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P02533 (K1C14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type I cytoskeletal 14
Alternative name(s):
Cytokeratin-14
Short name=CK-14
Keratin-14
Short name=K14
Gene names
Name:KRT14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

Heterotetramer of two type I and two type II keratins. disulfide-linked keratin-14 associates with keratin-5. Interacts with TRADD and with keratin filaments. Associates with other type I keratins. Ref.12 Ref.13 Ref.16

Subcellular location

Cytoplasm. Nucleus. Note: Expressed in both as a filamentous pattern. Ref.13 Ref.16

Tissue specificity

Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the outer root sheath of anagen follicles but not in the germinative matrix, inner root sheath or hair. Found in keratinocytes surrounding the club hair during telogen. Ref.11

Post-translational modification

A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus.

Involvement in disease

Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS) [MIM:131760]: A severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Epidermolysis bullosa simplex, Koebner type (K-EBS) [MIM:131900]: A form of intraepidermal epidermolysis bullosa characterized by generalized skin blistering. The phenotype is not fundamentally distinct from the Dowling-Meara type, although it is less severe.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.17 Ref.19 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.41

Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1) [MIM:601001]: An intraepidermal epidermolysis bullosa characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

Keywords
   Cellular componentCytoplasm
Intermediate filament
Keratin
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Ectodermal dysplasia
Epidermolysis bullosa
Palmoplantar keratoderma
   DomainCoiled coil
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from direct assay PubMed 21916889. Source: UniProt

cell junction assembly

Traceable author statement. Source: Reactome

epidermis development

Traceable author statement PubMed 7525408. Source: ProtInc

epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

hair cycle

Inferred from direct assay PubMed 21916889. Source: UniProt

hemidesmosome assembly

Traceable author statement. Source: Reactome

intermediate filament bundle assembly

Inferred from mutant phenotype Ref.13. Source: UniProtKB

response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell periphery

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.13. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

intermediate filament

Inferred from direct assay PubMed 10852826. Source: BHF-UCL

keratin filament

Inferred from direct assay PubMed 7679677. Source: MGI

nucleus

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functionkeratin filament binding

Inferred from physical interaction PubMed 20346438. Source: UniProt

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement PubMed 7525408. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKP1Q13835-22EBI-702178,EBI-9087684

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Keratin, type I cytoskeletal 14
PRO_0000063653

Regions

Region1 – 114114Head
Region115 – 422308Rod
Region115 – 15036Coil 1A
Region151 – 16818Linker 1
Region169 – 26092Coil 1B
Region261 – 28323Linker 12
Region284 – 422139Coil 2
Region423 – 47250Tail
Region425 – 47248Interaction with Type I keratins and keratin filaments

Sites

Site3641Stutter

Amino acid modifications

Disulfide bond367Interchain Ref.16

Natural variations

Natural variant631C → Y. Ref.2 Ref.3 Ref.5
Corresponds to variant rs6503640 [ dbSNP | Ensembl ].
VAR_055347
Natural variant941A → T. Ref.3 Ref.5 Ref.29
Corresponds to variant rs3826550 [ dbSNP | Ensembl ].
VAR_010437
Natural variant1161K → N in WC-EBS. Ref.29
Corresponds to variant rs59271739 [ dbSNP | Ensembl ].
VAR_010438
Natural variant1191M → I in WC-EBS at heterozygosity; more severe phenotype is associated with homozygosity. Ref.23 Ref.24
Corresponds to variant rs57358989 [ dbSNP | Ensembl ].
VAR_010439
Natural variant1191M → T in DM-EBS. Ref.25 Ref.33
Corresponds to variant rs28928893 [ dbSNP | Ensembl ].
VAR_010440
Natural variant1191M → V in K-EBS and WC-EBS. Ref.33 Ref.40
Corresponds to variant rs61263401 [ dbSNP | Ensembl ].
VAR_023719
Natural variant1201Q → R in DM-EBS. Ref.23
Corresponds to variant rs60993843 [ dbSNP | Ensembl ].
VAR_010441
Natural variant1221L → F in DM-EBS and K-EBS. Ref.8 Ref.9
Corresponds to variant rs59110575 [ dbSNP | Ensembl ].
VAR_010442
Natural variant1231N → K in DM-EBS. Ref.38 Ref.41
Corresponds to variant rs3826549 [ dbSNP | Ensembl ].
VAR_023720
Natural variant1231N → S in DM-EBS. Ref.29
Corresponds to variant rs60171927 [ dbSNP | Ensembl ].
VAR_010443
Natural variant1251R → C in DM-EBS. Ref.8 Ref.23 Ref.27 Ref.31 Ref.32 Ref.40 Ref.41
Corresponds to variant rs60399023 [ dbSNP | Ensembl ].
VAR_003837
Natural variant1251R → G in DM-EBS. Ref.38
VAR_023721
Natural variant1251R → H in DM-EBS. Ref.8 Ref.20 Ref.30 Ref.31 Ref.34 Ref.40 Ref.41
Corresponds to variant rs58330629 [ dbSNP | Ensembl ].
VAR_003838
Natural variant1251R → S in DM-EBS. Ref.23
VAR_010444
Natural variant1281Missing in DM-EBS. Ref.37
VAR_031634
Natural variant1291Y → D in DM-EBS. Ref.7
Corresponds to variant rs60470268 [ dbSNP | Ensembl ].
VAR_010445
Natural variant1301L → P in DM-EBS. Ref.36
Corresponds to variant rs57522245 [ dbSNP | Ensembl ].
VAR_023722
Natural variant1331V → A.
Corresponds to variant rs642601 [ dbSNP | Ensembl ].
VAR_033496
Natural variant1331V → L in WC-EBS and K-EBS. Ref.38 Ref.41
Corresponds to variant rs61027685 [ dbSNP | Ensembl ].
VAR_023723
Natural variant1341R → P in K-EBS. Ref.32
Corresponds to variant rs61540016 [ dbSNP | Ensembl ].
VAR_031635
Natural variant1431L → P in K-EBS. Ref.29
Corresponds to variant rs61326242 [ dbSNP | Ensembl ].
VAR_010446
Natural variant1441E → A in EBSB1. Ref.21
Corresponds to variant rs57121345 [ dbSNP | Ensembl ].
VAR_003839
Natural variant1481R → C in WC-EBS. Ref.37
Corresponds to variant rs58378809 [ dbSNP | Ensembl ].
VAR_031636
Natural variant2111R → P in WC-EBS. Ref.41
Corresponds to variant rs60589227 [ dbSNP | Ensembl ].
VAR_027718
Natural variant2151E → K.
Corresponds to variant rs11551755 [ dbSNP | Ensembl ].
VAR_049784
Natural variant2471A → D in K-EBS. Ref.31
VAR_010447
Natural variant2701V → M in WC-EBS. Ref.22
Corresponds to variant rs58560979 [ dbSNP | Ensembl ].
VAR_003840
Natural variant2721M → R in K-EBS. Ref.19
Corresponds to variant rs61371557 [ dbSNP | Ensembl ].
VAR_003841
Natural variant2721M → T in K-EBS. Ref.41
VAR_027719
Natural variant2731D → G in WC-EBS. Ref.26
Corresponds to variant rs59375065 [ dbSNP | Ensembl ].
VAR_010448
Natural variant2741A → D in WC-EBS. Ref.23
Corresponds to variant rs58785777 [ dbSNP | Ensembl ].
VAR_010449
Natural variant3751Missing in WC-EBS. Ref.18
VAR_003842
Natural variant3771I → N in WC-EBS. Ref.23
Corresponds to variant rs61536893 [ dbSNP | Ensembl ].
VAR_010450
Natural variant3841L → P in K-EBS. Ref.17 Ref.41
Corresponds to variant rs59629244 [ dbSNP | Ensembl ].
VAR_003843
Natural variant3881R → C in WC-EBS. Ref.23
Corresponds to variant rs59966597 [ dbSNP | Ensembl ].
VAR_010451
Natural variant3881R → H in WC-EBS. Ref.34
Corresponds to variant rs58645163 [ dbSNP | Ensembl ].
VAR_031637
Natural variant4081L → M in WC-EBS. Ref.36
Corresponds to variant rs57200223 [ dbSNP | Ensembl ].
VAR_023724
Natural variant4111Missing in WC-EBS. Ref.41
VAR_027720
Natural variant4131A → T in K-EBS. Ref.10
Corresponds to variant rs59780231 [ dbSNP | Ensembl ].
VAR_023725
Natural variant4151Y → C in WC-EBS. Ref.34
VAR_031638
Natural variant4151Y → H in K-EBS. Ref.28 Ref.31 Ref.32
VAR_003844
Natural variant4161R → P in DM-EBS. Ref.37
VAR_031639
Natural variant4171R → P in DM-EBS. Ref.41
VAR_027721
Natural variant4191L → Q in DM-EBS. Ref.28 Ref.31 Ref.36
VAR_003845
Natural variant4221E → K in WC-EBS. Ref.31
VAR_010452

Experimental info

Sequence conflict261G → A Ref.1
Sequence conflict261G → A in AAB59562. Ref.2
Sequence conflict441S → N Ref.1
Sequence conflict441S → N in AAB59562. Ref.2

Secondary structure

... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02533 [UniParc].

Last modified May 5, 2009. Version 4.
Checksum: 120BA30BA2F8E397

FASTA47251,561
        10         20         30         40         50         60 
MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG 

        70         80         90        100        110        120 
GACGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGAGLGGGF GGGFAGGDGL LVGSEKVTMQ 

       130        140        150        160        170        180 
NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK DYSPYFKTIE DLRNKILTAT 

       190        200        210        220        230        240 
VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE 

       250        260        270        280        290        300 
SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK 

       310        320        330        340        350        360 
DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN LEIELQSQLS MKASLENSLE 

       370        380        390        400        410        420 
ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE 

       430        440        450        460        470 
GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN 

« Hide

References

« Hide 'large scale' references
[1]"Remarkable conservation of structure among intermediate filament genes."
Marchuk D., McCrohon S., Fuchs E.
Cell 39:491-498(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of a gene encoding a human type I keratin: sequences homologous to enhancer elements in the regulatory region of the gene."
Marchuk D., McCrohon S., Fuchs E.
Proc. Natl. Acad. Sci. U.S.A. 82:1609-1613(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-63.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS TYR-63 AND THR-94.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS TYR-63 AND THR-94.
Tissue: Brain, Pancreas and Skin.
[6]"The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins."
Hanukoglu I., Fuchs E.
Cell 31:243-252(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-472.
Tissue: Epidermis.
[7]"Genetic analysis of a severe case of Dowling-Meara epidermolysis bullosa simplex."
Chan Y.-M., Cheng J., Gedde-Dahl T. Jr., Niemi K.M., Fuchs E.
J. Invest. Dermatol. 106:327-334(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-132, VARIANT DM-EBS ASP-129.
[8]"Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses."
Coulombe P.A., Hutton M.E., Letai A., Hebert A., Paller A.S., Fuchs E.
Cell 66:1301-1311(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, VARIANTS DM-EBS PHE-122; CYS-125 AND HIS-125.
[9]"A novel mutation of Leu122 to Phe at a highly conserved hydrophobic residue in the helix initiation motif of keratin 14 in epidermolysis bullosa simplex."
Yamanishi K., Matsuki M., Konishi K., Yasuno H.
Hum. Mol. Genet. 3:1171-1172(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, VARIANT K-EBS PHE-122.
[10]"A novel mutation of cytokeratin 14 in a Japanese epidermolysis bullosa simplex family."
Fujiwara H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-424, VARIANT K-EBS THR-413.
[11]"Characterization and chromosomal localization of human hair-specific keratin genes and comparative expression during the hair growth cycle."
Bowden P.E., Hainey S.D., Parker G., Jones D.O., Zimonjic D., Popescu N., Hodgins M.B.
J. Invest. Dermatol. 110:158-164(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD."
Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., Momoi T., Inagaki M.
J. Cell Biol. 155:415-426(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRADD.
[13]"The nonhelical tail domain of keratin 14 promotes filament bundling and enhances the mechanical properties of keratin intermediate filaments in vitro."
Bousquet O., Ma L., Yamada S., Gu C., Idei T., Takahashi K., Wirtz D., Coulombe P.A.
J. Cell Biol. 155:747-754(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KERATIN FILAMENTS, SUBCELLULAR LOCATION.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structural basis for heteromeric assembly and perinuclear organization of keratin filaments."
Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.
Nat. Struct. Mol. Biol. 19:707-715(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 295-422 IN COMPLEX WITH KRT5, DISULFIDE BOND, SUBCELLULAR LOCATION.
[17]"Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities."
Bonifas J.M., Rothman A.L., Epstein E.H. Jr.
Science 254:1202-1205(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT K-EBS PRO-384.
[18]"A novel three-nucleotide deletion in the helix 2B region of keratin 14 in epidermolysis bullosa simplex: delta E375."
Chen M.A., Bonifas J.M., Matsumura K., Blumenfeld A., Epstein E.H. Jr.
Hum. Mol. Genet. 2:1971-1972(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS GLU-375 DEL.
[19]"A mutation (Met-->Arg) in the type I keratin (K14) gene responsible for autosomal dominant epidermolysis bullosa simplex."
Humphries M.M., Sheils D.M., Farrar G.J., Kumar-Singh R., Kenna P.F., Mansergh F.C., Jordan S.A., Young M.M., Humphries P.
Hum. Mutat. 2:37-42(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT K-EBS ARG-272.
[20]"A keratin 14 mutational hot spot for epidermolysis bullosa simplex, Dowling-Meara: implications for diagnosis."
Stephens K., Sybert V.P., Wijsman E.M., Ehrlich P., Spencer A.
J. Invest. Dermatol. 101:240-243(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DM-EBS HIS-125.
[21]"A missense mutation in the rod domain of keratin 14 associated with recessive epidermolysis bullosa simplex."
Hovnanian A., Pollack E., Hilal L., Rochat A., Prost C., Barrandon Y., Goossens M.
Nat. Genet. 3:327-331(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EBSB1 ALA-144.
[22]"Missing links: Weber-Cockayne keratin mutations implicate the L12 linker domain in effective cytoskeleton function."
Rugg E.L., Morley S.M., Smith F.J.D., Boxer M., Tidman M.J., Navsaria H.A., Leigh I.M., Lane E.B.
Nat. Genet. 5:294-300(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS MET-270.
[23]"Keratin 14 gene mutations in patients with epidermolysis bullosa simplex."
Chen H., Bonifas J.M., Matsumura K., Ikeda S., Leyden W.A., Epstein E.H. Jr.
J. Invest. Dermatol. 105:629-632(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WC-EBS ILE-119; ASP-274; ASN-377 AND CYS-388, VARIANTS DM-EBS ARG-120; CYS-125 AND SER-125.
[24]"Partial dominance of a keratin 14 mutation in epidermolysis bullosa simplex: increased severity of disease in a homozygote."
Hu Z.L., Smith L., Martins S., Bonifas J.M., Chen H., Epstein E.H. Jr.
J. Invest. Dermatol. 109:360-364(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS ILE-119.
[25]"Severe palmo-plantar hyperkeratosis in Dowling-Meara epidermolysis bullosa simplex caused by a mutation in the keratin 14 gene (KRT14)."
Shemanko C.S., Mellerio J.E., Tidman M.J., Lane E.B., Eady R.A.J.
J. Invest. Dermatol. 111:893-895(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DM-EBS THR-119.
[26]"Novel K5 and K14 mutations in German patients with the Weber-Cockayne variant of epidermolysis bullosa simplex."
Mueller F.B., Kuester W., Bruckner-Tuderman L., Korge B.P.
J. Invest. Dermatol. 111:900-902(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS GLY-273.
[27]"A recurrent keratin 14 mutation in Dowling-Meara epidermolysis bullosa simplex."
Sasaki Y., Shimizu H., Akiyama M., Hiraoka Y., Takizawa Y., Yamada S., Morishima Y., Yamanishi K., Aiso S., Nishikawa T.
Br. J. Dermatol. 141:747-748(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DM-EBS CYS-125.
[28]"Genomic keratin 14 mutation detection in epidermolysis bullosa simplex."
Hut P.H.L., van der Vlies P., Jonkman M.F., Shimizu H., Buys C.H.C.M., Scheffer H.
Eur. J. Hum. Genet. Suppl. 7:121-121(1999)
Cited for: VARIANT K-EBS HIS-415, VARIANT DM-EBS GLN-419.
[29]"Identification of novel and known mutations in the genes for keratin 5 and 14 in Danish patients with epidermolysis bullosa simplex: correlation between genotype and phenotype."
Soerensen C.B., Ladekjaer-Mikkelsen A.-S., Andresen B.S., Brandrup F., Veien N.K., Buus S.K., Anton-Lamprecht I., Kruse T.A., Jensen P.K.A., Eiberg H., Bolund L., Gregersen N.
J. Invest. Dermatol. 112:184-190(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS ASN-116, VARIANT DM-EBS SER-123, VARIANT K-EBS PRO-143, VARIANT THR-94, SEQUENCE REVISION TO 25 AND 43.
[30]"Laryngeal involvement in the Dowling-Meara variant of epidermolysis bullosa simplex with keratin mutations of severely disruptive potential."
Shemanko C.S., Horn H.M., Keohane S.G., Hepburn N., Kerr A.I.G., Atherton D.J., Tidman M.J., Lane E.B.
Br. J. Dermatol. 142:315-320(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DM-EBS HIS-125.
[31]"Exempting homologous pseudogene sequences from polymerase chain reaction amplification allows genomic keratin 14 hotspot analysis."
Hut P.H.L., van der Vlies P., Jonkman M.F., Verlind E., Shimizu H., Buys C.H.C.M., Scheffer H.
J. Invest. Dermatol. 114:616-619(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS CYS-125; HIS-125 AND GLN-419, VARIANTS K-EBS ASP-247 AND HIS-415, VARIANT WC-EBS LYS-422.
[32]"DNA based prenatal testing for the skin blistering disorder epidermolysis bullosa simplex."
Rugg E.L., Baty D., Shemanko C.S., Magee G., Polak S., Bergman R., Kadar T., Boxer M., Falik-Zaccai T., Borochowitz Z., Lane E.B.
Prenat. Diagn. 20:371-377(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS CYS-125 AND HIS-415, VARIANT K-EBS PRO-134.
[33]"Keratin 14 point mutations at codon 119 of helix 1A resulting in different epidermolysis bullosa simplex phenotypes."
Cummins R.E., Klingberg S., Wesley J., Rogers M., Zhao Y., Murrell D.F.
J. Invest. Dermatol. 117:1103-1107(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DM-EBS THR-119, VARIANT K-EBS VAL-119.
[34]"Epidermolysis bullosa simplex in Israel: clinical and genetic features."
Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E., Petronius D., Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I., Uitto J., Sprecher E.
Arch. Dermatol. 139:498-505(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS WC-EBS HIS-388 AND CYS-415, VARIANT DM-EBS HIS-125.
[35]Erratum
Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E., Petronius D., Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I., Uitto J., Sprecher E.
Arch. Dermatol. 139:1084-1084(2003)
[36]"Mutation analysis of the entire keratin 5 and 14 genes in patients with epidermolysis bullosa simplex and identification of novel mutations."
Schuilenga-Hut P.H.L., Vlies P., Jonkman M.F., Waanders E., Buys C.H.C.M., Scheffer H.
Hum. Mutat. 21:447-447(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS PRO-130 AND GLN-419, VARIANT WC-EBS MET-408.
[37]"Long-range polymerase chain reaction for specific full-length amplification of the human keratin 14 gene and novel keratin 14 mutations in epidermolysis bullosa simplex patients."
Wood P., Baty D.U., Lane E.B., McLean W.H.I.
J. Invest. Dermatol. 120:495-497(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS SER-128 DEL AND PRO-416, VARIANT WC-EBS CYS-148.
[38]"Novel keratin 14 gene mutations in patients from Hungary with epidermolysis bullosa simplex."
Csikos M., Szalai Z., Becker K., Sebok B., Schneider I., Horvath A., Karpati S.
Exp. Dermatol. 13:185-191(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS LYS-123 AND GLY-125, VARIANT WC-EBS LEU-133.
[39]"Naegeli-Franceschetti-Jadassohn syndrome and dermatopathia pigmentosa reticularis: two allelic ectodermal dysplasias caused by dominant mutations in KRT14."
Lugassy J., Itin P., Ishida-Yamamoto A., Holland K., Huson S., Geiger D., Hennies H.C., Indelman M., Bercovich D., Uitto J., Bergman R., McGrath J.A., Richard G., Sprecher E.
Am. J. Hum. Genet. 79:724-730(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN NFJS, INVOLVEMENT IN DPR.
[40]"Epidermolysis bullosa simplex in Japanese and Korean patients: genetic studies in 19 cases."
Yasukawa K., Sawamura D., Goto M., Nakamura H., Jung S.-Y., Kim S.-C., Shimizu H.
Br. J. Dermatol. 155:313-317(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WC-EBS VAL-119, VARIANTS DM-EBS HIS-125 AND CYS-125.
[41]"Novel and recurrent mutations in keratin KRT5 and KRT14 genes in epidermolysis bullosa simplex: implications for disease phenotype and keratin filament assembly."
Mueller F.B., Kuester W., Wodecki K., Almeida H. Jr., Bruckner-Tuderman L., Krieg T., Korge B.P., Arin M.J.
Hum. Mutat. 27:719-720(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DM-EBS LYS-123; CYS-125; HIS-125 AND PRO-417, VARIANTS K-EBS LEU-133; THR-272 AND PRO-384, VARIANTS WC-EBS PRO-211 AND GLU-411 DEL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00124 Genomic DNA. Translation: AAB59562.1.
BT007186 mRNA. Translation: AAP35850.1.
AC019349 Genomic DNA. No translation available.
BC002690 mRNA. Translation: AAH02690.1.
BC019097 mRNA. Translation: AAH19097.1.
BC042437 mRNA. Translation: AAH42437.1.
BC094830 mRNA. Translation: AAH94830.1.
D28807 Genomic DNA. Translation: BAA05967.1.
AF186085 Genomic DNA. Translation: AAF04034.1.
AF186086 Genomic DNA. Translation: AAF04035.1.
AF186087 Genomic DNA. Translation: AAF04036.1.
AF186088 Genomic DNA. Translation: AAF04037.1.
AF186089 Genomic DNA. Translation: AAF04038.1.
AF186090 Genomic DNA. Translation: AAF04039.1.
CCDSCCDS11400.1.
PIRKRHUE. A26763.
RefSeqNP_000517.2. NM_000526.4.
UniGeneHs.654380.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00A295-422[»]
ProteinModelPortalP02533.
SMRP02533. Positions 165-263, 279-421.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110059. 41 interactions.
DIPDIP-33874N.
IntActP02533. 19 interactions.
STRING9606.ENSP00000167586.

PTM databases

PhosphoSiteP02533.

Polymorphism databases

DMDM229463044.

Proteomic databases

MaxQBP02533.
PaxDbP02533.
PRIDEP02533.
ProMEXP02533.

Protocols and materials databases

DNASU3861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000167586; ENSP00000167586; ENSG00000186847.
GeneID3861.
KEGGhsa:3861.
UCSCuc002hxf.2. human.

Organism-specific databases

CTD3861.
GeneCardsGC17M039738.
GeneReviewsKRT14.
HGNCHGNC:6416. KRT14.
HPACAB000134.
HPA000452.
HPA000453.
HPA023040.
MIM125595. phenotype.
131760. phenotype.
131800. phenotype.
131900. phenotype.
148066. gene.
161000. phenotype.
601001. phenotype.
neXtProtNX_P02533.
Orphanet89838. Autosomal recessive epidermolysis bullosa simplex.
86920. Dermatopathia pigmentosa reticularis.
79397. Epidermolysis bullosa simplex with mottled pigmentation.
79396. Epidermolysis bullosa simplex, Dowling-Meara type.
79399. Generalized epidermolysis bullosa simplex, non-Dowling-Meara type.
79400. Localized epidermolysis bullosa simplex.
69087. Naegeli-Franceschetti-Jadassohn syndrome.
PharmGKBPA30203.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148784.
HOVERGENHBG013015.
InParanoidP02533.
KOK07604.
OMATMTTCSR.
OrthoDBEOG7FV3Q8.
PhylomeDBP02533.
TreeFamTF332742.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP02533.
BgeeP02533.
CleanExHS_KRT14.
GenevestigatorP02533.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
SUPFAMSSF46579. SSF46579. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKeratin_14.
GenomeRNAi3861.
NextBio15195.
PROP02533.
SOURCESearch...

Entry information

Entry nameK1C14_HUMAN
AccessionPrimary (citable) accession number: P02533
Secondary accession number(s): Q14715 expand/collapse secondary AC list , Q53XY3, Q9BUE3, Q9UBN2, Q9UBN3, Q9UCY4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM