Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Keratin, type I cytoskeletal 13 (Cytokeratin-13) (CK-13) (Keratin-13) (K13)

 K1C13_HUMAN             Reviewed;         458 AA.
P13646; Q53G54; Q6AZK5; Q8N240;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
18-JUL-2018, entry version 191.
RecName: Full=Keratin, type I cytoskeletal 13;
AltName: Full=Cytokeratin-13;
Short=CK-13;
AltName: Full=Keratin-13;
Short=K13;
Name=KRT13;
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 1), AND VARIANTS VAL-187 AND
ALA-298.
PubMed=2475110; DOI=10.1016/0006-291X(89)90847-4;
Schulz P., Wachter E., Hochstrasser K., Wild A.G., Mischke D.;
"Sequence of a human keratin 13 specific cDNA encompassing coil 1B
through the 3' end.";
Biochem. Biophys. Res. Commun. 162:1522-1527(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, PROTEIN
SEQUENCE OF 291-299, AND VARIANTS VAL-187 AND ALA-298.
PubMed=2477803; DOI=10.1093/nar/17.19.7984;
Mischke D., Schulz P., Wild A.G.;
"The N-, but not the C-terminal domains of human keratins 13 and 15
are closely related.";
Nucleic Acids Res. 17:7984-7984(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
VARIANTS VAL-187 AND ALA-298.
PubMed=2483837; DOI=10.1111/j.1432-0436.1989.tb00612.x;
Kuruc N., Leube R.E., Moll I., Bader B.L., Franke W.W.;
"Synthesis of cytokeratin 13, a component characteristic of internal
stratified epithelia, is not induced in human epidermal tumors.";
Differentiation 42:111-123(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS VAL-187
AND ALA-298.
PubMed=9714826; DOI=10.1016/S0378-1119(98)00297-2;
Waseem A., Alam Y., Dogan B., White K.N., Leigh I.M., Waseem N.H.;
"Isolation, sequence and expression of the gene encoding human keratin
13.";
Gene 215:269-279(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
VAL-187 AND ALA-298.
TISSUE=Tongue;
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] (ISOFORM 1), AND VARIANTS
VAL-187 AND ALA-298.
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
VAL-187 AND ALA-298.
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).
[9]
PROTEIN SEQUENCE OF 124-135; 176-222; 291-318 AND 416-429,
PHOSPHORYLATION AT SER-427, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
Submitted (OCT-2008) to UniProtKB.
[10]
GLYCOSYLATION.
PubMed=2474541;
King I.A., Hounsell E.F.;
"Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine
residues.";
J. Biol. Chem. 264:14022-14028(1989).
[11]
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[16]
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).
[17]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27 AND ARG-35, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[18]
VARIANT WSN2 PRO-119.
PubMed=7493031; DOI=10.1038/ng1295-453;
Richard G., de Laurenzi V., Didona B., Bale S.J., Compton J.G.;
"Keratin 13 point mutation underlies the hereditary mucosal epithelial
disorder white sponge nevus.";
Nat. Genet. 11:453-455(1995).
[19]
VARIANTS WSN2 THR-108 AND PRO-115.
PubMed=10561721;
Rugg E.L., Magee G., Wilson N., Brandrup F., Hamburger J., Lane E.B.;
"Identification of two novel mutations in keratin 13 as the cause of
white sponge naevus.";
Oral Dis. 5:321-324(1999).
[20]
VARIANT WSN2 SER-112.
PubMed=11379896; DOI=10.1177/00220345010800031401;
Terrinoni A., Rugg E.L., Lane E.B., Melino G., Felix D.H., Munro C.S.,
McLean W.H.I.;
"A novel mutation in the keratin 13 gene causing oral white sponge
nevus.";
J. Dent. Res. 80:919-923(2001).
[21]
VARIANT WSN2 PRO-111.
PubMed=14600690; DOI=10.1016/S1079-2104(03)00372-X;
Shibuya Y., Zhang J., Yokoo S., Umeda M., Komori T.;
"Constitutional mutation of keratin 13 gene in familial white sponge
nevus.";
Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod.
96:561-565(2003).
[22]
VARIANT [LARGE SCALE ANALYSIS] VAL-187, AND 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).
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
keratin-13 is generally associated with keratin-4.
-!- INTERACTION:
P14136:GFAP; NbExp=5; IntAct=EBI-1223876, EBI-744302;
A0A0S2Z4Q4:HGS; NbExp=3; IntAct=EBI-1223876, EBI-16429135;
O14964:HGS; NbExp=5; IntAct=EBI-1223876, EBI-740220;
P35908:KRT2; NbExp=3; IntAct=EBI-1223876, EBI-1247312;
P02538:KRT6A; NbExp=5; IntAct=EBI-1223876, EBI-702198;
P07196:NEFL; NbExp=3; IntAct=EBI-1223876, EBI-475646;
A0A0S2Z5X4:ZNF688; NbExp=3; IntAct=EBI-1223876, EBI-16429014;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=A;
IsoId=P13646-1; Sequence=Displayed;
Name=2;
IsoId=P13646-2; Sequence=VSP_016376, VSP_016377;
Note=No experimental confirmation available.;
Name=3;
IsoId=P13646-3; Sequence=VSP_038433;
-!- TISSUE SPECIFICITY: Expressed in some epidermal sweat gland ducts
(at protein level) and in exocervix, esophagus and placenta.
{ECO:0000269|PubMed:2483837}.
-!- PTM: O-glycosylated; glycans consist of single N-acetylglucosamine
residues. {ECO:0000269|PubMed:2474541}.
-!- DISEASE: White sponge nevus 2 (WSN2) [MIM:615785]: A rare disorder
characterized by the presence of soft, white, and spongy plaques
in the oral mucosa. The characteristic histopathologic features
are epithelial thickening, parakeratosis, and vacuolization of the
suprabasal layer of oral epithelial keratinocytes. Less frequently
the mucous membranes of the nose, esophagus, genitalia and rectum
are involved. {ECO:0000269|PubMed:10561721,
ECO:0000269|PubMed:11379896, ECO:0000269|PubMed:14600690,
ECO:0000269|PubMed:7493031}. 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";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-13 entry;
URL="https://en.wikipedia.org/wiki/Keratin_13";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X14640; CAA32786.1; -; mRNA.
EMBL; X52426; CAA36673.1; -; mRNA.
EMBL; AF049259; AAC35754.1; -; Genomic_DNA.
EMBL; AK092276; BAC03847.1; -; mRNA.
EMBL; AK223051; BAD96771.1; -; mRNA.
EMBL; AK223077; BAD96797.1; -; mRNA.
EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002661; AAH02661.3; -; mRNA.
EMBL; BC077718; AAH77718.2; -; mRNA.
CCDS; CCDS11396.1; -. [P13646-1]
CCDS; CCDS11397.1; -. [P13646-3]
PIR; A37343; A37343.
PIR; S06088; KRHU3.
RefSeq; NP_002265.2; NM_002274.3.
RefSeq; NP_705694.2; NM_153490.2.
UniGene; Hs.654550; -.
ProteinModelPortal; P13646; -.
SMR; P13646; -.
BioGrid; 110058; 59.
IntAct; P13646; 32.
STRING; 9606.ENSP00000246635; -.
GlyConnect; 311; -.
iPTMnet; P13646; -.
PhosphoSitePlus; P13646; -.
SwissPalm; P13646; -.
UniCarbKB; P13646; -.
BioMuta; KRT13; -.
DMDM; 269849755; -.
PaxDb; P13646; -.
PeptideAtlas; P13646; -.
PRIDE; P13646; -.
ProteomicsDB; 52951; -.
ProteomicsDB; 52952; -. [P13646-2]
ProteomicsDB; 52953; -. [P13646-3]
DNASU; 3860; -.
Ensembl; ENST00000246635; ENSP00000246635; ENSG00000171401. [P13646-1]
Ensembl; ENST00000336861; ENSP00000336604; ENSG00000171401. [P13646-3]
GeneID; 3860; -.
KEGG; hsa:3860; -.
UCSC; uc002hwu.2; human. [P13646-1]
CTD; 3860; -.
DisGeNET; 3860; -.
EuPathDB; HostDB:ENSG00000171401.14; -.
GeneCards; KRT13; -.
HGNC; HGNC:6415; KRT13.
HPA; CAB000133; -.
HPA; HPA030877; -.
HPA; HPA069771; -.
MalaCards; KRT13; -.
MIM; 148065; gene.
MIM; 615785; phenotype.
neXtProt; NX_P13646; -.
OpenTargets; ENSG00000171401; -.
Orphanet; 171723; White sponge nevus.
PharmGKB; PA30202; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00900000140820; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; P13646; -.
KO; K07604; -.
OMA; KIRDWHL; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; P13646; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
ChiTaRS; KRT13; human.
GeneWiki; Keratin_13; -.
GenomeRNAi; 3860; -.
PRO; PR:P13646; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171401; -.
CleanEx; HS_KRT13; -.
ExpressionAtlas; P13646; baseline and differential.
Genevisible; P13646; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:UniProtKB.
GO; GO:0045095; C:keratin filament; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein;
Intermediate filament; Keratin; Methylation; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 458 Keratin, type I cytoskeletal 13.
/FTId=PRO_0000063647.
DOMAIN 104 416 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 103 Head.
REGION 104 139 Coil 1A.
REGION 140 158 Linker 1.
REGION 159 250 Coil 1B.
REGION 251 273 Linker 12.
REGION 274 412 Coil 2.
REGION 413 458 Tail.
COMPBIAS 13 102 Gly-rich.
MOD_RES 27 27 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 35 35 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.9}.
VAR_SEQ 62 73 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016376.
VAR_SEQ 351 458 ETECRYALQLQQIQGLISSIEAQLSELRSEMECQNQEYKML
LDIKTRLEQEIATYRSLLEGQDAKMIGFPSSAGSVSPRSTS
VTTTSSASVTTTSNASGRRTSDVRRP -> DPGTHQQHRGP
AERAPQ (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016377.
VAR_SEQ 416 458 MIGFPSSAGSVSPRSTSVTTTSSASVTTTSNASGRRTSDVR
RP -> KRQPP (in isoform 3).
{ECO:0000303|PubMed:2483837}.
/FTId=VSP_038433.
VARIANT 81 81 F -> Y (in dbSNP:rs12150581).
/FTId=VAR_059376.
VARIANT 108 108 M -> T (in WSN2; dbSNP:rs60364670).
{ECO:0000269|PubMed:10561721}.
/FTId=VAR_016035.
VARIANT 111 111 L -> P (in WSN2; dbSNP:rs59897026).
{ECO:0000269|PubMed:14600690}.
/FTId=VAR_023924.
VARIANT 112 112 N -> S (in WSN2; dbSNP:rs59970018).
{ECO:0000269|PubMed:11379896}.
/FTId=VAR_016036.
VARIANT 115 115 L -> P (in WSN2; dbSNP:rs60906702).
{ECO:0000269|PubMed:10561721}.
/FTId=VAR_016037.
VARIANT 119 119 L -> P (in WSN2; dbSNP:rs60440396).
{ECO:0000269|PubMed:7493031}.
/FTId=VAR_003836.
VARIANT 146 146 A -> G (in dbSNP:rs760134).
/FTId=VAR_024488.
VARIANT 187 187 A -> V (in dbSNP:rs9891361).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2475110,
ECO:0000269|PubMed:2477803,
ECO:0000269|PubMed:2483837,
ECO:0000269|PubMed:9714826,
ECO:0000269|Ref.6}.
/FTId=VAR_060724.
VARIANT 298 298 T -> A (in dbSNP:rs4796697).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2475110,
ECO:0000269|PubMed:2477803,
ECO:0000269|PubMed:2483837,
ECO:0000269|PubMed:9714826,
ECO:0000269|Ref.6}.
/FTId=VAR_059377.
CONFLICT 46 46 G -> R (in Ref. 6; BAD96771/BAD96797).
{ECO:0000305}.
CONFLICT 58 58 G -> D (in Ref. 1; CAA32786 and 2).
{ECO:0000305}.
SEQUENCE 458 AA; 49588 MW; A51AECFD6195ACB4 CRC64;
MSLRLQSSSA SYGGGFGGGS CQLGGGRGVS TCSTRFVSGG SAGGYGGGVS CGFGGGAGSG
FGGGYGGGLG GGYGGGLGGG FGGGFAGGFV DFGACDGGLL TGNEKITMQN LNDRLASYLE
KVRALEEANA DLEVKIRDWH LKQSPASPER DYSPYYKTIE ELRDKILTAT IENNRVILEI
DNARLAADDF RLKYENELAL RQSVEADING LRRVLDELTL SKTDLEMQIE SLNEELAYMK
KNHEEEMKEF SNQVVGQVNV EMDATPGIDL TRVLAEMREQ YEAMAERNRR DAEEWFHTKS
AELNKEVSTN TAMIQTSKTE ITELRRTLQG LEIELQSQLS MKAGLENTVA ETECRYALQL
QQIQGLISSI EAQLSELRSE MECQNQEYKM LLDIKTRLEQ EIATYRSLLE GQDAKMIGFP
SSAGSVSPRS TSVTTTSSAS VTTTSNASGR RTSDVRRP


Related products :

Catalog number Product name Quantity
E1427h ELISA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
U1427h CLIA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
E1427h ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
E1427r ELISA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
U1427r CLIA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
E1427r ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
U2288m CLIA kit 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T
E2288m ELISA 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T
U2288m CLIA 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T
E2288m ELISA kit 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T
U1427m CLIA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2-17,Krt2a,Mouse,Mus musculus,Type-II keratin Kb2 96T
E1427m ELISA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2-17,Krt2a,Mouse,Mus musculus,Type-II keratin Kb2 96T
E1427m ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2-17,Krt2a,Mouse,Mus musculus,Type-II keratin Kb2 96T
E2288m 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus
U1231m CLIA CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E1231m ELISA kit CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E1231m ELISA CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E2282h ELISA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
E2282h ELISA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
E2282h 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1
E2287m ELISA 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
U2287r CLIA kit 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
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur