[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-79 AND THR-387. PubMed=2456903 [NCBI, ExPASy, EBI, Israel, Japan] Eckert R.L., Rorke E.A.; "The sequence of the human epidermal 58-kD (#5) type II keratin reveals an absence of 5' upstream sequence conservation between coexpressed epidermal keratins."; DNA 7:337-345(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-197. PubMed=2476664 [NCBI, ExPASy, EBI, Israel, Japan] Lersch R., Stellmach V., Stocks X., Giudice G., Fuchs E.; "Isolation, sequence, and expression of a human keratin K5 gene: transcriptional regulation of keratins and insights into pairwise control."; Mol. Cell. Biol. 9:3685-3697(1989).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-79 AND THR-387. DOI=10.1006/bbrc.2000.3110; PubMed=10903910 [NCBI, ExPASy, EBI, Israel, Japan] Whittock N.V., Eady R.A.J., McGrath J.A.; "Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5."; Biochem. Biophys. Res. Commun. 274:149-152(2000).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-528 AND SER-543. TISSUE=Brain, and Pancreas; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 83-590, AND VARIANT GLU-197. PubMed=2447486 [NCBI, ExPASy, EBI, Israel, Japan] Lersch R., Fuchs E.; "Sequence and expression of a type II keratin, K5, in human epidermal cells."; Mol. Cell. Biol. 8:486-493(1988).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 186-256, AND VARIANT WC-EBS THR-199. DOI=10.1111/j.1365-2230.2004.01434.x; PubMed=14723728 [NCBI, ExPASy, EBI, Israel, Japan] Xu Z., Dong H., Sun X., Zhu X., Yang Y.; "A new keratin 5 mutation (K199T) in a family with Weber-Cockayne epidermolysis bullosa simplex."; Clin. Exp. Dermatol. 29:74-76(2004).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 348-590, AND VARIANT SER-543. DOI=10.1111/1523-1747.ep12463286; PubMed=2455002 [NCBI, ExPASy, EBI, Israel, Japan] Galup C., Darmon M.Y.; "Isolation and characterization of a cDNA clone coding for human epidermal keratin K5. Sequence of the carboxyterminal half of this keratin."; J. Invest. Dermatol. 91:39-42(1988).
[8]	INTERACTION WITH TCHP. DOI=10.1242/jcs.01667; PubMed=15731013 [NCBI, ExPASy, EBI, Israel, Japan] Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M.; "Identification of trichoplein, a novel keratin filament-binding protein."; J. Cell Sci. 118:1081-1090(2005).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60 AND TYR-66, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[10]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[11]	VARIANT DM-EBS GLY-475. DOI=10.1038/356244a0; PubMed=1372711 [NCBI, ExPASy, EBI, Israel, Japan] Lane E.B., Rugg E.L., Navsaria H.A., Leigh I.M., Heagerty A.H.M., Ishida-Yamamoto A., Eady R.A.J.; "A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering."; Nature 356:244-246(1992).
[12]	VARIANT K-EBS PRO-463. DOI=10.1002/humu.1380020206; PubMed=7686424 [NCBI, ExPASy, EBI, Israel, Japan] Dong W., Ryynaenen M., Uitto J.; "Identification of a leucine-to-proline mutation in the keratin 5 gene in a family with the generalized Kobner type of epidermolysis bullosa simplex."; Hum. Mutat. 2:94-102(1993).
[13]	VARIANT GLU-138. DOI=10.1111/1523-1747.ep12475671; PubMed=7684424 [NCBI, ExPASy, EBI, Israel, Japan] Wanner R., Foerster H.-H., Tilmans I., Mischke D.; "Allelic variations of human keratins K4 and K5 provide polymorphic markers within the type II keratin gene cluster on chromosome 12."; J. Invest. Dermatol. 100:735-741(1993).
[14]	VARIANT DM-EBS LYS-193. 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.; "Clustering of epidermolysis bullosa simplex mutations in relation to disease phenotype: data from Weber-Cockayne EBS."; J. Invest. Dermatol. 101:481A-481A(1993).
[15]	VARIANT WC-EBS CYS-331. DOI=10.1038/ng1193-294; PubMed=7506097 [NCBI, ExPASy, EBI, Israel, Japan] Rugg E.L., Morley S.M., Smith F.J.D., Boxer M., Tidman M.J., Navsaria H.A., Leigh I.M., Lane E.B.; "Missing links: Weber-Cockayne keratin mutations implicate the L12 linker domain in effective cytoskeleton function."; Nat. Genet. 5:294-300(1993).
[16]	VARIANT WC-EBS SER-161. DOI=10.1073/pnas.90.15.7414; PubMed=7688477 [NCBI, ExPASy, EBI, Israel, Japan] Chan Y.-M., Yu Q.-C., Fine J.-D., Fuchs E.; "The genetic basis of Weber-Cockayne epidermolysis bullosa simplex."; Proc. Natl. Acad. Sci. U.S.A. 90:7414-7418(1993).
[17]	VARIANTS WC-EBS THR-327 AND LYS-329. PubMed=7520042 [NCBI, ExPASy, EBI, Israel, Japan] Chan Y.-M., Yu Q.-C., LeBlanc-Straceski J., Christiano A., Pulkkinen L., Kucherlapati R.S., Uitto J., Fuchs E.; "Mutations in the non-helical linker segment L1-2 of keratin 5 in patients with Weber-Cockayne epidermolysis bullosa simplex."; J. Cell Sci. 107:765-774(1994).
[18]	VARIANT K-EBS ASN-173. PubMed=7534039 [NCBI, ExPASy, EBI, Israel, Japan] Stephens K., Zlotogorski A., Smith L., Ehrlich P., Wijsman E.M., Livingston R.J., Sybert V.P.; "Epidermolysis bullosa simplex: a keratin 5 mutation is a fully dominant allele in epidermal cytoskeleton function."; Am. J. Hum. Genet. 56:577-585(1995).
[19]	VARIANT WC-EBS VAL-328. DOI=10.1093/hmg/4.10.1999; PubMed=8595431 [NCBI, ExPASy, EBI, Israel, Japan] Matsuki M., Hashimoto K., Yoshikawa K., Yasuno H., Yamanishi K.; "Epidermolysis bullosa simplex (Weber-Cockayne) associated with a novel missense mutation of Asp328 to Val in linker 12 domain of keratin 5."; Hum. Mol. Genet. 4:1999-2000(1995).
[20]	VARIANTS WC-EBS LYS-193 AND THR-327. DOI=10.1002/(SICI)1098-1004(1996)8:1<57::AID-HUMU8>3.3.CO;2-Q; PubMed=8807337 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Three keratin gene mutations account for the majority of dominant simplex epidermolysis bullosa cases within the population of Ireland."; Hum. Mutat. 8:57-63(1996).
[21]	VARIANT DM-EBS PHE-175. DOI=10.1111/1523-1747.ep12329741; PubMed=8757772 [NCBI, ExPASy, EBI, Israel, Japan] Nomura K., Shimizu H., Meng X., Umeki K., Tamai K., Sawamura D., Nagao K., Kawakami T., Nishikawa T., Hashimoto I.; "A novel keratin K5 gene mutation in Dowling-Meara epidermolysis bullosa simplex."; J. Invest. Dermatol. 107:253-254(1996).
[22]	VARIANT MP-EBS LEU-25. DOI=10.1073/pnas.93.17.9079; PubMed=8799157 [NCBI, ExPASy, EBI, Israel, Japan] Uttam J., Hutton M.E., Coulombe P.A., Anton-Lamprecht I., Yu Q.-C., Gedde-Dahl T. Jr., Fine J.-D., Fuchs E.; "The genetic basis of epidermolysis bullosa simplex with mottled pigmentation."; Proc. Natl. Acad. Sci. U.S.A. 93:9079-9084(1996).
