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Protein

Keratin, type I cytoskeletal 14

Gene

KRT14

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

Functioni

The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei364Stutter1

GO - Molecular functioni

  • keratin filament binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  • aging Source: UniProtKB
  • epidermis development Source: ProtInc
  • epithelial cell differentiation Source: Ensembl
  • hair cycle Source: UniProtKB
  • hemidesmosome assembly Source: Reactome
  • intermediate filament bundle assembly Source: UniProtKB
  • response to ionizing radiation Source: Ensembl
  • response to zinc ion Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171401-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 I cytoskeletal 14
Alternative name(s):
Cytokeratin-14
Short name:
CK-14
Keratin-14
Short name:
K14
Gene namesi
Name:KRT14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6416. KRT14.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS)18 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_010440119M → T in DM-EBS. 2 PublicationsCorresponds to variant rs28928893dbSNPEnsembl.1
Natural variantiVAR_010441120Q → R in DM-EBS. 1 PublicationCorresponds to variant rs60993843dbSNPEnsembl.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant rs59110575dbSNPEnsembl.1
Natural variantiVAR_023720123N → K in DM-EBS. 2 PublicationsCorresponds to variant rs3826549dbSNPEnsembl.1
Natural variantiVAR_010443123N → S in DM-EBS. 1 PublicationCorresponds to variant rs60171927dbSNPEnsembl.1
Natural variantiVAR_003837125R → C in DM-EBS. 7 PublicationsCorresponds to variant rs60399023dbSNPEnsembl.1
Natural variantiVAR_023721125R → G in DM-EBS. 1 PublicationCorresponds to variant rs60399023dbSNPEnsembl.1
Natural variantiVAR_003838125R → H in DM-EBS. 7 PublicationsCorresponds to variant rs58330629dbSNPEnsembl.1
Natural variantiVAR_010444125R → S in DM-EBS. 1 Publication1
Natural variantiVAR_031634128Missing in DM-EBS. 1 Publication1
Natural variantiVAR_010445129Y → D in DM-EBS. 1 PublicationCorresponds to variant rs60470268dbSNPEnsembl.1
Natural variantiVAR_023722130L → P in DM-EBS. 1 PublicationCorresponds to variant rs57522245dbSNPEnsembl.1
Natural variantiVAR_031639416R → P in DM-EBS. 1 PublicationCorresponds to variant rs60622724dbSNPEnsembl.1
Natural variantiVAR_027721417R → P in DM-EBS. 1 PublicationCorresponds to variant rs61085704dbSNPEnsembl.1
Natural variantiVAR_003845419L → Q in DM-EBS. 3 PublicationsCorresponds to variant rs57364972dbSNPEnsembl.1
Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS)13 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_010438116K → N in WC-EBS. 1 PublicationCorresponds to variant rs59271739dbSNPEnsembl.1
Natural variantiVAR_010439119M → I in WC-EBS at heterozygosity; more severe phenotype is associated with homozygosity. 2 PublicationsCorresponds to variant rs57358989dbSNPEnsembl.1
Natural variantiVAR_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant rs61263401dbSNPEnsembl.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant rs61027685dbSNPEnsembl.1
Natural variantiVAR_031636148R → C in WC-EBS. 1 PublicationCorresponds to variant rs58378809dbSNPEnsembl.1
Natural variantiVAR_027718211R → P in WC-EBS. 1 PublicationCorresponds to variant rs60589227dbSNPEnsembl.1
Natural variantiVAR_003840270V → M in WC-EBS. 1 PublicationCorresponds to variant rs58560979dbSNPEnsembl.1
Natural variantiVAR_010448273D → G in WC-EBS. 1 PublicationCorresponds to variant rs59375065dbSNPEnsembl.1
Natural variantiVAR_010449274A → D in WC-EBS. 1 PublicationCorresponds to variant rs58785777dbSNPEnsembl.1
Natural variantiVAR_003842375Missing in WC-EBS. 1 Publication1
Natural variantiVAR_010450377I → N in WC-EBS. 1 PublicationCorresponds to variant rs61536893dbSNPEnsembl.1
Natural variantiVAR_010451388R → C in WC-EBS. 1 PublicationCorresponds to variant rs59966597dbSNPEnsembl.1
Natural variantiVAR_031637388R → H in WC-EBS. 1 PublicationCorresponds to variant rs58645163dbSNPEnsembl.1
Natural variantiVAR_023724408L → M in WC-EBS. 1 PublicationCorresponds to variant rs57200223dbSNPEnsembl.1
Natural variantiVAR_027720411Missing in WC-EBS. 1 Publication1
Natural variantiVAR_031638415Y → C in WC-EBS. 1 PublicationCorresponds to variant rs59442925dbSNPEnsembl.1
Natural variantiVAR_010452422E → K in WC-EBS. 1 PublicationCorresponds to variant rs58762773dbSNPEnsembl.1
Epidermolysis bullosa simplex, Koebner type (K-EBS)10 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_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant rs61263401dbSNPEnsembl.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant rs59110575dbSNPEnsembl.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant rs61027685dbSNPEnsembl.1
Natural variantiVAR_031635134R → P in K-EBS. 1 PublicationCorresponds to variant rs61540016dbSNPEnsembl.1
Natural variantiVAR_010446143L → P in K-EBS. 1 PublicationCorresponds to variant rs61326242dbSNPEnsembl.1
Natural variantiVAR_010447247A → D in K-EBS. 1 PublicationCorresponds to variant rs147611635dbSNPEnsembl.1
Natural variantiVAR_003841272M → R in K-EBS. 1 PublicationCorresponds to variant rs61371557dbSNPEnsembl.1
Natural variantiVAR_027719272M → T in K-EBS. 1 PublicationCorresponds to variant rs61371557dbSNPEnsembl.1
Natural variantiVAR_003843384L → P in K-EBS. 2 PublicationsCorresponds to variant rs59629244dbSNPEnsembl.1
Natural variantiVAR_023725413A → T in K-EBS. 1 PublicationCorresponds to variant rs59780231dbSNPEnsembl.1
Natural variantiVAR_003844415Y → H in K-EBS. 3 PublicationsCorresponds to variant rs58380626dbSNPEnsembl.1
Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn intraepidermal epidermolysis bullosa characterized by localized blistering on the dorsal, lateral and plantar surfaces of the feet.
See also OMIM:601001
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003839144E → A in EBSB1. 1 PublicationCorresponds to variant rs57121345dbSNPEnsembl.1
Naegeli-Franceschetti-Jadassohn syndrome (NFJS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare autosomal dominant form of ectodermal dysplasia. The cardinal features are absence of dermatoglyphics (fingerprints), reticular cutaneous hyperpigmentation (starting at about the age of 2 years without a preceding inflammatory stage), palmoplantar keratoderma, hypohidrosis with diminished sweat gland function and discomfort provoked by heat, nail dystrophy, and tooth enamel defects.
See also OMIM:161000
Dermatopathia pigmentosa reticularis (DPR)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare ectodermal dysplasia characterized by lifelong persistent reticulate hyperpigmentation, non-cicatricial alopecia, and nail dystrophy. Variable features include adermatoglyphia, hypohidrosis or hyperhidrosis, and palmoplantar hyperkeratosis.
See also OMIM:125595

