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P05784 (K1C18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type I cytoskeletal 18
Alternative name(s):
Cytokeratin endo B
Short name=Keratin D
Cytokeratin-18
Short name=CK-18
Keratin-18
Short name=K18
Gene names
Name:Krt18
Synonyms:Kerd, Krt1-18
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells By similarity. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. Ref.11

Subunit structure

Heterotetramer of two type I and two type II keratins. KRT18 associates with KRT8. Interacts with PNN, HCV core protein and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with the thrombin-antithrombin complex. Interacts with DNAJB6, TCHP and TRADD By similarity.

Subcellular location

Nucleus matrix By similarity. Nucleusnucleolus By similarity. Cytoplasm By similarity.

Tissue specificity

Expressed in endoderm, intestinal epithelial cells and in most extraembryonic tissues. Ref.1 Ref.6 Ref.7 Ref.11

Developmental stage

During embryogenesis, expressed in a complex spatial and temporal pattern in various embryonic epithelia. In 7.5 and 13.5 day old embryo, expressed in most endodermal epithelia, ectodermal and nascent mesodermal tissues. When the neural plate forms, expression begins in the cells of skin ectoderm, head process/notochord, periderm, whisker buds, choroid plexus and the epithelia of auditory duct and inner ear. High expression in the lining endodermal cells when the foregut and hindgut invaginations form. Expression in all three layers of the urothelium starts at day 15 in the embryo and is not visible after day 18. By day 11 and 12, the entire embryonic palatal epithelium shows expression as well as the nasal passages and the roof of the mouth; which disappears progresively from day 13 to 15. Ref.7 Ref.8 Ref.10

Induction

By retinoic acid and IL-6. Ref.1 Ref.11

Post-translational modification

Phosphorylation increases by IL-6.

Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7. Ref.9

O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 423422Keratin, type I cytoskeletal 18
PRO_0000063667

Regions

Region2 – 7170Head
Region62 – 366305Necessary for interaction with PNN By similarity
Region69 – 12153Interaction with TRADD By similarity
Region72 – 380309Rod
Region72 – 10736Coil 1A
Region108 – 12518Linker 1
Region126 – 21792Coil 1B
Region218 – 24124Linker 12
Region236 – 384149Interaction with DNAJB6 By similarity
Region242 – 380139Coil 2
Region381 – 42343Tail

Sites

Site231 – 2322Cleavage; by caspase-3, caspase-6 or caspase-7
Site2641Stutter
Site3241Stutter

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue71Phosphoserine By similarity
Modified residue111Phosphoserine By similarity
Modified residue161Phosphoserine By similarity
Modified residue191Phosphoserine By similarity
Modified residue311Phosphoserine; alternate Ref.12
Modified residue321Phosphoserine; alternate Ref.12
Modified residue351Phosphoserine Ref.12
Modified residue371Phosphotyrosine By similarity
Modified residue431Phosphoserine By similarity
Modified residue521Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.13
Modified residue601Phosphoserine By similarity
Modified residue921Phosphoserine By similarity
Modified residue1241N6-acetyllysine By similarity
Modified residue1701Phosphoserine By similarity
Modified residue2951Phosphothreonine By similarity
Modified residue3161Phosphoserine Ref.12
Modified residue3921Phosphoserine By similarity
Modified residue3971Phosphothreonine By similarity
Glycosylation311O-linked (GlcNAc); alternate By similarity
Glycosylation321O-linked (GlcNAc); alternate By similarity
Glycosylation501O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict1341F → L in AAA39390. Ref.1
Sequence conflict1341F → L in AAA39373. Ref.2
Sequence conflict2141V → A in BAE26424. Ref.4
Sequence conflict2141V → A in BAE39378. Ref.4
Sequence conflict2441D → N in AAA39373. Ref.2
Sequence conflict2531A → G in AAA39373. Ref.2
Sequence conflict3001E → G in BAE39725. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P05784 [UniParc].

Last modified May 29, 2007. Version 5.
Checksum: A67ACD6814A02118

FASTA42347,538
        10         20         30         40         50         60 
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS 

        70         80         90        100        110        120 
AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL ESKIREHLEK KGPQGVRDWG 

       130        140        150        160        170        180 
HYFKIIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK 

       190        200        210        220        230        240 
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK 

       250        260        270        280        290        300 
IMADIRAQYE ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE 

       310        320        330        340        350        360 
IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ RQAQEYEALL 

       370        380        390        400        410        420 
NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK TTTRKIVDGR VVSETNDTRV 


LRH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the Endo B cytokeratin expressed in preimplantation mouse embryos."
Singer P.A., Trevor K., Oshima R.G.
J. Biol. Chem. 261:538-547(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Tissue: Endoderm.
[2]"Cloning and characterization of keratin D, a murine endodermal cytoskeletal protein induced during in vitro differentiation of F9 teratocarcinoma cells."
Alonso A., Weber T., Jorcano J.L.
Roux's Arch. Dev. Biol. 196:16-21(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Teratocarcinoma.
[3]"Nucleotide sequence and structure of the mouse cytokeratin endoB gene."
Ichinose Y., Morita T., Zhang F., Srimahasongcram S., Tondella M.L.C., Matsumoto M., Nozaki M., Matsushiro A.
Gene 70:85-95(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Blastocyst, Embryo and Placenta.
[5]"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: C57BL/6.
Tissue: Eye.
[6]"Identification of the gene coding for the Endo B murine cytokeratin and its methylated, stable inactive state in mouse nonepithelial cells."
Oshima R.G., Trevor K., Shevinsky L.H., Ryder O.A., Cecena G.
Genes Dev. 2:505-516(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, TISSUE SPECIFICITY.
[7]"Embryonic expression of human keratin 18 and K18-beta-galactosidase fusion genes in transgenic mice."
Thorey I.S., Meneses J.J., Neznanov N., Kulesh D.A., Pedersen R.A., Oshima R.G.
Dev. Biol. 160:519-534(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[8]"Monoclonal antibodies recognising stage and region specific epitopes in embryonic mouse palatal epithelial cells."
Dixon M.J., Robinson V., White A., Ferguson M.W.
J. Anat. 183:423-438(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[9]"Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis."
Caulin C., Salvesen G.S., Oshima R.G.
J. Cell Biol. 138:1379-1394(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY CASPASES.
[10]"Superficial cell differentiation during embryonic and postnatal development of mouse urothelium."
Erman A., Veranic P., Psenicnik M., Jezernik K.
Tissue Cell 38:293-301(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[11]"Interleukin-6 induces keratin expression in intestinal epithelial cells: potential role of keratin-8 in interleukin-6-induced barrier function alterations."
Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.
J. Biol. Chem. 282:8219-8227(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INDUCTION.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35 AND SER-316, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins."
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O., Seidler U., Omary M.B., Kotlyarov A., Gaestel M.
J. Biol. Chem. 285:33242-33251(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-52 BY MAPKAPK2 AND MAPKAPK3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11686 mRNA. Translation: AAA39390.1.
M36376 mRNA. Translation: AAA39373.1.
M22832 Genomic DNA. Translation: AAA37552.1.
AK145413 mRNA. Translation: BAE26424.1.
AK167072 mRNA. Translation: BAE39232.1.
AK167265 mRNA. Translation: BAE39378.1.
AK167432 mRNA. Translation: BAE39519.1.
AK167469 mRNA. Translation: BAE39553.1.
AK167676 mRNA. Translation: BAE39725.1.
BC089022 mRNA. Translation: AAH89022.1.
Y00217 Genomic DNA. Translation: CAA68365.1.
CCDSCCDS27869.1.
PIRI59463.
RefSeqNP_034794.2. NM_010664.2.
UniGeneMm.22479.

3D structure databases

ProteinModelPortalP05784.
SMRP05784. Positions 122-221, 290-378.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201023. 1 interaction.
IntActP05784. 4 interactions.
MINTMINT-1866927.

PTM databases

PhosphoSiteP05784.

2D gel databases

SWISS-2DPAGEP05784.

Proteomic databases

MaxQBP05784.
PaxDbP05784.
PRIDEP05784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023803; ENSMUSP00000023803; ENSMUSG00000023043.
GeneID16668.
KEGGmmu:16668.
UCSCuc007xuj.2. mouse.

Organism-specific databases

CTD3875.
MGIMGI:96692. Krt18.

Phylogenomic databases

eggNOGNOG150427.
GeneTreeENSGT00740000115001.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidP05784.
KOK07604.
OMARAKYEKM.
OrthoDBEOG7V1FR3.
PhylomeDBP05784.
TreeFamTF332742.

Gene expression databases

BgeeP05784.
CleanExMM_KRT18.
GenevestigatorP05784.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKRT18. mouse.
NextBio290387.
PROP05784.
SOURCESearch...

Entry information

Entry nameK1C18_MOUSE
AccessionPrimary (citable) accession number: P05784
Secondary accession number(s): Q3TIX1 expand/collapse secondary AC list , Q3TJH6, Q3TJW7, Q61766
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 130 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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