[23]	VARIANTS DM-EBS SER-176; SER-179 AND LYS-477. DOI=10.1111/1523-1747.ep12286486; PubMed=9036937 [NCBI, ExPASy, EBI, Israel, Japan] Stephens K., Ehrlich P., Weaver M., Le R., Spencer A., Sybert V.P.; "Primers for exon-specific amplification of the KRT5 gene: identification of novel and recurrent mutations in epidermolysis bullosa simplex patients."; J. Invest. Dermatol. 108:349-353(1997).
[24]	VARIANT DM-EBS THR-467. DOI=10.1111/1523-1747.ep12341024; PubMed=9406827 [NCBI, ExPASy, EBI, Israel, Japan] Irvine A.D., McKenna K.E., Bingham A., Nevin N.C., Hughes A.E.; "A novel mutation in the helix termination peptide of keratin 5 causing epidermolysis bullosa simplex Dowling-Meara."; J. Invest. Dermatol. 109:815-816(1997).
[25]	VARIANT K-EBS ALA-323. DOI=10.1046/j.1523-1747.1998.00308.x; PubMed=9740251 [NCBI, ExPASy, EBI, Israel, Japan] Galligan P., Listwan P., Siller G.M., Rothnagel J.A.; "A novel mutation in the L12 domain of keratin 5 in the Koebner variant of epidermolysis bullosa simplex."; J. Invest. Dermatol. 111:524-527(1998).
[26]	VARIANTS WC-EBS LEU-152; LYS-327 AND HIS-328. DOI=10.1046/j.1523-1747.1998.00374.x; PubMed=9804357 [NCBI, ExPASy, EBI, Israel, Japan] Mueller F.B., Kuester W., Bruckner-Tuderman L., Korge B.P.; "Novel K5 and K14 mutations in German patients with the Weber-Cockayne variant of epidermolysis bullosa simplex."; J. Invest. Dermatol. 111:900-902(1998).
[27]	VARIANT MP-EBS LEU-25. DOI=10.1002/(SICI)1096-8628(19991008)86:4<376::AID-AJMG12>3.0.CO;2-W; PubMed=10494094 [NCBI, ExPASy, EBI, Israel, Japan] Moog U., de Die-Smulders C.E.M., Scheffer H., van der Vlies P., Henquet C.J.M., Jonkman M.F.; "Epidermolysis bullosa simplex with mottled pigmentation: clinical aspects and confirmation of the P24L mutation in the KRT5 gene in further patients."; Am. J. Med. Genet. 86:376-379(1999).
[28]	VARIANT DM-EBS SER-176, AND VARIANT K-EBS PRO-325. DOI=10.1046/j.1523-1747.1999.00495.x; PubMed=9989794 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; J. Invest. Dermatol. 112:184-190(1999).
[29]	VARIANT DM-EBS PRO-181. DOI=10.1046/j.1365-2133.2000.03304.x; PubMed=10730767 [NCBI, ExPASy, EBI, Israel, Japan] Shemanko C.S., Horn H.M., Keohane S.G., Hepburn N., Kerr A.I.G., Atherton D.J., Tidman M.J., Lane E.B.; "Laryngeal involvement in the Dowling-Meara variant of epidermolysis bullosa simplex with keratin mutations of severely disruptive potential."; Br. J. Dermatol. 142:315-320(2000).
[30]	VARIANT WC-EBS GLU-328. DOI=10.1159/000022921; PubMed=10782015 [NCBI, ExPASy, EBI, Israel, Japan] Liovic M., Podrumac B., Dragos V., Vouk K., Komel R.; "K5 D328E: a novel missense mutation in the linker 12 domain of keratin 5 associated with epidermolysis bullosa simplex (Weber-Cockayne)."; Hum. Hered. 50:234-236(2000).
[31]	VARIANT K-EBS LEU-186. DOI=10.1046/j.1523-1747.2001.01334.x; PubMed=11407988 [NCBI, ExPASy, EBI, Israel, Japan] Liovic M., Stojan J., Bowden P.E., Gibbs D., Vahlquist A., Lane E.B., Komel R.; "A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a conservative substitution can lead to development of different disease phenotypes."; J. Invest. Dermatol. 116:964-969(2001).
[32]	VARIANTS K-EBS LYS-170 AND LYS-418. DOI=10.1074/jbc.M200974200; PubMed=11973334 [NCBI, ExPASy, EBI, Israel, Japan] Yasukawa K., Sawamura D., McMillan J.R., Nakamura H., Shimizu H.; "Dominant and recessive compound heterozygous mutations in epidermolysis bullosa simplex demonstrate the role of the stutter region in keratin intermediate filament assembly."; J. Biol. Chem. 277:23670-23674(2002).
[33]	VARIANTS WC-EBS LYS-167; PRO-311 AND ASP-324. DOI=10.1001/archderm.139.4.498; PubMed=12707098 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Epidermolysis bullosa simplex in Israel: clinical and genetic features."; Arch. Dermatol. 139:498-505(2003).
[34]	VARIANTS WC-EBS GLU-404 AND ASP-438, AND VARIANTS DM-EBS LYS-475 AND LYS-477. DOI=10.1002/humu.9124; PubMed=12655565 [NCBI, ExPASy, EBI, Israel, Japan] Schuilenga-Hut P.H.L., Vlies P., Jonkman M.F., Waanders E., Buys C.H.C.M., Scheffer H.; "Mutation analysis of the entire keratin 5 and 14 genes in patients with epidermolysis bullosa simplex and identification of novel mutations."; Hum. Mutat. 21:447-447(2003).
[35]	INVOLVEMENT IN EBS WITH MIGRATORY CIRCINATE ERYTHEMA. DOI=10.1046/j.1523-1747.2003.12424.x; PubMed=12925204 [NCBI, ExPASy, EBI, Israel, Japan] Gu L.-H., Kim S.-C., Ichiki Y., Park J., Nagai M., Kitajima Y.; "A usual frameshift and delayed termination codon mutation in keratin 5 causes a novel type of epidermolysis bullosa simplex with migratory circinate erythema."; J. Invest. Dermatol. 121:482-485(2003).
[36]	VARIANT WC-EBS GLY-328. DOI=10.1111/j.1365-2230.2004.01565.x; PubMed=15347343 [NCBI, ExPASy, EBI, Israel, Japan] Li J.-G., Feng J., Xiao S.-X., Ai Y.-L., Wang J.-M., Peng Z.-H.; "A new mutation in the linker 12 domain of keratin 5 in a Chinese family with Weber-Cockayne epidermolysis bullosa simplex."; Clin. Exp. Dermatol. 29:539-541(2004).
[37]	VARIANT WC-EBS SER-177. DOI=10.1111/j.0906-6705.2004.00171.x; PubMed=15140024 [NCBI, ExPASy, EBI, Israel, Japan] Liovic M., Bowden P.E., Marks R., Komel R.; "A mutation (N177S) in the structurally conserved helix initiation peptide motif of keratin 5 causes a mild EBS phenotype."; Exp. Dermatol. 13:332-334(2004).
[38]	INVOLVEMENT IN DOWLING-DEGOS DISEASE. DOI=10.1086/500850; PubMed=16465624 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Loss-of-function mutations in the keratin 5 gene lead to Dowling-Degos disease."; Am. J. Hum. Genet. 78:510-519(2006).
[39]	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, AND VARIANT MP-EBS LEU-25. DOI=10.1111/j.1365-2133.2006.07285.x; PubMed=16882168 [NCBI, ExPASy, EBI, Israel, Japan] Yasukawa K., Sawamura D., Goto M., Nakamura H., Jung S.-Y., Kim S.-C., Shimizu H.; "Epidermolysis bullosa simplex in Japanese and Korean patients: genetic studies in 19 cases."; Br. J. Dermatol. 155:313-317(2006).
[40]	VARIANTS DM-EBS LYS-168; PRO-169 AND PRO-469, AND VARIANTS WC-EBS LYS-190 AND HIS-331. DOI=10.1002/humu.9437; PubMed=16786515 [NCBI, ExPASy, EBI, Israel, Japan] Mueller F.B., Kuester W., Wodecki K., Almeida H. Jr., Bruckner-Tuderman L., Krieg T., Korge B.P., Arin M.J.; "Novel and recurrent mutations in keratin KRT5 and KRT14 genes in epidermolysis bullosa simplex: implications for disease phenotype and keratin filament assembly."; Hum. Mutat. 27:719-720(2006).

