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Protein

Keratin, type I cytoskeletal 14

Gene

Krt14

Organism
Mus musculus (Mouse)
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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei370 – 3701Stutter

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-446107. Type I hemidesmosome assembly.

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
Synonyms:Krt1-14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:96688. 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: MGI
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: MGI
  • intermediate filament Source: MGI
  • intracellular Source: MGI
  • keratin filament Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Keratin, type I cytoskeletal 14PRO_0000063654Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi373 – 373Interchain1 Publication
Modified residuei447 – 4471PhosphoserineCombined sources

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

MaxQBiQ61781.
PaxDbiQ61781.
PRIDEiQ61781.

PTM databases

iPTMnetiQ61781.
PhosphoSiteiQ61781.

Expressioni

Tissue specificityi

Basal cells of epidermis and other stratified epithelia.

Gene expression databases

BgeeiQ61781.
CleanExiMM_KRT14.
GenevisibleiQ61781. MM.

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.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201019. 6 interactions.
IntActiQ61781. 1 interaction.
MINTiMINT-1859102.
STRINGi10090.ENSMUSP00000007272.

Structurei

3D structure databases

ProteinModelPortaliQ61781.
SMRiQ61781. Positions 171-269, 285-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 120120HeadAdd
BLAST
Regioni121 – 428308RodAdd
BLAST
Regioni121 – 15636Coil 1AAdd
BLAST
Regioni157 – 17418Linker 1Add
BLAST
Regioni175 – 26692Coil 1BAdd
BLAST
Regioni267 – 28923Linker 12Add
BLAST
Regioni290 – 428139Coil 2Add
BLAST
Regioni429 – 48456TailAdd
BLAST
Regioni431 – 48454Interaction with Type I keratins and keratin filamentsBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ61781.
KOiK07604.
OMAiNLRMSVG.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ61781.
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.

Q61781-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATCSRQFTS SSSMKGSCGI GGGSSRMSSI LAGGSCRAPS TYGGMSVTSS
60 70 80 90 100
RFSSGGACGI GGGYGGSFSS SSFGGGLGSG FGGRFDGFGG GFGGGLGGGF
110 120 130 140 150
GGGLGGGLGG GIGDGLLVGS EKVTMQNLND RLATYLDKVR ALEEANTELE
160 170 180 190 200
VKIRDWYQRQ RPTEIKDYSP YFKTIEDLKS KILAATVDNA NVLLQIDNAR
210 220 230 240 250
LAADDFRTKF ETEQSLRMSV EADINGLRRV LDELTLARAD LEMQIESLKE
260 270 280 290 300
ELAYLKKNHE EEMASMRGQV GGDVNVEMDA APGVDLSRIL NEMRDQYEKM
310 320 330 340 350
AEKNRKDAEE WFFSKTEELN REVATNSELV QSGKSEISEL RRTMQNLEIE
360 370 380 390 400
LQSQLSMKAS LENNLEETKG RYCMQLAQIQ EMIGSVEEQL AQLRCEMEQQ
410 420 430 440 450
NQEYKILLDV KTRLEQEIAT YRRLLEGEDA HLSSSQFSSS SQFSSGSQSS
460 470 480
RDVTSTNRQI RTKVMDVHDG KVVSTHEQVL RTKN
Length:484
Mass (Da):52,867
Last modified:July 25, 2003 - v2
Checksum:iA9B6BA66B2F46668
GO

Sequence cautioni

The sequence AAH03325.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590873 Genomic DNA. Translation: CAM17776.1.
BC003325 mRNA. Translation: AAH03325.1. Different initiation.
BC011074 mRNA. Translation: AAH11074.1.
M13806 mRNA. Translation: AAA39392.1.
CCDSiCCDS25413.1.
PIRiB26135.
RefSeqiNP_001300886.1. NM_001313957.1.
NP_058654.1. NM_016958.2.
UniGeneiMm.439898.

Genome annotation databases

EnsembliENSMUST00000007272; ENSMUSP00000007272; ENSMUSG00000045545.
GeneIDi16664.
KEGGimmu:16664.
UCSCiuc007lko.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590873 Genomic DNA. Translation: CAM17776.1.
BC003325 mRNA. Translation: AAH03325.1. Different initiation.
BC011074 mRNA. Translation: AAH11074.1.
M13806 mRNA. Translation: AAA39392.1.
CCDSiCCDS25413.1.
PIRiB26135.
RefSeqiNP_001300886.1. NM_001313957.1.
NP_058654.1. NM_016958.2.
UniGeneiMm.439898.

3D structure databases

ProteinModelPortaliQ61781.
SMRiQ61781. Positions 171-269, 285-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201019. 6 interactions.
IntActiQ61781. 1 interaction.
MINTiMINT-1859102.
STRINGi10090.ENSMUSP00000007272.

PTM databases

iPTMnetiQ61781.
PhosphoSiteiQ61781.

Proteomic databases

MaxQBiQ61781.
PaxDbiQ61781.
PRIDEiQ61781.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007272; ENSMUSP00000007272; ENSMUSG00000045545.
GeneIDi16664.
KEGGimmu:16664.
UCSCiuc007lko.1. mouse.

Organism-specific databases

CTDi3861.
MGIiMGI:96688. Krt14.

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
GeneTreeiENSGT00760000118808.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiQ61781.
KOiK07604.
OMAiNLRMSVG.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ61781.
TreeFamiTF332742.

Enzyme and pathway databases

ReactomeiR-MMU-446107. Type I hemidesmosome assembly.

Miscellaneous databases

NextBioi290371.
PROiQ61781.
SOURCEiSearch...

Gene expression databases

BgeeiQ61781.
CleanExiMM_KRT14.
GenevisibleiQ61781. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Liver, Lung and Pancreas.
  3. "Structural basis for heteromeric assembly and perinuclear organization of keratin filaments."
    Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.
    Nat. Struct. Mol. Biol. 19:707-715(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DISULFIDE BOND.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 123-131; 201-207; 218-228; 322-334 AND 414-422, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  6. "Three cDNA sequences of mouse type I keratins: cellular localization of the mRNAs in normal and hyperproliferative tissues."
    Knapp B., Rentrop M., Schweizer J., Winter H.
    J. Biol. Chem. 262:938-945(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-484.
  7. "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent fashion."
    Tong X., Coulombe P.A.
    Genes Dev. 20:1353-1364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRADD.

Entry informationi

Entry nameiK1C14_MOUSE
AccessioniPrimary (citable) accession number: Q61781
Secondary accession number(s): A2A4G4, Q91VQ4, Q99LE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 25, 2003
Last modified: May 11, 2016
This is version 132 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.