Keratin, type I cytoskeletal 14 - Mus musculus (Mouse)

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Q61781 (K1C14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 14

Alternative name(s):
Cytokeratin-14
Short name=CK-14
Keratin-14
Short name=K14

Gene names

Name:	Krt14
Synonyms:	Krt1-14

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.2 Ref.6
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Expressed in both as a filamentous pattern By similarity.
Tissue specificity	Basal cells of epidermis and other stratified epithelia.
Post-translational modification	A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus.
Miscellaneous	There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
Sequence similarities	Belongs to the intermediate filament family.
Sequence caution	The sequence AAH03325.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Intermediate filament Keratin Nucleus
Domain	Coiled coil
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	epithelial cell differentiation Inferred from direct assay PubMed 19303854. Source: MGI intermediate filament bundle assembly Inferred from sequence or structural similarity. Source: UniProtKB response to ionizing radiation Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara
Cellular_component	cell periphery Inferred from direct assay PubMed 11698679 PubMed 16682203 PubMed 18692037 PubMed 21464233. Source: MGI cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB keratin filament Inferred from direct assay PubMed 14673151 PubMed 19487454. Source: MGI nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 484

484

Keratin, type I cytoskeletal 14

PRO_0000063654

Regions

Region

1 – 120

120

Head

Region

121 – 428

308

Rod

Region

121 – 156

Coil 1A

Region

157 – 174

Linker 1

Region

175 – 266

Coil 1B

Region

267 – 289

Linker 12

Region

290 – 428

139

Coil 2

Region

429 – 484

Tail

Region

431 – 484

Interaction with Type I keratins and keratin filaments By similarity

Sites

Site

370

Stutter

Amino acid modifications

Disulfide bond

373

Interchain Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q61781 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: A9B6BA66B2F46668
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FASTA

484

52,867

        10         20         30         40         50         60 
MATCSRQFTS SSSMKGSCGI GGGSSRMSSI LAGGSCRAPS TYGGMSVTSS RFSSGGACGI 

        70         80         90        100        110        120 
GGGYGGSFSS SSFGGGLGSG FGGRFDGFGG GFGGGLGGGF GGGLGGGLGG GIGDGLLVGS 

       130        140        150        160        170        180 
EKVTMQNLND RLATYLDKVR ALEEANTELE VKIRDWYQRQ RPTEIKDYSP YFKTIEDLKS 

       190        200        210        220        230        240 
KILAATVDNA NVLLQIDNAR LAADDFRTKF ETEQSLRMSV EADINGLRRV LDELTLARAD 

       250        260        270        280        290        300 
LEMQIESLKE ELAYLKKNHE EEMASMRGQV GGDVNVEMDA APGVDLSRIL NEMRDQYEKM 

       310        320        330        340        350        360 
AEKNRKDAEE WFFSKTEELN REVATNSELV QSGKSEISEL RRTMQNLEIE LQSQLSMKAS 

       370        380        390        400        410        420 
LENNLEETKG RYCMQLAQIQ EMIGSVEEQL AQLRCEMEQQ NQEYKILLDV KTRLEQEIAT 

       430        440        450        460        470        480 
YRRLLEGEDA HLSSSQFSSS SQFSSGSQSS RDVTSTNRQI RTKVMDVHDG KVVSTHEQVL 


RTKN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"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.
[3]	"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.
[4]	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, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"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.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590873 Genomic DNA. Translation: CAM17776.1. BC003325 mRNA. Translation: AAH03325.1. Different initiation. BC011074 mRNA. Translation: AAH11074.1. M13806 mRNA. Translation: AAA39392.1.
IPI	IPI00227140.
PIR	B26135.
RefSeq	NP_058654.1. NM_016958.1.
UniGene	Mm.439898.
3D structure databases
ProteinModelPortal	Q61781.
SMR	Q61781. Positions 171-269, 285-427.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61781. 1 interaction.
PTM databases
PhosphoSite	Q61781.
Proteomic databases
PaxDb	Q61781.
PRIDE	Q61781.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000007272; ENSMUSP00000007272; ENSMUSG00000045545.
GeneID	16664.
KEGG	mmu:16664.
UCSC	uc007lko.1. mouse.
Organism-specific databases
CTD	3861.
MGI	MGI:96688. Krt14.
Phylogenomic databases
eggNOG	NOG148784.
GeneTree	ENSGT00610000085921.
HOGENOM	HOG000230975.
HOVERGEN	HBG013015.
InParanoid	Q99LE0.
KO	K07604.
OMA	QELISSV.
OrthoDB	EOG483D4W.
Gene expression databases
Bgee	Q61781.
CleanEx	MM_KRT14.
Genevestigator	Q61781.
GermOnline	ENSMUSG00000045545. Mus musculus.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. IPR009053. Prefoldin. [Graphical view]
PANTHER	PTHR23239. PTHR23239. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
SUPFAM	SSF46579. Prefoldin. 1 hit.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	290371.
SOURCE	Search...

Entry information

Entry name

K1C14_MOUSE

Accession

Primary (citable) accession number: Q61781
Secondary accession number(s): A2A4G4, Q91VQ4, Q99LE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 25, 2003
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents