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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Defects in KRT5 are a cause of epidermolysis bullosa simplex Dowling-Meara type (DM-EBS) [MIM:131760]. DM-EBS is a severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement. Ref.13 Ref.16 Ref.23 Ref.25 Ref.26 Ref.30 Ref.31 Ref.36 Ref.40 Ref.41 Ref.42 Defects in KRT5 are the cause of epidermolysis bullosa simplex with migratory circinate erythema (EBSMCE) [MIM:609352]. EBSMCE is 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. Ref.40 Defects in KRT5 are a cause of epidermolysis bullosa simplex Weber-Cockayne type (WC-EBS) [MIM:131800]. WC-EBS is a form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin. Defects in KRT5 are a cause of epidermolysis bullosa simplex Koebner type (K-EBS) [MIM:131900]. K-EBS is a form of intraepidermal epidermolysis bullosa characterized by generalized skin blistering. The phenotype is not fundamentally distinct from the Dowling-Meara type, althought it is less severe. Defects in KRT5 are the cause of epidermolysis bullosa simplex with mottled pigmentation (MP-EBS) [MIM:131960]. MP-EBS is 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. Defects in KRT5 are the cause of Dowling-Degos disease (DDD) [MIM:179850]; also known as Dowling-Degos-Kitamura disease or reticulate acropigmentation of Kitamura. DDD is an 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. Ref.40
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	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	epidermis development Traceable author statement. Source: ProtInc hemidesmosome assembly Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome keratin filament Inferred from direct assay. Source: MGI
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural constituent of cytoskeleton Traceable author statement. 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	60	1	Phosphotyrosine Ref.9 Ref.10 Ref.11
	Modified residue	64	1	Phosphoserine By similarity
	Modified residue	66	1	Phosphotyrosine Ref.9 Ref.11
	Modified residue	75	1	Phosphoserine By similarity
Natural variations
	Natural variant	25	1	P → L in MP-EBS. Ref.24 Ref.29 Ref.41 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.15 Corresponds to variant rs11170164 [ dbSNP | Ensembl ].		VAR_003871
	Natural variant	143	1	V → D in K-EBS. Ref.41 Corresponds to variant rs59851104 [ dbSNP | Ensembl ].		VAR_031640
	Natural variant	152	1	P → L in WC-EBS. Ref.28 Corresponds to variant rs60617604 [ dbSNP | Ensembl ].		VAR_010454
	Natural variant	158	1	D → V in WC-EBS. Ref.41 Corresponds to variant rs61222761 [ dbSNP | Ensembl ].		VAR_031641
	Natural variant	161	1	I → S in WC-EBS. Ref.18 Corresponds to variant rs58058996 [ dbSNP | Ensembl ].		VAR_003872
	Natural variant	167	1	E → K in WC-EBS. Ref.35 Corresponds to variant rs57378129 [ dbSNP | Ensembl ].		VAR_026536
	Natural variant	168	1	E → K in DM-EBS. Ref.42 Corresponds to variant rs58619430 [ dbSNP | Ensembl ].		VAR_027722
	Natural variant	169	1	R → P in DM-EBS. Ref.42 Corresponds to variant rs60720877 [ dbSNP | Ensembl ].		VAR_027723
	Natural variant	170	1	E → K in K-EBS. Ref.34 Corresponds to variant rs59115483 [ dbSNP | Ensembl ].		VAR_026537
	Natural variant	173	1	K → N in K-EBS. Ref.20 Corresponds to variant rs58163069 [ dbSNP | Ensembl ].		VAR_010455
	Natural variant	175	1	L → F in DM-EBS. Ref.23 Corresponds to variant rs57890479 [ dbSNP | Ensembl ].		VAR_010456
	Natural variant	176	1	N → S in DM-EBS. Ref.25 Ref.30 Ref.41 Corresponds to variant rs59092197 [ dbSNP | Ensembl ].		VAR_010457
	Natural variant	177	1	N → S in WC-EBS. Ref.39 Corresponds to variant rs61495052 [ dbSNP | Ensembl ].		VAR_026538
	Natural variant	179	1	F → S in DM-EBS. Ref.25 Corresponds to variant rs57781042 [ dbSNP | Ensembl ].		VAR_010458
	Natural variant	181	1	S → P in DM-EBS; with laryngeal involvment. Ref.31 Corresponds to variant rs60715293 [ dbSNP | Ensembl ].		VAR_010459
	Natural variant	186	1	V → L in K-EBS. Ref.33 Ref.41 Corresponds to variant rs61305583 [ dbSNP | Ensembl ].		VAR_013829
	Natural variant	186	1	V → M in K-EBS. Ref.41		VAR_031642
	Natural variant	190	1	E → K in WC-EBS; requires 2 nucleotide substitutions. Ref.42 Corresponds to variant rs58976397 [ dbSNP | Ensembl ].		VAR_027724
	Natural variant	191	1	Q → P in K-EBS. Ref.41 Corresponds to variant rs57751134 [ dbSNP | Ensembl ].		VAR_031643
	Natural variant	193	1	N → K in DM-EBS and WC-EBS. Ref.16 Ref.22 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.35		VAR_026540
	Natural variant	323	1	V → A in K-EBS. Ref.27 Corresponds to variant rs59840738 [ dbSNP | Ensembl ].		VAR_010460
	Natural variant	324	1	V → D in WC-EBS. Ref.35 Corresponds to variant rs59335325 [ dbSNP | Ensembl ].		VAR_026541
	Natural variant	325	1	L → P in K-EBS. Ref.30 Corresponds to variant rs58107458 [ dbSNP | Ensembl ].		VAR_010461
	Natural variant	327	1	M → K in WC-EBS. Ref.28		VAR_010462
	Natural variant	327	1	M → T in WC-EBS. Ref.19 Ref.22 Corresponds to variant rs58072617 [ dbSNP | Ensembl ].		VAR_003874
	Natural variant	328	1	D → E in WC-EBS. Ref.32 Corresponds to variant rs59464425 [ dbSNP | Ensembl ].		VAR_026542
	Natural variant	328	1	D → G in WC-EBS. Ref.38		VAR_026543
	Natural variant	328	1	D → H in WC-EBS. Ref.28 Corresponds to variant rs56790237 [ dbSNP | Ensembl ].		VAR_010463
	Natural variant	328	1	D → V in WC-EBS. Ref.21 Corresponds to variant rs57142010 [ dbSNP | Ensembl ].		VAR_010464
	Natural variant	329	1	N → K in WC-EBS. Ref.19 Corresponds to variant rs59730172 [ dbSNP | Ensembl ].		VAR_010465
	Natural variant	331	1	R → C in WC-EBS. Ref.17		VAR_003875
	Natural variant	331	1	R → H in WC-EBS. Ref.42		VAR_027725
	Natural variant	352	1	R → S in WC-EBS. Ref.41		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.36		VAR_023726
	Natural variant	418	1	E → K in K-EBS. Ref.34		VAR_026544
	Natural variant	438	1	A → D in WC-EBS. Ref.36		VAR_023727
	Natural variant	463	1	L → P in K-EBS. Ref.14		VAR_003876
	Natural variant	467	1	I → T in DM-EBS. Ref.26		VAR_010466
	Natural variant	469	1	T → P in DM-EBS. Ref.42		VAR_027726
	Natural variant	475	1	E → G in DM-EBS. Ref.13		VAR_003877
	Natural variant	475	1	E → K in DM-EBS. Ref.36 Ref.41		VAR_023728
	Natural variant	477	1	E → K in DM-EBS. Ref.25 Ref.36 Ref.41		VAR_010467
	Natural variant	517	1	G → D in K-EBS. Ref.41		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

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: 2456903] [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: 2476664] [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: 10903910] [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: 15489334] [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: 2447486] [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: 14723728] [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: 2455002] [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: 15731013] [Abstract] Cited for: INTERACTION WITH TCHP.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60 AND TYR-66, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[10]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[11]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60 AND TYR-66, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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: 1372711] [Abstract] Cited for: VARIANT DM-EBS GLY-475.
[14]	"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: 7686424] [Abstract] Cited for: VARIANT K-EBS PRO-463.
[15]	"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: 7684424] [Abstract] Cited for: VARIANT GLU-138.
[16]	"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.
[17]	"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: 7506097] [Abstract] Cited for: VARIANT WC-EBS CYS-331.
[18]	"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: 7688477] [Abstract] Cited for: VARIANT WC-EBS SER-161.
[19]	"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: 7520042] [Abstract] Cited for: VARIANTS WC-EBS THR-327 AND LYS-329.
[20]	"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: 7534039] [Abstract] Cited for: VARIANT K-EBS ASN-173.
[21]	"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: 8595431] [Abstract] Cited for: VARIANT WC-EBS VAL-328.
[22]	"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: 8807337] [Abstract] Cited for: VARIANTS WC-EBS LYS-193 AND THR-327.
[23]	"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: 8757772] [Abstract] Cited for: VARIANT DM-EBS PHE-175.
[24]	"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: 8799157] [Abstract] Cited for: VARIANT MP-EBS LEU-25.
[25]	"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: 9036937] [Abstract] Cited for: VARIANTS DM-EBS SER-176; SER-179 AND LYS-477.
[26]	"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: 9406827] [Abstract] Cited for: VARIANT DM-EBS THR-467.
[27]	"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: 9740251] [Abstract] Cited for: VARIANT K-EBS ALA-323.
[28]	"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: 9804357] [Abstract] Cited for: VARIANTS WC-EBS LEU-152; LYS-327 AND HIS-328.
[29]	"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: 10494094] [Abstract] Cited for: VARIANT MP-EBS LEU-25.
[30]	"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: 9989794] [Abstract] Cited for: VARIANT DM-EBS SER-176, VARIANT K-EBS PRO-325.
[31]	"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: 10730767] [Abstract] Cited for: VARIANT DM-EBS PRO-181.
[32]	"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: 10782015] [Abstract] Cited for: VARIANT WC-EBS GLU-328.
[33]	"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: 11407988] [Abstract] Cited for: VARIANT K-EBS LEU-186.
[34]	"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: 11973334] [Abstract] Cited for: VARIANTS K-EBS LYS-170 AND LYS-418.
[35]	"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: 12707098] [Abstract] Cited for: VARIANTS WC-EBS LYS-167; PRO-311 AND ASP-324.
[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: 12655565] [Abstract] Cited for: VARIANTS WC-EBS GLU-404 AND ASP-438, VARIANTS DM-EBS LYS-475 AND LYS-477.
[37]	"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: 12925204] [Abstract] Cited for: INVOLVEMENT IN EBS WITH MIGRATORY CIRCINATE ERYTHEMA.
[38]	"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: 15347343] [Abstract] Cited for: VARIANT WC-EBS GLY-328.
[39]	"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: 15140024] [Abstract] Cited for: VARIANT WC-EBS SER-177.
[40]	"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: 16465624] [Abstract] Cited for: INVOLVEMENT IN DOWLING-DEGOS DISEASE.
[41]	"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: 16882168] [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.
[42]	"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: 16786515] [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
ProteinModelPortal	P13647.
SMR	P13647. Positions 166-203, 211-317, 334-479.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39N.
IntAct	P13647. 13 interactions.
STRING	P13647.
PTM databases
PhosphoSite	P13647.
Polymorphism databases
DMDM	143811411.
Proteomic databases
PRIDE	P13647.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252242; ENSP00000252242; ENSG00000186081.
GeneID	3852.
KEGG	hsa:3852.
NMPDR	fig|9606.3.peg.7589.
UCSC	uc001san.1. human.
Organism-specific databases
CTD	3852.
GeneCards	GC12M052938.
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. 79396. Epidermolysis bullosa simplex, Dowling-Meara type. 79399. Epidermolysis bullosa simplex, Koebner type. 79400. Epidermolysis bullosa simplex, Weber-Cockayne type.
PharmGKB	PA30230.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06442.
HOGENOM	HBG715391.
HOVERGEN	HBG013015.
InParanoid	P13647.
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]
KO	K07605.
PANTHER	PTHR23239. IF. 1 hit. PTHR23239:SF18. Keratin_II. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 144 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.