Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Keratin, type II cytoskeletal 5

Gene

KRT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei419Stutter1

GO - Molecular functioni

  • scaffold protein binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  • epidermis development Source: ProtInc
  • hemidesmosome assembly Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170477-MONOMER.
ReactomeiR-HSA-446107. Type I hemidesmosome assembly.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Names & Taxonomyi

Protein namesi
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 namesi
Name:KRT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6442. KRT5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • intermediate filament Source: BHF-UCL
  • keratin filament Source: MGI
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement.
See also OMIM:131760
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071630165R → S in DM-EBS. 1 PublicationCorresponds to variant rs267607456dbSNPEnsembl.1
Natural variantiVAR_027722168E → K in DM-EBS. 1 PublicationCorresponds to variant rs58619430dbSNPEnsembl.1
Natural variantiVAR_027723169R → P in DM-EBS. 1 PublicationCorresponds to variant rs60720877dbSNPEnsembl.1
Natural variantiVAR_010456175L → F in DM-EBS. 1 PublicationCorresponds to variant rs57890479dbSNPEnsembl.1
Natural variantiVAR_010457176N → S in DM-EBS. 3 PublicationsCorresponds to variant rs59092197dbSNPEnsembl.1
Natural variantiVAR_010458179F → S in DM-EBS. 1 PublicationCorresponds to variant rs57781042dbSNPEnsembl.1
Natural variantiVAR_010459181S → P in DM-EBS; with laryngeal involvement. 1 PublicationCorresponds to variant rs60715293dbSNPEnsembl.1
Natural variantiVAR_003873193N → K in DM-EBS and WC-EBS. 3 PublicationsCorresponds to variant rs60586163dbSNPEnsembl.1
Natural variantiVAR_010466467I → T in DM-EBS. 1 PublicationCorresponds to variant rs60271599dbSNPEnsembl.1
Natural variantiVAR_027726469T → P in DM-EBS. 1 PublicationCorresponds to variant rs60596287dbSNPEnsembl.1
Natural variantiVAR_003877475E → G in DM-EBS. 1 PublicationCorresponds to variant rs61348633dbSNPEnsembl.1
Natural variantiVAR_023728475E → K in DM-EBS. 2 PublicationsCorresponds to variant rs57155193dbSNPEnsembl.1
Natural variantiVAR_010467477E → K in DM-EBS. 4 PublicationsCorresponds to variant rs59190510dbSNPEnsembl.1
Epidermolysis bullosa simplex, with migratory circinate erythema (EBSMCE)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609352
Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin.
See also OMIM:131800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010454152P → L in WC-EBS. 1 PublicationCorresponds to variant rs60617604dbSNPEnsembl.1
Natural variantiVAR_031641158D → V in WC-EBS. 1 PublicationCorresponds to variant rs61222761dbSNPEnsembl.1
Natural variantiVAR_003872161I → S in WC-EBS. 1 PublicationCorresponds to variant rs58058996dbSNPEnsembl.1
Natural variantiVAR_026536167E → K in WC-EBS. 1 PublicationCorresponds to variant rs57378129dbSNPEnsembl.1
Natural variantiVAR_026538177N → S in WC-EBS. 1 PublicationCorresponds to variant rs61495052dbSNPEnsembl.1
Natural variantiVAR_071631186V → E in WC-EBS. 1 PublicationCorresponds to variant rs267607457dbSNPEnsembl.1
Natural variantiVAR_027724190E → K in WC-EBS; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant rs58976397dbSNPEnsembl.1
Natural variantiVAR_003873193N → K in DM-EBS and WC-EBS. 3 PublicationsCorresponds to variant rs60586163dbSNPEnsembl.1
Natural variantiVAR_026539199K → T in WC-EBS. 1 PublicationCorresponds to variant rs58766676dbSNPEnsembl.1
Natural variantiVAR_026540311L → P in WC-EBS. 1 PublicationCorresponds to variant rs59864957dbSNPEnsembl.1
Natural variantiVAR_071632321T → P in WC-EBS. 1 Publication1
Natural variantiVAR_026541324V → D in WC-EBS. 1 PublicationCorresponds to variant rs59335325dbSNPEnsembl.1
Natural variantiVAR_010462327M → K in WC-EBS. 1 PublicationCorresponds to variant rs58072617dbSNPEnsembl.1
Natural variantiVAR_003874327M → T in WC-EBS. 2 PublicationsCorresponds to variant rs58072617dbSNPEnsembl.1
Natural variantiVAR_026542328D → E in WC-EBS. 1 PublicationCorresponds to variant rs59464425dbSNPEnsembl.1
Natural variantiVAR_026543328D → G in WC-EBS. 1 PublicationCorresponds to variant rs57142010dbSNPEnsembl.1
Natural variantiVAR_010463328D → H in WC-EBS. 1 PublicationCorresponds to variant rs56790237dbSNPEnsembl.1
Natural variantiVAR_010464328D → V in WC-EBS. 2 PublicationsCorresponds to variant rs57142010dbSNPEnsembl.1
Natural variantiVAR_010465329N → K in WC-EBS. 1 PublicationCorresponds to variant rs59730172dbSNPEnsembl.1
Natural variantiVAR_003875331R → C in WC-EBS. 1 PublicationCorresponds to variant rs61297109dbSNPEnsembl.1
Natural variantiVAR_027725331R → H in WC-EBS. 1 PublicationCorresponds to variant rs56729325dbSNPEnsembl.1
Natural variantiVAR_031644352R → S in WC-EBS. 1 PublicationCorresponds to variant rs59112594dbSNPEnsembl.1
Natural variantiVAR_023726404K → E in WC-EBS. 1 PublicationCorresponds to variant rs60809982dbSNPEnsembl.1
Natural variantiVAR_071633428A → T in WC-EBS. 1 PublicationCorresponds to variant rs267607458dbSNPEnsembl.1
Natural variantiVAR_023727438A → D in WC-EBS. 1 PublicationCorresponds to variant rs57845028dbSNPEnsembl.1
Epidermolysis bullosa simplex, Koebner type (K-EBS)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:131900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031640143V → D in K-EBS. 1 PublicationCorresponds to variant rs59851104dbSNPEnsembl.1
Natural variantiVAR_026537170E → K in K-EBS. 1 PublicationCorresponds to variant rs59115483dbSNPEnsembl.1
Natural variantiVAR_010455173K → N in K-EBS. 1 PublicationCorresponds to variant rs58163069dbSNPEnsembl.1
Natural variantiVAR_013829186V → L in K-EBS. 2 PublicationsCorresponds to variant rs61305583dbSNPEnsembl.1
Natural variantiVAR_031642186V → M in K-EBS. 1 PublicationCorresponds to variant rs121912475dbSNPEnsembl.1
Natural variantiVAR_031643191Q → P in K-EBS. 1 PublicationCorresponds to variant rs57751134dbSNPEnsembl.1
Natural variantiVAR_010460323V → A in K-EBS. 1 PublicationCorresponds to variant rs59840738dbSNPEnsembl.1
Natural variantiVAR_010461325L → P in K-EBS. 1 PublicationCorresponds to variant rs58107458dbSNPEnsembl.1
Natural variantiVAR_026544418E → K in K-EBS. 1 PublicationCorresponds to variant rs121912476dbSNPEnsembl.1
Natural variantiVAR_003876463L → P in K-EBS. 2 PublicationsCorresponds to variant rs57599352dbSNPEnsembl.1
Natural variantiVAR_031645517G → D in K-EBS. 1 PublicationCorresponds to variant rs58608695dbSNPEnsembl.1
Epidermolysis bullosa simplex, with mottled pigmentation (MP-EBS)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:131960
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01045325P → L in MP-EBS. 4 PublicationsCorresponds to variant rs57499817dbSNPEnsembl.1
Dowling-Degos disease 1 (DDD1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:179850

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa

Organism-specific databases

DisGeNETi3852.
MalaCardsiKRT5.
MIMi131760. phenotype.
131800. phenotype.
131900. phenotype.
131960. phenotype.
179850. phenotype.
609352. phenotype.
OpenTargetsiENSG00000186081.
Orphaneti79145. 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.
PharmGKBiPA30230.

Protein family/group databases

Allergomei415. Hom s 5.

Polymorphism and mutation databases

BioMutaiKRT5.
DMDMi143811411.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000637271 – 590Keratin, type II cytoskeletal 5Add BLAST590

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineBy similarity1
Modified residuei8PhosphoserineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei21PhosphoserineBy similarity1
Modified residuei26PhosphoserineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei64PhosphoserineBy similarity1
Modified residuei71PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei82PhosphoserineBy similarity1
Cross-linki276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP13647.
PeptideAtlasiP13647.
PRIDEiP13647.

PTM databases

iPTMnetiP13647.
PhosphoSitePlusiP13647.
SwissPalmiP13647.

Expressioni

Gene expression databases

BgeeiENSG00000186081.
CleanExiHS_KRT5.
ExpressionAtlasiP13647. baseline and differential.
GenevisibleiP13647. HS.

Organism-specific databases

HPAiCAB000027.
CAB000129.
HPA059479.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-5 associates with keratin-14. Interacts with TCHP. Interacts with KEPPK1 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALOX12P180547EBI-702187,EBI-1633210
KIFC3Q9BVG83EBI-702187,EBI-2125614
KRT15P190123EBI-702187,EBI-739566
KRT31Q153235EBI-702187,EBI-948001
KRT38O760155EBI-702187,EBI-1047263
KRT40Q6A1625EBI-702187,EBI-10171697
PKP1Q13835-22EBI-702187,EBI-9087684

GO - Molecular functioni

  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110050. 60 interactors.
DIPiDIP-39N.
IntActiP13647. 32 interactors.
STRINGi9606.ENSP00000252242.

Structurei

Secondary structure

1590
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi383 – 472Combined sources90

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00B350-477[»]
ProteinModelPortaliP13647.
SMRiP13647.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 167HeadAdd BLAST167
Regioni168 – 477RodAdd BLAST310
Regioni168 – 203Coil 1AAdd BLAST36
Regioni204 – 222Linker 1Add BLAST19
Regioni223 – 315Coil 1BAdd BLAST93
Regioni316 – 338Linker 12Add BLAST23
Regioni339 – 477Coil 2Add BLAST139
Regioni478 – 590TailAdd BLAST113

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi39 – 139Gly-richAdd BLAST101
Compositional biasi528 – 590Ser-richAdd BLAST63

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP13647.
KOiK07605.
OMAiMHTHISD.
OrthoDBiEOG091G09KR.
PhylomeDBiP13647.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13647-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRQSSVSFR SGGSRSFSTA SAITPSVSRT SFTSVSRSGG GGGGGFGRVS
60 70 80 90 100
LAGACGVGGY GSRSLYNLGG SKRISISTSG GSFRNRFGAG AGGGYGFGGG
110 120 130 140 150
AGSGFGFGGG AGGGFGLGGG AGFGGGFGGP GFPVCPPGGI QEVTVNQSLL
160 170 180 190 200
TPLNLQIDPS IQRVRTEERE QIKTLNNKFA SFIDKVRFLE QQNKVLDTKW
210 220 230 240 250
TLLQEQGTKT VRQNLEPLFE QYINNLRRQL DSIVGERGRL DSELRNMQDL
260 270 280 290 300
VEDFKNKYED EINKRTTAEN EFVMLKKDVD AAYMNKVELE AKVDALMDEI
310 320 330 340 350
NFMKMFFDAE LSQMQTHVSD TSVVLSMDNN RNLDLDSIIA EVKAQYEEIA
360 370 380 390 400
NRSRTEAESW YQTKYEELQQ TAGRHGDDLR NTKHEISEMN RMIQRLRAEI
410 420 430 440 450
DNVKKQCANL QNAIADAEQR GELALKDARN KLAELEEALQ KAKQDMARLL
460 470 480 490 500
REYQELMNTK LALDVEIATY RKLLEGEECR LSGEGVGPVN ISVVTSSVSS
510 520 530 540 550
GYGSGSGYGG GLGGGLGGGL GGGLAGGSSG SYYSSSSGGV GLGGGLSVGG
560 570 580 590
SGFSASSGRG LGVGFGSGGG SSSSVKFVST TSSSRKSFKS
Length:590
Mass (Da):62,378
Last modified:April 3, 2007 - v3
Checksum:iE9D5318E01F55145
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9 – 11FRS → SGA (PubMed:2476664).Curated3
Sequence conflicti261E → Q in AAA36145 (PubMed:2447486).Curated1
Sequence conflicti271E → H in AAA36145 (PubMed:2447486).Curated1
Sequence conflicti375H → E (PubMed:2455002).Curated1
Sequence conflicti558G → S (PubMed:2476664).Curated1
Sequence conflicti558G → S in AAA36145 (PubMed:2447486).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01045325P → L in MP-EBS. 4 PublicationsCorresponds to variant rs57499817dbSNPEnsembl.1
Natural variantiVAR_02876379S → R.2 PublicationsCorresponds to variant rs1065115dbSNPEnsembl.1
Natural variantiVAR_003871138G → E.1 PublicationCorresponds to variant rs11170164dbSNPEnsembl.1
Natural variantiVAR_031640143V → D in K-EBS. 1 PublicationCorresponds to variant rs59851104dbSNPEnsembl.1
Natural variantiVAR_010454152P → L in WC-EBS. 1 PublicationCorresponds to variant rs60617604dbSNPEnsembl.1
Natural variantiVAR_031641158D → V in WC-EBS. 1 PublicationCorresponds to variant rs61222761dbSNPEnsembl.1
Natural variantiVAR_003872161I → S in WC-EBS. 1 PublicationCorresponds to variant rs58058996dbSNPEnsembl.1
Natural variantiVAR_071630165R → S in DM-EBS. 1 PublicationCorresponds to variant rs267607456dbSNPEnsembl.1
Natural variantiVAR_026536167E → K in WC-EBS. 1 PublicationCorresponds to variant rs57378129dbSNPEnsembl.1
Natural variantiVAR_027722168E → K in DM-EBS. 1 PublicationCorresponds to variant rs58619430dbSNPEnsembl.1
Natural variantiVAR_027723169R → P in DM-EBS. 1 PublicationCorresponds to variant rs60720877dbSNPEnsembl.1
Natural variantiVAR_026537170E → K in K-EBS. 1 PublicationCorresponds to variant rs59115483dbSNPEnsembl.1
Natural variantiVAR_010455173K → N in K-EBS. 1 PublicationCorresponds to variant rs58163069dbSNPEnsembl.1
Natural variantiVAR_010456175L → F in DM-EBS. 1 PublicationCorresponds to variant rs57890479dbSNPEnsembl.1
Natural variantiVAR_010457176N → S in DM-EBS. 3 PublicationsCorresponds to variant rs59092197dbSNPEnsembl.1
Natural variantiVAR_026538177N → S in WC-EBS. 1 PublicationCorresponds to variant rs61495052dbSNPEnsembl.1
Natural variantiVAR_010458179F → S in DM-EBS. 1 PublicationCorresponds to variant rs57781042dbSNPEnsembl.1
Natural variantiVAR_010459181S → P in DM-EBS; with laryngeal involvement. 1 PublicationCorresponds to variant rs60715293dbSNPEnsembl.1
Natural variantiVAR_071631186V → E in WC-EBS. 1 PublicationCorresponds to variant rs267607457dbSNPEnsembl.1
Natural variantiVAR_013829186V → L in K-EBS. 2 PublicationsCorresponds to variant rs61305583dbSNPEnsembl.1
Natural variantiVAR_031642186V → M in K-EBS. 1 PublicationCorresponds to variant rs121912475dbSNPEnsembl.1
Natural variantiVAR_027724190E → K in WC-EBS; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant rs58976397dbSNPEnsembl.1
Natural variantiVAR_031643191Q → P in K-EBS. 1 PublicationCorresponds to variant rs57751134dbSNPEnsembl.1
Natural variantiVAR_003873193N → K in DM-EBS and WC-EBS. 3 PublicationsCorresponds to variant rs60586163dbSNPEnsembl.1
Natural variantiVAR_028764197D → E.2 PublicationsCorresponds to variant rs641615dbSNPEnsembl.1
Natural variantiVAR_026539199K → T in WC-EBS. 1 PublicationCorresponds to variant rs58766676dbSNPEnsembl.1
Natural variantiVAR_028765232S → N.Corresponds to variant rs3194286dbSNPEnsembl.1
Natural variantiVAR_026540311L → P in WC-EBS. 1 PublicationCorresponds to variant rs59864957dbSNPEnsembl.1
Natural variantiVAR_071632321T → P in WC-EBS. 1 Publication1
Natural variantiVAR_010460323V → A in K-EBS. 1 PublicationCorresponds to variant rs59840738dbSNPEnsembl.1
Natural variantiVAR_026541324V → D in WC-EBS. 1 PublicationCorresponds to variant rs59335325dbSNPEnsembl.1
Natural variantiVAR_010461325L → P in K-EBS. 1 PublicationCorresponds to variant rs58107458dbSNPEnsembl.1
Natural variantiVAR_010462327M → K in WC-EBS. 1 PublicationCorresponds to variant rs58072617dbSNPEnsembl.1
Natural variantiVAR_003874327M → T in WC-EBS. 2 PublicationsCorresponds to variant rs58072617dbSNPEnsembl.1
Natural variantiVAR_026542328D → E in WC-EBS. 1 PublicationCorresponds to variant rs59464425dbSNPEnsembl.1
Natural variantiVAR_026543328D → G in WC-EBS. 1 PublicationCorresponds to variant rs57142010dbSNPEnsembl.1
Natural variantiVAR_010463328D → H in WC-EBS. 1 PublicationCorresponds to variant rs56790237dbSNPEnsembl.1
Natural variantiVAR_010464328D → V in WC-EBS. 2 PublicationsCorresponds to variant rs57142010dbSNPEnsembl.1
Natural variantiVAR_010465329N → K in WC-EBS. 1 PublicationCorresponds to variant rs59730172dbSNPEnsembl.1
Natural variantiVAR_003875331R → C in WC-EBS. 1 PublicationCorresponds to variant rs61297109dbSNPEnsembl.1
Natural variantiVAR_027725331R → H in WC-EBS. 1 PublicationCorresponds to variant rs56729325dbSNPEnsembl.1
Natural variantiVAR_031644352R → S in WC-EBS. 1 PublicationCorresponds to variant rs59112594dbSNPEnsembl.1
Natural variantiVAR_028766387S → T.2 PublicationsCorresponds to variant rs2669875dbSNPEnsembl.1
Natural variantiVAR_023726404K → E in WC-EBS. 1 PublicationCorresponds to variant rs60809982dbSNPEnsembl.1
Natural variantiVAR_026544418E → K in K-EBS. 1 PublicationCorresponds to variant rs121912476dbSNPEnsembl.1
Natural variantiVAR_071633428A → T in WC-EBS. 1 PublicationCorresponds to variant rs267607458dbSNPEnsembl.1
Natural variantiVAR_023727438A → D in WC-EBS. 1 PublicationCorresponds to variant rs57845028dbSNPEnsembl.1
Natural variantiVAR_003876463L → P in K-EBS. 2 PublicationsCorresponds to variant rs57599352dbSNPEnsembl.1
Natural variantiVAR_010466467I → T in DM-EBS. 1 PublicationCorresponds to variant rs60271599dbSNPEnsembl.1
Natural variantiVAR_027726469T → P in DM-EBS. 1 PublicationCorresponds to variant rs60596287dbSNPEnsembl.1
Natural variantiVAR_003877475E → G in DM-EBS. 1 PublicationCorresponds to variant rs61348633dbSNPEnsembl.1
Natural variantiVAR_023728475E → K in DM-EBS. 2 PublicationsCorresponds to variant rs57155193dbSNPEnsembl.1
Natural variantiVAR_010467477E → K in DM-EBS. 4 PublicationsCorresponds to variant rs59190510dbSNPEnsembl.1
Natural variantiVAR_031645517G → D in K-EBS. 1 PublicationCorresponds to variant rs58608695dbSNPEnsembl.1
Natural variantiVAR_028767528S → G.1 PublicationCorresponds to variant rs11549950dbSNPEnsembl.1
Natural variantiVAR_028768543G → S.2 PublicationsCorresponds to variant rs11549949dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8830.1.
PIRiA29904.
RefSeqiNP_000415.2. NM_000424.3.
UniGeneiHs.433845.

Genome annotation databases

EnsembliENST00000252242; ENSP00000252242; ENSG00000186081.
GeneIDi3852.
KEGGihsa:3852.
UCSCiuc001san.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS8830.1.
PIRiA29904.
RefSeqiNP_000415.2. NM_000424.3.
UniGeneiHs.433845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00B350-477[»]
ProteinModelPortaliP13647.
SMRiP13647.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110050. 60 interactors.
DIPiDIP-39N.
IntActiP13647. 32 interactors.
STRINGi9606.ENSP00000252242.

Protein family/group databases

Allergomei415. Hom s 5.

PTM databases

iPTMnetiP13647.
PhosphoSitePlusiP13647.
SwissPalmiP13647.

Polymorphism and mutation databases

BioMutaiKRT5.
DMDMi143811411.

Proteomic databases

PaxDbiP13647.
PeptideAtlasiP13647.
PRIDEiP13647.

Protocols and materials databases

DNASUi3852.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252242; ENSP00000252242; ENSG00000186081.
GeneIDi3852.
KEGGihsa:3852.
UCSCiuc001san.4. human.

Organism-specific databases

CTDi3852.
DisGeNETi3852.
GeneCardsiKRT5.
GeneReviewsiKRT5.
H-InvDBHIX0010655.
HGNCiHGNC:6442. KRT5.
HPAiCAB000027.
CAB000129.
HPA059479.
MalaCardsiKRT5.
MIMi131760. phenotype.
131800. phenotype.
131900. phenotype.
131960. phenotype.
148040. gene.
179850. phenotype.
609352. phenotype.
neXtProtiNX_P13647.
OpenTargetsiENSG00000186081.
Orphaneti79145. 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.
PharmGKBiPA30230.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiP13647.
KOiK07605.
OMAiMHTHISD.
OrthoDBiEOG091G09KR.
PhylomeDBiP13647.
TreeFamiTF317854.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000170477-MONOMER.
ReactomeiR-HSA-446107. Type I hemidesmosome assembly.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Miscellaneous databases

ChiTaRSiKRT5. human.
GeneWikiiKeratin_5.
GenomeRNAii3852.
PROiP13647.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186081.
CleanExiHS_KRT5.
ExpressionAtlasiP13647. baseline and differential.
GenevisibleiP13647. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK2C5_HUMAN
AccessioniPrimary (citable) accession number: P13647
Secondary accession number(s): Q6PI71, Q6UBJ0, Q8TA91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 196 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.