P13647 (K2C5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type II cytoskeletal 5

Alternative name(s):
58 kDa cytokeratin
Cytokeratin-5
Short name=CK-5
Keratin-5
Short name=K5
Type-II keratin Kb5

Gene names

Name:

KRT5

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	590 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Heterotetramer of two type I and two type II keratins. Keratin-5 associates with keratin-14. Interacts with TCHP. Ref.8
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. Ref.38 Epidermolysis bullosa simplex, with migratory circinate erythema (EBSMCE) [MIM:609352]: A form of intraepidermal epidermolysis bullosa characterized by unusual migratory circinate erythema. Skin lesions appear from birth primarily on the hands, feet, and legs but spare nails, ocular epithelia and mucosae. Lesions heal with brown pigmentation but no scarring. Electron microscopy findings are distinct from those seen in the DM-EBS, with no evidence of tonofilament clumping. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 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. Ref.38 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.12 Ref.18 Ref.25 Ref.28 Ref.31 Ref.32 Ref.38 Ref.39 Epidermolysis bullosa simplex, with mottled pigmentation (MP-EBS) [MIM:131960]: A form of intraepidermal epidermolysis bullosa characterized by blistering at acral sites and 'mottled' pigmentation of the trunk and proximal extremities with hyper- and hypopigmentation macules. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.27 Ref.38 Ref.39 Dowling-Degos disease (DDD) [MIM:179850]: Autosomal dominant genodermatosis. Affected individuals develop a postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38
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	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation Epidermolysis bullosa
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	epidermis development Traceable author statement Ref.17. Source: ProtInc hemidesmosome assembly Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome keratin filament Inferred from direct assay PubMed 7679677. Source: MGI mitochondrion Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.17. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALOX12	P18054	7	EBI-702187,EBI-1633210

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 590

590

Keratin, type II cytoskeletal 5

PRO_0000063727

Regions

Region

1 – 167

167

Head

Region

168 – 477

310

Rod

Region

168 – 203

36

Coil 1A

Region

204 – 222

19

Linker 1

Region

223 – 315

93

Coil 1B

Region

316 – 338

23

Linker 12

Region

339 – 477

139

Coil 2

Region

478 – 590

113

Tail

Compositional bias

39 – 139

101

Gly-rich

Compositional bias

528 – 590

63

Ser-rich

Sites

Site

419

1

Stutter

Amino acid modifications

Modified residue

21

1

Phosphoserine By similarity

Modified residue

64

1

Phosphoserine By similarity

Modified residue

75

1

Phosphoserine By similarity

Natural variations

Natural variant

25

1

P → L in MP-EBS. Ref.22 Ref.27 Ref.39
Corresponds to variant rs57499817 [ dbSNP | Ensembl ].

VAR_010453

Natural variant

79

1

S → R. Ref.1 Ref.3
Corresponds to variant rs1065115 [ dbSNP | Ensembl ].

VAR_028763

Natural variant

138

1

G → E. Ref.13
Corresponds to variant rs11170164 [ dbSNP | Ensembl ].

VAR_003871

Natural variant

143

1

V → D in K-EBS. Ref.39
Corresponds to variant rs59851104 [ dbSNP | Ensembl ].

VAR_031640

Natural variant

152

1

P → L in WC-EBS. Ref.26
Corresponds to variant rs60617604 [ dbSNP | Ensembl ].

VAR_010454

Natural variant

158

1

D → V in WC-EBS. Ref.39
Corresponds to variant rs61222761 [ dbSNP | Ensembl ].

VAR_031641

Natural variant

161

1

I → S in WC-EBS. Ref.16
Corresponds to variant rs58058996 [ dbSNP | Ensembl ].

VAR_003872

Natural variant

167

1

E → K in WC-EBS. Ref.33
Corresponds to variant rs57378129 [ dbSNP | Ensembl ].

VAR_026536

Natural variant

168

1

E → K in DM-EBS. Ref.40
Corresponds to variant rs58619430 [ dbSNP | Ensembl ].

VAR_027722

Natural variant

169

1

R → P in DM-EBS. Ref.40
Corresponds to variant rs60720877 [ dbSNP | Ensembl ].

VAR_027723

Natural variant

170

1

E → K in K-EBS. Ref.32
Corresponds to variant rs59115483 [ dbSNP | Ensembl ].

VAR_026537

Natural variant

173

1

K → N in K-EBS. Ref.18
Corresponds to variant rs58163069 [ dbSNP | Ensembl ].

VAR_010455

Natural variant

175

1

L → F in DM-EBS. Ref.21
Corresponds to variant rs57890479 [ dbSNP | Ensembl ].

VAR_010456

Natural variant

176

1

N → S in DM-EBS. Ref.23 Ref.28 Ref.39
Corresponds to variant rs59092197 [ dbSNP | Ensembl ].

VAR_010457

Natural variant

177

1

N → S in WC-EBS. Ref.37
Corresponds to variant rs61495052 [ dbSNP | Ensembl ].

VAR_026538

Natural variant

179

1

F → S in DM-EBS. Ref.23
Corresponds to variant rs57781042 [ dbSNP | Ensembl ].

VAR_010458

Natural variant

181

1

S → P in DM-EBS; with laryngeal involvement. Ref.29
Corresponds to variant rs60715293 [ dbSNP | Ensembl ].

VAR_010459

Natural variant

186

1

V → L in K-EBS. Ref.31 Ref.39
Corresponds to variant rs61305583 [ dbSNP | Ensembl ].

VAR_013829

Natural variant

186

1

V → M in K-EBS. Ref.39

VAR_031642

Natural variant

190

1

E → K in WC-EBS; requires 2 nucleotide substitutions. Ref.40
Corresponds to variant rs58976397 [ dbSNP | Ensembl ].

VAR_027724

Natural variant

191

1

Q → P in K-EBS. Ref.39
Corresponds to variant rs57751134 [ dbSNP | Ensembl ].

VAR_031643

Natural variant

193

1

N → K in DM-EBS and WC-EBS. Ref.14 Ref.20
Corresponds to variant rs60586163 [ dbSNP | Ensembl ].

VAR_003873

Natural variant

197

1

D → E. Ref.2 Ref.5
Corresponds to variant rs641615 [ dbSNP | Ensembl ].

VAR_028764

Natural variant

199

1

K → T in WC-EBS. Ref.6
Corresponds to variant rs58766676 [ dbSNP | Ensembl ].

VAR_026539

Natural variant

232

1

S → N.
Corresponds to variant rs3194286 [ dbSNP | Ensembl ].

VAR_028765

Natural variant

311

1

L → P in WC-EBS. Ref.33

VAR_026540

Natural variant

323

1

V → A in K-EBS. Ref.25
Corresponds to variant rs59840738 [ dbSNP | Ensembl ].

VAR_010460

Natural variant

324

1

V → D in WC-EBS. Ref.33
Corresponds to variant rs59335325 [ dbSNP | Ensembl ].

VAR_026541

Natural variant

325

1

L → P in K-EBS. Ref.28
Corresponds to variant rs58107458 [ dbSNP | Ensembl ].

VAR_010461

Natural variant

327

1

M → K in WC-EBS. Ref.26

VAR_010462

Natural variant

327

1

M → T in WC-EBS. Ref.17 Ref.20
Corresponds to variant rs58072617 [ dbSNP | Ensembl ].

VAR_003874

Natural variant

328

1

D → E in WC-EBS. Ref.30
Corresponds to variant rs59464425 [ dbSNP | Ensembl ].

VAR_026542

Natural variant

328

1

D → G in WC-EBS. Ref.36

VAR_026543

Natural variant

328

1

D → H in WC-EBS. Ref.26
Corresponds to variant rs56790237 [ dbSNP | Ensembl ].

VAR_010463

Natural variant

328

1

D → V in WC-EBS. Ref.19
Corresponds to variant rs57142010 [ dbSNP | Ensembl ].

VAR_010464

Natural variant

329

1

N → K in WC-EBS. Ref.17
Corresponds to variant rs59730172 [ dbSNP | Ensembl ].

VAR_010465

Natural variant

331

1

R → C in WC-EBS. Ref.15

VAR_003875

Natural variant

331

1

R → H in WC-EBS. Ref.40

VAR_027725

Natural variant

352

1

R → S in WC-EBS. Ref.39

VAR_031644

Natural variant

387

1

S → T. Ref.1 Ref.3
Corresponds to variant rs2669875 [ dbSNP | Ensembl ].

VAR_028766

Natural variant

404

1

K → E in WC-EBS. Ref.34

VAR_023726

Natural variant

418

1

E → K in K-EBS. Ref.32

VAR_026544

Natural variant

438

1

A → D in WC-EBS. Ref.34

VAR_023727

Natural variant

463

1

L → P in K-EBS. Ref.12

VAR_003876

Natural variant

467

1

I → T in DM-EBS. Ref.24

VAR_010466

Natural variant

469

1

T → P in DM-EBS. Ref.40

VAR_027726

Natural variant

475

1

E → G in DM-EBS. Ref.11

VAR_003877

Natural variant

475

1

E → K in DM-EBS. Ref.34 Ref.39

VAR_023728

Natural variant

477

1

E → K in DM-EBS. Ref.23 Ref.34 Ref.39

VAR_010467

Natural variant

517

1

G → D in K-EBS. Ref.39

VAR_031645

Natural variant

528

1

S → G. Ref.4
Corresponds to variant rs11549950 [ dbSNP | Ensembl ].

VAR_028767

Natural variant

543

1

G → S. Ref.4 Ref.7
Corresponds to variant rs11549949 [ dbSNP | Ensembl ].

VAR_028768

Experimental info

Sequence conflict

9 – 11

3

FRS → SGA Ref.2

Sequence conflict

261

1

E → Q in AAA36145. Ref.5

Sequence conflict

271

1

E → H in AAA36145. Ref.5

Sequence conflict

375

1

H → E Ref.7

Sequence conflict

558

1

G → S Ref.2

Sequence conflict

558

1

G → S in AAA36145. Ref.5

Secondary structure

1

.

.

.

590

Helix Strand Turn

Details...

