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P05784

- K1C18_MOUSE

UniProt

P05784 - K1C18_MOUSE

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Protein

Keratin, type I cytoskeletal 18

Gene
Krt18, Kerd, Krt1-18
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei231 – 2322Cleavage; by caspase-3, caspase-6 or caspase-7
Sitei264 – 2641Stutter
Sitei324 – 3241Stutter

GO - Molecular functioni

  1. protein binding Source: MGI
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. extrinsic apoptotic signaling pathway Source: MGI
  2. Golgi to plasma membrane CFTR protein transport Source: Ensembl
  3. hepatocyte apoptotic process Source: MGI
  4. negative regulation of apoptotic process Source: Ensembl
  5. tumor necrosis factor-mediated signaling pathway Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Krt18
Synonyms:Kerd, Krt1-18
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:96692. Krt18.

Subcellular locationi

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

GO - Cellular componenti

  1. cell periphery Source: MGI
  2. centriolar satellite Source: Ensembl
  3. intermediate filament Source: MGI
  4. keratin filament Source: MGI
  5. nuclear matrix Source: UniProtKB-SubCell
  6. nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 423422Keratin, type I cytoskeletal 18PRO_0000063667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei7 – 71Phosphoserine By similarity
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei16 – 161Phosphoserine By similarity
Modified residuei19 – 191Phosphoserine By similarity
Modified residuei31 – 311Phosphoserine; alternate1 Publication
Glycosylationi31 – 311O-linked (GlcNAc); alternate By similarity
Modified residuei32 – 321Phosphoserine; alternate1 Publication
Glycosylationi32 – 321O-linked (GlcNAc); alternate By similarity
Modified residuei35 – 351Phosphoserine1 Publication
Modified residuei37 – 371Phosphotyrosine By similarity
Modified residuei43 – 431Phosphoserine By similarity
Glycosylationi50 – 501O-linked (GlcNAc) By similarity
Modified residuei52 – 521Phosphoserine; by MAPKAPK2 and MAPKAPK31 Publication
Modified residuei60 – 601Phosphoserine By similarity
Modified residuei92 – 921Phosphoserine By similarity
Modified residuei124 – 1241N6-acetyllysine By similarity
Modified residuei170 – 1701Phosphoserine By similarity
Modified residuei295 – 2951Phosphothreonine By similarity
Modified residuei316 – 3161Phosphoserine1 Publication
Modified residuei392 – 3921Phosphoserine By similarity
Modified residuei397 – 3971Phosphothreonine By similarity

Post-translational modificationi

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-7.1 Publication
O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation By similarity.

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP05784.
PaxDbiP05784.
PRIDEiP05784.

2D gel databases

SWISS-2DPAGEP05784.

PTM databases

PhosphoSiteiP05784.

Expressioni

Tissue specificityi

Expressed in endoderm, intestinal epithelial cells and in most extraembryonic tissues.4 Publications

Developmental stagei

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 15.3 Publications

Inductioni

By retinoic acid and IL-6.2 Publications

Gene expression databases

BgeeiP05784.
CleanExiMM_KRT18.
GenevestigatoriP05784.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi201023. 1 interaction.
IntActiP05784. 4 interactions.
MINTiMINT-1866927.

Structurei

3D structure databases

ProteinModelPortaliP05784.
SMRiP05784. Positions 122-221, 290-378.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7170HeadAdd
BLAST
Regioni62 – 366305Necessary for interaction with PNN By similarityAdd
BLAST
Regioni69 – 12153Interaction with TRADD By similarityAdd
BLAST
Regioni72 – 380309RodAdd
BLAST
Regioni72 – 10736Coil 1AAdd
BLAST
Regioni108 – 12518Linker 1Add
BLAST
Regioni126 – 21792Coil 1BAdd
BLAST
Regioni218 – 24124Linker 12Add
BLAST
Regioni236 – 384149Interaction with DNAJB6 By similarityAdd
BLAST
Regioni242 – 380139Coil 2Add
BLAST
Regioni381 – 42343TailAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG150427.
GeneTreeiENSGT00740000115001.
HOGENOMiHOG000230975.
HOVERGENiHBG013015.
InParanoidiP05784.
KOiK07604.
OMAiRAKYEKM.
OrthoDBiEOG7V1FR3.
PhylomeDBiP05784.
TreeFamiTF332742.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05784-1 [UniParc]FASTAAdd to Basket

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MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS    50
RSVWGGSVGS AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL 100
ESKIREHLEK KGPQGVRDWG HYFKIIEDLR AQIFANSVDN ARIVLQIDNA 150
RLAADDFRVK YETELAMRQS VESDIHGLRK VVDDTNITRL QLETEIEALK 200
EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK IMADIRAQYE 250
ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE 300
IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ 350
RQAQEYEALL NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK 400
TTTRKIVDGR VVSETNDTRV LRH 423
Length:423
Mass (Da):47,538
Last modified:May 29, 2007 - v5
Checksum:iA67ACD6814A02118
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341F → L in AAA39390. 1 Publication
Sequence conflicti134 – 1341F → L in AAA39373. 1 Publication
Sequence conflicti214 – 2141V → A in BAE26424. 1 Publication
Sequence conflicti214 – 2141V → A in BAE39378. 1 Publication
Sequence conflicti244 – 2441D → N in AAA39373. 1 Publication
Sequence conflicti253 – 2531A → G in AAA39373. 1 Publication
Sequence conflicti300 – 3001E → G in BAE39725. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS27869.1.
PIRiI59463.
RefSeqiNP_034794.2. NM_010664.2.
UniGeneiMm.22479.

Genome annotation databases

EnsembliENSMUST00000023803; ENSMUSP00000023803; ENSMUSG00000023043.
GeneIDi16668.
KEGGimmu:16668.
UCSCiuc007xuj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS27869.1.
PIRi I59463.
RefSeqi NP_034794.2. NM_010664.2.
UniGenei Mm.22479.

3D structure databases

ProteinModelPortali P05784.
SMRi P05784. Positions 122-221, 290-378.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201023. 1 interaction.
IntActi P05784. 4 interactions.
MINTi MINT-1866927.

PTM databases

PhosphoSitei P05784.

2D gel databases

SWISS-2DPAGE P05784.

Proteomic databases

MaxQBi P05784.
PaxDbi P05784.
PRIDEi P05784.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023803 ; ENSMUSP00000023803 ; ENSMUSG00000023043 .
GeneIDi 16668.
KEGGi mmu:16668.
UCSCi uc007xuj.2. mouse.

Organism-specific databases

CTDi 3875.
MGIi MGI:96692. Krt18.

Phylogenomic databases

eggNOGi NOG150427.
GeneTreei ENSGT00740000115001.
HOGENOMi HOG000230975.
HOVERGENi HBG013015.
InParanoidi P05784.
KOi K07604.
OMAi RAKYEKM.
OrthoDBi EOG7V1FR3.
PhylomeDBi P05784.
TreeFami TF332742.

Miscellaneous databases

ChiTaRSi KRT18. mouse.
NextBioi 290387.
PROi P05784.
SOURCEi Search...

Gene expression databases

Bgeei P05784.
CleanExi MM_KRT18.
Genevestigatori P05784.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR027695. Keratin-18.
IPR002957. Keratin_I.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
PTHR23239:SF35. PTHR23239:SF35. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01248. TYPE1KERATIN.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiK1C18_MOUSE
AccessioniPrimary (citable) accession number: P05784
Secondary accession number(s): Q3TIX1
, Q3TJH6, Q3TJW7, Q61766
Entry historyi
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 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi