K2C7_HUMAN
ID K2C7_HUMAN Reviewed; 469 AA.
AC P08729; Q92676; Q9BUD8; Q9Y3R7;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 5.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Keratin, type II cytoskeletal 7;
DE AltName: Full=Cytokeratin-7;
DE Short=CK-7;
DE AltName: Full=Keratin-7;
DE Short=K7;
DE AltName: Full=Sarcolectin;
DE AltName: Full=Type-II keratin Kb7;
GN Name=KRT7; Synonyms=SCL;
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 [MRNA], TISSUE SPECIFICITY, AND VARIANTS ARG-186 AND
RP ALA-364.
RC TISSUE=Mesothelium;
RX PubMed=2415537; DOI=10.1083/jcb.101.6.2366;
RA Glass C., Kim K.H., Fuchs E.;
RT "Sequence and expression of a human type II mesothelial keratin.";
RL J. Cell Biol. 101:2366-2373(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, AND
RP VARIANTS ARG-186 AND ALA-364.
RX PubMed=2459129; DOI=10.1083/jcb.107.4.1337;
RA Glass C., Fuchs E.;
RT "Isolation, sequence, and differential expression of a human K7 gene in
RT simple epithelial cells.";
RL J. Cell Biol. 107:1337-1350(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS ARG-186 AND ALA-364.
RC TISSUE=Placenta;
RX PubMed=10492017; DOI=10.1016/s0300-9084(99)80128-x;
RA Kaba A., Jiang P., Chany-Fournier F., Chany C.;
RT "Sarcolectin (SCL): structure and expression of the recombinant molecule.";
RL Biochimie 81:709-715(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND VARIANTS
RP ARG-186 AND ALA-364.
RC TISSUE=Keratinocyte;
RX PubMed=12359226; DOI=10.1016/s0006-291x(02)02288-x;
RA Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B.,
RA McLean W.H.I.;
RT "Cloning of human, murine, and marsupial keratin 7 and a survey of K7
RT expression in the mouse.";
RL Biochem. Biophys. Res. Commun. 297:818-827(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-186 AND ALA-364.
RC TISSUE=Pancreas;
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 [7]
RP PROTEIN SEQUENCE OF 2-48; 53-96; 102-110; 123-130; 137-161; 178-208;
RP 215-273; 277-296; 306-313; 318-326; 330-348; 352-363 AND 374-402, CLEAVAGE
RP OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-20, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP INTERACTION WITH EIF3S10.
RX PubMed=11169732;
RX DOI=10.1002/1097-4644(20010315)80:4<483::aid-jcb1002>3.0.co;2-b;
RA Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
RT "Molecular interaction between human tumor marker protein p150, the largest
RT subunit of eIF3, and intermediate filament protein K7.";
RL J. Cell. Biochem. 80:483-490(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH HPV16 E7 (MICROBIAL INFECTION).
RX PubMed=12072504; DOI=10.1128/jvi.76.14.7040-7048.2002;
RA Kanduc D.;
RT "Translational regulation of human papillomavirus type 16 E7 mRNA by the
RT peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7.";
RL J. Virol. 76:7040-7048(2002).
RN [10]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-254, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND IDENTIFICATION BY
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-6; SER-7; SER-53;
RP SER-71; SER-83; THR-97; SER-254 AND THR-289, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP 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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
RP 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-130; LYS-265; LYS-286; LYS-296
RP AND LYS-331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-186, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Blocks interferon-dependent interphase and stimulates DNA
CC synthesis in cells. Involved in the translational regulation of the
CC human papillomavirus type 16 E7 mRNA (HPV16 E7).
CC {ECO:0000269|PubMed:10492017, ECO:0000269|PubMed:12072504}.
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit
CC EIF3S10. Interacts with GPER1. {ECO:0000269|PubMed:11169732,
CC ECO:0000269|PubMed:21149639}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
CC 16/HPV16 protein E7. {ECO:0000269|PubMed:12072504}.
CC -!- INTERACTION:
CC P08729; Q14152: EIF3A; NbExp=3; IntAct=EBI-297833, EBI-366617;
CC P08729; P09429: HMGB1; NbExp=6; IntAct=EBI-297833, EBI-389432;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2459129}.
CC -!- TISSUE SPECIFICITY: Expressed in cultured epidermal, bronchial and
CC mesothelial cells but absent in colon, ectocervix and liver. Observed
CC throughout the glandular cells in the junction between stomach and
CC esophagus but is absent in the esophagus. {ECO:0000269|PubMed:12359226,
CC ECO:0000269|PubMed:2415537}.
CC -!- INDUCTION: Up-regulated by retinoic acid. {ECO:0000269|PubMed:2459129}.
CC -!- PTM: Arg-20 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- MASS SPECTROMETRY: Mass=51203.48; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA26956.2; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; X03212; CAA26956.2; ALT_SEQ; mRNA.
DR EMBL; X13320; CAA31695.1; -; Genomic_DNA.
DR EMBL; X13346; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13347; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13348; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13349; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13350; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13351; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13352; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; X13353; CAA31695.1; JOINED; Genomic_DNA.
DR EMBL; AJ238246; CAB41416.1; -; mRNA.
DR EMBL; AF509887; AAN64031.1; -; mRNA.
DR EMBL; AF509892; AAN64035.1; -; Genomic_DNA.
DR EMBL; AF509891; AAN64035.1; JOINED; Genomic_DNA.
DR EMBL; AC007338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002700; AAH02700.1; -; mRNA.
DR CCDS; CCDS8822.1; -.
DR PIR; B24177; B24177.
DR PIR; S05602; S05602.
DR RefSeq; NP_005547.3; NM_005556.3.
DR PDB; 4XIF; X-ray; 3.20 A; E/F/G/H=8-16.
DR PDBsum; 4XIF; -.
DR AlphaFoldDB; P08729; -.
DR SMR; P08729; -.
DR BioGRID; 110053; 45.
DR IntAct; P08729; 13.
DR MINT; P08729; -.
DR STRING; 9606.ENSP00000329243; -.
DR DrugBank; DB01087; Primaquine.
DR DrugBank; DB04959; Verpasep caltespen.
DR GlyGen; P08729; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P08729; -.
DR MetOSite; P08729; -.
DR PhosphoSitePlus; P08729; -.
DR SwissPalm; P08729; -.
DR BioMuta; KRT7; -.
DR DMDM; 317373583; -.
DR SWISS-2DPAGE; P08729; -.
DR CPTAC; CPTAC-1520; -.
DR CPTAC; CPTAC-1521; -.
DR jPOST; P08729; -.
DR MassIVE; P08729; -.
DR PaxDb; P08729; -.
DR PeptideAtlas; P08729; -.
DR PRIDE; P08729; -.
DR ProteomicsDB; 52163; -.
DR TopDownProteomics; P08729; -.
DR Antibodypedia; 1535; 2533 antibodies from 57 providers.
DR CPTC; P08729; 2 antibodies.
DR DNASU; 3855; -.
DR Ensembl; ENST00000331817.6; ENSP00000329243.5; ENSG00000135480.17.
DR GeneID; 3855; -.
DR KEGG; hsa:3855; -.
DR MANE-Select; ENST00000331817.6; ENSP00000329243.5; NM_005556.4; NP_005547.3.
DR UCSC; uc001saa.2; human.
DR CTD; 3855; -.
DR DisGeNET; 3855; -.
DR GeneCards; KRT7; -.
DR HGNC; HGNC:6445; KRT7.
DR HPA; ENSG00000135480; Tissue enhanced (salivary gland, thyroid gland).
DR MIM; 148059; gene.
DR neXtProt; NX_P08729; -.
DR OpenTargets; ENSG00000135480; -.
DR PharmGKB; PA30233; -.
DR VEuPathDB; HostDB:ENSG00000135480; -.
DR eggNOG; ENOG502QURK; Eukaryota.
DR GeneTree; ENSGT00940000161303; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; P08729; -.
DR OMA; QRSKQEM; -.
DR OrthoDB; 824246at2759; -.
DR PhylomeDB; P08729; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; P08729; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; P08729; -.
DR SIGNOR; P08729; -.
DR BioGRID-ORCS; 3855; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; KRT7; human.
DR GeneWiki; Keratin_7; -.
DR GenomeRNAi; 3855; -.
DR Pharos; P08729; Tbio.
DR PRO; PR:P08729; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P08729; protein.
DR Bgee; ENSG00000135480; Expressed in left lobe of thyroid gland and 135 other tissues.
DR ExpressionAtlas; P08729; baseline and differential.
DR Genevisible; P08729; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Intermediate filament;
KW Isopeptide bond; Keratin; Methylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..469
FT /note="Keratin, type II cytoskeletal 7"
FT /id="PRO_0000063725"
FT DOMAIN 91..403
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 2..90
FT /note="Head"
FT REGION 90..126
FT /note="Coil 1A"
FT REGION 92..97
FT /note="Interaction with HPV16 E7"
FT /evidence="ECO:0000269|PubMed:12072504"
FT REGION 127..144
FT /note="Linker 1"
FT REGION 145..236
FT /note="Coil 1B"
FT REGION 237..260
FT /note="Linker 12"
FT REGION 261..399
FT /note="Coil 2"
FT REGION 400..469
FT /note="Tail"
FT SITE 343
FT /note="Stutter"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 20
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 20
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 130
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 265
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 286
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 186
FT /note="H -> R (in dbSNP:rs6580870)"
FT /evidence="ECO:0000269|PubMed:10492017,
FT ECO:0000269|PubMed:12359226, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2415537, ECO:0000269|PubMed:2459129,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_060731"
FT VARIANT 364
FT /note="G -> A (in dbSNP:rs2608009)"
FT /evidence="ECO:0000269|PubMed:10492017,
FT ECO:0000269|PubMed:12359226, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2415537, ECO:0000269|PubMed:2459129"
FT /id="VAR_016321"
FT CONFLICT 79
FT /note="D -> G (in Ref. 3; CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="SL -> FS (in Ref. 3; CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="T -> A (in Ref. 1; CAA26956 and 2; CAA31695)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="L -> M (in Ref. 3; CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> Q (in Ref. 1; CAA26956, 2; CAA31695 and 3;
FT CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> G (in Ref. 1; CAA26956, 2; CAA31695 and 3;
FT CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> T (in Ref. 1; CAA26956, 2; CAA31695 and 3;
FT CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> C (in Ref. 1; CAA26956 and 2; CAA31695)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="V -> A (in Ref. 3; CAB41416)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="A -> T (in Ref. 3; CAB41416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51386 MW; 070CBE8F66A62497 CRC64;
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA VRSAYGGPVG
AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN KFASFIDKVR FLEQQNKLLE
TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG QLEALQVDGG RLEAELRSMQ DVVEDFKNKY
EDEINHRTAA ENEFVVLKKD VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI
SDTSVVLSMD NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD
LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA RAKQEELEAA
LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE SRLAGDGVGA VNISVMNSTG
GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG LLKAYSIRTA SASRRSARD