Comments

SUBUNIT: Heterotetramer of two type I and two type II keratins. Keratin-5 associates with keratin-14. Interacts with TCHP.
INTERACTION:
P18054:ALOX12; NbExp=3; IntAct=EBI-702187, EBI-1633210;
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.
DISEASE: 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.
DISEASE: 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.
DISEASE: 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.
DISEASE: 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.
DISEASE: 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.
MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
SIMILARITY: Belongs to the intermediate filament family.
WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=KRT5";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M21389; AAA36143.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M28496; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
AF274874; AAF97931.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024292; AAH24292.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042132; AAH42132.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071906; AAH71906.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19723; AAA36145.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY373434; AAQ81588.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00009867; -.

A29904; A29904.

NP_000415.2; -.

3D structure databases

HSSP

P08670; 1GK7. [HSSP ENTRY / PDB]

ModBase

P13647.

Protein-protein interaction databases

DIP

DIP:39N; -.

IntAct

P13647; 5.

PTM databases

PhosphoSite

P13647; -.

Organism-specific databases

GC12M051194; -.

HGNC:6442; KRT5.

CAB000027; -.
CAB000129; -.

MIM

131760; phenotype. [NCBI / EBI]
131800; phenotype. [NCBI / EBI]
131900; phenotype. [NCBI / EBI]
131960; phenotype. [NCBI / EBI]
148040; gene. [NCBI / EBI]
179850; phenotype. [NCBI / EBI]
609352; phenotype. [NCBI / EBI]

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, Koebner type.
79400; Epidermolysis bullosa simplex, Weber-Cockayne type.
304; Epidermolysis bullosa, epidermolytic.

PharmGKB

PA30230; -.

Gene expression databases

P13647; -.

P13647; -.

HS_KRT5; -.

ENSG00000186081; Homo sapiens.

Ontologies

GO:0045095;	Cellular component: keratin filament (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005200;	Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
GO:0008544;	Biological process: epidermis development (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016044; F.
IPR001664; IF.
IPR018039; Intermediate_filament_CS.
IPR003054; Keratin_II.
Graphical view of domain structure.

PANTHER

PTHR23239; IF; 1.
PTHR23239:SF18; Keratin_II; 1.

Pfam

PF00038; Filament; 1.
Pfam graphical view of domain structure.

PRINTS

PR01276; TYPE2KERATIN.

PROSITE

PS00226; IF; 1.

Proteomic databases

PRIDE

P13647; -.

Genome annotation databases

Ensembl

ENSG00000186081; Homo sapiens. [Contig view]

GeneID

3852; -.

KEGG

hsa:3852; -.

NMPDR

fig|9606.3.peg.7589; -.

Phylogenomic databases

HOGENOM

P13647; -.

HOVERGEN

P13647; -.

OMA

P13647; FGRVSLG.

Other

15157; -.

KRT5; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Coiled coil; Disease mutation; Epidermolysis bullosa; Intermediate filament; Keratin; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 590`	`590`	`Keratin, type II cytoskeletal 5.`	`PRO_0000063727`
`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.`
`COMPBIAS`	`39 139`	`101`	`Gly-rich.`
`COMPBIAS`	`528 590`	`63`	`Ser-rich.`
`SITE`	`419 419`	`1`	`Stutter.`
`MOD_RES`	`60 60`		`Phosphotyrosine.`
`MOD_RES`	`64 64`		`Phosphoserine (By similarity).`
`MOD_RES`	`66 66`		`Phosphotyrosine.`
`VARIANT`	`25 25`	`1`	`P -> L (in MP-EBS).`	`VAR_010453`
`VARIANT`	`79 79`	`1`	`S -> R (in dbSNP:rs1065115 [NCBI]).`	`VAR_028763`
`VARIANT`	`138 138`	`1`	`G -> E (in dbSNP:rs11170164 [NCBI]).`	`VAR_003871`
`VARIANT`	`143 143`	`1`	`V -> D (in K-EBS).`	`VAR_031640`
`VARIANT`	`152 152`	`1`	`P -> L (in WC-EBS).`	`VAR_010454`
`VARIANT`	`158 158`	`1`	`D -> V (in WC-EBS).`	`VAR_031641`
`VARIANT`	`161 161`	`1`	`I -> S (in WC-EBS).`	`VAR_003872`
`VARIANT`	`167 167`	`1`	`E -> K (in WC-EBS).`	`VAR_026536`
`VARIANT`	`168 168`	`1`	`E -> K (in DM-EBS).`	`VAR_027722`
`VARIANT`	`169 169`	`1`	`R -> P (in DM-EBS).`	`VAR_027723`
`VARIANT`	`170 170`	`1`	`E -> K (in K-EBS).`	`VAR_026537`
`VARIANT`	`173 173`	`1`	`K -> N (in K-EBS).`	`VAR_010455`
`VARIANT`	`175 175`	`1`	`L -> F (in DM-EBS).`	`VAR_010456`
`VARIANT`	`176 176`	`1`	`N -> S (in DM-EBS).`	`VAR_010457`
`VARIANT`	`177 177`	`1`	`N -> S (in WC-EBS).`	`VAR_026538`
`VARIANT`	`179 179`	`1`	`F -> S (in DM-EBS).`	`VAR_010458`
`VARIANT`	`181 181`	`1`	`S -> P (in DM-EBS; with laryngeal involvment).`	`VAR_010459`
`VARIANT`	`186 186`	`1`	`V -> L (in K-EBS).`	`VAR_013829`
`VARIANT`	`186 186`	`1`	`V -> M (in K-EBS).`	`VAR_031642`
`VARIANT`	`190 190`	`1`	`E -> K (in WC-EBS; requires 2 nucleotide substitutions).`	`VAR_027724`
`VARIANT`	`191 191`	`1`	`Q -> P (in K-EBS).`	`VAR_031643`
`VARIANT`	`193 193`	`1`	`N -> K (in DM-EBS and WC-EBS).`	`VAR_003873`
`VARIANT`	`197 197`	`1`	`D -> E (in dbSNP:rs641615 [NCBI]).`	`VAR_028764`
`VARIANT`	`199 199`	`1`	`K -> T (in WC-EBS).`	`VAR_026539`
`VARIANT`	`232 232`	`1`	`S -> N (in dbSNP:rs3194286 [NCBI]).`	`VAR_028765`
`VARIANT`	`311 311`	`1`	`L -> P (in WC-EBS).`	`VAR_026540`
`VARIANT`	`323 323`	`1`	`V -> A (in K-EBS).`	`VAR_010460`
`VARIANT`	`324 324`	`1`	`V -> D (in WC-EBS).`	`VAR_026541`
`VARIANT`	`325 325`	`1`	`L -> P (in K-EBS).`	`VAR_010461`
`VARIANT`	`327 327`	`1`	`M -> K (in WC-EBS).`	`VAR_010462`
`VARIANT`	`327 327`	`1`	`M -> T (in WC-EBS).`	`VAR_003874`
`VARIANT`	`328 328`	`1`	`D -> E (in WC-EBS).`	`VAR_026542`
`VARIANT`	`328 328`	`1`	`D -> G (in WC-EBS).`	`VAR_026543`
`VARIANT`	`328 328`	`1`	`D -> H (in WC-EBS).`	`VAR_010463`
`VARIANT`	`328 328`	`1`	`D -> V (in WC-EBS).`	`VAR_010464`
`VARIANT`	`329 329`	`1`	`N -> K (in WC-EBS).`	`VAR_010465`
`VARIANT`	`331 331`	`1`	`R -> C (in WC-EBS).`	`VAR_003875`
`VARIANT`	`331 331`	`1`	`R -> H (in WC-EBS).`	`VAR_027725`
`VARIANT`	`352 352`	`1`	`R -> S (in WC-EBS).`	`VAR_031644`
`VARIANT`	`387 387`	`1`	`S -> T (in dbSNP:rs2669875 [NCBI]).`	`VAR_028766`
`VARIANT`	`404 404`	`1`	`K -> E (in WC-EBS).`	`VAR_023726`
`VARIANT`	`418 418`	`1`	`E -> K (in K-EBS).`	`VAR_026544`
`VARIANT`	`438 438`	`1`	`A -> D (in WC-EBS).`	`VAR_023727`
`VARIANT`	`463 463`	`1`	`L -> P (in K-EBS).`	`VAR_003876`
`VARIANT`	`467 467`	`1`	`I -> T (in DM-EBS).`	`VAR_010466`
`VARIANT`	`469 469`	`1`	`T -> P (in DM-EBS).`	`VAR_027726`
`VARIANT`	`475 475`	`1`	`E -> G (in DM-EBS).`	`VAR_003877`
`VARIANT`	`475 475`	`1`	`E -> K (in DM-EBS).`	`VAR_023728`
`VARIANT`	`477 477`	`1`	`E -> K (in DM-EBS).`	`VAR_010467`
`VARIANT`	`517 517`	`1`	`G -> D (in K-EBS).`	`VAR_031645`
`VARIANT`	`528 528`	`1`	`S -> G (in dbSNP:rs11549950 [NCBI]).`	`VAR_028767`
`VARIANT`	`543 543`	`1`	`G -> S (in dbSNP:rs11549949 [NCBI]).`	`VAR_028768`
`CONFLICT`	`9 11`		`FRS -> SGA (in Ref. 2).`
`CONFLICT`	`261 261`		`E -> Q (in Ref. 5; AAA36145).`
`CONFLICT`	`271 271`		`E -> H (in Ref. 5; AAA36145).`
`CONFLICT`	`375 375`		`H -> E (in Ref. 7).`
`CONFLICT`	`558 558`		`G -> S (in Ref. 2 and 5; AAA36145).`

Sequence information

Length: 590 AA [This is the length of the unprocessed precursor]

Molecular weight: 62378 Da [This is the MW of the unprocessed precursor]

CRC64: E9D5318E01F55145 [This is a checksum on the sequence]

        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

P13647 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools