K2C8_HUMAN
ID K2C8_HUMAN Reviewed; 483 AA.
AC P05787; A8K4H3; B0AZN5; F8VXB4; Q14099; Q14716; Q14717; Q53GJ0; Q6DHW5;
AC Q6GMY0; Q6P4C7; Q96J60;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 7.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Keratin, type II cytoskeletal 8;
DE AltName: Full=Cytokeratin-8;
DE Short=CK-8;
DE AltName: Full=Keratin-8;
DE Short=K8;
DE AltName: Full=Type-II keratin Kb8;
GN Name=KRT8; Synonyms=CYK8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-417.
RX PubMed=1691124; DOI=10.1016/0378-1119(90)90285-y;
RA Krauss S., Franke W.W.;
RT "Organization and sequence of the human gene encoding cytokeratin 8.";
RL Gene 86:241-249(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1692965; DOI=10.1210/mend-4-3-370;
RA Yamamoto R., Kao L.C., McKnight C.E., Strauss J.F. III;
RT "Cloning and sequence of cDNA for human placental cytokeratin 8. Regulation
RT of the mRNA in trophoblastic cells by cAMP.";
RL Mol. Endocrinol. 4:370-374(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=1705144;
RA Waseem A., Alexander C.M., Steel J.B., Lane E.B.;
RT "Embryonic simple epithelial keratins 8 and 18: chromosomal location
RT emphasizes difference from other keratin pairs.";
RL New Biol. 2:464-478(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION AT SER-24 AND
RP SER-432.
RX PubMed=9054461; DOI=10.1074/jbc.272.11.7556;
RA Ku N.-O., Omary M.B.;
RT "Phosphorylation of human keratin 8 in vivo at conserved head domain serine
RT 23 and at epidermal growth factor-stimulated tail domain serine 431.";
RL J. Biol. Chem. 272:7556-7564(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-62.
RC TISSUE=Colon, Liver, Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-231 (ISOFORM 1).
RX PubMed=2471065; DOI=10.1128/mcb.9.4.1553-1565.1989;
RA Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., Oshima R.G.;
RT "Posttranslational regulation of keratins: degradation of mouse and human
RT keratins 18 and 8.";
RL Mol. Cell. Biol. 9:1553-1565(1989).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-483 (ISOFORM 1), AND VARIANTS GLY-417 AND
RP ASP-429.
RX PubMed=2434381; DOI=10.1111/j.1432-0436.1986.tb00412.x;
RA Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W.;
RT "Cytokeratin expression in simple epithelia. III. Detection of mRNAs
RT encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by
RT hybridization with cDNA sequences in vitro and in situ.";
RL Differentiation 33:69-85(1986).
RN [12]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [13]
RP GLYCOSYLATION.
RX PubMed=1371281; DOI=10.1016/s0021-9258(19)50611-1;
RA Chou C.F., Smith A.J., Omary M.B.;
RT "Characterization and dynamics of O-linked glycosylation of human
RT cytokeratin 8 and 18.";
RL J. Biol. Chem. 267:3901-3906(1992).
RN [14]
RP PHOSPHORYLATION AT SER-9 AND SER-24.
RX PubMed=1374067; DOI=10.1083/jcb.117.3.583;
RA Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y., Strulovici B.;
RT "PKC epsilon-related kinase associates with and phosphorylates cytokeratin
RT 8 and 18.";
RL J. Cell Biol. 117:583-593(1992).
RN [15]
RP INTERACTION WITH KRT20, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10973561; DOI=10.1016/s0003-9969(00)00050-9;
RA Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B.;
RT "An immunohistological study of cytokeratin 20 in human and mammalian oral
RT epithelium.";
RL Arch. Oral Biol. 45:879-887(2000).
RN [16]
RP INTERACTION WITH PNN.
RX PubMed=10809736; DOI=10.1074/jbc.275.20.14910;
RA Shi J., Sugrue S.P.;
RT "Dissection of protein linkage between keratins and pinin, a protein with
RT dual location at desmosome-intermediate filament complex and in the
RT nucleus.";
RL J. Biol. Chem. 275:14910-14915(2000).
RN [17]
RP PHOSPHORYLATION AT SER-74.
RX PubMed=11781324; DOI=10.1074/jbc.m111436200;
RA He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E.;
RT "The intermediate filament protein keratin 8 is a novel cytoplasmic
RT substrate for c-Jun N-terminal kinase.";
RL J. Biol. Chem. 277:10767-10774(2002).
RN [18]
RP PHOSPHORYLATION AT SER-74, AND MUTAGENESIS OF LEU-72 AND SER-74.
RX PubMed=11788583; DOI=10.1074/jbc.m107623200;
RA Ku N.O., Azhar S., Omary M.B.;
RT "Keratin 8 phosphorylation by p38 kinase regulates cellular keratin
RT filament reorganization: modulation by a keratin 1-like disease causing
RT mutation.";
RL J. Biol. Chem. 277:10775-10782(2002).
RN [19]
RP INTERACTION WITH TCHP.
RX PubMed=15731013; DOI=10.1242/jcs.01667;
RA Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
RA Usukura J., Inagaki M.;
RT "Identification of trichoplein, a novel keratin filament-binding protein.";
RL J. Cell Sci. 118:1081-1090(2005).
RN [20]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=16000376; DOI=10.1091/mbc.e05-02-0112;
RA Stone M.R., O'Neill A., Catino D., Bloch R.J.;
RT "Specific interaction of the actin-binding domain of dystrophin with
RT intermediate filaments containing keratin 19.";
RL Mol. Biol. Cell 16:4280-4293(2005).
RN [21]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=15846844; DOI=10.1002/pmic.200401093;
RA Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.;
RT "Proteomic profiling of cellular proteins interacting with the hepatitis C
RT virus core protein.";
RL Proteomics 5:2227-2237(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [23]
RP INTERACTION WITH KRT20.
RX PubMed=16608857; DOI=10.1074/jbc.m512284200;
RA Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J.,
RA Burlingame A.L., Omary M.B.;
RT "Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet
RT cell marker.";
RL J. Biol. Chem. 281:16453-16461(2006).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-27; SER-43;
RP SER-253; SER-258; SER-274; SER-400; SER-410; SER-432; SER-475 AND SER-478,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [27]
RP INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19188445; DOI=10.1128/mcb.01337-08;
RA Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
RA Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
RA Quadrifoglio F., Tell G.;
RT "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the
RT rRNA quality control process.";
RL Mol. Cell. Biol. 29:1834-1854(2009).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-207; LYS-295 AND LYS-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [30]
RP GLYCOSYLATION.
RX PubMed=20729549; DOI=10.1074/jbc.m109.098996;
RA Srikanth B., Vaidya M.M., Kalraiya R.D.;
RT "O-GlcNAcylation determines the solubility, filament organization, and
RT stability of keratins 8 and 18.";
RL J. Biol. Chem. 285:34062-34071(2010).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; SER-475 AND SER-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [33]
RP MALONYLATION AT LYS-101.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [34]
RP INTERACTION WITH GPER1.
RX PubMed=21149639; DOI=10.1124/mol.110.069500;
RA Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J.,
RA Martensson U.E., Olde B., Leeb-Lundberg L.M.;
RT "G protein-coupled estrogen receptor 1/G protein-coupled receptor 30
RT localizes in the plasma membrane and traffics intracellularly on
RT cytokeratin intermediate filaments.";
RL Mol. Pharmacol. 79:400-410(2011).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-43; SER-253 AND
RP SER-258, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [36]
RP GLYCOSYLATION.
RX PubMed=22967762; DOI=10.1016/j.bbagen.2012.08.024;
RA Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F.,
RA Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.;
RT "Characterization of O-GlcNAc cycling and proteomic identification of
RT differentially O-GlcNAcylated proteins during G1/S transition.";
RL Biochim. Biophys. Acta 1820:1839-1848(2012).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-21; SER-31; SER-34;
RP SER-39; SER-43; SER-253; SER-258; SER-274; SER-291; SER-330; SER-404;
RP SER-410; SER-475 AND SER-477, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP IDENTIFICATION IN A COMPLEX WITH KRT18, AND INTERACTION WITH KRT18 AND
RP PLEC.
RX PubMed=24940650; DOI=10.1038/jid.2014.255;
RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.;
RT "Interaction of plectin with keratins 5 and 14: dependence on several
RT plectin domains and keratin quaternary structure.";
RL J. Invest. Dermatol. 134:2776-2783(2014).
RN [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-22; SER-253; SER-258;
RP SER-410 AND SER-475, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [40]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-23; ARG-32; ARG-40 AND ARG-47,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285; LYS-304 AND LYS-472, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-285 AND LYS-472, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-122; LYS-130; LYS-197;
RP LYS-264; LYS-285; LYS-295; LYS-304; LYS-325; LYS-393 AND LYS-472, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [44]
RP VARIANTS CIRRH VAL-53; CYS-54 AND CYS-62, AND VARIANT VAL-63.
RX PubMed=12724528; DOI=10.1073/pnas.0936165100;
RA Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B.,
RA Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.;
RT "Keratin 8 and 18 mutations are risk factors for developing liver disease
RT of multiple etiologies.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003).
CC -!- FUNCTION: Together with KRT19, helps to link the contractile apparatus
CC to dystrophin at the costameres of striated muscle.
CC {ECO:0000269|PubMed:16000376}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins
CC (PubMed:16000376). Forms a heterodimer with KRT18 (PubMed:24940650).
CC Associates with KRT20 (PubMed:10973561, PubMed:16608857). Interacts
CC with PLEC isoform 1C, when in a heterodimer with KRT18
CC (PubMed:24940650). Interacts with PNN (PubMed:10809736). When
CC associated with KRT19, interacts with DMD. Interacts with TCHP
CC (PubMed:15731013). Interacts with APEX1 (PubMed:19188445). Interacts
CC with GPER1 (PubMed:21149639). Interacts with EPPK1 (By similarity).
CC {ECO:0000250|UniProtKB:P11679, ECO:0000269|PubMed:10809736,
CC ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:15731013,
CC ECO:0000269|PubMed:16000376, ECO:0000269|PubMed:16608857,
CC ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:21149639,
CC ECO:0000269|PubMed:24940650}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis C virus/HCV
CC core protein. {ECO:0000269|PubMed:15846844}.
CC -!- INTERACTION:
CC P05787; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-297852, EBI-11752486;
CC P05787; P13569: CFTR; NbExp=7; IntAct=EBI-297852, EBI-349854;
CC P05787; P62993: GRB2; NbExp=3; IntAct=EBI-297852, EBI-401755;
CC P05787; Q9Y6K9: IKBKG; NbExp=2; IntAct=EBI-297852, EBI-81279;
CC P05787; A1A4E9: KRT13; NbExp=3; IntAct=EBI-297852, EBI-10171552;
CC P05787; P19012: KRT15; NbExp=6; IntAct=EBI-297852, EBI-739566;
CC P05787; P08779: KRT16; NbExp=3; IntAct=EBI-297852, EBI-356410;
CC P05787; P05783: KRT18; NbExp=16; IntAct=EBI-297852, EBI-297888;
CC P05787; P08727: KRT19; NbExp=3; IntAct=EBI-297852, EBI-742756;
CC P05787; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-297852, EBI-2952736;
CC P05787; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-297852, EBI-11980019;
CC P05787; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-297852, EBI-3044087;
CC P05787; Q7Z3Y7: KRT28; NbExp=5; IntAct=EBI-297852, EBI-11980489;
CC P05787; Q15323: KRT31; NbExp=6; IntAct=EBI-297852, EBI-948001;
CC P05787; Q14525: KRT33B; NbExp=5; IntAct=EBI-297852, EBI-1049638;
CC P05787; O76011: KRT34; NbExp=3; IntAct=EBI-297852, EBI-1047093;
CC P05787; Q92764: KRT35; NbExp=3; IntAct=EBI-297852, EBI-1058674;
CC P05787; O76013-2: KRT36; NbExp=3; IntAct=EBI-297852, EBI-11958506;
CC P05787; O76015: KRT38; NbExp=7; IntAct=EBI-297852, EBI-1047263;
CC P05787; Q6A162: KRT40; NbExp=6; IntAct=EBI-297852, EBI-10171697;
CC P05787; O75022: LILRB3; NbExp=3; IntAct=EBI-297852, EBI-2830524;
CC P05787; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-297852, EBI-11750983;
CC P05787; Q13835-2: PKP1; NbExp=3; IntAct=EBI-297852, EBI-9087684;
CC P05787; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-297852, EBI-1105213;
CC P05787; P08670: VIM; NbExp=2; IntAct=EBI-297852, EBI-353844;
CC P05787; P14079: tax; Xeno; NbExp=3; IntAct=EBI-297852, EBI-9675698;
CC P05787-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-10194642, EBI-11954292;
CC P05787-2; A1A4E9: KRT13; NbExp=3; IntAct=EBI-10194642, EBI-10171552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561,
CC ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q10758}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05787-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05787-2; Sequence=VSP_046000;
CC -!- TISSUE SPECIFICITY: Observed in muscle fibers accumulating in the
CC costameres of myoplasm at the sarcolemma membrane in structures that
CC contain dystrophin and spectrin. Expressed in gingival mucosa and hard
CC palate of the oral cavity. {ECO:0000269|PubMed:10973561,
CC ECO:0000269|PubMed:16000376}.
CC -!- PTM: Phosphorylation on serine residues is enhanced during EGF
CC stimulation and mitosis. Ser-74 phosphorylation plays an important role
CC in keratin filament reorganization. {ECO:0000269|PubMed:11781324,
CC ECO:0000269|PubMed:11788583, ECO:0000269|PubMed:1374067,
CC ECO:0000269|PubMed:9054461}.
CC -!- PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases
CC solubility, and decreases stability by inducing proteasomal
CC degradation.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC -!- DISEASE: Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized
CC by severe panlobular liver-cell swelling with Mallory body formation,
CC prominent pericellular fibrosis, and marked deposits of copper.
CC Clinical features include abdomen swelling, jaundice and pulmonary
CC hypertension. {ECO:0000269|PubMed:12724528}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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DR EMBL; M34482; AAA35763.1; -; Genomic_DNA.
DR EMBL; M34225; AAA35748.1; -; mRNA.
DR EMBL; X74929; CAA52882.1; -; mRNA.
DR EMBL; X74981; CAA52916.1; -; Genomic_DNA.
DR EMBL; U76549; AAB18966.1; -; mRNA.
DR EMBL; AK290938; BAF83627.1; -; mRNA.
DR EMBL; AK310257; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK315826; BAF98717.1; -; mRNA.
DR EMBL; AK222941; BAD96661.1; -; mRNA.
DR EMBL; AC107016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96653.1; -; Genomic_DNA.
DR EMBL; BC000654; AAH00654.3; -; mRNA.
DR EMBL; BC063513; AAH63513.2; -; mRNA.
DR EMBL; BC073760; AAH73760.1; -; mRNA.
DR EMBL; BC075839; AAH75839.1; -; mRNA.
DR EMBL; M26512; AAA51542.1; -; mRNA.
DR EMBL; X12882; CAA31376.1; -; mRNA.
DR EMBL; X98614; CAA67203.1; -; mRNA.
DR CCDS; CCDS58234.1; -. [P05787-2]
DR CCDS; CCDS8841.1; -. [P05787-1]
DR PIR; A34720; A34720.
DR RefSeq; NP_001243222.1; NM_001256293.1. [P05787-1]
DR RefSeq; NP_002264.1; NM_002273.3. [P05787-1]
DR AlphaFoldDB; P05787; -.
DR SMR; P05787; -.
DR BioGRID; 110054; 358.
DR ComplexPortal; CPX-5661; Keratin-8 - Keratin-18 dimer complex.
DR DIP; DIP-424N; -.
DR ELM; P05787; -.
DR IntAct; P05787; 100.
DR MINT; P05787; -.
DR STRING; 9606.ENSP00000449404; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB06245; Lanoteplase.
DR DrugBank; DB00031; Tenecteplase.
DR GlyConnect; 313; 2 N-Linked glycans (1 site), 1 O-Linked glycan (2 sites).
DR GlyGen; P05787; 8 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (7 sites).
DR iPTMnet; P05787; -.
DR MetOSite; P05787; -.
DR PhosphoSitePlus; P05787; -.
DR SwissPalm; P05787; -.
DR BioMuta; KRT8; -.
DR DMDM; 90110027; -.
DR SWISS-2DPAGE; P05787; -.
DR CPTAC; CPTAC-1524; -.
DR CPTAC; CPTAC-1525; -.
DR EPD; P05787; -.
DR jPOST; P05787; -.
DR MassIVE; P05787; -.
DR PaxDb; P05787; -.
DR PeptideAtlas; P05787; -.
DR PRIDE; P05787; -.
DR ProteomicsDB; 29093; -.
DR ProteomicsDB; 51858; -. [P05787-1]
DR TopDownProteomics; P05787-1; -. [P05787-1]
DR TopDownProteomics; P05787-2; -. [P05787-2]
DR ABCD; P05787; 2 sequenced antibodies.
DR Antibodypedia; 3437; 3611 antibodies from 52 providers.
DR DNASU; 3856; -.
DR Ensembl; ENST00000293308.11; ENSP00000293308.6; ENSG00000170421.13. [P05787-1]
DR Ensembl; ENST00000546897.5; ENSP00000447402.1; ENSG00000170421.13. [P05787-1]
DR Ensembl; ENST00000552150.5; ENSP00000449404.1; ENSG00000170421.13. [P05787-2]
DR Ensembl; ENST00000552551.5; ENSP00000447566.1; ENSG00000170421.13. [P05787-1]
DR Ensembl; ENST00000692008.1; ENSP00000509398.1; ENSG00000170421.13. [P05787-1]
DR GeneID; 3856; -.
DR KEGG; hsa:3856; -.
DR MANE-Select; ENST00000692008.1; ENSP00000509398.1; NM_002273.4; NP_002264.1.
DR UCSC; uc001sbd.3; human. [P05787-1]
DR CTD; 3856; -.
DR DisGeNET; 3856; -.
DR GeneCards; KRT8; -.
DR HGNC; HGNC:6446; KRT8.
DR HPA; ENSG00000170421; Tissue enhanced (intestine, stomach).
DR MalaCards; KRT8; -.
DR MIM; 148060; gene.
DR MIM; 215600; phenotype.
DR neXtProt; NX_P05787; -.
DR OpenTargets; ENSG00000170421; -.
DR PharmGKB; PA30234; -.
DR VEuPathDB; HostDB:ENSG00000170421; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000153339; -.
DR InParanoid; P05787; -.
DR OMA; AEMWYKQ; -.
DR PhylomeDB; P05787; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; P05787; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P05787; -.
DR SIGNOR; P05787; -.
DR BioGRID-ORCS; 3856; 187 hits in 1021 CRISPR screens.
DR ChiTaRS; KRT8; human.
DR GeneWiki; Keratin_8; -.
DR GenomeRNAi; 3856; -.
DR Pharos; P05787; Tbio.
DR PRO; PR:P05787; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P05787; protein.
DR Bgee; ENSG00000170421; Expressed in mucosa of transverse colon and 116 other tissues.
DR ExpressionAtlas; P05787; baseline and differential.
DR Genevisible; P05787; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0045095; C:keratin filament; IPI:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IBA:GO_Central.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disease variant; Glycoprotein;
KW Host-virus interaction; Intermediate filament; Isopeptide bond; Keratin;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..483
FT /note="Keratin, type II cytoskeletal 8"
FT /id="PRO_0000063740"
FT DOMAIN 91..402
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..90
FT /note="Head"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..126
FT /note="Coil 1A"
FT REGION 127..143
FT /note="Linker 1"
FT REGION 144..235
FT /note="Coil 1B"
FT REGION 236..259
FT /note="Linker 12"
FT REGION 260..398
FT /note="Coil 2"
FT REGION 261..382
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000269|PubMed:10809736"
FT REGION 399..483
FT /note="Tail"
FT SITE 342
FT /note="Stutter"
FT MOD_RES 9
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000269|PubMed:1374067"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 23
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 24
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000269|PubMed:1374067,
FT ECO:0000269|PubMed:9054461, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 47
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 47
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 74
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:11781324,
FT ECO:0000269|PubMed:11788583"
FT MOD_RES 101
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 228
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 325
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q10758"
FT MOD_RES 432
FT /note="Phosphoserine; by CaMK2 and MAPK"
FT /evidence="ECO:0000269|PubMed:9054461,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 264
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 304
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 393
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MNGVSWSQDLQEGISAWFGPPASTPASTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046000"
FT VARIANT 53
FT /note="G -> V (in CIRRH; dbSNP:rs61710484)"
FT /evidence="ECO:0000269|PubMed:12724528"
FT /id="VAR_023058"
FT VARIANT 54
FT /note="Y -> C (in CIRRH)"
FT /evidence="ECO:0000269|PubMed:12724528"
FT /id="VAR_023059"
FT VARIANT 62
FT /note="G -> C (in CIRRH; dbSNP:rs11554495)"
FT /evidence="ECO:0000269|PubMed:12724528,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023060"
FT VARIANT 63
FT /note="I -> V (in dbSNP:rs59536457)"
FT /evidence="ECO:0000269|PubMed:12724528"
FT /id="VAR_023061"
FT VARIANT 401
FT /note="R -> W (in dbSNP:rs2277330)"
FT /id="VAR_049805"
FT VARIANT 417
FT /note="S -> G"
FT /evidence="ECO:0000269|PubMed:1691124,
FT ECO:0000269|PubMed:2434381"
FT /id="VAR_069106"
FT VARIANT 429
FT /note="G -> D (in dbSNP:rs1065648)"
FT /evidence="ECO:0000269|PubMed:2434381"
FT /id="VAR_069107"
FT MUTAGEN 72
FT /note="L->P: Increases phosphorylation."
FT /evidence="ECO:0000269|PubMed:11788583"
FT MUTAGEN 74
FT /note="S->A: Generates normal-appearing filaments, that
FT remain stable after okadaic acid treatment."
FT /evidence="ECO:0000269|PubMed:11788583"
FT MUTAGEN 74
FT /note="S->D: Generates normal-appearing filaments, that are
FT destabilized by okadaic acid."
FT /evidence="ECO:0000269|PubMed:11788583"
FT CONFLICT 56
FT /note="G -> V (in Ref. 5; BAF83627)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="V -> S (in Ref. 2; AAA35748)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> DVD (in Ref. 3; CAA52882)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="I -> L (in Ref. 11; CAA67203)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="D -> E (in Ref. 2; AAA35748)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="M -> I (in Ref. 11; CAA31376)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="L -> F (in Ref. 6; BAD96661)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="L -> M (in Ref. 11; CAA67203)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="E -> D (in Ref. 2; AAA35748)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> P (in Ref. 2; AAA35748)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..433
FT /note="LTSP -> SQA (in Ref. 1; AAA35763)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="T -> A (in Ref. 11; CAA67203)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="S -> D (in Ref. 2; AAA35748 and 11; CAA67203/
FT CAA31376)"
FT /evidence="ECO:0000305"
SQ 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
