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P05787 (K2C8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Keratin, type II cytoskeletal 8
Alternative name(s):
Cytokeratin-8
Short name=CK-8
Keratin-8
Short name=K8
Type-II keratin Kb8
Gene names
Name:KRT8
Synonyms:CYK8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. Ref.20

Subunit structure

Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with HCV core protein and PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1. Interacts with GPER1. Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.23 Ref.27 Ref.34

Subcellular location

Cytoplasm. Nucleusnucleoplasm By similarity. Nucleus matrix By similarity Ref.15 Ref.27.

Tissue specificity

Observed in muscle fibers accumulating in the costameres of myoplasm at the sarcolemma membrane in structures that contain dystrophin and spectrin. Expressed in gingival mucosa and hard palate of the oral cavity. Ref.15 Ref.20

Post-translational modification

Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization.

O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation. Ref.13 Ref.30 Ref.36

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. Ref.13 Ref.30 Ref.36

Involvement in disease

Cirrhosis (CIRRH) [MIM:215600]: A liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37

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.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Intermediate filament
Keratin
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation involved in embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

response to hydrostatic pressure

Inferred from electronic annotation. Source: Ensembl

response to other organism

Inferred from electronic annotation. Source: Ensembl

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

tumor necrosis factor-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

costamere

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.27. Source: UniProtKB

dystrophin-associated glycoprotein complex

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

intermediate filament

Inferred from direct assay PubMed 10852826. Source: BHF-UCL

keratin filament

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 10954706PubMed 11684708Ref.23Ref.27Ref.34. Source: UniProtKB

scaffold protein binding

Inferred from physical interaction PubMed 10852826. Source: BHF-UCL

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05787-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05787-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MNGVSWSQDLQEGISAWFGPPASTPASTM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 483483Keratin, type II cytoskeletal 8
PRO_0000063740

Regions

Region1 – 9090Head
Region91 – 398308Rod
Region91 – 12636Coil 1A
Region127 – 14317Linker 1
Region144 – 23592Coil 1B
Region236 – 25924Linker 12
Region260 – 398139Coil 2
Region261 – 382122Necessary for interaction with PNN
Region399 – 48385Tail
Compositional bias9 – 4941Ser-rich

Sites

Site3421Stutter

Amino acid modifications

Modified residue91Phosphoserine; by PKC/PRKCE Ref.14
Modified residue131Phosphoserine By similarity
Modified residue211Phosphoserine Ref.26
Modified residue241Phosphoserine; by PKC/PRKCE Ref.4 Ref.14 Ref.26 Ref.35
Modified residue271Phosphoserine Ref.26
Modified residue341Phosphoserine Ref.26 Ref.35
Modified residue361Phosphoserine Ref.26
Modified residue371Phosphoserine Ref.26 Ref.35
Modified residue431Phosphoserine Ref.26 Ref.35
Modified residue741Phosphoserine; by MAPK Ref.17 Ref.18
Modified residue1011N6-malonyllysine Ref.33
Modified residue1171N6-acetyllysine Ref.29
Modified residue2071N6-acetyllysine Ref.29
Modified residue2531Phosphoserine Ref.22 Ref.25 Ref.26 Ref.28 Ref.35
Modified residue2581Phosphoserine Ref.25 Ref.26 Ref.35
Modified residue2951N6-acetyllysine Ref.29
Modified residue3251N6-acetyllysine Ref.29
Modified residue3301Phosphoserine Ref.22
Modified residue3471N6-acetyllysine Ref.29
Modified residue4001Phosphoserine Ref.26
Modified residue4101Phosphoserine Ref.26
Modified residue4171Phosphoserine By similarity
Modified residue4241Phosphoserine By similarity
Modified residue4321Phosphoserine; by CaMK2 and MAPK Ref.4 Ref.26
Modified residue4751Phosphoserine Ref.26 Ref.31
Modified residue4781Phosphoserine Ref.26 Ref.31

Natural variations

Alternative sequence11M → MNGVSWSQDLQEGISAWFGP PASTPASTM in isoform 2.
VSP_046000
Natural variant531G → V in CIRRH. Ref.37
Corresponds to variant rs61710484 [ dbSNP | Ensembl ].
VAR_023058
Natural variant541Y → C in CIRRH. Ref.37
VAR_023059
Natural variant621G → C in CIRRH. Ref.9 Ref.37
Corresponds to variant rs11554495 [ dbSNP | Ensembl ].
VAR_023060
Natural variant631I → V. Ref.37
Corresponds to variant rs59536457 [ dbSNP | Ensembl ].
VAR_023061
Natural variant4011R → W.
Corresponds to variant rs2277330 [ dbSNP | Ensembl ].
VAR_049805
Natural variant4171S → G. Ref.1 Ref.11
Corresponds to variant rs1065591 [ dbSNP | Ensembl ].
VAR_069106
Natural variant4291G → D. Ref.11
Corresponds to variant rs1065648 [ dbSNP | Ensembl ].
VAR_069107

Experimental info

Mutagenesis721L → P: Increases phosphorylation. Ref.18
Mutagenesis741S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. Ref.18
Mutagenesis741S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. Ref.18
Sequence conflict561G → V in BAF83627. Ref.5
Sequence conflict771V → S in AAA35748. Ref.2
Sequence conflict2011D → DVD in CAA52882. Ref.3
Sequence conflict2321I → L in CAA67203. Ref.11
Sequence conflict2571D → E in AAA35748. Ref.2
Sequence conflict3101M → I in CAA31376. Ref.11
Sequence conflict3241L → F in BAD96661. Ref.6
Sequence conflict3841L → M in CAA67203. Ref.11
Sequence conflict3871E → D in AAA35748. Ref.2
Sequence conflict4011R → P in AAA35748. Ref.2
Sequence conflict430 – 4334LTSP → SQA in AAA35763. Ref.1
Sequence conflict4311T → A in CAA67203. Ref.11
Sequence conflict4321S → D in AAA35748. Ref.2
Sequence conflict4321S → D in CAA67203. Ref.11
Sequence conflict4321S → D in CAA31376. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 7.
Checksum: B0BC730B65929D37

FASTA48353,704
        10         20         30         40         50         60 
MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL GGGYGGASGM 

        70         80         90        100        110        120 
GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN KFASFIDKVR FLEQQNKMLE 

       130        140        150        160        170        180 
TKWSLLQQQK TARSNMDNMF ESYINNLRRQ LETLGQEKLK LEAELGNMQG LVEDFKNKYE 

       190        200        210        220        230        240 
DEINKRTEME NEFVLIKKDV DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS 

       250        260        270        280        290        300 
DTSVVLSMDN SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL 

       310        320        330        340        350        360 
RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN AKLSELEAAL 

       370        380        390        400        410        420 
QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES RLESGMQNMS IHTKTTSGYA 

       430        440        450        460        470        480 
GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS SFSRTSSSRA VVVKKIETRD GKLVSESSDV 


LPK 

« Hide

Isoform 2 [UniParc].

Checksum: DB55C0367CD6C37C
Show »

FASTA51156,608

References

« Hide 'large scale' references
[1]"Organization and sequence of the human gene encoding cytokeratin 8."
Krauss S., Franke W.W.
Gene 86:241-249(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-417.
[2]"Cloning and sequence of cDNA for human placental cytokeratin 8. Regulation of the mRNA in trophoblastic cells by cAMP."
Yamamoto R., Kao L.C., McKnight C.E., Strauss J.F. III
Mol. Endocrinol. 4:370-374(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Embryonic simple epithelial keratins 8 and 18: chromosomal location emphasizes difference from other keratin pairs."
Waseem A., Alexander C.M., Steel J.B., Lane E.B.
New Biol. 2:464-478(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Placenta.
[4]"Phosphorylation of human keratin 8 in vivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431."
Ku N.-O., Omary M.B.
J. Biol. Chem. 272:7556-7564(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT SER-24 AND SER-432.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Kidney.
[7]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1), VARIANT CYS-62.
Tissue: Colon, Liver, Lung and Placenta.
[10]"Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8."
Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., Oshima R.G.
Mol. Cell. Biol. 9:1553-1565(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-231 (ISOFORM 1).
[11]"Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ."
Leube R.E., Bosch F.X., Romano V., Zimbelmann R., Hofler H., Franke W.W.
Differentiation 33:69-85(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-483 (ISOFORM 1), VARIANTS GLY-417 AND ASP-429.
[12]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Colon carcinoma.
[13]"Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18."
Chou C.F., Smith A.J., Omary M.B.
J. Biol. Chem. 267:3901-3906(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[14]"PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18."
Omary M.B., Baxter G.T., Chou C.F., Riopel C.L., Lin W.Y., Strulovici B.
J. Cell Biol. 117:583-593(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-9 AND SER-24.
[15]"An immunohistological study of cytokeratin 20 in human and mammalian oral epithelium."
Barrett A.W., Cort E.M., Patel P., Berkovitz B.K.B.
Arch. Oral Biol. 45:879-887(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KRT20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]"Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus."
Shi J., Sugrue S.P.
J. Biol. Chem. 275:14910-14915(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNN.
[17]"The intermediate filament protein keratin 8 is a novel cytoplasmic substrate for c-Jun N-terminal kinase."
He T., Stepulak A., Holmstrom T.H., Omary M.B., Eriksson J.E.
J. Biol. Chem. 277:10767-10774(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-74.
[18]"Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation."
Ku N.O., Azhar S., Omary M.B.
J. Biol. Chem. 277:10775-10782(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-74, MUTAGENESIS OF LEU-72 AND SER-74.
[19]"Identification of trichoplein, a novel keratin filament-binding protein."
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T., Usukura J., Inagaki M.
J. Cell Sci. 118:1081-1090(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TCHP.
[20]"Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19."
Stone M.R., O'Neill A., Catino D., Bloch R.J.
Mol. Biol. Cell 16:4280-4293(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
[21]"Proteomic profiling of cellular proteins interacting with the hepatitis C virus core protein."
Kang S.-M., Shin M.-J., Kim J.-H., Oh J.-W.
Proteomics 5:2227-2237(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[22]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Keratin 20 serine 13 phosphorylation is a stress and intestinal goblet cell marker."
Zhou Q., Cadrin M., Herrmann H., Chen C.-H., Chalkley R.J., Burlingame A.L., Omary M.B.
J. Biol. Chem. 281:16453-16461(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KRT20.
[24]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-27; SER-34; SER-36; SER-37; SER-43; SER-253; SER-258; SER-400; SER-410; SER-432; SER-475 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[28]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117; LYS-207; LYS-295; LYS-325 AND LYS-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18."
Srikanth B., Vaidya M.M., Kalraiya R.D.
J. Biol. Chem. 285:34062-34071(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[31]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-101.
[34]"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPER1.
[35]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-34; SER-37; SER-43; SER-253 AND SER-258, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
[37]"Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies."
Ku N.-O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., Omary M.B.
Proc. Natl. Acad. Sci. U.S.A. 100:6063-6068(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CIRRH VAL-53; CYS-54 AND CYS-62, VARIANT VAL-63.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34482 Genomic DNA. Translation: AAA35763.1.
M34225 mRNA. Translation: AAA35748.1.
X74929 mRNA. Translation: CAA52882.1.
X74981 Genomic DNA. Translation: CAA52916.1.
U76549 mRNA. Translation: AAB18966.1.
AK290938 mRNA. Translation: BAF83627.1.
AK310257 mRNA. No translation available.
AK315826 mRNA. Translation: BAF98717.1.
AK222941 mRNA. Translation: BAD96661.1.
AC107016 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96653.1.
BC000654 mRNA. Translation: AAH00654.3.
BC063513 mRNA. Translation: AAH63513.2.
BC073760 mRNA. Translation: AAH73760.1.
BC075839 mRNA. Translation: AAH75839.1.
M26512 mRNA. Translation: AAA51542.1.
X12882 mRNA. Translation: CAA31376.1.
X98614 mRNA. Translation: CAA67203.1.
CCDSCCDS58234.1. [P05787-2]
CCDS8841.1. [P05787-1]
PIRA34720.
RefSeqNP_001243222.1. NM_001256293.1. [P05787-1]
NP_002264.1. NM_002273.3. [P05787-1]
UniGeneHs.533782.
Hs.708445.

3D structure databases

ProteinModelPortalP05787.
SMRP05787. Positions 88-239, 303-397.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110054. 47 interactions.
DIPDIP-424N.
IntActP05787. 24 interactions.
MINTMINT-256526.

Chemistry

DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP05787.
UniCarbKBP05787.

Polymorphism databases

DMDM90110027.

2D gel databases

SWISS-2DPAGEP05787.

Proteomic databases

MaxQBP05787.
PaxDbP05787.
PeptideAtlasP05787.
PRIDEP05787.

Protocols and materials databases

DNASU3856.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
GeneID3856.
KEGGhsa:3856.
UCSCuc001sbd.2. human. [P05787-1]

Organism-specific databases

CTD3856.
GeneCardsGC12M053290.
H-InvDBHIX0026255.
HIX0034365.
HIX0168895.
HGNCHGNC:6446. KRT8.
HPACAB000131.
CAB001696.
HPA049866.
MIM148060. gene.
215600. phenotype.
neXtProtNX_P05787.
PharmGKBPA30234.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146769.
HOVERGENHBG013015.
InParanoidP05787.
KOK07605.
OMAXRASLEA.
OrthoDBEOG7FV3Q8.
PhylomeDBP05787.
TreeFamTF317854.

Enzyme and pathway databases

SignaLinkP05787.

Gene expression databases

BgeeP05787.
GenevestigatorP05787.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
SUPFAMSSF46579. SSF46579. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKeratin_8.
GenomeRNAi3856.
NextBio15173.
PMAP-CutDBP05787.
PROP05787.
SOURCESearch...

Entry information

Entry nameK2C8_HUMAN
AccessionPrimary (citable) accession number: P05787
Secondary accession number(s): A8K4H3 expand/collapse secondary AC list , B0AZN5, F8VXB4, Q14099, Q14716, Q14717, Q53GJ0, Q6DHW5, Q6GMY0, Q6P4C7, Q96J60
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 178 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM