. Mutat. 8:57-63(1996).
[23]
VARIANT DM-EBS PHE-175.
PubMed=8757772; DOI=10.1111/1523-1747.ep12329741;
Nomura K., Shimizu H., Meng X., Umeki K., Tamai K., Sawamura D.,
Nagao K., Kawakami T., Nishikawa T., Hashimoto I.;
"A novel keratin K5 gene mutation in Dowling-Meara epidermolysis
bullosa simplex.";
J. Invest. Dermatol. 107:253-254(1996).
[24]
VARIANT MP-EBS LEU-25.
PubMed=8799157; DOI=10.1073/pnas.93.17.9079;
Uttam J., Hutton M.E., Coulombe P.A., Anton-Lamprecht I., Yu Q.-C.,
Gedde-Dahl T. Jr., Fine J.-D., Fuchs E.;
"The genetic basis of epidermolysis bullosa simplex with mottled
pigmentation.";
Proc. Natl. Acad. Sci. U.S.A. 93:9079-9084(1996).
[25]
VARIANTS DM-EBS SER-176; SER-179 AND LYS-477.
PubMed=9036937; DOI=10.1111/1523-1747.ep12286486;
Stephens K., Ehrlich P., Weaver M., Le R., Spencer A., Sybert V.P.;
"Primers for exon-specific amplification of the KRT5 gene:
identification of novel and recurrent mutations in epidermolysis
bullosa simplex patients.";
J. Invest. Dermatol. 108:349-353(1997).
[26]
VARIANT DM-EBS THR-467.
PubMed=9406827; DOI=10.1111/1523-1747.ep12341024;
Irvine A.D., McKenna K.E., Bingham A., Nevin N.C., Hughes A.E.;
"A novel mutation in the helix termination peptide of keratin 5
causing epidermolysis bullosa simplex Dowling-Meara.";
J. Invest. Dermatol. 109:815-816(1997).
[27]
VARIANT K-EBS ALA-323.
PubMed=9740251; DOI=10.1046/j.1523-1747.1998.00308.x;
Galligan P., Listwan P., Siller G.M., Rothnagel J.A.;
"A novel mutation in the L12 domain of keratin 5 in the Koebner
variant of epidermolysis bullosa simplex.";
J. Invest. Dermatol. 111:524-527(1998).
[28]
VARIANTS WC-EBS LEU-152; LYS-327 AND HIS-328.
PubMed=9804357; DOI=10.1046/j.1523-1747.1998.00374.x;
Mueller F.B., Kuester W., Bruckner-Tuderman L., Korge B.P.;
"Novel K5 and K14 mutations in German patients with the Weber-Cockayne
variant of epidermolysis bullosa simplex.";
J. Invest. Dermatol. 111:900-902(1998).
[29]
VARIANT MP-EBS LEU-25.
PubMed=10494094;
DOI=10.1002/(SICI)1096-8628(19991008)86:4<376::AID-AJMG12>3.0.CO;2-W;
Moog U., de Die-Smulders C.E.M., Scheffer H., van der Vlies P.,
Henquet C.J.M., Jonkman M.F.;
"Epidermolysis bullosa simplex with mottled pigmentation: clinical
aspects and confirmation of the P24L mutation in the KRT5 gene in
further patients.";
Am. J. Med. Genet. 86:376-379(1999).
[30]
VARIANT DM-EBS SER-176, AND VARIANT K-EBS PRO-325.
PubMed=9989794; DOI=10.1046/j.1523-1747.1999.00495.x;
Soerensen C.B., Ladekjaer-Mikkelsen A.-S., Andresen B.S., Brandrup F.,
Veien N.K., Buus S.K., Anton-Lamprecht I., Kruse T.A., Jensen P.K.A.,
Eiberg H., Bolund L., Gregersen N.;
"Identification of novel and known mutations in the genes for keratin
5 and 14 in Danish patients with epidermolysis bullosa simplex:
correlation between genotype and phenotype.";
J. Invest. Dermatol. 112:184-190(1999).
[31]
VARIANT DM-EBS PRO-181.
PubMed=10730767; DOI=10.1046/j.1365-2133.2000.03304.x;
Shemanko C.S., Horn H.M., Keohane S.G., Hepburn N., Kerr A.I.G.,
Atherton D.J., Tidman M.J., Lane E.B.;
"Laryngeal involvement in the Dowling-Meara variant of epidermolysis
bullosa simplex with keratin mutations of severely disruptive
potential.";
Br. J. Dermatol. 142:315-320(2000).
[32]
VARIANT WC-EBS GLU-328.
PubMed=10782015; DOI=10.1159/000022921;
Liovic M., Podrumac B., Dragos V., Vouk K., Komel R.;
"K5 D328E: a novel missense mutation in the linker 12 domain of
keratin 5 associated with epidermolysis bullosa simplex (Weber-
Cockayne).";
Hum. Hered. 50:234-236(2000).
[33]
VARIANT K-EBS LEU-186.
PubMed=11407988; DOI=10.1046/j.1523-1747.2001.01334.x;
Liovic M., Stojan J., Bowden P.E., Gibbs D., Vahlquist A., Lane E.B.,
Komel R.;
"A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a
conservative substitution can lead to development of different disease
phenotypes.";
J. Invest. Dermatol. 116:964-969(2001).
[34]
VARIANTS K-EBS LYS-170 AND LYS-418.
PubMed=11973334; DOI=10.1074/jbc.M200974200;
Yasukawa K., Sawamura D., McMillan J.R., Nakamura H., Shimizu H.;
"Dominant and recessive compound heterozygous mutations in
epidermolysis bullosa simplex demonstrate the role of the stutter
region in keratin intermediate filament assembly.";
J. Biol. Chem. 277:23670-23674(2002).
[35]
VARIANTS WC-EBS LYS-167; PRO-311 AND ASP-324.
PubMed=12707098; DOI=10.1001/archderm.139.4.498;
Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E.,
Petronius D., Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I.,
Uitto J., Sprecher E.;
"Epidermolysis bullosa simplex in Israel: clinical and genetic
features.";
Arch. Dermatol. 139:498-505(2003).
[36]
VARIANTS WC-EBS GLU-404 AND ASP-438, AND VARIANTS DM-EBS LYS-475 AND
LYS-477.
PubMed=12655565; DOI=10.1002/humu.9124;
Schuilenga-Hut P.H.L., Vlies P., Jonkman M.F., Waanders E.,
Buys C.H.C.M., Scheffer H.;
"Mutation analysis of the entire keratin 5 and 14 genes in patients
with epidermolysis bullosa simplex and identification of novel
mutations.";
Hum. Mutat. 21:447-447(2003).
[37]
INVOLVEMENT IN EBS WITH MIGRATORY CIRCINATE ERYTHEMA.
PubMed=12925204; DOI=10.1046/j.1523-1747.2003.12424.x;
Gu L.-H., Kim S.-C., Ichiki Y., Park J., Nagai M., Kitajima Y.;
"A usual frameshift and delayed termination codon mutation in keratin
5 causes a novel type of epidermolysis bullosa simplex with migratory
circinate erythema.";
J. Invest. Dermatol. 121:482-485(2003).
[38]
VARIANT WC-EBS GLY-328.
PubMed=15347343; DOI=10.1111/j.1365-2230.2004.01565.x;
Li J.-G., Feng J., Xiao S.-X., Ai Y.-L., Wang J.-M., Peng Z.-H.;
"A new mutation in the linker 12 domain of keratin 5 in a Chinese
family with Weber-Cockayne epidermolysis bullosa simplex.";
Clin. Exp. Dermatol. 29:539-541(2004).
[39]
VARIANT WC-EBS SER-177.
PubMed=15140024; DOI=10.1111/j.0906-6705.2004.00171.x;
Liovic M., Bowden P.E., Marks R., Komel R.;
"A mutation (N177S) in the structurally conserved helix initiation
peptide motif of keratin 5 causes a mild EBS phenotype.";
Exp. Dermatol. 13:332-334(2004).
[40]
INVOLVEMENT IN DDD1.
PubMed=16465624; DOI=10.1086/500850;
Betz R.C., Planko L., Eigelshoven S., Hanneken S., Pasternack S.M.,
Buessow H., Bogaert K.V., Wenzel J., Braun-Falco M., Ruetten A.,
Rogers M.A., Ruzicka T., Noethen M.M., Magin T.M., Kruse R.;
"Loss-of-function mutations in the keratin 5 gene lead to Dowling-
Degos disease.";
Am. J. Hum. Genet. 78:510-519(2006).
[41]
VARIANTS WC-EBS LEU-25; VAL-158 AND SER-352, VARIANTS K-EBS ASP-143;
MET-186; LEU-186; PRO-191 AND ASP-517, VARIANTS DM-EBS SER-176;
LYS-475 AND LYS-477, AND VARIANT MP-EBS LEU-25.
PubMed=16882168; DOI=10.1111/j.1365-2133.2006.07285.x;
Yasukawa K., Sawamura D., Goto M., Nakamura H., Jung S.-Y., Kim S.-C.,
Shimizu H.;
"Epidermolysis bullosa simplex in Japanese and Korean patients:
genetic studies in 19 cases.";
Br. J. Dermatol. 155:313-317(2006).
[42]
VARIANTS DM-EBS LYS-168; PRO-169 AND PRO-469, AND VARIANTS WC-EBS
LYS-190 AND HIS-331.
PubMed=16786515; DOI=10.1002/humu.9437;
Mueller F.B., Kuester W., Wodecki K., Almeida H. Jr.,
Bruckner-Tuderman L., Krieg T., Korge B.P., Arin M.J.;
"Novel and recurrent mutations in keratin KRT5 and KRT14 genes in
epidermolysis bullosa simplex: implications for disease phenotype and
keratin filament assembly.";
Hum. Mutat. 27:719-720(2006).
[43]
VARIANTS WC-EBS GLU-186; LYS-193; PRO-321; VAL-328 AND THR-428,
VARIANTS DM-EBS SER-165 AND LYS-477, VARIANT MP-EBS LEU-25, AND
VARIANT K-EBS PRO-463.
PubMed=21623745; DOI=10.1111/j.1365-2133.2011.10428.x;
Garcia M., Santiago J.L., Terron A., Hernandez-Martin A., Vicente A.,
Fortuny C., De Lucas R., Lopez J.C., Cuadrado-Corrales N., Holguin A.,
Illera N., Duarte B., Sanchez-Jimeno C., Llames S., Garcia E.,
Ayuso C., Martinez-Santamaria L., Castiglia D., De Luca N.,
Torrelo A., Mechan D., Baty D., Zambruno G., Escamez M.J., Del Rio M.;
"Two novel recessive mutations in KRT14 identified in a cohort of 21
Spanish families with epidermolysis bullosa simplex.";
Br. J. Dermatol. 165:683-692(2011).
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Keratin-5 associates with keratin-14. Interacts with TCHP.
Interacts with KEPPK1 (By similarity).
{ECO:0000250|UniProtKB:Q922U2, ECO:0000269|PubMed:15731013,
ECO:0000269|PubMed:22705788}.
-!- INTERACTION:
P18054:ALOX12; NbExp=7; IntAct=EBI-702187, EBI-1633210;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-702187, EBI-2125614;
P02533:KRT14; NbExp=8; IntAct=EBI-702187, EBI-702178;
P19012:KRT15; NbExp=7; IntAct=EBI-702187, EBI-739566;
P08727:KRT19; NbExp=4; IntAct=EBI-702187, EBI-742756;
Q7Z3Y8:KRT27; NbExp=4; IntAct=EBI-702187, EBI-3044087;
Q7Z3Y7:KRT28; NbExp=4; IntAct=EBI-702187, EBI-11980489;
Q15323:KRT31; NbExp=5; IntAct=EBI-702187, EBI-948001;
O76015:KRT38; NbExp=5; IntAct=EBI-702187, EBI-1047263;
Q6A162:KRT40; NbExp=5; IntAct=EBI-702187, EBI-10171697;
Q13835-2:PKP1; NbExp=2; IntAct=EBI-702187, EBI-9087684;
-!- DISEASE: Epidermolysis bullosa simplex, Dowling-Meara type (DM-
EBS) [MIM:131760]: A severe form of intraepidermal epidermolysis
bullosa characterized by generalized herpetiform blistering, milia
formation, dystrophic nails, and mucous membrane involvement.
{ECO:0000269|PubMed:10730767, ECO:0000269|PubMed:12655565,
ECO:0000269|PubMed:1372711, ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:8757772, ECO:0000269|PubMed:9036937,
ECO:0000269|PubMed:9406827, ECO:0000269|PubMed:9989794,
ECO:0000269|Ref.16}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa simplex, with migratory circinate
erythema (EBSMCE) [MIM:609352]: A form of intraepidermal
epidermolysis bullosa characterized by unusual migratory circinate
erythema. Skin lesions appear from birth primarily on the hands,
feet, and legs but spare nails, ocular epithelia and mucosae.
