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Protein

Keratin, type I cytoskeletal 14

Gene

Krt14

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei371StutterBy similarity1

GO - Molecular functioni

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiR-RNO-446107. Type I hemidesmosome assembly.
R-RNO-6805567. Keratinization.
R-RNO-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
Type I keratin Ka14
Gene namesi
Name:Krt14
Synonyms:Ka14Imported, Krt1-14
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1307463. Krt14.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Expressed in both as a filamentous pattern.By similarity

GO - Cellular componenti

  • cell periphery Source: Ensembl
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • keratin filament Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000636551 – 485Keratin, type I cytoskeletal 14Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi374InterchainBy similarity
Modified residuei448PhosphoserineBy 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.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ6IFV1.
PRIDEiQ6IFV1.

PTM databases

iPTMnetiQ6IFV1.
PhosphoSitePlusiQ6IFV1.

Expressioni

Tissue specificityi

Expressed in most cells of squamous cell carcinomas, in spinous and suprabasal cells around the branching papillary region of papillomas, and weakly in a few proliferative cells of hyperplastic tissue.1 Publication

Gene expression databases

BgeeiENSRNOG00000003899.
ExpressionAtlasiQ6IFV1. differential.
GenevisibleiQ6IFV1. RN.

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 (By similarity). Interacts with EPPK1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ6IFV1. 1 interactor.
STRINGi10116.ENSRNOP00000005285.

Structurei

3D structure databases

ProteinModelPortaliQ6IFV1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 121HeadBy similarityAdd BLAST121
Regioni122 – 429RodBy similarityAdd BLAST308
Regioni122 – 157Coil 1ABy similarityAdd BLAST36
Regioni158 – 175Linker 1By similarityAdd BLAST18
Regioni176 – 267Coil 1BBy similarityAdd BLAST92
Regioni268 – 290Linker 12By similarityAdd BLAST23
Regioni291 – 429Coil 2By similarityAdd BLAST139
Regioni430 – 485TailBy similarityAdd BLAST56
Regioni432 – 485Interaction with Type I keratins and keratin filamentsBy similarityAdd BLAST54

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFV1.
KOiK07604.
OMAiEYYEQKG.
OrthoDBiEOG091G087I.
PhylomeDBiQ6IFV1.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
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.

Q6IFV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATCSRQFTS SSSMKGSCGI GGGSSRMSSV LAGGSCRAPS TYGGMSRFSS
60 70 80 90 100
AGAYAVGSGY GGGFSSSSFG GGFGGGIGGG IGGGLGGGIG GGFGGGIGGG
110 120 130 140 150
FGGGIGSGFG GGLGDGLLVG SEKVTMQNLN DRLATYLDKV RALEEANSDL
160 170 180 190 200
EVKIRDWYQR QRPTEIKDYS PYFKTIEDLK SKILAATVDN ANVLLQIDNA
210 220 230 240 250
RLAADDFRTK FETEQSLRIN VESDINGLRR VLDELTLARA DLEMQIESLK
260 270 280 290 300
EELAYLKKNH EEEMASMRGQ VGGDVNVEMD AAPGVDLSRI LNEMRDQYEK
310 320 330 340 350
MAEKNRKDAE DWFFTKTEEL NREVATNSEL VQSGKSEISE LRRTMQNLEI
360 370 380 390 400
ELQSQLSMKA SLENNLEETK GRYCMQLAQI QEMIGSVEEQ LAQLRCEMEQ
410 420 430 440 450
QNQEYKILLD VKTRLEQEIA TYRRLLEGED AHLSSAQFSS SSQFSSGSQS
460 470 480
SRDVTSTNRQ IRTKVMDVHD GKVVSTHEQV LRTKN
Length:485
Mass (Da):52,684
Last modified:July 5, 2004 - v1
Checksum:iC12CC69E59CD8DBE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti77I → L in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti81I → F in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti84G → R in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti88 – 107Missing in BAA22371 (PubMed:8950218).CuratedAdd BLAST20
Sequence conflicti205 – 207DDF → NDL in BAA22371 (PubMed:8950218).Curated3
Sequence conflicti211 – 215FETEQ → YDNET in BAA22371 (PubMed:8950218).Curated5
Sequence conflicti219 – 220IN → QL in BAA22371 (PubMed:8950218).Curated2
Sequence conflicti227G → N in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti230R → C in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti237 – 238LA → MS in BAA22371 (PubMed:8950218).Curated2
Sequence conflicti250K → T in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti265 – 271ASMRGQV → LALRVRL in BAA22371 (PubMed:8950218).Curated7
Sequence conflicti300K → Q in BAA22371 (PubMed:8950218).Curated1
Sequence conflicti309 – 317AEDWFFTKT → VEAWLEATS in BAA22371 (PubMed:8950218).Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073469 Genomic DNA. No translation available.
D63774 mRNA. Translation: BAA22371.1.
BK004047 mRNA. Translation: DAA04481.1.
RefSeqiNP_001008751.1. NM_001008751.1.
UniGeneiRn.145931.
Rn.153972.

Genome annotation databases

EnsembliENSRNOT00000005285; ENSRNOP00000005285; ENSRNOG00000003899.
GeneIDi287701.
KEGGirno:287701.
UCSCiRGD:1307463. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073469 Genomic DNA. No translation available.
D63774 mRNA. Translation: BAA22371.1.
BK004047 mRNA. Translation: DAA04481.1.
RefSeqiNP_001008751.1. NM_001008751.1.
UniGeneiRn.145931.
Rn.153972.

3D structure databases

ProteinModelPortaliQ6IFV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6IFV1. 1 interactor.
STRINGi10116.ENSRNOP00000005285.

PTM databases

iPTMnetiQ6IFV1.
PhosphoSitePlusiQ6IFV1.

Proteomic databases

PaxDbiQ6IFV1.
PRIDEiQ6IFV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005285; ENSRNOP00000005285; ENSRNOG00000003899.
GeneIDi287701.
KEGGirno:287701.
UCSCiRGD:1307463. rat.

Organism-specific databases

CTDi3861.
RGDi1307463. Krt14.

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ6IFV1.
KOiK07604.
OMAiEYYEQKG.
OrthoDBiEOG091G087I.
PhylomeDBiQ6IFV1.
TreeFamiTF332742.

Enzyme and pathway databases

ReactomeiR-RNO-446107. Type I hemidesmosome assembly.
R-RNO-6805567. Keratinization.
R-RNO-6809371. Formation of the cornified envelope.

Miscellaneous databases

PROiQ6IFV1.

Gene expression databases

BgeeiENSRNOG00000003899.
ExpressionAtlasiQ6IFV1. differential.
GenevisibleiQ6IFV1. RN.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
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_RAT
AccessioniPrimary (citable) accession number: Q6IFV1
Secondary accession number(s): O35813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Complete proteome, Reference proteome

Documents

  1. 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.