KRT14
entrez
3861
canonical
uniprot
P02533
canonical
ensembl
ENSG00000186847
resolver
ensp
ENSP00000167586
resolver
enst
ENST00000167586
resolver
genesymbol
KRT14
resolver
hgnc
HGNC:6416
resolver
uniprot
Q14715
resolver
uniprot
Q53XY3
resolver
uniprot
Q9BUE3
resolver
uniprot
Q9UBN2
resolver
uniprot
Q9UBN3
resolver
uniprot
Q9UCY4
resolver
uniprot_entry
K1C14_HUMAN
resolver
uniprot_sec
Q14715
resolver
uniprot_sec
Q53XY3
resolver
uniprot_sec
Q9BUE3
resolver
uniprot_sec
Q9UBN2
resolver
uniprot_sec
Q9UBN3
resolver
uniprot_sec
Q9UCY4
resolver
amino_acid_sequence
MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN
uniprot
proteins
disease_involvement
DISEASE: Epidermolysis bullosa simplex 1A, generalized severe (EBS1A) [MIM:131760]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1A is an autosomal dominant form characterized by generalized intraepidermal skin blistering that begins and is very prominent at birth. EBS1A may be life-threatening in the first year of life. Tendency to blistering diminishes in adolescence. {ECO:0000269|PubMed:10583131, ECO:0000269|PubMed:10730767, ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:1717157, ECO:0000269|PubMed:21375516, ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:7688405, ECO:0000269|PubMed:8601736, ECO:0000269|PubMed:9804355, ECO:0000269|PubMed:9989794, ECO:0000269|Ref.38}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex 1C, localized (EBS1C) [MIM:131800]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1C is an autosomal dominant form with intraepidermal blistering mainly restricted to hands and feet beginning in infancy. Nails may be thick and dystrophic. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:21375516, ECO:0000269|PubMed:26432462, ECO:0000269|PubMed:7506606, ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:9284105, ECO:0000269|PubMed:9804357, ECO:0000269|PubMed:9989794}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex 1B, generalized intermediate (EBS1B) [MIM:131900]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1B is an autosomal dominant form characterized by generalized intraepidermal blistering beginning at birth. The tendency to blistering diminishes in adolescence, when it may become localized to hands and feet. {ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:1720261, ECO:0000269|PubMed:7526926, ECO:0000269|PubMed:7682883, ECO:0000269|PubMed:9989794, ECO:0000269|Ref.10, ECO:0000269|Ref.38}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Epidermolysis bullosa simplex 1D, generalized, intermediate or severe, autosomal recessive (EBS1D) [MIM:601001]: A form of epidermolysis bullosa simplex, a group of skin fragility disorders characterized by skin blistering due to cleavage within the basal layer of keratinocytes, and erosions caused by minor mechanical trauma. There is a broad spectrum of clinical severity ranging from minor blistering on the feet, to subtypes with extracutaneous involvement and a lethal outcome. EBS1D is an autosomal recessive form characterized by blistering beginning at birth or early childhood. In some patients hands and feet are primarily affected, and in others blistering anywhere on the body may occur. In some patients the condition improves with age. {ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:22832485, ECO:0000269|PubMed:7526933}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Naegeli-Franceschetti-Jadassohn syndrome (NFJS) [MIM:161000]: A rare autosomal dominant form of ectodermal dysplasia. The cardinal features are absence of dermatoglyphics (fingerprints), reticular cutaneous hyperpigmentation (starting at about the age of 2 years without a preceding inflammatory stage), palmoplantar keratoderma, hypohidrosis with diminished sweat gland function and discomfort provoked by heat, nail dystrophy, and tooth enamel defects. {ECO:0000269|PubMed:16960809}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Dermatopathia pigmentosa reticularis (DPR) [MIM:125595]: A rare ectodermal dysplasia characterized by lifelong persistent reticulate hyperpigmentation, non-cicatricial alopecia, and nail dystrophy. Variable features include adermatoglyphia, hypohidrosis or hyperhidrosis, and palmoplantar hyperkeratosis. {ECO:0000269|PubMed:16960809}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Structural component of intermediate filaments in basal keratinocytes of stratified epithelia. Forms heteropolymers with type II keratin KRT5, contributing to the keratin intermediate filament network that confers mechanical strength and structural integrity to the basal layer of the epidermis and other stratified epithelial (PubMed:11724817, PubMed:1694855, PubMed:1720261, PubMed:41511042). The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro (PubMed:11724817). Displays an antagonist role with KRT15 in basal epithelial cells, where KRT14 promotes cell differentiation while KRT15 maintains the progenitor state and promotes proliferation and clonogenicity (PubMed:41511042). Promotes cell differentiation by retaining YAP1 in the cytoplasm of basal keratinocytes via regulatory residue C367 and stratifin/SNF interaction (PubMed:41511042). Contributes to airway basal cell differentiation after injury (PubMed:36512409). {ECO:0000269|PubMed:11724817, ECO:0000269|PubMed:1694855, ECO:0000269|PubMed:1720261, ECO:0000269|PubMed:36512409, ECO:0000269|PubMed:41511042}.
uniprot
proteins
mass_dalton
51561
uniprot
proteins
mutagenesis
MUTAGEN 39..43; /note="SCRAP->GFGGG: Loss of SFN-YAP proximity."; /evidence="ECO:0000269|PubMed:41511042"; MUTAGEN 335; /note="R->A: Increase in keratin-positive aggregates and keratin intermediate filament networks that are very thin and sparse with short filaments."; /evidence="ECO:0000269|PubMed:31995743"; MUTAGEN 342; /note="E->A: Increase in keratin-positive aggregates and keratin intermediate filament networks that are very thin and sparse with short filaments."; /evidence="ECO:0000269|PubMed:31995743"; MUTAGEN 346; /note="Q->A: Increase in keratin-positive aggregates and keratin intermediate filament networks that are very thin and sparse with short filaments."; /evidence="ECO:0000269|PubMed:31995743"; MUTAGEN 365; /note="R->A: No effect on interaction with KRT5 or keratin intermediate filament networks."; /evidence="ECO:0000269|PubMed:31995743"; MUTAGEN 366; /note="Y->A: No effect on interaction with KRT5 or keratin intermediate filament networks."; /evidence="ECO:0000269|PubMed:31995743"; MUTAGEN 367; /note="C->A: Loss of SFN-YAP proximity."; /evidence="ECO:0000269|PubMed:41511042"; MUTAGEN 372; /note="Q->A: No effect on interaction with KRT5 or keratin intermediate filament networks."; /evidence="ECO:0000269|PubMed:31995743
uniprot
proteins
post_translational_modification
PTM: A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus. {ECO:0000250|UniProtKB:Q61781}.; PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:27798626}.; PTM: Phosphorylated. {ECO:0000269|PubMed:41511042}.
uniprot
proteins
protein_family
Intermediate filament family
uniprot
proteins
pubmed
10583131
uniprot
proteins
pubmed
10730767
uniprot
proteins
pubmed
10733662
uniprot
proteins
pubmed
10820403
uniprot
proteins
pubmed
10852826
uniprot
proteins
pubmed
11684708
uniprot
proteins
pubmed
11710919
uniprot
proteins
pubmed
11724817
uniprot
proteins
pubmed
12603865
uniprot
proteins
pubmed
12655565
uniprot
proteins
pubmed
12707098
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14987259
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16786515
uniprot
proteins
pubmed
16882168
uniprot
proteins
pubmed
1694855
uniprot
proteins
pubmed
16960809
uniprot
proteins
pubmed
1717157
uniprot
proteins
pubmed
1720261
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21375516
uniprot
proteins
pubmed
22705788
uniprot
proteins
pubmed
22832485
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24940650
uniprot
proteins
pubmed
24981776
uniprot
proteins
pubmed
2580298
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26432462
uniprot
proteins
pubmed
26758872
uniprot
proteins
pubmed
27798626
uniprot
proteins
pubmed
31995743
uniprot
proteins
pubmed
32179842
uniprot
proteins
pubmed
36512409
uniprot
proteins
pubmed
41511042
uniprot
proteins
pubmed
6186381
uniprot
proteins
pubmed
6210150
uniprot
proteins
pubmed
7506097
uniprot
proteins
pubmed
7506606
uniprot
proteins
pubmed
7526926
uniprot
proteins
pubmed
7526933
uniprot
proteins
pubmed
7561171
uniprot
proteins
pubmed
7682883
uniprot
proteins
pubmed
7688405
uniprot
proteins
pubmed
8601736
uniprot
proteins
pubmed
9284105
uniprot
proteins
pubmed
9457912
uniprot
proteins
pubmed
9804355
uniprot
proteins
pubmed
9804357
uniprot
proteins
pubmed
9989794
uniprot
proteins
sequence_length
472
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11724817, ECO:0000269|PubMed:31995743, ECO:0000269|PubMed:32179842}. Nucleus {ECO:0000269|PubMed:11724817}. Note=Expressed in both as a filamentous pattern. {ECO:0000269|PubMed:11724817}.
uniprot
proteins