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P13647 (K2C5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. 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 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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.

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.12 Ref.18 Ref.25 Ref.28 Ref.31 Ref.32 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.39

Dowling-Degos disease 1 (DDD1) [MIM:179850]: 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.
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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590Keratin, type II cytoskeletal 5
PRO_0000063727

Regions

Region1 – 167167Head
Region168 – 477310Rod
Region168 – 20336Coil 1A
Region204 – 22219Linker 1
Region223 – 31593Coil 1B
Region316 – 33823Linker 12
Region339 – 477139Coil 2
Region478 – 590113Tail
Compositional bias39 – 139101Gly-rich
Compositional bias528 – 59063Ser-rich

Sites

Site4191Stutter

Natural variations

Natural variant251P → L in MP-EBS. Ref.22 Ref.27 Ref.39
Corresponds to variant rs57499817 [ dbSNP | Ensembl ].
VAR_010453
Natural variant791S → R. Ref.1 Ref.3
Corresponds to variant rs1065115 [ dbSNP | Ensembl ].
VAR_028763
Natural variant1381G → E. Ref.13
Corresponds to variant rs11170164 [ dbSNP | Ensembl ].
VAR_003871
Natural variant1431V → D in K-EBS. Ref.39
Corresponds to variant rs59851104 [ dbSNP | Ensembl ].
VAR_031640
Natural variant1521P → L in WC-EBS. Ref.26
Corresponds to variant rs60617604 [ dbSNP | Ensembl ].
VAR_010454
Natural variant1581D → V in WC-EBS. Ref.39
Corresponds to variant rs61222761 [ dbSNP | Ensembl ].
VAR_031641
Natural variant1611I → S in WC-EBS. Ref.16
Corresponds to variant rs58058996 [ dbSNP | Ensembl ].
VAR_003872
Natural variant1671E → K in WC-EBS. Ref.33
Corresponds to variant rs57378129 [ dbSNP | Ensembl ].
VAR_026536
Natural variant1681E → K in DM-EBS. Ref.40
Corresponds to variant rs58619430 [ dbSNP | Ensembl ].
VAR_027722
Natural variant1691R → P in DM-EBS. Ref.40
Corresponds to variant rs60720877 [ dbSNP | Ensembl ].
VAR_027723
Natural variant1701E → K in K-EBS. Ref.32
Corresponds to variant rs59115483 [ dbSNP | Ensembl ].
VAR_026537
Natural variant1731K → N in K-EBS. Ref.18
Corresponds to variant rs58163069 [ dbSNP | Ensembl ].
VAR_010455
Natural variant1751L → F in DM-EBS. Ref.21
Corresponds to variant rs57890479 [ dbSNP | Ensembl ].
VAR_010456
Natural variant1761N → S in DM-EBS. Ref.23 Ref.28 Ref.39
Corresponds to variant rs59092197 [ dbSNP | Ensembl ].
VAR_010457
Natural variant1771N → S in WC-EBS. Ref.37
Corresponds to variant rs61495052 [ dbSNP | Ensembl ].
VAR_026538
Natural variant1791F → S in DM-EBS. Ref.23
Corresponds to variant rs57781042 [ dbSNP | Ensembl ].
VAR_010458
Natural variant1811S → P in DM-EBS; with laryngeal involvement. Ref.29
Corresponds to variant rs60715293 [ dbSNP | Ensembl ].
VAR_010459
Natural variant1861V → L in K-EBS. Ref.31 Ref.39
Corresponds to variant rs61305583 [ dbSNP | Ensembl ].
VAR_013829
Natural variant1861V → M in K-EBS. Ref.39
VAR_031642
Natural variant1901E → K in WC-EBS; requires 2 nucleotide substitutions. Ref.40
Corresponds to variant rs58976397 [ dbSNP | Ensembl ].
VAR_027724
Natural variant1911Q → P in K-EBS. Ref.39
Corresponds to variant rs57751134 [ dbSNP | Ensembl ].
VAR_031643
Natural variant1931N → K in DM-EBS and WC-EBS. Ref.14 Ref.20
Corresponds to variant rs60586163 [ dbSNP | Ensembl ].
VAR_003873
Natural variant1971D → E. Ref.2 Ref.5
Corresponds to variant rs641615 [ dbSNP | Ensembl ].
VAR_028764
Natural variant1991K → T in WC-EBS. Ref.6
Corresponds to variant rs58766676 [ dbSNP | Ensembl ].
VAR_026539
Natural variant2321S → N.
Corresponds to variant rs3194286 [ dbSNP | Ensembl ].
VAR_028765
Natural variant3111L → P in WC-EBS. Ref.33
VAR_026540
Natural variant3231V → A in K-EBS. Ref.25
Corresponds to variant rs59840738 [ dbSNP | Ensembl ].
VAR_010460
Natural variant3241V → D in WC-EBS. Ref.33
Corresponds to variant rs59335325 [ dbSNP | Ensembl ].
VAR_026541
Natural variant3251L → P in K-EBS. Ref.28
Corresponds to variant rs58107458 [ dbSNP | Ensembl ].
VAR_010461
Natural variant3271M → K in WC-EBS. Ref.26
VAR_010462
Natural variant3271M → T in WC-EBS. Ref.17 Ref.20
Corresponds to variant rs58072617 [ dbSNP | Ensembl ].
VAR_003874
Natural variant3281D → E in WC-EBS. Ref.30
Corresponds to variant rs59464425 [ dbSNP | Ensembl ].
VAR_026542
Natural variant3281D → G in WC-EBS. Ref.36
VAR_026543
Natural variant3281D → H in WC-EBS. Ref.26
Corresponds to variant rs56790237 [ dbSNP | Ensembl ].
VAR_010463
Natural variant3281D → V in WC-EBS. Ref.19
Corresponds to variant rs57142010 [ dbSNP | Ensembl ].
VAR_010464
Natural variant3291N → K in WC-EBS. Ref.17
Corresponds to variant rs59730172 [ dbSNP | Ensembl ].
VAR_010465
Natural variant3311R → C in WC-EBS. Ref.15
VAR_003875
Natural variant3311R → H in WC-EBS. Ref.40
VAR_027725
Natural variant3521R → S in WC-EBS. Ref.39
VAR_031644
Natural variant3871S → T. Ref.1 Ref.3
Corresponds to variant rs2669875 [ dbSNP | Ensembl ].
VAR_028766
Natural variant4041K → E in WC-EBS. Ref.34
VAR_023726
Natural variant4181E → K in K-EBS. Ref.32
VAR_026544
Natural variant4381A → D in WC-EBS. Ref.34
VAR_023727
Natural variant4631L → P in K-EBS. Ref.12
VAR_003876
Natural variant4671I → T in DM-EBS. Ref.24
VAR_010466
Natural variant4691T → P in DM-EBS. Ref.40
VAR_027726
Natural variant4751E → G in DM-EBS. Ref.11
VAR_003877
Natural variant4751E → K in DM-EBS. Ref.34 Ref.39
VAR_023728
Natural variant4771E → K in DM-EBS. Ref.23 Ref.34 Ref.39
VAR_010467
Natural variant5171G → D in K-EBS. Ref.39
VAR_031645
Natural variant5281S → G. Ref.4
Corresponds to variant rs11549950 [ dbSNP | Ensembl ].
VAR_028767
Natural variant5431G → S. Ref.4 Ref.7
Corresponds to variant rs11549949 [ dbSNP | Ensembl ].
VAR_028768

Experimental info

Sequence conflict9 – 113FRS → SGA Ref.2
Sequence conflict2611E → Q in AAA36145. Ref.5
Sequence conflict2711E → H in AAA36145. Ref.5
Sequence conflict3751H → E Ref.7
Sequence conflict5581G → S Ref.2
Sequence conflict5581G → S in AAA36145. Ref.5

Secondary structure

... 590
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13647 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: E9D5318E01F55145

FASTA59062,378
        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 

« Hide

References

« Hide '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 DDD1.
[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.

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.
CCDSCCDS8830.1.
PIRA29904.
RefSeqNP_000415.2. NM_000424.3.
UniGeneHs.433845.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00B350-477[»]
ProteinModelPortalP13647.
SMRP13647. Positions 165-304, 334-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110050. 42 interactions.
DIPDIP-39N.
IntActP13647. 17 interactions.
STRING9606.ENSP00000252242.

Protein family/group databases

Allergome415. Hom s 5.

PTM databases

PhosphoSiteP13647.

Polymorphism databases

DMDM143811411.

Proteomic databases

MaxQBP13647.
PaxDbP13647.
PRIDEP13647.
ProMEXP13647.

Protocols and materials databases

DNASU3852.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252242; ENSP00000252242; ENSG00000186081.
GeneID3852.
KEGGhsa:3852.
UCSCuc001san.3. human.

Organism-specific databases

CTD3852.
GeneCardsGC12M052908.
GeneReviewsKRT5.
H-InvDBHIX0010655.
HGNCHGNC:6442. KRT5.
HPACAB000027.
CAB000129.
HPA059479.
MIM131760. phenotype.
131800. phenotype.
131900. phenotype.
131960. phenotype.
148040. gene.
179850. phenotype.
609352. phenotype.
neXtProtNX_P13647.
Orphanet79145. Dowling-Degos disease.
158681. Epidermolysis bullosa simplex with circinate migratory erythema.
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.
PharmGKBPA30230.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146769.
HOGENOMHOG000230976.
HOVERGENHBG013015.
InParanoidP13647.
KOK07605.
OMACGVGGYG.
OrthoDBEOG7FV3Q8.
PhylomeDBP13647.
TreeFamTF317854.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressP13647.
BgeeP13647.
CleanExHS_KRT5.
GenevestigatorP13647.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKRT5. human.
GeneWikiKeratin_5.
GenomeRNAi3852.
NextBio15157.
PROP13647.
SOURCESearch...

Entry information

Entry nameK2C5_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 171 of the entry and version 3 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 12

Human chromosome 12: entries, gene names and cross-references to MIM