Lesions heal with brown pigmentation but no scarring. Electron
microscopy findings are distinct from those seen in the DM-EBS,
with no evidence of tonofilament clumping. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC-
EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa
characterized by blistering limited to palmar and plantar areas of
the skin. {ECO:0000269|PubMed:10782015,
ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098,
ECO:0000269|PubMed:14723728, ECO:0000269|PubMed:15140024,
ECO:0000269|PubMed:15347343, ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7520042,
ECO:0000269|PubMed:7688477, ECO:0000269|PubMed:8595431,
ECO:0000269|PubMed:8807337, ECO:0000269|PubMed:9804357}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Epidermolysis bullosa simplex, Koebner type (K-EBS)
[MIM:131900]: A form of intraepidermal epidermolysis bullosa
characterized by generalized skin blistering. The phenotype is not
fundamentally distinct from the Dowling-Meara type, although it is
less severe. {ECO:0000269|PubMed:11407988,
ECO:0000269|PubMed:11973334, ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:21623745, ECO:0000269|PubMed:7534039,
ECO:0000269|PubMed:7686424, ECO:0000269|PubMed:9740251,
ECO:0000269|PubMed:9989794}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa simplex, with mottled pigmentation
(MP-EBS) [MIM:131960]: A form of intraepidermal epidermolysis
bullosa characterized by blistering at acral sites and 'mottled'
pigmentation of the trunk and proximal extremities with hyper- and
hypopigmentation macules. {ECO:0000269|PubMed:10494094,
ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:8799157}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Dowling-Degos disease 1 (DDD1) [MIM:179850]: An autosomal
dominant genodermatosis. Affected individuals develop a
postpubertal reticulate hyperpigmentation that is progressive and
disfiguring, and small hyperkeratotic dark brown papules that
affect mainly the flexures and great skin folds. Patients usually
show no abnormalities of the hair or nails.
{ECO:0000269|PubMed:16465624}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-----------------------------------------------------------------------
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EMBL; M21389; AAA36143.1; -; mRNA.
EMBL; M28496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF274874; AAF97931.1; -; Genomic_DNA.
EMBL; BC024292; AAH24292.1; -; mRNA.
EMBL; BC042132; AAH42132.1; -; mRNA.
EMBL; BC071906; AAH71906.1; -; mRNA.
EMBL; M19723; AAA36145.1; -; mRNA.
EMBL; AY373434; AAQ81588.1; -; mRNA.
CCDS; CCDS8830.1; -.
PIR; A29904; A29904.
RefSeq; NP_000415.2; NM_000424.3.
UniGene; Hs.433845; -.
PDB; 3TNU; X-ray; 3.00 A; B=350-477.
PDBsum; 3TNU; -.
ProteinModelPortal; P13647; -.
SMR; P13647; -.
BioGrid; 110050; 64.
DIP; DIP-39N; -.
IntAct; P13647; 32.
STRING; 9606.ENSP00000252242; -.
Allergome; 415; Hom s 5.
iPTMnet; P13647; -.
PhosphoSitePlus; P13647; -.
SwissPalm; P13647; -.
BioMuta; KRT5; -.
DMDM; 143811411; -.
PaxDb; P13647; -.
PeptideAtlas; P13647; -.
PRIDE; P13647; -.
DNASU; 3852; -.
Ensembl; ENST00000252242; ENSP00000252242; ENSG00000186081.
GeneID; 3852; -.
KEGG; hsa:3852; -.
UCSC; uc001san.4; human.
CTD; 3852; -.
DisGeNET; 3852; -.
EuPathDB; HostDB:ENSG00000186081.11; -.
GeneCards; KRT5; -.
GeneReviews; KRT5; -.
H-InvDB; HIX0010655; -.
HGNC; HGNC:6442; KRT5.
HPA; CAB000027; -.
HPA; CAB000129; -.
HPA; HPA059479; -.
MalaCards; KRT5; -.
MIM; 131760; phenotype.
MIM; 131800; phenotype.
MIM; 131900; phenotype.
MIM; 131960; phenotype.
MIM; 148040; gene.
MIM; 179850; phenotype.
MIM; 609352; phenotype.
neXtProt; NX_P13647; -.
OpenTargets; ENSG00000186081; -.
Orphanet; 79145; Dowling-Degos disease.
Orphanet; 158681; Epidermolysis bullosa simplex with circinate migratory erythema.
Orphanet; 79397; Epidermolysis bullosa simplex with mottled pigmentation.
Orphanet; 79396; Epidermolysis bullosa simplex, Dowling-Meara type.
Orphanet; 79399; Generalized epidermolysis bullosa simplex, non-Dowling-Meara type.
Orphanet; 79400; Localized epidermolysis bullosa simplex.
PharmGKB; PA30230; -.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P13647; -.
KO; K07605; -.
OMA; YLYFNES; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P13647; -.
TreeFam; TF317854; -.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P13647; -.
ChiTaRS; KRT5; human.
GeneWiki; Keratin_5; -.
GenomeRNAi; 3852; -.
PRO; PR:P13647; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000186081; -.
CleanEx; HS_KRT5; -.
ExpressionAtlas; P13647; baseline and differential.
Genevisible; P13647; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
GO; GO:0045095; C:keratin filament; IDA:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
GO; GO:0031424; P:keratinization; TAS:Reactome.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Disease mutation;
Epidermolysis bullosa; Intermediate filament; Keratin; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 590 Keratin, type II cytoskeletal 5.
/FTId=PRO_0000063727.
DOMAIN 168 481 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 167 Head.
REGION 168 203 Coil 1A.
REGION 204 222 Linker 1.
REGION 223 315 Coil 1B.
REGION 316 338 Linker 12.
REGION 339 477 Coil 2.
REGION 478 590 Tail.
COMPBIAS 39 139 Gly-rich.
COMPBIAS 528 590 Ser-rich.
SITE 419 419 Stutter.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:Q922U2}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:Q922U2}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:Q922U2}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:Q922U2}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:Q922U2}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6Q2}.
VARIANT 25 25 P -> L (in MP-EBS; dbSNP:rs57499817).
{ECO:0000269|PubMed:10494094,
ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:8799157}.
/FTId=VAR_010453.
VARIANT 79 79 S -> R (in dbSNP:rs1065115).
{ECO:0000269|PubMed:10903910,
ECO:0000269|PubMed:2456903}.
/FTId=VAR_028763.
VARIANT 138 138 G -> E (in dbSNP:rs11170164).
{ECO:0000269|PubMed:7684424}.
/FTId=VAR_003871.
VARIANT 143 143 V -> D (in K-EBS; dbSNP:rs59851104).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031640.
VARIANT 152 152 P -> L (in WC-EBS; dbSNP:rs60617604).
{ECO:0000269|PubMed:9804357}.
/FTId=VAR_010454.
VARIANT 158 158 D -> V (in WC-EBS; dbSNP:rs61222761).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031641.
VARIANT 161 161 I -> S (in WC-EBS; dbSNP:rs58058996).
{ECO:0000269|PubMed:7688477}.
/FTId=VAR_003872.
VARIANT 165 165 R -> S (in DM-EBS; dbSNP:rs267607456).
{ECO:0000269|PubMed:21623745}.
/FTId=VAR_071630.
VARIANT 167 167 E -> K (in WC-EBS; dbSNP:rs57378129).
{ECO:0000269|PubMed:12707098}.
/FTId=VAR_026536.
VARIANT 168 168 E -> K (in DM-EBS; dbSNP:rs58619430).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027722.
VARIANT 169 169 R -> P (in DM-EBS; dbSNP:rs60720877).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027723.
VARIANT 170 170 E -> K (in K-EBS; dbSNP:rs59115483).
{ECO:0000269|PubMed:11973334}.
/FTId=VAR_026537.
VARIANT 173 173 K -> N (in K-EBS; dbSNP:rs58163069).
{ECO:0000269|PubMed:7534039}.
/FTId=VAR_010455.
VARIANT 175 175 L -> F (in DM-EBS; dbSNP:rs57890479).
{ECO:0000269|PubMed:8757772}.
/FTId=VAR_010456.
VARIANT 176 176 N -> S (in DM-EBS; dbSNP:rs59092197).
{ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:9036937,
ECO:0000269|PubMed:9989794}.
/FTId=VAR_010457.
VARIANT 177 177 N -> S (in WC-EBS; dbSNP:rs61495052).
{ECO:0000269|PubMed:15140024}.
/FTId=VAR_026538.
VARIANT 179 179 F -> S (in DM-EBS; dbSNP:rs57781042).
{ECO:0000269|PubMed:9036937}.
/FTId=VAR_010458.
VARIANT 181 181 S -> P (in DM-EBS; with laryngeal
involvement; dbSNP:rs60715293).
{ECO:0000269|PubMed:10730767}.
/FTId=VAR_010459.
VARIANT 186 186 V -> E (in WC-EBS; dbSNP:rs267607457).
{ECO:0000269|PubMed:21623745}.
/FTId=VAR_071631.
VARIANT 186 186 V -> L (in K-EBS; dbSNP:rs121912475).
{ECO:0000269|PubMed:11407988,
ECO:0000269|PubMed:16882168}.
/FTId=VAR_013829.
VARIANT 186 186 V -> M (in K-EBS; dbSNP:rs121912475).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031642.
VARIANT 190 190 E -> K (in WC-EBS; requires 2 nucleotide
substitutions; dbSNP:rs58976397).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027724.
VARIANT 191 191 Q -> P (in K-EBS; dbSNP:rs57751134).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031643.
VARIANT 193 193 N -> K (in DM-EBS and WC-EBS;
dbSNP:rs60586163).
{ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:8807337,
ECO:0000269|Ref.16}.
/FTId=VAR_003873.
VARIANT 197 197 D -> E (in dbSNP:rs641615).
{ECO:0000269|PubMed:2447486,
ECO:0000269|PubMed:2476664}.
/FTId=VAR_028764.
VARIANT 199 199 K -> T (in WC-EBS; dbSNP:rs58766676).
{ECO:0000269|PubMed:14723728}.
/FTId=VAR_026539.
VARIANT 232 232 S -> N (in dbSNP:rs3194286).
/FTId=VAR_028765.
VARIANT 311 311 L -> P (in WC-EBS; dbSNP:rs59864957).
{ECO:0000269|PubMed:12707098}.
/FTId=VAR_026540.
VARIANT 321 321 T -> P (in WC-EBS).
{ECO:0000269|PubMed:21623745}.
/FTId=VAR_071632.
VARIANT 323 323 V -> A (in K-EBS; dbSNP:rs59840738).
{ECO:0000269|PubMed:9740251}.
/FTId=VAR_010460.
VARIANT 324 324 V -> D (in WC-EBS; dbSNP:rs59335325).
{ECO:0000269|PubMed:12707098}.
/FTId=VAR_026541.
VARIANT 325 325 L -> P (in K-EBS; dbSNP:rs58107458).
{ECO:0000269|PubMed:9989794}.
/FTId=VAR_010461.
VARIANT 327 327 M -> K (in WC-EBS; dbSNP:rs58072617).
{ECO:0000269|PubMed:9804357}.
/FTId=VAR_010462.
VARIANT 327 327 M -> T (in WC-EBS; dbSNP:rs58072617).
{ECO:0000269|PubMed:7520042,
ECO:0000269|PubMed:8807337}.
/FTId=VAR_003874.
VARIANT 328 328 D -> E (in WC-EBS; dbSNP:rs59464425).
{ECO:0000269|PubMed:10782015}.
/FTId=VAR_026542.
VARIANT 328 328 D -> G (in WC-EBS; dbSNP:rs57142010).
{ECO:0000269|PubMed:15347343}.
/FTId=VAR_026543.
VARIANT 328 328 D -> H (in WC-EBS; dbSNP:rs56790237).
{ECO:0000269|PubMed:9804357}.
/FTId=VAR_010463.
VARIANT 328 328 D -> V (in WC-EBS; dbSNP:rs57142010).
{ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:8595431}.
/FTId=VAR_010464.
VARIANT 329 329 N -> K (in WC-EBS; dbSNP:rs59730172).
{ECO:0000269|PubMed:7520042}.
/FTId=VAR_010465.
VARIANT 331 331 R -> C (in WC-EBS; dbSNP:rs61297109).
{ECO:0000269|PubMed:7506097}.
/FTId=VAR_003875.
VARIANT 331 331 R -> H (in WC-EBS; dbSNP:rs56729325).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027725.
VARIANT 352 352 R -> S (in WC-EBS; dbSNP:rs59112594).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031644.
VARIANT 387 387 S -> T (in dbSNP:rs2669875).
{ECO:0000269|PubMed:10903910,
ECO:0000269|PubMed:2456903}.
/FTId=VAR_028766.
VARIANT 404 404 K -> E (in WC-EBS; dbSNP:rs60809982).
{ECO:0000269|PubMed:12655565}.
/FTId=VAR_023726.
VARIANT 418 418 E -> K (in K-EBS; dbSNP:rs121912476).
{ECO:0000269|PubMed:11973334}.
/FTId=VAR_026544.
VARIANT 428 428 A -> T (in WC-EBS; dbSNP:rs267607458).
{ECO:0000269|PubMed:21623745}.
/FTId=VAR_071633.
VARIANT 438 438 A -> D (in WC-EBS; dbSNP:rs57845028).
{ECO:0000269|PubMed:12655565}.
/FTId=VAR_023727.
VARIANT 463 463 L -> P (in K-EBS; dbSNP:rs57599352).
{ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:7686424}.
/FTId=VAR_003876.
VARIANT 467 467 I -> T (in DM-EBS; dbSNP:rs60271599).
{ECO:0000269|PubMed:9406827}.
/FTId=VAR_010466.
VARIANT 469 469 T -> P (in DM-EBS; dbSNP:rs60596287).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027726.
VARIANT 475 475 E -> G (in DM-EBS; dbSNP:rs61348633).
{ECO:0000269|PubMed:1372711}.
/FTId=VAR_003877.
VARIANT 475 475 E -> K (in DM-EBS; dbSNP:rs57155193).
{ECO:0000269|PubMed:12655565,
ECO:0000269|PubMed:16882168}.
/FTId=VAR_023728.
VARIANT 477 477 E -> K (in DM-EBS; dbSNP:rs59190510).
{ECO:0000269|PubMed:12655565,
ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:21623745,
ECO:0000269|PubMed:9036937}.
/FTId=VAR_010467.
VARIANT 517 517 G -> D (in K-EBS; dbSNP:rs58608695).
{ECO:0000269|PubMed:16882168}.
/FTId=VAR_031645.
VARIANT 528 528 S -> G (in dbSNP:rs11549950).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028767.
VARIANT 543 543 G -> S (in dbSNP:rs11549949).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2455002}.
/FTId=VAR_028768.
CONFLICT 9 11 FRS -> SGA (in Ref. 2). {ECO:0000305}.
CONFLICT 261 261 E -> Q (in Ref. 5; AAA36145).
{ECO:0000305}.
CONFLICT 271 271 E -> H (in Ref. 5; AAA36145).
{ECO:0000305}.
CONFLICT 375 375 H -> E (in Ref. 7). {ECO:0000305}.
CONFLICT 558 558 G -> S (in Ref. 2 and 5; AAA36145).
{ECO:0000305}.
HELIX 383 472 {ECO:0000244|PDB:3TNU}.
SEQUENCE 590 AA; 62378 MW; E9D5318E01F55145 CRC64;
MSRQSSVSFR SGGSRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS LAGACGVGGY
GSRSLYNLGG SKRISISTSG GSFRNRFGAG AGGGYGFGGG AGSGFGFGGG AGGGFGLGGG
AGFGGGFGGP GFPVCPPGGI QEVTVNQSLL TPLNLQIDPS IQRVRTEERE QIKTLNNKFA
SFIDKVRFLE QQNKVLDTKW TLLQEQGTKT VRQNLEPLFE QYINNLRRQL DSIVGERGRL
DSELRNMQDL VEDFKNKYED EINKRTTAEN EFVMLKKDVD AAYMNKVELE AKVDALMDEI
NFMKMFFDAE LSQMQTHVSD TSVVLSMDNN RNLDLDSIIA EVKAQYEEIA NRSRTEAESW
YQTKYEELQQ TAGRHGDDLR NTKHEISEMN RMIQRLRAEI DNVKKQCANL QNAIADAEQR
GELALKDARN KLAELEEALQ KAKQDMARLL REYQELMNTK LALDVEIATY RKLLEGEECR
LSGEGVGPVN ISVVTSSVSS GYGSGSGYGG GLGGGLGGGL GGGLAGGSSG SYYSSSSGGV
GLGGGLSVGG SGFSASSGRG LGVGFGSGGG SSSSVKFVST TSSSRKSFKS


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U2287m CLIA kit CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
E2287r ELISA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T


 

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