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia, Epidermolysis bullosa, Palmoplantar keratoderma

Organism-specific databases

DisGeNETi3861.
MalaCardsiKRT14.
MIMi125595. phenotype.
131760. phenotype.
131800. phenotype.
131900. phenotype.
161000. phenotype.
601001. phenotype.
OpenTargetsiENSG00000186847.
Orphaneti86920. Dermatopathia pigmentosa reticularis.
79397. Epidermolysis bullosa simplex with mottled pigmentation.
79396. Epidermolysis bullosa simplex, Dowling-Meara type.
79399. Generalized epidermolysis bullosa simplex, non-Dowling-Meara type.
89838. KRT14-related epidermolysis bullosa simplex.
79400. Localized epidermolysis bullosa simplex.
69087. Naegeli-Franceschetti-Jadassohn syndrome.
PharmGKBiPA30203.

Polymorphism and mutation databases

BioMutaiKRT14.
DMDMi229463044.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000636531 – 472Keratin, type I cytoskeletal 14Add BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi367Interchain1 Publication
Modified residuei435PhosphoserineBy similarity1

Post-translational modificationi

A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP02533.
PeptideAtlasiP02533.
PRIDEiP02533.

PTM databases

iPTMnetiP02533.
PhosphoSitePlusiP02533.
SwissPalmiP02533.

Expressioni

Tissue specificityi

Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the outer root sheath of anagen follicles but not in the germinative matrix, inner root sheath or hair. Found in keratinocytes surrounding the club hair during telogen.1 Publication

Gene expression databases

BgeeiENSG00000186847.
CleanExiHS_KRT14.
GenevisibleiP02533. HS.

Organism-specific databases

HPAiCAB000134.
HPA000452.
HPA023040.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. disulfide-linked keratin-14 associates with keratin-5. Interacts with TRADD and with keratin filaments. Associates with other type I keratins. Interacts with EPPK1 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PKP1Q13835-22EBI-702178,EBI-9087684

GO - Molecular functioni

  • keratin filament binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110059. 42 interactors.
DIPiDIP-33874N.
IntActiP02533. 21 interactors.
STRINGi9606.ENSP00000167586.

Structurei

Secondary structure

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi333 – 418Combined sources86

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00A295-422[»]
ProteinModelPortaliP02533.
SMRiP02533.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 114HeadAdd BLAST114
Regioni115 – 422RodAdd BLAST308
Regioni115 – 150Coil 1AAdd BLAST36
Regioni151 – 168Linker 1Add BLAST18
Regioni169 – 260Coil 1BAdd BLAST92
Regioni261 – 283Linker 12Add BLAST23
Regioni284 – 422Coil 2Add BLAST139
Regioni423 – 472TailAdd BLAST50
Regioni425 – 472Interaction with Type I keratins and keratin filamentsAdd BLAST48

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOVERGENiHBG013015.
InParanoidiP02533.
KOiK07604.
OMAiNLRMSVG.
OrthoDBiEOG091G087I.
PhylomeDBiP02533.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02533-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL
60 70 80 90 100
SVSSSRFSSG GACGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGAGLGGGF
110 120 130 140 150
GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW
160 170 180 190 200
YQRQRPAEIK DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF
210 220 230 240 250
RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK
260 270 280 290 300
KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK
310 320 330 340 350
DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN LEIELQSQLS
360 370 380 390 400
MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI
410 420 430 440 450
LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT
460 470
KVMDVHDGKV VSTHEQVLRT KN
Length:472
Mass (Da):51,561
Last modified:May 5, 2009 - v4
Checksum:i120BA30BA2F8E397
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti26G → A (PubMed:6210150).Curated1
Sequence conflicti26G → A in AAB59562 (PubMed:2580298).Curated1
Sequence conflicti44S → N (PubMed:6210150).Curated1
Sequence conflicti44S → N in AAB59562 (PubMed:2580298).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05534763C → Y.3 PublicationsCorresponds to variant rs6503640dbSNPEnsembl.1
Natural variantiVAR_01043794A → T.3 PublicationsCorresponds to variant rs3826550dbSNPEnsembl.1
Natural variantiVAR_010438116K → N in WC-EBS. 1 PublicationCorresponds to variant rs59271739dbSNPEnsembl.1
Natural variantiVAR_010439119M → I in WC-EBS at heterozygosity; more severe phenotype is associated with homozygosity. 2 PublicationsCorresponds to variant rs57358989dbSNPEnsembl.1
Natural variantiVAR_010440119M → T in DM-EBS. 2 PublicationsCorresponds to variant rs28928893dbSNPEnsembl.1
Natural variantiVAR_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant rs61263401dbSNPEnsembl.1
Natural variantiVAR_010441120Q → R in DM-EBS. 1 PublicationCorresponds to variant rs60993843dbSNPEnsembl.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant rs59110575dbSNPEnsembl.1
Natural variantiVAR_023720123N → K in DM-EBS. 2 PublicationsCorresponds to variant rs3826549dbSNPEnsembl.1
Natural variantiVAR_010443123N → S in DM-EBS. 1 PublicationCorresponds to variant rs60171927dbSNPEnsembl.1
Natural variantiVAR_003837125R → C in DM-EBS. 7 PublicationsCorresponds to variant rs60399023dbSNPEnsembl.1
Natural variantiVAR_023721125R → G in DM-EBS. 1 PublicationCorresponds to variant rs60399023dbSNPEnsembl.1
Natural variantiVAR_003838125R → H in DM-EBS. 7 PublicationsCorresponds to variant rs58330629dbSNPEnsembl.1
Natural variantiVAR_010444125R → S in DM-EBS. 1 Publication1
