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 27-MAR-2024, entry version 229. 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] {ECO:0007744|PDB:4XIF} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 8-16 IN COMPLEX WITH OGT, AND RP GLYCOSYLATION AT SER-12. RX PubMed=26237509; DOI=10.1038/nsmb.3063; RA Pathak S., Alonso J., Schimpl M., Rafie K., Blair D.E., Borodkin V.S., RA Albarbarawi O., van Aalten D.M.F.; RT "The active site of O-GlcNAc transferase imposes constraints on substrate RT sequence."; RL Nat. Struct. Mol. Biol. 22:744-750(2015). RN [22] 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 53. DR IntAct; P08729; 15. 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 CPTAC; CPTAC-1520; -. DR CPTAC; CPTAC-1521; -. DR CPTAC; CPTAC-5843; -. DR CPTAC; CPTAC-5844; -. DR CPTAC; CPTAC-5868; -. DR CPTAC; CPTAC-5869; -. DR jPOST; P08729; -. DR MassIVE; P08729; -. DR PaxDb; 9606-ENSP00000329243; -. DR PeptideAtlas; P08729; -. DR PRIDE; P08729; -. DR ProteomicsDB; 52163; -. DR TopDownProteomics; P08729; -. DR Antibodypedia; 1535; 2931 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 AGR; HGNC:6445; -. 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; 4640531at2759; -. 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; 11 hits in 1157 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 137 other cell types or tissues. DR ExpressionAtlas; P08729; baseline and differential. 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 Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR032444; Keratin_2_head. DR InterPro; IPR003054; Keratin_II. DR PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR45616:SF21; KERATIN, TYPE II CYTOSKELETAL 7; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF16208; Keratin_2_head; 1. DR PRINTS; PR01276; TYPE2KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 3. DR SUPFAM; SSF46579; Prefoldin; 1. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR SWISS-2DPAGE; P08729; -. DR Genevisible; P08729; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; KW Direct protein sequencing; Glycoprotein; Host-virus interaction; KW Intermediate filament; Isopeptide bond; Keratin; Methylation; KW Phosphoprotein; Reference proteome; 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 CARBOHYD 12 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000269|PubMed:26237509" 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 //