KRT18
entrez
3875
canonical
uniprot
P05783
canonical
ensembl
ENSG00000111057
resolver
ensp
ENSP00000373487
resolver
ensp
ENSP00000373489
resolver
ensp
ENSP00000542096
resolver
ensp
ENSP00000600646
resolver
ensp
ENSP00000600647
resolver
ensp
ENSP00000600648
resolver
ensp
ENSP00000600649
resolver
enst
ENST00000388835
resolver
enst
ENST00000388837
resolver
enst
ENST00000872037
resolver
enst
ENST00000930587
resolver
enst
ENST00000930588
resolver
enst
ENST00000930589
resolver
enst
ENST00000930590
resolver
genesymbol
KRT18
resolver
genesymbol_syn
CYK18
resolver
hgnc
HGNC:6430
resolver
uniprot
Q53G38
resolver
uniprot
Q5U0N8
resolver
uniprot
Q9BW26
resolver
uniprot_entry
K1C18_HUMAN
resolver
uniprot_sec
Q53G38
resolver
uniprot_sec
Q5U0N8
resolver
uniprot_sec
Q9BW26
resolver
amino_acid_sequence
MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSNSMQTIQKTTTRRIVDGKVVSETNDTKVLRH
uniprot
proteins
disease_involvement
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, ECO:0000269|PubMed:9011570}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Structural component of intermediate filaments in simple epithelial cells. Forms intermediate filaments by heterodimerizing with the type II keratin KRT8, providing mechanical stability and resilience to epithelial cells (PubMed:15529338, PubMed:26823019). Involved in ARHGEF40-mediated actin stress fiber formation and tensional force-induced stress fiber formation and reinforcement (PubMed:26823019). Integrates into the intermediate filament network of skeletal muscle fibers alongside desmin and KRT19, contributing to force transmission (By similarity). Organization and orientation of KRT8/KRT18 filaments are responsible for the properly elongated morphology of epithelial tubules (By similarity). Also acts downstream of ROCK kinase activation as part of a positive feedback mechanism in response to cellular mechanical stress loading (PubMed:26823019). Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization (PubMed:7523419, PubMed:8522591, PubMed:9298992, PubMed:9524113). Involved in the delivery of mutated CFTR to the plasma membrane (PubMed:15529338, PubMed:16424149). Involved in interleukin-6 (IL-6)-mediated barrier protection (PubMed:17213200). {ECO:0000250|UniProtKB:A0A8I3PJ84, ECO:0000250|UniProtKB:P05784, ECO:0000250|UniProtKB:Q5BJY9, ECO:0000269|PubMed:15529338, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:26823019, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8522591, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113}.
uniprot
proteins
mass_dalton
48058
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="S->A: No effect on phosphorylation; when associated with A-7 and A-10."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 7; /note="S->A: No effect on phosphorylation; when associated with A-2 and A-10."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 10; /note="S->A: No effect on phosphorylation; when associated with A-2 and A-7."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 15; /note="S->A: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 18; /note="S->A: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 23; /note="S->A: No effect on phosphorylation; when associated with A-15 and A-18."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 30; /note="S->A: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:7538124"; MUTAGEN 31; /note="S->A: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:7538124"; MUTAGEN 34; /note="S->A: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:9524113"; MUTAGEN 34; /note="S->D,E: Abolishes binding to YWHAE and YWHAZ."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:9524113"; MUTAGEN 42; /note="S->A: No effect on phosphorylation; when associated with A-44."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 44; /note="S->A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 47; /note="S->A: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 49; /note="S->A: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:7538124"; MUTAGEN 51; /note="S->A: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53."; /evidence="ECO:0000269|PubMed:7523419"; MUTAGEN 53; /note="S->A: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis."; /evidence="ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:9298992, ECO:0000269|PubMed:9524113"; MUTAGEN 90; /note="R->C,H: In transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation."; /evidence="ECO:0000269|PubMed:8522591"; MUTAGEN 238; /note="D->E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization."; /evidence="ECO:0000269|PubMed:9298992
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6. {ECO:0000269|PubMed:15368451, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8609167, ECO:0000269|PubMed:9524113}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.
uniprot
proteins
protein_family
Intermediate filament family
uniprot
proteins
pubmed
10809736
uniprot
proteins
pubmed
10852826
uniprot
proteins
pubmed
10954706
uniprot
proteins
pubmed
11684708
uniprot
proteins
pubmed
12724528
uniprot
proteins
pubmed
1371281
uniprot
proteins
pubmed
14756564
uniprot
proteins
pubmed
15368451
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15529338
uniprot
proteins
pubmed
15731013
uniprot
proteins
pubmed
15846844
uniprot
proteins
pubmed
16424149
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17213200
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20729549
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22002106
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23902688
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
2422083
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2434380
uniprot
proteins
pubmed
2434381
uniprot
proteins
pubmed
2454392
uniprot
proteins
pubmed
24940650
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
26823019
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30929300
uniprot
proteins
pubmed
7523419
uniprot
proteins
pubmed
7538124
uniprot
proteins
pubmed
8522591
uniprot
proteins
pubmed
8609167
uniprot
proteins
pubmed
9011570
uniprot
proteins
pubmed
9150948
uniprot
proteins
pubmed
9298992
uniprot
proteins
pubmed
9524113
uniprot
proteins
sequence_length
430
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
uniprot
proteins