Krt18
entrez
16668
canonical
uniprot
P05784
canonical
ensembl
ENSMUSG00000023043
resolver
ensp
ENSMUSP00000023803
resolver
enst
ENSMUST00000023803
resolver
genesymbol
Krt18
resolver
genesymbol_syn
Kerd
resolver
genesymbol_syn
Krt1-18
resolver
uniprot
Q3TIX1
resolver
uniprot
Q3TJH6
resolver
uniprot
Q3TJW7
resolver
uniprot
Q61766
resolver
uniprot_entry
K1C18_MOUSE
resolver
uniprot_sec
Q3TIX1
resolver
uniprot_sec
Q3TJH6
resolver
uniprot_sec
Q3TJW7
resolver
uniprot_sec
Q61766
resolver
amino_acid_sequence
MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLNDRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDVEARYKAQMEQLNGVLLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFSLNDALDSSNSMQTVQKTTTRKIVDGRVVSETNDTRVLRH
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:1691189). Involved in ARHGEF40-mediated actin stress fiber formation and tensional force-induced stress fiber formation and reinforcement (By similarity). Integrates into the intermediate filament network of skeletal muscle fibers alongside desmin and KRT19, contributing to force transmission (PubMed:31721615). 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 (By similarity). Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane (By similarity). Involved in interleukin-6 (IL-6)-mediated barrier protection (PubMed:17213200). {ECO:0000250|UniProtKB:A0A8I3PJ84, ECO:0000250|UniProtKB:P05783, ECO:0000250|UniProtKB:Q5BJY9, ECO:0000269|PubMed:1691189, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:31721615}.
uniprot
proteins
mass_dalton
47538
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-35 increases during mitosis. Phosphorylation increases by IL-6. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:20724476}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation. {ECO:0000250}.
uniprot
proteins
protein_family
Intermediate filament family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1691189
uniprot
proteins
pubmed
16973199
uniprot
proteins
pubmed
17213200
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
20724476
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2416755
uniprot
proteins
pubmed
2454868
uniprot
proteins
pubmed
2467843
uniprot
proteins
pubmed
24940650
uniprot
proteins
pubmed
25617501
uniprot
proteins
pubmed
31721615
uniprot
proteins
pubmed
7504637
uniprot
proteins
pubmed
7507912
uniprot
proteins
pubmed
9298992
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
uniprot
proteins