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Keratin, type II cytoskeletal 8 (Cytokeratin-8) (CK-8) (Keratin-8) (K8) (Type-II keratin Kb8)

 K2C8_HUMAN              Reviewed;         483 AA.
P05787; A8K4H3; B0AZN5; F8VXB4; Q14099; Q14716; Q14717; Q53GJ0;
Q6DHW5; Q6GMY0; Q6P4C7; Q96J60;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 7.
25-OCT-2017, entry version 212.
RecName: Full=Keratin, type II cytoskeletal 8;
AltName: Full=Cytokeratin-8;
Short=CK-8;
AltName: Full=Keratin-8;
Short=K8;
AltName: Full=Type-II keratin Kb8;
Name=KRT8; Synonyms=CYK8;
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 VARIANT GLY-417.
PubMed=1691124; DOI=10.1016/0378-1119(90)90285-Y;
Krauss S., Franke W.W.;
"Organization and sequence of the human gene encoding cytokeratin 8.";
Gene 86:241-249(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1692965; DOI=10.1210/mend-4-3-370;
Yamamoto R., Kao L.C., McKnight C.E., Strauss J.F. III;
"Cloning and sequence of cDNA for human placental cytokeratin 8.
Regulation of the mRNA in trophoblastic cells by cAMP.";
Mol. Endocrinol. 4:370-374(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=1705144;
Waseem A., Alexander C.M., Steel J.B., Lane E.B.;
"Embryonic simple epithelial keratins 8 and 18: chromosomal location
emphasizes difference from other keratin pairs.";
New Biol. 2:464-478(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION AT SER-24
AND SER-432.
PubMed=9054461; DOI=10.1074/jbc.272.11.7556;
Ku N.-O., Omary M.B.;
"Phosphorylation of human keratin 8 in vivo at conserved head domain
serine 23 and at epidermal growth factor-stimulated tail domain serine
431.";
J. Biol. Chem. 272:7556-7564(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
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).
TISSUE=Kidney;
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=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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
CYS-62.
TISSUE=Colon, Liver, Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-231 (ISOFORM 1).
PubMed=2471065; DOI=10.1128/MCB.9.4.1553;
Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., Oshima R.G.;
"Posttranslational regulation of keratins: degradation of mouse and
human keratins 18 and 8.";
Mol. Cell. Biol. 9:1553-1565(1989).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 205-483 (ISOFORM 1), AND VARIANTS
GLY-417 AND ASP-429.
PubMed=2434381; DOI=10.1111/j.1432-0436.1986.tb00412.x;
Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H.,
Franke W.W.;
"Cytokeratin expression in simple epithelia. III. Detection of mRNAs
encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by
hybridization with cDNA sequences in vitro and in situ.";
Differentiation 33:69-85(1986).
[12]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[13]
GLYCOSYLATION.
PubMed=1371281;
Chou C.F., Smith A.J., Omary M.B.;
"Characterization and dynamics of O-linked glycosylation of human
cytokeratin 8 and 18.";
J. Biol. Chem. 267:3901-3906(1992).
[14]
PHOSPHORYLATION AT SER-9 AND SER-24.
PubMed=1374067; DOI=10.1083/jcb.117.3.583;
Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y.,
Strulovici B.;
"PKC epsilon-related kinase associates with and phosphorylates
cytokeratin 8 and 18.";
J. Cell Biol. 117:583-593(1992).
[15]
INTERACTION WITH KRT20, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10973561; DOI=10.1016/S0003-9969(00)00050-9;
Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B.;
"An immunohistological study of cytokeratin 20 in human and mammalian
oral epithelium.";
Arch. Oral Biol. 45:879-887(2000).
[16]
INTERACTION WITH PNN.
PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
Shi J., Sugrue S.P.;
"Dissection of protein linkage between keratins and pinin, a protein
with dual location at desmosome-intermediate filament complex and in
the nucleus.";
J. Biol. Chem. 275:14910-14915(2000).
[17]
PHOSPHORYLATION AT SER-74.
PubMed=11781324; DOI=10.1074/jbc.M111436200;
He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E.;
"The intermediate filament protein keratin 8 is a novel cytoplasmic
substrate for c-Jun N-terminal kinase.";
J. Biol. Chem. 277:10767-10774(2002).
[18]
PHOSPHORYLATION AT SER-74, AND MUTAGENESIS OF LEU-72 AND SER-74.
PubMed=11788583; DOI=10.1074/jbc.M107623200;
Ku N.O., Azhar S., Omary M.B.;
"Keratin 8 phosphorylation by p38 kinase regulates cellular keratin
filament reorganization: modulation by a keratin 1-like disease
causing mutation.";
J. Biol. Chem. 277:10775-10782(2002).
[19]
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).
[20]
FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=16000376; DOI=10.1091/mbc.E05-02-0112;
Stone M.R., O'Neill A., Catino D., Bloch R.J.;
"Specific interaction of the actin-binding domain of dystrophin with
intermediate filaments containing keratin 19.";
Mol. Biol. Cell 16:4280-4293(2005).
[21]
INTERACTION WITH HCV CORE PROTEIN.
PubMed=15846844; DOI=10.1002/pmic.200401093;
Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
"Proteomic profiling of cellular proteins interacting with the
hepatitis C virus core protein.";
Proteomics 5:2227-2237(2005).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[23]
INTERACTION WITH KRT20.
PubMed=16608857; DOI=10.1074/jbc.M512284200;
Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J.,
Burlingame A.L., Omary M.B.;
"Keratin 20 serine 13 phosphorylation is a stress and intestinal
goblet cell marker.";
J. Biol. Chem. 281:16453-16461(2006).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-27;
SER-43; SER-253; SER-258; SER-274; SER-400; SER-410; SER-432; SER-475
AND SER-478, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19188445; DOI=10.1128/MCB.01337-08;
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
Quadrifoglio F., Tell G.;
"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in
the rRNA quality control process.";
Mol. Cell. Biol. 29:1834-1854(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND 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).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-207; LYS-295 AND LYS-325,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[30]
GLYCOSYLATION.
PubMed=20729549; DOI=10.1074/jbc.M109.098996;
Srikanth B., Vaidya M.M., Kalraiya R.D.;
"O-GlcNAcylation determines the solubility, filament organization, and
stability of keratins 8 and 18.";
J. Biol. Chem. 285:34062-34071(2010).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; SER-475 AND
SER-478, 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).
[32]
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).
[33]
MALONYLATION AT LYS-101.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[34]
INTERACTION WITH GPER1.
PubMed=21149639; DOI=10.1124/mol.110.069500;
Sanden C., Broselid S., Cornmark L., Andersson K.,
Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.;
"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30
localizes in the plasma membrane and traffics intracellularly on
cytokeratin intermediate filaments.";
Mol. Pharmacol. 79:400-410(2011).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-43; SER-253 AND
SER-258, 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).
[36]
GLYCOSYLATION.
PubMed=22967762; DOI=10.1016/j.bbagen.2012.08.024;
Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F.,
Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.;
"Characterization of O-GlcNAc cycling and proteomic identification of
differentially O-GlcNAcylated proteins during G1/S transition.";
Biochim. Biophys. Acta 1820:1839-1848(2012).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-21; SER-31;
SER-34; SER-39; SER-43; SER-253; SER-258; SER-274; SER-291; SER-330;
SER-404; SER-410; SER-475 AND SER-477, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-22; SER-253;
SER-258; SER-410 AND SER-475, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-23; ARG-32; ARG-40 AND
ARG-47, 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).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285; LYS-304 AND LYS-472,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-285 AND LYS-472,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-122; LYS-130;
LYS-197; LYS-264; LYS-285; LYS-295; LYS-304; LYS-325; LYS-393 AND
LYS-472, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[43]
VARIANTS CIRRH VAL-53; CYS-54 AND CYS-62, AND VARIANT VAL-63.
PubMed=12724528; DOI=10.1073/pnas.0936165100;
Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B.,
Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.;
"Keratin 8 and 18 mutations are risk factors for developing liver
disease of multiple etiologies.";
Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003).
-!- FUNCTION: Together with KRT19, helps to link the contractile
apparatus to dystrophin at the costameres of striated muscle.
{ECO:0000269|PubMed:16000376}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
KRT8 associates with KRT18. Associates with KRT20. Interacts with
HCV core protein and PNN. When associated with KRT19, interacts
with DMD. Interacts with TCHP. Interacts with APEX1. Interacts
with GPER1. Interacts with EPPK1 (By similarity).
{ECO:0000250|UniProtKB:P11679, ECO:0000269|PubMed:10809736,
ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:15731013,
ECO:0000269|PubMed:15846844, ECO:0000269|PubMed:16000376,
ECO:0000269|PubMed:16608857, ECO:0000269|PubMed:19188445,
ECO:0000269|PubMed:21149639}.
-!- INTERACTION:
P13569:CFTR; NbExp=7; IntAct=EBI-297852, EBI-349854;
P62993:GRB2; NbExp=3; IntAct=EBI-297852, EBI-401755;
Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-297852, EBI-81279;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-297852, EBI-10171552;
P19012:KRT15; NbExp=5; IntAct=EBI-297852, EBI-739566;
P05783:KRT18; NbExp=12; IntAct=EBI-297852, EBI-297888;
P08727:KRT19; NbExp=4; IntAct=EBI-297852, EBI-742756;
Q7Z3Y7:KRT28; NbExp=4; IntAct=EBI-297852, EBI-11980489;
Q15323:KRT31; NbExp=5; IntAct=EBI-297852, EBI-948001;
O76015:KRT38; NbExp=5; IntAct=EBI-297852, EBI-1047263;
Q6A162:KRT40; NbExp=5; IntAct=EBI-297852, EBI-10171697;
Q13835-2:PKP1; NbExp=3; IntAct=EBI-297852, EBI-9087684;
P14079:tax (xeno); NbExp=3; IntAct=EBI-297852, EBI-9675698;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-297852, EBI-1105213;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561,
ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm {ECO:0000250}.
Nucleus matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05787-1; Sequence=Displayed;
Name=2;
IsoId=P05787-2; Sequence=VSP_046000;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Observed in muscle fibers accumulating in the
costameres of myoplasm at the sarcolemma membrane in structures
that contain dystrophin and spectrin. Expressed in gingival mucosa
and hard palate of the oral cavity. {ECO:0000269|PubMed:10973561,
ECO:0000269|PubMed:16000376}.
-!- PTM: Phosphorylation on serine residues is enhanced during EGF
stimulation and mitosis. Ser-74 phosphorylation plays an important
role in keratin filament reorganization.
{ECO:0000269|PubMed:11781324, ECO:0000269|PubMed:11788583,
ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:9054461}.
-!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
solubility, and decreases stability by inducing proteasomal
degradation.
-!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent
manner.
-!- DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease
characterized by severe panlobular liver-cell swelling with
Mallory body formation, prominent pericellular fibrosis, and
marked deposits of copper. Clinical features include abdomen
swelling, jaundice and pulmonary hypertension.
{ECO:0000269|PubMed:12724528}. 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; M34482; AAA35763.1; -; Genomic_DNA.
EMBL; M34225; AAA35748.1; -; mRNA.
EMBL; X74929; CAA52882.1; -; mRNA.
EMBL; X74981; CAA52916.1; -; Genomic_DNA.
EMBL; U76549; AAB18966.1; -; mRNA.
EMBL; AK290938; BAF83627.1; -; mRNA.
EMBL; AK310257; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK315826; BAF98717.1; -; mRNA.
EMBL; AK222941; BAD96661.1; -; mRNA.
EMBL; AC107016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96653.1; -; Genomic_DNA.
EMBL; BC000654; AAH00654.3; -; mRNA.
EMBL; BC063513; AAH63513.2; -; mRNA.
EMBL; BC073760; AAH73760.1; -; mRNA.
EMBL; BC075839; AAH75839.1; -; mRNA.
EMBL; M26512; AAA51542.1; -; mRNA.
EMBL; X12882; CAA31376.1; -; mRNA.
EMBL; X98614; CAA67203.1; -; mRNA.
CCDS; CCDS58234.1; -. [P05787-2]
CCDS; CCDS8841.1; -. [P05787-1]
PIR; A34720; A34720.
RefSeq; NP_001243222.1; NM_001256293.1. [P05787-1]
RefSeq; NP_002264.1; NM_002273.3. [P05787-1]
UniGene; Hs.533782; -.
UniGene; Hs.708445; -.
ProteinModelPortal; P05787; -.
SMR; P05787; -.
BioGrid; 110054; 56.
DIP; DIP-424N; -.
ELM; P05787; -.
IntAct; P05787; 46.
MINT; MINT-256526; -.
STRING; 9606.ENSP00000293308; -.
DrugBank; DB00031; Tenecteplase.
iPTMnet; P05787; -.
PhosphoSitePlus; P05787; -.
SwissPalm; P05787; -.
UniCarbKB; P05787; -.
BioMuta; KRT8; -.
DMDM; 90110027; -.
SWISS-2DPAGE; P05787; -.
EPD; P05787; -.
PaxDb; P05787; -.
PeptideAtlas; P05787; -.
PRIDE; P05787; -.
TopDownProteomics; P05787-1; -. [P05787-1]
TopDownProteomics; P05787-2; -. [P05787-2]
DNASU; 3856; -.
Ensembl; ENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
Ensembl; ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
Ensembl; ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
Ensembl; ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
GeneID; 3856; -.
KEGG; hsa:3856; -.
UCSC; uc001sbd.3; human. [P05787-1]
CTD; 3856; -.
DisGeNET; 3856; -.
EuPathDB; HostDB:ENSG00000170421.12; -.
GeneCards; KRT8; -.
H-InvDB; HIX0026255; -.
H-InvDB; HIX0034365; -.
H-InvDB; HIX0168895; -.
HGNC; HGNC:6446; KRT8.
HPA; CAB000131; -.
HPA; CAB001696; -.
HPA; HPA049866; -.
MalaCards; KRT8; -.
MIM; 148060; gene.
MIM; 215600; phenotype.
neXtProt; NX_P05787; -.
OpenTargets; ENSG00000170421; -.
PharmGKB; PA30234; -.
eggNOG; ENOG410IG4R; Eukaryota.
eggNOG; ENOG410YY6B; LUCA.
GeneTree; ENSGT00760000118796; -.
HOVERGEN; HBG013015; -.
InParanoid; P05787; -.
KO; K07605; -.
OMA; IQKRTDM; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P05787; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SignaLink; P05787; -.
SIGNOR; P05787; -.
ChiTaRS; KRT8; human.
GeneWiki; Keratin_8; -.
GenomeRNAi; 3856; -.
PMAP-CutDB; P05787; -.
PRO; PR:P05787; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000170421; -.
ExpressionAtlas; P05787; baseline and differential.
Genevisible; P05787; HS.
GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0043034; C:costamere; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IEA:Ensembl.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0051707; P:response to other organism; IEA:Ensembl.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; Glycoprotein;
Host-virus interaction; Intermediate filament; Isopeptide bond;
Keratin; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 483 Keratin, type II cytoskeletal 8.
/FTId=PRO_0000063740.
DOMAIN 91 402 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 90 Head.
REGION 91 126 Coil 1A.
REGION 127 143 Linker 1.
REGION 144 235 Coil 1B.
REGION 236 259 Linker 12.
REGION 260 398 Coil 2.
REGION 261 382 Necessary for interaction with PNN.
{ECO:0000269|PubMed:10809736}.
REGION 399 483 Tail.
COMPBIAS 9 49 Ser-rich.
SITE 342 342 Stutter.
MOD_RES 9 9 Phosphoserine; by PKC/PRKCE.
{ECO:0000269|PubMed:1374067}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 24 24 Phosphoserine; by PKC/PRKCE.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:1374067,
ECO:0000269|PubMed:9054461}.
MOD_RES 26 26 Phosphothreonine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 32 32 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 47 47 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 47 47 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 74 74 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:11781324,
ECO:0000269|PubMed:11788583}.
MOD_RES 101 101 N6-malonyllysine.
{ECO:0000269|PubMed:21908771}.
MOD_RES 207 207 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 228 228 Phosphotyrosine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 253 253 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 295 295 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 325 325 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:Q10758}.
MOD_RES 432 432 Phosphoserine; by CaMK2 and MAPK.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:9054461}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 197 197 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 264 264 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 295 295 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 393 393 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MNGVSWSQDLQEGISAWFGPPASTPASTM (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046000.
VARIANT 53 53 G -> V (in CIRRH; dbSNP:rs61710484).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023058.
VARIANT 54 54 Y -> C (in CIRRH).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023059.
VARIANT 62 62 G -> C (in CIRRH; dbSNP:rs11554495).
{ECO:0000269|PubMed:12724528,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_023060.
VARIANT 63 63 I -> V (in dbSNP:rs59536457).
{ECO:0000269|PubMed:12724528}.
/FTId=VAR_023061.
VARIANT 401 401 R -> W (in dbSNP:rs2277330).
/FTId=VAR_049805.
VARIANT 417 417 S -> G. {ECO:0000269|PubMed:1691124,
ECO:0000269|PubMed:2434381}.
/FTId=VAR_069106.
VARIANT 429 429 G -> D (in dbSNP:rs1065648).
{ECO:0000269|PubMed:2434381}.
/FTId=VAR_069107.
MUTAGEN 72 72 L->P: Increases phosphorylation.
{ECO:0000269|PubMed:11788583}.
MUTAGEN 74 74 S->A: Generates normal-appearing
filaments, that remain stable after
okadaic acid treatment.
{ECO:0000269|PubMed:11788583}.
MUTAGEN 74 74 S->D: Generates normal-appearing
filaments, that are destabilized by
okadaic acid.
{ECO:0000269|PubMed:11788583}.
CONFLICT 56 56 G -> V (in Ref. 5; BAF83627).
{ECO:0000305}.
CONFLICT 77 77 V -> S (in Ref. 2; AAA35748).
{ECO:0000305}.
CONFLICT 201 201 D -> DVD (in Ref. 3; CAA52882).
{ECO:0000305}.
CONFLICT 232 232 I -> L (in Ref. 11; CAA67203).
{ECO:0000305}.
CONFLICT 257 257 D -> E (in Ref. 2; AAA35748).
{ECO:0000305}.
CONFLICT 310 310 M -> I (in Ref. 11; CAA31376).
{ECO:0000305}.
CONFLICT 324 324 L -> F (in Ref. 6; BAD96661).
{ECO:0000305}.
CONFLICT 384 384 L -> M (in Ref. 11; CAA67203).
{ECO:0000305}.
CONFLICT 387 387 E -> D (in Ref. 2; AAA35748).
{ECO:0000305}.
CONFLICT 401 401 R -> P (in Ref. 2; AAA35748).
{ECO:0000305}.
CONFLICT 430 433 LTSP -> SQA (in Ref. 1; AAA35763).
{ECO:0000305}.
CONFLICT 431 431 T -> A (in Ref. 11; CAA67203).
{ECO:0000305}.
CONFLICT 432 432 S -> D (in Ref. 2; AAA35748 and 11;
CAA67203/CAA31376). {ECO:0000305}.
SEQUENCE 483 AA; 53704 MW; B0BC730B65929D37 CRC64;
MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL GGGYGGASGM
GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN KFASFIDKVR FLEQQNKMLE
TKWSLLQQQK TARSNMDNMF ESYINNLRRQ LETLGQEKLK LEAELGNMQG LVEDFKNKYE
DEINKRTEME NEFVLIKKDV DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS
DTSVVLSMDN SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL
RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN AKLSELEAAL
QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES RLESGMQNMS IHTKTTSGYA
GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS SFSRTSSSRA VVVKKIETRD GKLVSESSDV
LPK


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