{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P08727","secondaryAccessions":["B2R874","Q5XG83","Q6NW33","Q7L5M9","Q96A53","Q96FV1","Q9BYF9","Q9P1Y4"],"uniProtkbId":"K1C19_HUMAN","entryAudit":{"firstPublicDate":"1988-08-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2010-11-02","entryVersion":236,"sequenceVersion":4},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Keratin, type I cytoskeletal 19"}},"alternativeNames":[{"fullName":{"value":"Cytokeratin-19"},"shortNames":[{"value":"CK-19"}]},{"fullName":{"value":"Keratin-19"},"shortNames":[{"value":"K19"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6436"}],"value":"KRT19"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19001"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16000376"}],"value":"Structural component of intermediate filaments in epithelial cells. Forms intermediate filaments by heterodimerizing with the type II keratin KRT8, providing mechanical integrity to epithelial cells (PubMed:16000376). Integrates into the intermediate filament network of skeletal muscle fibers alongside desmin and KRT18, contributing to force transmission (By similarity). Specifically interacts with the actin-binding domain of dystrophin, helping to link the contractile apparatus to dystrophin at the costameres of striated muscle (PubMed:16000376)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P13645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10809736"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16000376"}],"value":"Heterodimers composed of one type I and one type II keratins; forms parallel coiled-coil heterodimers (By similarity). Heterodimers associate in an antiparallel manner to form heterotetramers, which further assemble into higher-order keratin intermediate filaments (By similarity). Interacts with PNN and the actin-binding domain of DMD (PubMed:10809736, PubMed:16000376)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15846844"}],"value":"(Microbial infection) Interacts with hepatitis C virus/HCV core 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in a defined zone of basal keratinocytes in the deep outer root sheath of hair follicles. 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