Natural variantiVAR_031634128Missing in DM-EBS. 1 Publication1
Natural variantiVAR_010445129Y → D in DM-EBS. 1 PublicationCorresponds to variant rs60470268dbSNPEnsembl.1
Natural variantiVAR_023722130L → P in DM-EBS. 1 PublicationCorresponds to variant rs57522245dbSNPEnsembl.1
Natural variantiVAR_033496133V → A.Corresponds to variant rs56798071dbSNPEnsembl.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant rs61027685dbSNPEnsembl.1
Natural variantiVAR_031635134R → P in K-EBS. 1 PublicationCorresponds to variant rs61540016dbSNPEnsembl.1
Natural variantiVAR_010446143L → P in K-EBS. 1 PublicationCorresponds to variant rs61326242dbSNPEnsembl.1
Natural variantiVAR_003839144E → A in EBSB1. 1 PublicationCorresponds to variant rs57121345dbSNPEnsembl.1
Natural variantiVAR_031636148R → C in WC-EBS. 1 PublicationCorresponds to variant rs58378809dbSNPEnsembl.1
Natural variantiVAR_027718211R → P in WC-EBS. 1 PublicationCorresponds to variant rs60589227dbSNPEnsembl.1
Natural variantiVAR_049784215E → K.Corresponds to variant rs11551755dbSNPEnsembl.1
Natural variantiVAR_010447247A → D in K-EBS. 1 PublicationCorresponds to variant rs147611635dbSNPEnsembl.1
Natural variantiVAR_003840270V → M in WC-EBS. 1 PublicationCorresponds to variant rs58560979dbSNPEnsembl.1
Natural variantiVAR_003841272M → R in K-EBS. 1 PublicationCorresponds to variant rs61371557dbSNPEnsembl.1
Natural variantiVAR_027719272M → T in K-EBS. 1 PublicationCorresponds to variant rs61371557dbSNPEnsembl.1
Natural variantiVAR_010448273D → G in WC-EBS. 1 PublicationCorresponds to variant rs59375065dbSNPEnsembl.1
Natural variantiVAR_010449274A → D in WC-EBS. 1 PublicationCorresponds to variant rs58785777dbSNPEnsembl.1
Natural variantiVAR_003842375Missing in WC-EBS. 1 Publication1
Natural variantiVAR_010450377I → N in WC-EBS. 1 PublicationCorresponds to variant rs61536893dbSNPEnsembl.1
Natural variantiVAR_003843384L → P in K-EBS. 2 PublicationsCorresponds to variant rs59629244dbSNPEnsembl.1
Natural variantiVAR_010451388R → C in WC-EBS. 1 PublicationCorresponds to variant rs59966597dbSNPEnsembl.1
Natural variantiVAR_031637388R → H in WC-EBS. 1 PublicationCorresponds to variant rs58645163dbSNPEnsembl.1
Natural variantiVAR_023724408L → M in WC-EBS. 1 PublicationCorresponds to variant rs57200223dbSNPEnsembl.1
Natural variantiVAR_027720411Missing in WC-EBS. 1 Publication1
Natural variantiVAR_023725413A → T in K-EBS. 1 PublicationCorresponds to variant rs59780231dbSNPEnsembl.1
Natural variantiVAR_031638415Y → C in WC-EBS. 1 PublicationCorresponds to variant rs59442925dbSNPEnsembl.1
Natural variantiVAR_003844415Y → H in K-EBS. 3 PublicationsCorresponds to variant rs58380626dbSNPEnsembl.1
Natural variantiVAR_031639416R → P in DM-EBS. 1 PublicationCorresponds to variant rs60622724dbSNPEnsembl.1
Natural variantiVAR_027721417R → P in DM-EBS. 1 PublicationCorresponds to variant rs61085704dbSNPEnsembl.1
Natural variantiVAR_071705418L → Q Probable disease-associated mutation found in epidermolysis bullosa simplex with variable phenotype. 1 Publication1
Natural variantiVAR_003845419L → Q in DM-EBS. 3 PublicationsCorresponds to variant rs57364972dbSNPEnsembl.1
Natural variantiVAR_010452422E → K in WC-EBS. 1 PublicationCorresponds to variant rs58762773dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00124 Genomic DNA. Translation: AAB59562.1.
BT007186 mRNA. Translation: AAP35850.1.
AC019349 Genomic DNA. No translation available.
BC002690 mRNA. Translation: AAH02690.1.
BC019097 mRNA. Translation: AAH19097.1.
BC042437 mRNA. Translation: AAH42437.1.
BC094830 mRNA. Translation: AAH94830.1.
D28807 Genomic DNA. Translation: BAA05967.1.
AF186085 Genomic DNA. Translation: AAF04034.1.
AF186086 Genomic DNA. Translation: AAF04035.1.
AF186087 Genomic DNA. Translation: AAF04036.1.
AF186088 Genomic DNA. Translation: AAF04037.1.
AF186089 Genomic DNA. Translation: AAF04038.1.
AF186090 Genomic DNA. Translation: AAF04039.1.
CCDSiCCDS11400.1.
PIRiA26763. KRHUE.
RefSeqiNP_000517.2. NM_000526.4.
UniGeneiHs.654380.

Genome annotation databases

EnsembliENST00000167586; ENSP00000167586; ENSG00000186847.
GeneIDi3861.
KEGGihsa:3861.
UCSCiuc002hxf.3. 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
J00124 Genomic DNA. Translation: AAB59562.1.
BT007186 mRNA. Translation: AAP35850.1.
AC019349 Genomic DNA. No translation available.
BC002690 mRNA. Translation: AAH02690.1.
BC019097 mRNA. Translation: AAH19097.1.
BC042437 mRNA. Translation: AAH42437.1.
BC094830 mRNA. Translation: AAH94830.1.
D28807 Genomic DNA. Translation: BAA05967.1.
AF186085 Genomic DNA. Translation: AAF04034.1.
AF186086 Genomic DNA. Translation: AAF04035.1.
AF186087 Genomic DNA. Translation: AAF04036.1.
AF186088 Genomic DNA. Translation: AAF04037.1.
AF186089 Genomic DNA. Translation: AAF04038.1.
AF186090 Genomic DNA. Translation: AAF04039.1.
CCDSiCCDS11400.1.
PIRiA26763. KRHUE.
RefSeqiNP_000517.2. NM_000526.4.
UniGeneiHs.654380.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00A295-422[»]
ProteinModelPortaliP02533.
SMRiP02533.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110059. 42 interactors.
DIPiDIP-33874N.
IntActiP02533. 21 interactors.
STRINGi9606.ENSP00000167586.

PTM databases

iPTMnetiP02533.
PhosphoSitePlusiP02533.
SwissPalmiP02533.

Polymorphism and mutation databases

BioMutaiKRT14.
DMDMi229463044.

Proteomic databases

PaxDbiP02533.
PeptideAtlasiP02533.
PRIDEiP02533.

Protocols and materials databases

DNASUi3861.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000167586; ENSP00000167586; ENSG00000186847.
GeneIDi3861.
KEGGihsa:3861.
UCSCiuc002hxf.3. human.

Organism-specific databases

CTDi3861.
DisGeNETi3861.
GeneCardsiKRT14.
GeneReviewsiKRT14.
HGNCiHGNC:6416. KRT14.
HPAiCAB000134.
HPA000452.
HPA023040.
MalaCardsiKRT14.
MIMi125595. phenotype.
131760. phenotype.
131800. phenotype.
131900. phenotype.
148066. gene.
161000. phenotype.
601001. phenotype.
neXtProtiNX_P02533.
OpenTargetsiENSG00000186847.
Orphaneti86920. Dermatopathia pigmentosa reticularis.
79397. Epidermolysis bullosa simplex with mottled pigmentation.
79396. Epidermolysis bullosa simplex, Dowling-Meara type.
79399. Generalized epidermolysis bullosa simplex, non-Dowling-Meara type.
89838. KRT14-related epidermolysis bullosa simplex.
79400. Localized epidermolysis bullosa simplex.
69087. Naegeli-Franceschetti-Jadassohn syndrome.
PharmGKBiPA30203.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOVERGENiHBG013015.
InParanoidiP02533.
KOiK07604.
OMAiNLRMSVG.
OrthoDBiEOG091G087I.
PhylomeDBiP02533.
TreeFamiTF332742.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000171401-MONOMER.
ReactomeiR-HSA-446107. Type I hemidesmosome assembly.
R-HSA-6805567. Keratinization.
R-HSA-6809371. Formation of the cornified envelope.

Miscellaneous databases

GeneWikiiKeratin_14.
GenomeRNAii3861.
PROiP02533.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000186847.
CleanExiHS_KRT14.
GenevisibleiP02533. HS.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiK1C14_HUMAN
AccessioniPrimary (citable) accession number: P02533
Secondary accession number(s): Q14715
, Q53XY3, Q9BUE3, Q9UBN2, Q9UBN3, Q9UCY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 5, 2009
Last modified: November 30, 2016
This is version 189 of the entry and version 4 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 17
    Human chromosome 17: 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.