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Keratin, type II cytoskeletal 1 (67 kDa cytokeratin) (Cytokeratin-1) (CK-1) (Hair alpha protein) (Keratin-1) (K1) (Type-II keratin Kb1)

 K2C1_HUMAN              Reviewed;         644 AA.
P04264; B2RA01; P85925; P86104; Q14720; Q6GSJ0; Q9H298;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
26-MAY-2009, sequence version 6.
27-SEP-2017, entry version 211.
RecName: Full=Keratin, type II cytoskeletal 1;
AltName: Full=67 kDa cytokeratin;
AltName: Full=Cytokeratin-1;
Short=CK-1;
AltName: Full=Hair alpha protein;
AltName: Full=Keratin-1;
Short=K1;
AltName: Full=Type-II keratin Kb1;
Name=KRT1; Synonyms=KRTA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-358 AND ARG-633.
PubMed=2580302; DOI=10.1073/pnas.82.7.1896;
Johnson L.D., Idler W.W., Zhou X.-M., Roop D.R., Steinert P.M.;
"Structure of a gene for the human epidermal 67-kDa keratin.";
Proc. Natl. Acad. Sci. U.S.A. 82:1896-1900(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-358 AND ARG-633.
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NEPPK, AND VARIANT
ARG-633.
PubMed=11286630; DOI=10.1046/j.1523-1747.2001.13041234.x;
Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J.,
Leigh I.M., Munro C., Kelsell D.P.;
"Novel splice site mutation in keratin 1 underlies mild epidermolytic
palmoplantar keratoderma in three kindreds.";
J. Invest. Dermatol. 116:606-609(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-633.
TISSUE=Skin;
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).
[7]
PROTEIN SEQUENCE OF 2-8.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 13-30; 66-82; 186-240; 258-276; 278-298; 344-355;
365-386; 396-403; 408-416; 418-432; 442-455 AND 461-588, METHYLATION
AT ARG-82 AND LYS-276, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644, AND VARIANTS
CYS-537 AND ARG-633.
PubMed=2581964;
Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C.,
Roop D.R.;
"Amino acid sequences of mouse and human epidermal type II keratins of
Mr 67,000 provide a systematic basis for the structural and functional
diversity of the end domains of keratin intermediate filament
subunits.";
J. Biol. Chem. 260:7142-7149(1985).
[10]
PROTEIN SEQUENCE OF 377-386, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
CITRULLINATION.
PubMed=8780679; DOI=10.1006/bbrc.1996.1240;
Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.;
"Preferential deimination of keratin K1 and filaggrin during the
terminal differentiation of human epidermis.";
Biochem. Biophys. Res. Commun. 225:712-719(1996).
[12]
INVOLVEMENT IN IHCM.
PubMed=11286616; DOI=10.1046/j.1523-1747.2001.01292.x;
Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N.,
Miller C.J., Steinert P.M., Neldner K., Richard G.;
"Evidence for novel functions of the keratin tail emerging from a
mutation causing ichthyosis hystrix.";
J. Invest. Dermatol. 116:511-519(2001).
[13]
CITRULLINATION.
PubMed=11841545; DOI=10.1046/j.0022-202x.2001.01671.x;
Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H.,
Akiyama M., Iizuka H.;
"Sequential reorganization of cornified cell keratin filaments
involving filaggrin-mediated compaction and keratin 1 deimination.";
J. Invest. Dermatol. 118:282-287(2002).
[14]
INVOLVEMENT IN SPPK3.
PubMed=11982762; DOI=10.1046/j.1523-1747.2002.01750.x;
Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D.,
Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I.,
McGrath J.A.;
"Frameshift mutation in the V2 domain of human keratin 1 results in
striate palmoplantar keratoderma.";
J. Invest. Dermatol. 118:838-844(2002).
[15]
INTERACTION WITH EPPK1.
PubMed=16923132; DOI=10.1111/j.1346-8138.2006.00127.x;
Wang W., Sumiyoshi H., Yoshioka H., Fujiwara S.;
"Interactions between epiplakin and intermediate filaments.";
J. Dermatol. 33:518-527(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16529377; DOI=10.1094/MPMI-19-0150;
Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
Witthuhn B.A., David A.J., Gillman J.H.;
"Proteomic comparison of needles from blister rust-resistant and
susceptible Pinus strobus seedlings reveals upregulation of putative
disease resistance proteins.";
Mol. Plant Microbe Interact. 19:150-160(2006).
[17]
FUNCTION, INTERACTION WITH RACK1 AND ITGB1, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17956333; DOI=10.1042/BST0351292;
Chuang N.N., Huang C.C.;
"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma
NMB7 cells.";
Biochem. Soc. Trans. 35:1292-1294(2007).
[18]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
"A proteomics approach to identify proteins differentially expressed
in Douglas-fir seedlings infected by Phellinus sulphurascens.";
J. Proteomics 71:425-438(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND 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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Xylem;
PubMed=19412582; DOI=10.1007/s12010-009-8620-1;
Basha S.M., Mazhar H., Vasanthaiah H.K.N.;
"Proteomics approach to identify unique xylem sap proteins in Pierce's
disease-tolerant Vitis species.";
Appl. Biochem. Biotechnol. 160:932-944(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-66 AND SER-344,
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).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
FUNCTION, AND INTERACTION WITH C1QBP.
PubMed=21544310; DOI=10.1160/TH10-09-0591;
Pixley R.A., Espinola R.G., Ghebrehiwet B., Joseph K., Kao A.,
Bdeir K., Cines D.B., Colman R.W.;
"Interaction of high-molecular-weight kininogen with endothelial cell
binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface
plasmon resonance (BiaCore).";
Thromb. Haemost. 105:1053-1059(2011).
[25]
CORRECTION OF SPECIES OF ORIGIN.
PubMed=23895828; DOI=10.1016/j.jprot.2013.07.009;
Nawrot R., Barylski J., Schulze W.X.;
"Incorrectly annotated keratin derived peptide sequences lead to
misleading MS/MS data interpretation.";
J. Proteomics 91:270-273(2013).
[26]
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).
[27]
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).
[28]
VARIANT EHK PRO-161.
PubMed=1381288; DOI=10.1016/0092-8674(92)90315-4;
Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J.,
Compton J.G., Steinert P.M.;
"A leucine-->proline mutation in the H1 subdomain of keratin 1 causes
epidermolytic hyperkeratosis.";
Cell 70:821-828(1992).
[29]
VARIANT ALLELE 1B 560-GLY--TYR-566 DEL.
PubMed=1281859; DOI=10.1111/1523-1747.ep12614149;
Korge B.P., Compton J.G., Steinert P.M., Mischke D.;
"The two size alleles of human keratin 1 are due to a deletion in the
glycine-rich carboxyl-terminal V2 subdomain.";
J. Invest. Dermatol. 99:697-702(1992).
[30]
VARIANT EHK GLN-490.
PubMed=1380725; DOI=10.1126/science.257.5073.1128;
Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A.,
Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.;
"Mutations in the rod domains of keratins 1 and 10 in epidermolytic
hyperkeratosis.";
Science 257:1128-1130(1992).
[31]
VARIANT EHK CYS-482.
PubMed=7512983; DOI=10.1172/JCI117132;
Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.;
"Genetic mutations in the K1 and K10 genes of patients with
epidermolytic hyperkeratosis. Correlation between location and disease
severity.";
J. Clin. Invest. 93:1533-1542(1994).
[32]
VARIANTS EHK GLY-155; SER-188 AND PRO-193.
PubMed=7507151; DOI=10.1111/1523-1747.ep12371725;
Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N.,
Steinert P.M., Compton J.G.;
"Mutations in the H1 and 1A domains in the keratin 1 gene in
epidermolytic hyperkeratosis.";
J. Invest. Dermatol. 102:17-23(1994).
[33]
VARIANTS EHK PRO-186 AND SER-188.
PubMed=7507152; DOI=10.1111/1523-1747.ep12371726;
McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R.,
Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G.,
Morley S.M.;
"Mutations in the rod 1A domain of keratins 1 and 10 in bullous
congenital ichthyosiform erythroderma (BCIE).";
J. Invest. Dermatol. 102:24-30(1994).
[34]
VARIANT NEPPK ILE-74.
PubMed=7528239; DOI=10.1111/1523-1747.ep12412771;
Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J.,
Compton J.G.;
"A mutation in the V1 end domain of keratin 1 in non-epidermolytic
palmar-plantar keratoderma.";
J. Invest. Dermatol. 103:764-769(1994).
[35]
VARIANT EHK VAL-340.
PubMed=9856846; DOI=10.1046/j.1523-1747.1998.00389.x;
Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D.,
Ruiter D.J., Mariman E.C., Steijlen P.M.;
"An atypical form of bullous congenital ichthyosiform erythroderma is
caused by a mutation in the L12 linker region of keratin 1.";
J. Invest. Dermatol. 111:1224-1226(1998).
[36]
VARIANTS AEI PHE-479 AND THR-479.
PubMed=10053007; DOI=10.1086/302278;
Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M.,
Stephens K., McLean W.H.I.;
"Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype
conferred by mutations in the 2B domain of keratin K1.";
Am. J. Hum. Genet. 64:732-738(1999).
[37]
VARIANT EHK THR-188.
PubMed=10232403; DOI=10.1111/j.1600-0625.1999.tb00359.x;
Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A.,
Roop D.R.;
"An asparagine to threonine substitution in the 1A domain of keratin
1: a novel mutation that causes epidermolytic hyperkeratosis.";
Exp. Dermatol. 8:124-127(1999).
[38]
VARIANT AEI PHE-479.
PubMed=10597140; DOI=10.1111/j.1600-0625.1999.tb00309.x;
Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M.;
"Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques
resulting from a mutation in the keratin 1 gene.";
Exp. Dermatol. 8:501-503(1999).
[39]
VARIANT EHK PRO-214.
PubMed=10844506; DOI=10.1046/j.1365-2230.2000.00625.x;
Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M.,
Schneiderman P., Grossman M.E., Christiano A.M.;
"Epidermolytic hyperkeratosis in a Hispanic family resulting from a
mutation in the keratin 1 gene.";
Clin. Exp. Dermatol. 25:241-243(2000).
[40]
VARIANT EHK THR-479.
PubMed=10688370; DOI=10.1034/j.1600-0625.2000.009001016.x;
Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R.;
"Identification of a novel mutation in keratin 1 in a family with
epidermolytic hyperkeratosis.";
Exp. Dermatol. 9:16-19(2000).
[41]
VARIANT EHK ASP-155.
PubMed=11531804; DOI=10.1046/j.1365-2133.2001.04327.x;
Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J.,
McGrath J.A.;
"New mutations in keratin 1 that cause bullous congenital
ichthyosiform erythroderma and keratin 2e that cause ichthyosis
bullosa of Siemens.";
Br. J. Dermatol. 145:330-335(2001).
[42]
VARIANTS PALMOPLANTAR KERATODERMA VAL-176--LYS-197 DEL AND
ALA-459--466-GLN DEL.
PubMed=12406346; DOI=10.1046/j.1523-1747.2002.00186.x;
Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J.,
McLean W.H., Irvine A.D.;
"Two cases of primarily palmoplantar keratoderma associated with novel
mutations in keratin 1.";
J. Invest. Dermatol. 119:966-971(2002).
[43]
VARIANTS EHK LYS-188 AND PRO-486.
PubMed=12406348; DOI=10.1046/j.1523-1747.2002.00061.x;
Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S.,
Steinert P.M., Yang J.-M.;
"Two novel mutations in the keratin 1 gene in epidermolytic
hyperkeratosis.";
J. Invest. Dermatol. 119:976-977(2002).
[44]
VARIANTS EHK LYS-188; SER-188; GLN-478; THR-479; PRO-485; PRO-486 AND
LYS-490.
PubMed=21271994; DOI=10.1111/j.1365-2133.2010.10096.x;
Arin M.J., Oji V., Emmert S., Hausser I., Traupe H., Krieg T.,
Grimberg G.;
"Expanding the keratin mutation database: novel and recurrent
mutations and genotype-phenotype correlations in 28 patients with
epidermolytic ichthyosis.";
Br. J. Dermatol. 164:442-447(2011).
-!- FUNCTION: May regulate the activity of kinases such as PKC and SRC
via binding to integrin beta-1 (ITB1) and the receptor of
activated protein C kinase 1 (RACK1). In complex with C1QBP is a
high affinity receptor for kininogen-1/HMWK.
{ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21544310}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Keratin-1 is generally associated with keratin-10. Interacts with
ITGB1 in the presence of RACK1 and SRC, and with RACK1. Interacts
with C1QBP; the association represents a cell surface kininogen
receptor. Interacts with EPPK1; interaction is dependent of
higher-order structure of intermediate filament (PubMed:16923132).
{ECO:0000269|PubMed:16923132, ECO:0000269|PubMed:17956333,
ECO:0000269|PubMed:21544310}.
-!- INTERACTION:
Q08379:GOLGA2; NbExp=5; IntAct=EBI-298429, EBI-618309;
P19012:KRT15; NbExp=6; IntAct=EBI-298429, EBI-739566;
Q7Z3Y8:KRT27; NbExp=4; IntAct=EBI-298429, EBI-3044087;
Q14525:KRT33B; NbExp=6; IntAct=EBI-298429, EBI-1049638;
O76014:KRT37; NbExp=4; IntAct=EBI-298429, EBI-1045716;
P37198:NUP62; NbExp=6; IntAct=EBI-298429, EBI-347978;
P14373:TRIM27; NbExp=4; IntAct=EBI-298429, EBI-719493;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17956333}.
Note=Located on plasma membrane of neuroblastoma NMB7 cells.
-!- TISSUE SPECIFICITY: The source of this protein is neonatal
foreskin. The 67-kDa type II keratins are expressed in terminally
differentiating epidermis.
-!- PTM: Undergoes deimination of some arginine residues
(citrullination). {ECO:0000269|PubMed:11841545,
ECO:0000269|PubMed:8780679}.
-!- POLYMORPHISM: There are two size variants of KRT1, termed allele
1A and allele 1B with allelic frequencies of 0.61 and 0.39. Allele
1B lacks 7 residues compared to allele 1A.
-!- DISEASE: Epidermolytic hyperkeratosis (EHK) [MIM:113800]: An
autosomal dominant skin disorder characterized by widespread
blistering and an ichthyotic erythroderma at birth that persist
into adulthood. Histologically there is a diffuse epidermolytic
degeneration in the lower spinous layer of the epidermis. Within a
few weeks from birth, erythroderma and blister formation diminish
and hyperkeratoses develop. {ECO:0000269|PubMed:10232403,
ECO:0000269|PubMed:10688370, ECO:0000269|PubMed:10844506,
ECO:0000269|PubMed:11531804, ECO:0000269|PubMed:12406348,
ECO:0000269|PubMed:1380725, ECO:0000269|PubMed:1381288,
ECO:0000269|PubMed:21271994, ECO:0000269|PubMed:7507151,
ECO:0000269|PubMed:7507152, ECO:0000269|PubMed:7512983,
ECO:0000269|PubMed:9856846}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ichthyosis hystrix, Curth-Macklin type (IHCM)
[MIM:146590]: A genodermatosis with severe verrucous
hyperkeratosis. Affected individuals manifest congenital verrucous
black scale on the scalp, neck, and limbs with truncal erythema,
palmoplantar keratoderma and keratoses on the lips, ears, nipples
and buttocks. {ECO:0000269|PubMed:11286616}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Keratoderma, palmoplantar, non-epidermolytic (NEPPK)
[MIM:600962]: A dermatological disorder characterized by well-
demarcated hyperkeratosis is present over the palms and soles. A
red band is frequently present at the periphery of the keratosis.
It is usually non-transgredient, with a sharp demarcation of the
lesions at the wrists. {ECO:0000269|PubMed:11286630,
ECO:0000269|PubMed:7528239}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ichthyosis annular epidermolytic (AEI) [MIM:607602]: A
skin disorder resembling bullous congenital ichthyosiform
erythroderma. Affected individuals present with bullous ichthyosis
in early childhood and hyperkeratotic lichenified plaques in the
flexural areas and extensor surfaces at later ages. The feature
that distinguishes AEI from BCIE is dramatic episodes of flares of
annular polycyclic plaques with scale, which coalesce to involve
most of the body surface and can persist for several weeks or even
months. {ECO:0000269|PubMed:10053007,
ECO:0000269|PubMed:10597140}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Keratoderma, palmoplantar, striate 3 (SPPK3)
[MIM:607654]: A dermatological disorder characterized by
thickening of the stratum corneum and epidermal layers on palms
and soles. There is no involvement of non-palmoplantar skin, and
both hair and nails are normal. {ECO:0000269|PubMed:11982762}.
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:0000305}.
-!- CAUTION: A peptide corresponding to residues 278 to 289 was
isolated as part of plant proteomics studies and was originally
thought to be of plant origin (PubMed:18602030, PubMed:19412582,
PubMed:16529377). However, it was later shown that it is likely to
be human type II keratin, a common contaminant in proteomic
analyses (PubMed:23895828). {ECO:0000305|PubMed:23895828}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-1 entry;
URL="https://en.wikipedia.org/wiki/Keratin_1";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M98776; AAB47721.1; -; Genomic_DNA.
EMBL; AF237621; AAF60327.1; -; Genomic_DNA.
EMBL; AF304164; AAG41947.1; -; Genomic_DNA.
EMBL; AK313986; BAG36698.1; -; mRNA.
EMBL; AC055716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063697; AAH63697.1; -; mRNA.
EMBL; M10938; AAA36153.1; -; mRNA.
CCDS; CCDS8836.1; -.
PIR; A22940; KRHU2.
RefSeq; NP_006112.3; NM_006121.3.
UniGene; Hs.80828; -.
PDB; 4ZRY; X-ray; 3.30 A; B=370-489.
PDBsum; 4ZRY; -.
ProteinModelPortal; P04264; -.
SMR; P04264; -.
BioGrid; 110046; 71.
IntAct; P04264; 51.
MINT; MINT-4990403; -.
STRING; 9606.ENSP00000252244; -.
iPTMnet; P04264; -.
PhosphoSitePlus; P04264; -.
SwissPalm; P04264; -.
BioMuta; KRT1; -.
DMDM; 238054406; -.
REPRODUCTION-2DPAGE; P04264; -.
SWISS-2DPAGE; P04264; -.
EPD; P04264; -.
PaxDb; P04264; -.
PeptideAtlas; P04264; -.
PRIDE; P04264; -.
Ensembl; ENST00000252244; ENSP00000252244; ENSG00000167768.
GeneID; 3848; -.
KEGG; hsa:3848; -.
UCSC; uc001sau.1; human.
CTD; 3848; -.
DisGeNET; 3848; -.
EuPathDB; HostDB:ENSG00000167768.4; -.
GeneCards; KRT1; -.
H-InvDB; HIX0036813; -.
HGNC; HGNC:6412; KRT1.
HPA; CAB002153; -.
HPA; HPA017917; -.
HPA; HPA062908; -.
MalaCards; KRT1; -.
MIM; 113800; phenotype.
MIM; 139350; gene.
MIM; 146590; phenotype.
MIM; 600962; phenotype.
MIM; 607602; phenotype.
MIM; 607654; phenotype.
neXtProt; NX_P04264; -.
OpenTargets; ENSG00000167768; -.
Orphanet; 281139; Annular epidermolytic ichthyosis.
Orphanet; 312; Epidermolytic ichthyosis.
Orphanet; 2199; Epidermolytic palmoplantar keratoderma.
Orphanet; 79503; Ichthyosis hystrix of Curth-Macklin.
Orphanet; 50942; Keratosis palmoplantaris striata.
PharmGKB; PA30199; -.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P04264; -.
KO; K07605; -.
OMA; EKCICCE; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P04264; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P04264; -.
ChiTaRS; KRT1; human.
GeneWiki; Keratin_1; -.
GenomeRNAi; 3848; -.
PRO; PR:P04264; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167768; -.
CleanEx; HS_KRT1; -.
Genevisible; P04264; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0001533; C:cornified envelope; IDA:CAFA.
GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IPI:UniProtKB.
GO; GO:0004872; F:receptor activity; NAS:UniProtKB.
GO; GO:0030280; F:structural constituent of epidermis; IDA:CAFA.
GO; GO:0001867; P:complement activation, lectin pathway; IPI:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; NAS:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018149; P:peptide cross-linking; IDA:CAFA.
GO; GO:0045765; P:regulation of angiogenesis; NAS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; NAS:UniProtKB.
GO; GO:0001895; P:retina homeostasis; IEP:UniProtKB.
GO; GO:0098773; P:skin epidermis development; IC:CAFA.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032449; Keratin_2_1_tail.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
Pfam; PF16210; Keratin_2_tail; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Citrullination; Coiled coil;
Complete proteome; Direct protein sequencing; Disease mutation;
Ichthyosis; Intermediate filament; Keratin; Membrane; Methylation;
Palmoplantar keratoderma; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801}.
CHAIN 2 644 Keratin, type II cytoskeletal 1.
/FTId=PRO_0000063709.
REGION 2 179 Head.
REGION 180 489 Rod.
REGION 180 215 Coil 1A.
REGION 216 234 Linker 1.
REGION 235 326 Coil 1B.
REGION 327 350 Linker 12.
REGION 351 489 Coil 2.
REGION 490 644 Tail.
COMPBIAS 2 151 Gly/Phe/Ser-rich.
COMPBIAS 502 641 Gly/Ser-rich.
SITE 433 433 Stutter.
MOD_RES 12 12 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04104}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000250|UniProtKB:P04104}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 45 45 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04104}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 82 82 Omega-N-methylarginine.
{ECO:0000269|Ref.8}.
MOD_RES 276 276 N6,N6-dimethyllysine.
{ECO:0000269|Ref.8}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 518 518 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04104}.
MOD_RES 588 588 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04104}.
VARIANT 74 74 K -> I (in NEPPK; dbSNP:rs57977969).
{ECO:0000269|PubMed:7528239}.
/FTId=VAR_017819.
VARIANT 155 155 V -> D (in EHK; dbSNP:rs57959072).
{ECO:0000269|PubMed:11531804}.
/FTId=VAR_017820.
VARIANT 155 155 V -> G (in EHK; dbSNP:rs57959072).
{ECO:0000269|PubMed:7507151}.
/FTId=VAR_003853.
VARIANT 161 161 L -> P (in EHK; dbSNP:rs57695159).
{ECO:0000269|PubMed:1381288}.
/FTId=VAR_003854.
VARIANT 176 197 Missing (in palmoplantar keratoderma; and
mild ichthyosis largely limited to the
flexural areas).
/FTId=VAR_038627.
VARIANT 186 186 S -> P (in EHK; dbSNP:rs60022878).
{ECO:0000269|PubMed:7507152}.
/FTId=VAR_003855.
VARIANT 188 188 N -> K (in EHK; dbSNP:rs59429455).
{ECO:0000269|PubMed:12406348,
ECO:0000269|PubMed:21271994}.
/FTId=VAR_017821.
VARIANT 188 188 N -> S (in EHK; dbSNP:rs58928370).
{ECO:0000269|PubMed:21271994,
ECO:0000269|PubMed:7507151,
ECO:0000269|PubMed:7507152}.
/FTId=VAR_003856.
VARIANT 188 188 N -> T (in EHK; severe;
dbSNP:rs58928370).
{ECO:0000269|PubMed:10232403}.
/FTId=VAR_017822.
VARIANT 193 193 S -> P (in EHK; dbSNP:rs60937700).
{ECO:0000269|PubMed:7507151}.
/FTId=VAR_003857.
VARIANT 214 214 L -> P (in EHK; dbSNP:rs61549035).
{ECO:0000269|PubMed:10844506}.
/FTId=VAR_017823.
VARIANT 312 312 I -> V.
/FTId=VAR_003858.
VARIANT 330 330 I -> T.
/FTId=VAR_003859.
VARIANT 340 340 D -> V (in EHK; dbSNP:rs58062863).
{ECO:0000269|PubMed:9856846}.
/FTId=VAR_017824.
VARIANT 358 358 Y -> N (in dbSNP:rs1050872).
{ECO:0000269|PubMed:10903910,
ECO:0000269|PubMed:2580302}.
/FTId=VAR_003860.
VARIANT 454 454 A -> S (in dbSNP:rs17678945).
/FTId=VAR_038628.
VARIANT 459 466 Missing (in palmoplantar keratoderma; and
mild ichthyosis largely limited to the
flexural areas).
/FTId=VAR_038629.
VARIANT 478 478 E -> Q (in EHK; dbSNP:rs59089201).
{ECO:0000269|PubMed:21271994}.
/FTId=VAR_071986.
VARIANT 479 479 I -> F (in AEI; dbSNP:rs61218439).
{ECO:0000269|PubMed:10053007,
ECO:0000269|PubMed:10597140}.
/FTId=VAR_017825.
VARIANT 479 479 I -> T (in AEI and EHK;
dbSNP:rs57837128).
{ECO:0000269|PubMed:10053007,
ECO:0000269|PubMed:10688370,
ECO:0000269|PubMed:21271994}.
/FTId=VAR_017826.
VARIANT 482 482 Y -> C (in EHK; dbSNP:rs58420087).
{ECO:0000269|PubMed:7512983}.
/FTId=VAR_017827.
VARIANT 485 485 L -> P (in EHK; dbSNP:rs267607430).
{ECO:0000269|PubMed:21271994}.
/FTId=VAR_071987.
VARIANT 486 486 L -> P (in EHK; dbSNP:rs56914602).
{ECO:0000269|PubMed:12406348,
ECO:0000269|PubMed:21271994}.
/FTId=VAR_017828.
VARIANT 490 490 E -> K (in EHK; dbSNP:rs60279707).
{ECO:0000269|PubMed:21271994}.
/FTId=VAR_071988.
VARIANT 490 490 E -> Q (in EHK; dbSNP:rs60279707).
{ECO:0000269|PubMed:1380725}.
/FTId=VAR_003861.
VARIANT 537 537 G -> C. {ECO:0000269|PubMed:2581964}.
/FTId=VAR_003862.
VARIANT 560 566 Missing (in allele 1B).
{ECO:0000269|PubMed:1281859}.
/FTId=VAR_003864.
VARIANT 633 633 K -> R (in dbSNP:rs14024).
{ECO:0000269|PubMed:10903910,
ECO:0000269|PubMed:11286630,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2580302,
ECO:0000269|PubMed:2581964}.
/FTId=VAR_003863.
CONFLICT 201 201 L -> M (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 206 206 Q -> K (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 238 238 L -> S (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 344 345 SL -> QF (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 403 403 R -> H (in Ref. 4; BAG36698).
{ECO:0000305}.
CONFLICT 404 404 V -> M (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 447 447 L -> M (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 463 463 R -> C (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 466 466 Q -> H (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 504 504 S -> T (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 511 512 TI -> SM (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 564 564 G -> S (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 613 613 I -> S (in Ref. 9; AAA36153).
{ECO:0000305}.
CONFLICT 638 638 T -> S (in Ref. 9; AAA36153).
{ECO:0000305}.
HELIX 387 476 {ECO:0000244|PDB:4ZRY}.
HELIX 478 488 {ECO:0000244|PDB:4ZRY}.
SEQUENCE 644 AA; 66039 MW; CE5DDE97388F5017 CRC64;
MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG
GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GGGIGGGGFG
GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG GIQEVTINQS LLQPLNVEID PEIQKVKSRE
REQIKSLNNQ FASFIDKVRF LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR
RVDQLKSDQS RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD
LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI IAEVKAQYED
IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE LNRVIQRLRS EIDNVKKQIS
NLQQSISDAE QRGENALKDA KNKLNDLEDA LQQAKEDLAR LLRDYQELMN TKLALDLEIA
TYRTLLEGEE SRMSGECAPN VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG
SGGGGGGGRG SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG
GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVKFVSTTYS GVTR


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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
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
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
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
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
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 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
U2287m CLIA 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
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
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
U2287r CLIA 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 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
E2287m ELISA 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
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


 

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