Helix

383 – 472

90

Sequences

	Sequence		Length	Mass (Da)
	P13647 [UniParc]. Last modified April 3, 2007. Version 3. Checksum: E9D5318E01F55145	FASTA	590	62,378
	10 20 30 40 50 60 MSRQSSVSFR SGGSRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS LAGACGVGGY 70 80 90 100 110 120 GSRSLYNLGG SKRISISTSG GSFRNRFGAG AGGGYGFGGG AGSGFGFGGG AGGGFGLGGG 130 140 150 160 170 180 AGFGGGFGGP GFPVCPPGGI QEVTVNQSLL TPLNLQIDPS IQRVRTEERE QIKTLNNKFA 190 200 210 220 230 240 SFIDKVRFLE QQNKVLDTKW TLLQEQGTKT VRQNLEPLFE QYINNLRRQL DSIVGERGRL 250 260 270 280 290 300 DSELRNMQDL VEDFKNKYED EINKRTTAEN EFVMLKKDVD AAYMNKVELE AKVDALMDEI 310 320 330 340 350 360 NFMKMFFDAE LSQMQTHVSD TSVVLSMDNN RNLDLDSIIA EVKAQYEEIA NRSRTEAESW 370 380 390 400 410 420 YQTKYEELQQ TAGRHGDDLR NTKHEISEMN RMIQRLRAEI DNVKKQCANL QNAIADAEQR 430 440 450 460 470 480 GELALKDARN KLAELEEALQ KAKQDMARLL REYQELMNTK LALDVEIATY RKLLEGEECR 490 500 510 520 530 540 LSGEGVGPVN ISVVTSSVSS GYGSGSGYGG GLGGGLGGGL GGGLAGGSSG SYYSSSSGGV 550 560 570 580 590 GLGGGLSVGG SGFSASSGRG LGVGFGSGGG SSSSVKFVST TSSSRKSFKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of the human epidermal 58-kD (#5) type II keratin reveals an absence of 5' upstream sequence conservation between coexpressed epidermal keratins." Eckert R.L., Rorke E.A. DNA 7:337-345(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-79 AND THR-387.
[2]	"Isolation, sequence, and expression of a human keratin K5 gene: transcriptional regulation of keratins and insights into pairwise control." Lersch R., Stellmach V., Stocks X., Giudice G., Fuchs E. Mol. Cell. Biol. 9:3685-3697(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-197.
[3]	"Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5." Whittock N.V., Eady R.A.J., McGrath J.A. Biochem. Biophys. Res. Commun. 274:149-152(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-79 AND THR-387.
[4]	"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 GLY-528 AND SER-543. Tissue: Brain and Pancreas.
[5]	"Sequence and expression of a type II keratin, K5, in human epidermal cells." Lersch R., Fuchs E. Mol. Cell. Biol. 8:486-493(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-590, VARIANT GLU-197.
[6]	"A new keratin 5 mutation (K199T) in a family with Weber-Cockayne epidermolysis bullosa simplex." Xu Z., Dong H., Sun X., Zhu X., Yang Y. Clin. Exp. Dermatol. 29:74-76(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 186-256, VARIANT WC-EBS THR-199.
[7]	"Isolation and characterization of a cDNA clone coding for human epidermal keratin K5. Sequence of the carboxyterminal half of this keratin." Galup C., Darmon M.Y. J. Invest. Dermatol. 91:39-42(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 348-590, VARIANT SER-543.
[8]	"Identification of trichoplein, a novel keratin filament-binding protein." Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M. J. Cell Sci. 118:1081-1090(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TCHP.
[9]	"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].
[10]	"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 350-477 IN COMPLEX WITH KRT14.
[11]	"A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering." Lane E.B., Rugg E.L., Navsaria H.A., Leigh I.M., Heagerty A.H.M., Ishida-Yamamoto A., Eady R.A.J. Nature 356:244-246(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DM-EBS GLY-475.
[12]	"Identification of a leucine-to-proline mutation in the keratin 5 gene in a family with the generalized Kobner type of epidermolysis bullosa simplex." Dong W., Ryynaenen M., Uitto J. Hum. Mutat. 2:94-102(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT K-EBS PRO-463.
[13]	"Allelic variations of human keratins K4 and K5 provide polymorphic markers within the type II keratin gene cluster on chromosome 12." Wanner R., Foerster H.-H., Tilmans I., Mischke D. J. Invest. Dermatol. 100:735-741(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLU-138.
[14]	"Clustering of epidermolysis bullosa simplex mutations in relation to disease phenotype: data from Weber-Cockayne EBS." Smith F.J.D., Morley S.M., Rugg E.L., Navsaria H.A., Leigh I.M., Eady R.A.J., Tidman M.J., Lane E.B. J. Invest. Dermatol. 101:481A-481A(1993) Cited for: VARIANT DM-EBS LYS-193.
[15]	"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 CYS-331.
[16]	"The genetic basis of Weber-Cockayne epidermolysis bullosa simplex." Chan Y.-M., Yu Q.-C., Fine J.-D., Fuchs E. Proc. Natl. Acad. Sci. U.S.A. 90:7414-7418(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WC-EBS SER-161.
[17]	"Mutations in the non-helical linker segment L1-2 of keratin 5 in patients with Weber-Cockayne epidermolysis bullosa simplex." Chan Y.-M., Yu Q.-C., LeBlanc-Straceski J., Christiano A., Pulkkinen L., Kucherlapati R.S., Uitto J., Fuchs E. J. Cell Sci. 107:765-774(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS WC-EBS THR-327 AND LYS-329.
[18]	"Epidermolysis bullosa simplex: a keratin 5 mutation is a fully dominant allele in epidermal cytoskeleton function." Stephens K., Zlotogorski A., Smith L., Ehrlich P., Wijsman E.M., Livingston R.J., Sybert V.P. Am. J. Hum. Genet. 56:577-585(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT K-EBS ASN-173.
[19]	"Epidermolysis bullosa simplex (Weber-Cockayne) associated with a novel missense mutation of Asp328 to Val in linker 12 domain of keratin 5." Matsuki M., Hashimoto K., Yoshikawa K., Yasuno H., Yamanishi K. Hum. Mol. Genet. 4:1999-2000(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WC-EBS VAL-328.
[20]	"Three keratin gene mutations account for the majority of dominant simplex epidermolysis bullosa cases within the population of Ireland." Humphries M.M., Mansergh F.C., Kiang A.-S., Jordan S.A., Sheils D.M., Martin M.J., Farrar G.J., Kenna P.F., Young M.M., Humphries P. Hum. Mutat. 8:57-63(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS WC-EBS LYS-193 AND THR-327.
[21]	"A novel keratin K5 gene mutation in Dowling-Meara epidermolysis bullosa simplex." Nomura K., Shimizu H., Meng X., Umeki K., Tamai K., Sawamura D., Nagao K., Kawakami T., Nishikawa T., Hashimoto I. J. Invest. Dermatol. 107:253-254(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DM-EBS PHE-175.
[22]	"The genetic basis of epidermolysis bullosa simplex with mottled pigmentation." Uttam J., Hutton M.E., Coulombe P.A., Anton-Lamprecht I., Yu Q.-C., Gedde-Dahl T. Jr., Fine J.-D., Fuchs E. Proc. Natl. Acad. Sci. U.S.A. 93:9079-9084(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MP-EBS LEU-25.
[23]	"Primers for exon-specific amplification of the KRT5 gene: identification of novel and recurrent mutations in epidermolysis bullosa simplex patients." Stephens K., Ehrlich P., Weaver M., Le R., Spencer A., Sybert V.P. J. Invest. Dermatol. 108:349-353(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DM-EBS SER-176; SER-179 AND LYS-477.
[24]	"A novel mutation in the helix termination peptide of keratin 5 causing epidermolysis bullosa simplex Dowling-Meara." Irvine A.D., McKenna K.E., Bingham A., Nevin N.C., Hughes A.E. J. Invest. Dermatol. 109:815-816(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DM-EBS THR-467.
[25]	"A novel mutation in the L12 domain of keratin 5 in the Koebner variant of epidermolysis bullosa simplex." Galligan P., Listwan P., Siller G.M., Rothnagel J.A. J. Invest. Dermatol. 111:524-527(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT K-EBS ALA-323.
[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: VARIANTS WC-EBS LEU-152; LYS-327 AND HIS-328.
[27]	"Epidermolysis bullosa simplex with mottled pigmentation: clinical aspects and confirmation of the P24L mutation in the KRT5 gene in further patients." Moog U., de Die-Smulders C.E.M., Scheffer H., van der Vlies P., Henquet C.J.M., Jonkman M.F. Am. J. Med. Genet. 86:376-379(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MP-EBS LEU-25.
[28]	"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 DM-EBS SER-176, VARIANT K-EBS PRO-325.
[29]	"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 PRO-181.
[30]	"K5 D328E: a novel missense mutation in the linker 12 domain of keratin 5 associated with epidermolysis bullosa simplex (Weber-Cockayne)." Liovic M., Podrumac B., Dragos V., Vouk K., Komel R. Hum. Hered. 50:234-236(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WC-EBS GLU-328.
[31]	"A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a conservative substitution can lead to development of different disease phenotypes." Liovic M., Stojan J., Bowden P.E., Gibbs D., Vahlquist A., Lane E.B., Komel R. J. Invest. Dermatol. 116:964-969(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT K-EBS LEU-186.
[32]	"Dominant and recessive compound heterozygous mutations in epidermolysis bullosa simplex demonstrate the role of the stutter region in keratin intermediate filament assembly." Yasukawa K., Sawamura D., McMillan J.R., Nakamura H., Shimizu H. J. Biol. Chem. 277:23670-23674(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS K-EBS LYS-170 AND LYS-418.
[33]	"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 LYS-167; PRO-311 AND ASP-324.
[34]	"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 WC-EBS GLU-404 AND ASP-438, VARIANTS DM-EBS LYS-475 AND LYS-477.
[35]	"A usual frameshift and delayed termination codon mutation in keratin 5 causes a novel type of epidermolysis bullosa simplex with migratory circinate erythema." Gu L.-H., Kim S.-C., Ichiki Y., Park J., Nagai M., Kitajima Y. J. Invest. Dermatol. 121:482-485(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN EBS WITH MIGRATORY CIRCINATE ERYTHEMA.
[36]	"A new mutation in the linker 12 domain of keratin 5 in a Chinese family with Weber-Cockayne epidermolysis bullosa simplex." Li J.-G., Feng J., Xiao S.-X., Ai Y.-L., Wang J.-M., Peng Z.-H. Clin. Exp. Dermatol. 29:539-541(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WC-EBS GLY-328.
[37]	"A mutation (N177S) in the structurally conserved helix initiation peptide motif of keratin 5 causes a mild EBS phenotype." Liovic M., Bowden P.E., Marks R., Komel R. Exp. Dermatol. 13:332-334(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WC-EBS SER-177.
[38]	"Loss-of-function mutations in the keratin 5 gene lead to Dowling-Degos disease." Betz R.C., Planko L., Eigelshoven S., Hanneken S., Pasternack S.M., Buessow H., Bogaert K.V., Wenzel J., Braun-Falco M., Ruetten A., Rogers M.A., Ruzicka T., Noethen M.M., Magin T.M., Kruse R. Am. J. Hum. Genet. 78:510-519(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DOWLING-DEGOS DISEASE.
[39]	"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: VARIANTS WC-EBS LEU-25; VAL-158 AND SER-352, VARIANTS K-EBS ASP-143; MET-186; LEU-186; PRO-191 AND ASP-517, VARIANTS DM-EBS SER-176; LYS-475 AND LYS-477, VARIANT MP-EBS LEU-25.
[40]	"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-168; PRO-169 AND PRO-469, VARIANTS WC-EBS LYS-190 AND HIS-331.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21389 mRNA. Translation: AAA36143.1.
M28496 Genomic DNA. No translation available.
AF274874 Genomic DNA. Translation: AAF97931.1.
BC024292 mRNA. Translation: AAH24292.1.
BC042132 mRNA. Translation: AAH42132.1.
BC071906 mRNA. Translation: AAH71906.1.
M19723 mRNA. Translation: AAA36145.1.
AY373434 mRNA. Translation: AAQ81588.1.

IPI

IPI00009867.

PIR

A29904.

RefSeq

NP_000415.2. NM_000424.3.

UniGene

Hs.433845.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TNU	X-ray	3.00	B	350-477	[»]

ProteinModelPortal

P13647.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39N.

IntAct

P13647. 14 interactions.

STRING

9606.ENSP00000252242.

PTM databases

PhosphoSite

P13647.

Polymorphism databases

DMDM

143811411.

Proteomic databases

PaxDb

P13647.

PRIDE

P13647.

ProMEX

P13647.

Protocols and materials databases

DNASU

3852.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000252242; ENSP00000252242; ENSG00000186081.

GeneID

3852.

KEGG

hsa:3852.

UCSC

uc001san.3. human.

Organism-specific databases

CTD

3852.

GeneCards

GC12M052908.

H-InvDB

HIX0010655.

HGNC

HGNC:6442. KRT5.

HPA

CAB000027.
CAB000129.

MIM

131760. phenotype.
131800. phenotype.
131900. phenotype.
131960. phenotype.
148040. gene.
179850. phenotype.
609352. phenotype.

neXtProt

NX_P13647.

Orphanet

79145. Dowling-Degos disease.
158681. Epidermolysis bullosa simplex with migratory circinate erythema.
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.

PharmGKB

PA30230.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG146769.

HOGENOM

HOG000230976.

HOVERGEN

HBG013015.

InParanoid

P13647.

KO

K07605.

OMA

CGVGGYG.

PhylomeDB

P13647.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

P13647.

Bgee

P13647.

CleanEx

HS_KRT5.

Genevestigator

P13647.

GermOnline

ENSG00000186081. Homo sapiens.

Family and domain databases

InterPro

IPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]

PANTHER

PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF18. PTHR23239:SF18. 1 hit.

Pfam

PF00038. Filament. 1 hit.
[Graphical view]

PRINTS

PR01276. TYPE2KERATIN.

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KRT5. human.

GenomeRNAi

3852.

NextBio

15157.

SOURCE

Search...

Entry information

Entry name

K2C5_HUMAN

Accession

Primary (citable) accession number: P13647
Secondary accession number(s): Q6PI71, Q6UBJ0, Q8TA91

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 158 of the entry and version 3 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.