P02533 (K1C14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 14

Alternative name(s):
Cytokeratin-14
Short name=CK-14
Keratin-14
Short name=K14

Gene names

Name:

KRT14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Protein existence	Evidence 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 (AREBS) [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 component	Cytoplasm Intermediate filament Keratin Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ectodermal dysplasia Epidermolysis bullosa Palmoplantar keratoderma
Domain	Coiled coil
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epidermis development Traceable author statement PubMed 7525408. Source: ProtInc epithelial cell differentiation Inferred from electronic annotation. Source: Compara 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: Compara response to zinc ion Inferred from electronic annotation. Source: Compara
Cellular_component	cell periphery Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome keratin filament Inferred from direct assay PubMed 7679677. Source: MGI nucleus Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	structural constituent of cytoskeleton Traceable author statement PubMed 7525408. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 472

472

Keratin, type I cytoskeletal 14

PRO_0000063653

Regions

Region

1 – 114

114

Head

Region

115 – 422

308

Rod

Region

115 – 150

36

Coil 1A

Region

151 – 168

18

Linker 1

Region

169 – 260

92

Coil 1B

Region

261 – 283

23

Linker 12

Region

284 – 422

139

Coil 2

Region

423 – 472

50

Tail

Region

425 – 472

48

Interaction with Type I keratins and keratin filaments

Sites

Site

364

1

Stutter

Amino acid modifications

Disulfide bond

367

Interchain Ref.16

Natural variations

Natural variant

63

1

C → Y. Ref.2 Ref.3 Ref.5
Corresponds to variant rs6503640 [ dbSNP | Ensembl ].

VAR_055347

Natural variant

94

1

A → T. Ref.3 Ref.5 Ref.29
Corresponds to variant rs3826550 [ dbSNP | Ensembl ].

VAR_010437

Natural variant

116

1

K → N in WC-EBS. Ref.29
Corresponds to variant rs59271739 [ dbSNP | Ensembl ].

VAR_010438

Natural variant

119

1

M → 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 variant

119

1

M → T in DM-EBS. Ref.25 Ref.33
Corresponds to variant rs28928893 [ dbSNP | Ensembl ].

VAR_010440

Natural variant

119

1

M → V in K-EBS and WC-EBS. Ref.33 Ref.40
Corresponds to variant rs61263401 [ dbSNP | Ensembl ].

VAR_023719

Natural variant

120

1

Q → R in DM-EBS. Ref.23
Corresponds to variant rs60993843 [ dbSNP | Ensembl ].

VAR_010441

Natural variant

122

1

L → F in DM-EBS and K-EBS. Ref.8 Ref.9
Corresponds to variant rs59110575 [ dbSNP | Ensembl ].

VAR_010442

Natural variant

123

1

N → K in DM-EBS. Ref.38 Ref.41

VAR_023720

Natural variant

123

1

N → S in DM-EBS. Ref.29
Corresponds to variant rs60171927 [ dbSNP | Ensembl ].

VAR_010443

Natural variant

125

1

R → 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 variant

125

1

R → G in DM-EBS. Ref.38

VAR_023721

Natural variant

125

1

R → 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 variant

125

1

R → S in DM-EBS. Ref.23

VAR_010444

Natural variant

128

1

Missing in DM-EBS. Ref.37

VAR_031634

Natural variant

129

1

Y → D in DM-EBS. Ref.7
Corresponds to variant rs60470268 [ dbSNP | Ensembl ].

VAR_010445

Natural variant

130

1

L → P in DM-EBS. Ref.36
Corresponds to variant rs57522245 [ dbSNP | Ensembl ].

VAR_023722

Natural variant

133

1

V → A.
Corresponds to variant rs642601 [ dbSNP | Ensembl ].

VAR_033496

Natural variant

133

1

V → L in WC-EBS and K-EBS. Ref.38 Ref.41
Corresponds to variant rs61027685 [ dbSNP | Ensembl ].

VAR_023723

Natural variant

134

1

R → P in K-EBS. Ref.32
Corresponds to variant rs61540016 [ dbSNP | Ensembl ].

VAR_031635

Natural variant

143

1

L → P in K-EBS. Ref.29
Corresponds to variant rs61326242 [ dbSNP | Ensembl ].

VAR_010446

Natural variant

144

1

E → A in AREBS. Ref.21
Corresponds to variant rs57121345 [ dbSNP | Ensembl ].

VAR_003839

Natural variant

148

1

R → C in WC-EBS. Ref.37
Corresponds to variant rs58378809 [ dbSNP | Ensembl ].

VAR_031636

Natural variant

211

1

R → P in WC-EBS. Ref.41
Corresponds to variant rs60589227 [ dbSNP | Ensembl ].

VAR_027718

Natural variant

215

1

E → K.
Corresponds to variant rs11551755 [ dbSNP | Ensembl ].

VAR_049784

Natural variant

247

1

A → D in K-EBS. Ref.31

VAR_010447

Natural variant

270

1

V → M in WC-EBS. Ref.22
Corresponds to variant rs58560979 [ dbSNP | Ensembl ].

VAR_003840

Natural variant

272

1

M → R in K-EBS. Ref.19
Corresponds to variant rs61371557 [ dbSNP | Ensembl ].

VAR_003841

Natural variant

272

1

M → T in K-EBS. Ref.41

VAR_027719

Natural variant

273

1

D → G in WC-EBS. Ref.26
Corresponds to variant rs59375065 [ dbSNP | Ensembl ].

VAR_010448

Natural variant

274

1

A → D in WC-EBS. Ref.23
Corresponds to variant rs58785777 [ dbSNP | Ensembl ].

VAR_010449

Natural variant

375

1

Missing in WC-EBS. Ref.18

VAR_003842

Natural variant

377

1

I → N in WC-EBS. Ref.23
Corresponds to variant rs61536893 [ dbSNP | Ensembl ].

VAR_010450

Natural variant

384

1

L → P in K-EBS. Ref.17 Ref.41
Corresponds to variant rs59629244 [ dbSNP | Ensembl ].

VAR_003843

Natural variant

388

1

R → C in WC-EBS. Ref.23
Corresponds to variant rs59966597 [ dbSNP | Ensembl ].

VAR_010451

Natural variant

388

1

R → H in WC-EBS. Ref.34
Corresponds to variant rs58645163 [ dbSNP | Ensembl ].

VAR_031637

Natural variant

408

1

L → M in WC-EBS. Ref.36
Corresponds to variant rs57200223 [ dbSNP | Ensembl ].

VAR_023724

Natural variant

411

1

Missing in WC-EBS. Ref.41

VAR_027720

Natural variant

413

1

A → T in K-EBS. Ref.10
Corresponds to variant rs59780231 [ dbSNP | Ensembl ].

VAR_023725

Natural variant

415

1

Y → C in WC-EBS. Ref.34

VAR_031638

Natural variant

415

1

Y → H in K-EBS. Ref.28 Ref.31 Ref.32

VAR_003844

Natural variant

416

1

R → P in DM-EBS. Ref.37

VAR_031639

Natural variant

417

1

R → P in DM-EBS. Ref.41

VAR_027721

Natural variant

419

1

L → Q in DM-EBS. Ref.28 Ref.31 Ref.36

VAR_003845

Natural variant

422

1

E → K in WC-EBS. Ref.31

VAR_010452

Experimental info

Sequence conflict

26

1

G → A Ref.1

Sequence conflict

26

1

G → A in AAB59562. Ref.2

Sequence conflict

44

1

S → N Ref.1

Sequence conflict

44

1

S → N in AAB59562. Ref.2

Secondary structure

1

.

.

.

472

Helix Strand Turn

Details...

Helix

333 – 418

86

Sequences

	Sequence		Length	Mass (Da)
	P02533 [UniParc]. Last modified May 5, 2009. Version 4. Checksum: 120BA30BA2F8E397	FASTA	472	51,561
	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

References

	« Hide 'large scale' referencesShow '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. , 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 AREBS 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.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

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.

IPI

IPI00384444.

PIR

KRHUE. A26763.

RefSeq

NP_000517.2. NM_000526.4.

UniGene

Hs.654380.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TNU	X-ray	3.00	A	295-422	[»]

ProteinModelPortal

P02533.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33874N.

IntAct

P02533. 14 interactions.

STRING

9606.ENSP00000167586.

PTM databases

PhosphoSite

P02533.

Polymorphism databases

DMDM

229463044.

Proteomic databases

PaxDb

P02533.

PRIDE

P02533.

ProMEX

P02533.

Protocols and materials databases

DNASU

3861.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000167586; ENSP00000167586; ENSG00000186847.

GeneID

3861.

KEGG

hsa:3861.

UCSC

uc002hxf.2. human.

Organism-specific databases

CTD

3861.

GeneCards

GC17M039738.

HGNC

HGNC:6416. KRT14.

HPA

CAB000134.
HPA000452.
HPA000453.
HPA023040.

MIM

125595. phenotype.
131760. phenotype.
131800. phenotype.
131900. phenotype.
148066. gene.
161000. phenotype.
601001. phenotype.

neXtProt

NX_P02533.

Orphanet

89838. Autosomal recessive epidermolysis bullosa simplex.
86920. Dermatopathia pigmentosa reticularis.
79397. Epidermolysis bullosa simplex with mottled pigmentation.
79396. Epidermolysis bullosa simplex, Dowling-Meara type.
79399. Epidermolysis bullosa simplex, Kobner type.
79400. Epidermolysis bullosa simplex, Weber-Cockayne type.
69087. Naegeli-Franceschetti-Jadassohn syndrome.

PharmGKB

PA30203.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG148784.

HOVERGEN

HBG013015.

InParanoid

P02533.

KO

K07604.

OMA

QELISSV.

OrthoDB

EOG483D4W.

PhylomeDB

P02533.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

Bgee

P02533.

CleanEx

HS_KRT14.

Genevestigator

P02533.

GermOnline

ENSG00000186847. Homo sapiens.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]

PANTHER

PTHR23239. PTHR23239. 1 hit.

Pfam

PF00038. Filament. 1 hit.
[Graphical view]

PRINTS

PR01248. TYPE1KERATIN.

SUPFAM

SSF46579. Prefoldin. 1 hit.

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

3861.

NextBio

15195.

SOURCE

Search...

Entry information

Entry name

K1C14_HUMAN

Accession

Primary (citable) accession number: P02533
Secondary accession number(s): Q14715 , Q53XY3, Q9BUE3, Q9UBN2, Q9UBN3, Q9UCY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	May 5, 2009
Last modified:	May 1, 2013
This is version 151 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.