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P05787

- K2C8_HUMAN

UniProt

P05787 - K2C8_HUMAN

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Protein

Keratin, type II cytoskeletal 8

Gene
KRT8, CYK8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei342 – 3421Stutter

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. scaffold protein binding Source: BHF-UCL
  3. structural molecule activity Source: InterPro

GO - Biological processi

  1. cell differentiation involved in embryonic placenta development Source: Ensembl
  2. extrinsic apoptotic signaling pathway Source: Ensembl
  3. hepatocyte apoptotic process Source: Ensembl
  4. response to hydrostatic pressure Source: Ensembl
  5. response to other organism Source: Ensembl
  6. sarcomere organization Source: Ensembl
  7. tumor necrosis factor-mediated signaling pathway Source: Ensembl
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

SignaLinkiP05787.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KRT8
Synonyms:CYK8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:6446. KRT8.

Subcellular locationi

Cytoplasm. Nucleusnucleoplasm By similarity. Nucleus matrix By similarity 2 Publications

GO - Cellular componenti

  1. costamere Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. dystrophin-associated glycoprotein complex Source: Ensembl
  4. extracellular vesicular exosome Source: UniProt
  5. intermediate filament Source: BHF-UCL
  6. keratin filament Source: Ensembl
  7. nuclear matrix Source: UniProtKB-SubCell
  8. nucleoplasm Source: UniProtKB-SubCell
  9. nucleus Source: UniProt
  10. sarcolemma Source: Ensembl
  11. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531G → V in CIRRH. 1 Publication
Corresponds to variant rs61710484 [ dbSNP | Ensembl ].
VAR_023058
Natural varianti54 – 541Y → C in CIRRH. 1 Publication
VAR_023059
Natural varianti62 – 621G → C in CIRRH. 2 Publications
Corresponds to variant rs11554495 [ dbSNP | Ensembl ].
VAR_023060

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721L → P: Increases phosphorylation. 1 Publication
Mutagenesisi74 – 741S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. 1 Publication
Mutagenesisi74 – 741S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi215600. phenotype.
PharmGKBiPA30234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Keratin, type II cytoskeletal 8PRO_0000063740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by PKC/PRKCE1 Publication
Modified residuei13 – 131Phosphoserine By similarity
Modified residuei21 – 211Phosphoserine1 Publication
Modified residuei24 – 241Phosphoserine; by PKC/PRKCE4 Publications
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei34 – 341Phosphoserine2 Publications
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine2 Publications
Modified residuei43 – 431Phosphoserine2 Publications
Modified residuei74 – 741Phosphoserine; by MAPK2 Publications
Modified residuei101 – 1011N6-malonyllysine1 Publication
Modified residuei117 – 1171N6-acetyllysine1 Publication
Modified residuei207 – 2071N6-acetyllysine1 Publication
Modified residuei253 – 2531Phosphoserine5 Publications
Modified residuei258 – 2581Phosphoserine3 Publications
Modified residuei295 – 2951N6-acetyllysine1 Publication
Modified residuei325 – 3251N6-acetyllysine1 Publication
Modified residuei330 – 3301Phosphoserine1 Publication
Modified residuei347 – 3471N6-acetyllysine1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei410 – 4101Phosphoserine1 Publication
Modified residuei417 – 4171Phosphoserine By similarity
Modified residuei424 – 4241Phosphoserine By similarity
Modified residuei432 – 4321Phosphoserine; by CaMK2 and MAPK2 Publications
Modified residuei475 – 4751Phosphoserine2 Publications
Modified residuei478 – 4781Phosphoserine2 Publications

Post-translational modificationi

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.3 Publications
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.3 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP05787.
PaxDbiP05787.
PeptideAtlasiP05787.
PRIDEiP05787.

2D gel databases

SWISS-2DPAGEP05787.

PTM databases

PhosphoSiteiP05787.
UniCarbKBiP05787.

Miscellaneous databases

PMAP-CutDBP05787.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiP05787.
GenevestigatoriP05787.

Organism-specific databases

HPAiCAB000131.
CAB001696.
HPA049866.

Interactioni

Subunit structurei

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 GPER1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFTRP135697EBI-297852,EBI-349854
GRB2P629933EBI-297852,EBI-401755
IKBKGQ9Y6K92EBI-297852,EBI-81279
KRT18P0578310EBI-297852,EBI-297888
PKP1Q13835-23EBI-297852,EBI-9087684

Protein-protein interaction databases

BioGridi110054. 48 interactions.
DIPiDIP-424N.
IntActiP05787. 24 interactions.
MINTiMINT-256526.

Structurei

3D structure databases

ProteinModelPortaliP05787.
SMRiP05787. Positions 88-239, 303-397.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9090HeadAdd
BLAST
Regioni91 – 398308RodAdd
BLAST
Regioni91 – 12636Coil 1AAdd
BLAST
Regioni127 – 14317Linker 1Add
BLAST
Regioni144 – 23592Coil 1BAdd
BLAST
Regioni236 – 25924Linker 12Add
BLAST
Regioni260 – 398139Coil 2Add
BLAST
Regioni261 – 382122Necessary for interaction with PNNAdd
BLAST
Regioni399 – 48385TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 4941Ser-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG146769.
HOVERGENiHBG013015.
InParanoidiP05787.
KOiK07605.
OMAiXRASLEA.
OrthoDBiEOG7FV3Q8.
PhylomeDBiP05787.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P05787-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSIRVTQKSY KVSTSGPRAF SSRSYTSGPG SRISSSSFSR VGSSNFRGGL    50
GGGYGGASGM GGITAVTVNQ SLLSPLVLEV DPNIQAVRTQ EKEQIKTLNN 100
KFASFIDKVR FLEQQNKMLE TKWSLLQQQK TARSNMDNMF ESYINNLRRQ 150
LETLGQEKLK LEAELGNMQG LVEDFKNKYE DEINKRTEME NEFVLIKKDV 200
DEAYMNKVEL ESRLEGLTDE INFLRQLYEE EIRELQSQIS DTSVVLSMDN 250
SRSLDMDSII AEVKAQYEDI ANRSRAEAES MYQIKYEELQ SLAGKHGDDL 300
RRTKTEISEM NRNISRLQAE IEGLKGQRAS LEAAIADAEQ RGELAIKDAN 350
AKLSELEAAL QRAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES 400
RLESGMQNMS IHTKTTSGYA GGLSSAYGGL TSPGLSYSLG SSFGSGAGSS 450
SFSRTSSSRA VVVKKIETRD GKLVSESSDV LPK 483
Length:483
Mass (Da):53,704
Last modified:January 23, 2007 - v7
Checksum:iB0BC730B65929D37
GO
Isoform 2 (identifier: P05787-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MNGVSWSQDLQEGISAWFGPPASTPASTM

Note: No experimental confirmation available.

Show »
Length:511
Mass (Da):56,608
Checksum:iDB55C0367CD6C37C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531G → V in CIRRH. 1 Publication
Corresponds to variant rs61710484 [ dbSNP | Ensembl ].
VAR_023058
Natural varianti54 – 541Y → C in CIRRH. 1 Publication
VAR_023059
Natural varianti62 – 621G → C in CIRRH. 2 Publications
Corresponds to variant rs11554495 [ dbSNP | Ensembl ].
VAR_023060
Natural varianti63 – 631I → V.1 Publication
Corresponds to variant rs59536457 [ dbSNP | Ensembl ].
VAR_023061
Natural varianti401 – 4011R → W.
Corresponds to variant rs2277330 [ dbSNP | Ensembl ].
VAR_049805
Natural varianti417 – 4171S → G.2 Publications
Corresponds to variant rs1065591 [ dbSNP | Ensembl ].
VAR_069106
Natural varianti429 – 4291G → D.1 Publication
Corresponds to variant rs1065648 [ dbSNP | Ensembl ].
VAR_069107

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MNGVSWSQDLQEGISAWFGP PASTPASTM in isoform 2. VSP_046000

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561G → V in BAF83627. 1 Publication
Sequence conflicti77 – 771V → S in AAA35748. 1 Publication
Sequence conflicti201 – 2011D → DVD in CAA52882. 1 Publication
Sequence conflicti232 – 2321I → L in CAA67203. 1 Publication
Sequence conflicti257 – 2571D → E in AAA35748. 1 Publication
Sequence conflicti310 – 3101M → I in CAA31376. 1 Publication
Sequence conflicti324 – 3241L → F in BAD96661. 1 Publication
Sequence conflicti384 – 3841L → M in CAA67203. 1 Publication
Sequence conflicti387 – 3871E → D in AAA35748. 1 Publication
Sequence conflicti401 – 4011R → P in AAA35748. 1 Publication
Sequence conflicti430 – 4334LTSP → SQA in AAA35763. 1 Publication
Sequence conflicti431 – 4311T → A in CAA67203. 1 Publication
Sequence conflicti432 – 4321S → D in AAA35748. 1 Publication
Sequence conflicti432 – 4321S → D in CAA67203. 1 Publication
Sequence conflicti432 – 4321S → D in CAA31376. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS58234.1. [P05787-2]
CCDS8841.1. [P05787-1]
PIRiA34720.
RefSeqiNP_001243222.1. NM_001256293.1. [P05787-1]
NP_002264.1. NM_002273.3. [P05787-1]
UniGeneiHs.533782.
Hs.708445.

Genome annotation databases

EnsembliENST00000293308; ENSP00000293308; ENSG00000170421. [P05787-1]
ENST00000546897; ENSP00000447402; ENSG00000170421. [P05787-1]
ENST00000552150; ENSP00000449404; ENSG00000170421. [P05787-2]
ENST00000552551; ENSP00000447566; ENSG00000170421. [P05787-1]
GeneIDi3856.
KEGGihsa:3856.
UCSCiuc001sbd.2. human. [P05787-1]

Polymorphism databases

DMDMi90110027.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS58234.1. [P05787-2 ]
CCDS8841.1. [P05787-1 ]
PIRi A34720.
RefSeqi NP_001243222.1. NM_001256293.1. [P05787-1 ]
NP_002264.1. NM_002273.3. [P05787-1 ]
UniGenei Hs.533782.
Hs.708445.

3D structure databases

ProteinModelPortali P05787.
SMRi P05787. Positions 88-239, 303-397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110054. 48 interactions.
DIPi DIP-424N.
IntActi P05787. 24 interactions.
MINTi MINT-256526.

Chemistry

DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei P05787.
UniCarbKBi P05787.

Polymorphism databases

DMDMi 90110027.

2D gel databases

SWISS-2DPAGE P05787.

Proteomic databases

MaxQBi P05787.
PaxDbi P05787.
PeptideAtlasi P05787.
PRIDEi P05787.

Protocols and materials databases

DNASUi 3856.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293308 ; ENSP00000293308 ; ENSG00000170421 . [P05787-1 ]
ENST00000546897 ; ENSP00000447402 ; ENSG00000170421 . [P05787-1 ]
ENST00000552150 ; ENSP00000449404 ; ENSG00000170421 . [P05787-2 ]
ENST00000552551 ; ENSP00000447566 ; ENSG00000170421 . [P05787-1 ]
GeneIDi 3856.
KEGGi hsa:3856.
UCSCi uc001sbd.2. human. [P05787-1 ]

Organism-specific databases

CTDi 3856.
GeneCardsi GC12M053290.
H-InvDB HIX0026255.
HIX0034365.
HIX0168895.
HGNCi HGNC:6446. KRT8.
HPAi CAB000131.
CAB001696.
HPA049866.
MIMi 148060. gene.
215600. phenotype.
neXtProti NX_P05787.
PharmGKBi PA30234.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG146769.
HOVERGENi HBG013015.
InParanoidi P05787.
KOi K07605.
OMAi XRASLEA.
OrthoDBi EOG7FV3Q8.
PhylomeDBi P05787.
TreeFami TF317854.

Enzyme and pathway databases

SignaLinki P05787.

Miscellaneous databases

GeneWikii Keratin_8.
GenomeRNAii 3856.
NextBioi 15173.
PMAP-CutDB P05787.
PROi P05787.
SOURCEi Search...

Gene expression databases

Bgeei P05787.
Genevestigatori P05787.

Family and domain databases

InterProi IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
IPR009053. Prefoldin.
[Graphical view ]
PANTHERi PTHR23239. PTHR23239. 1 hit.
Pfami PF00038. Filament. 1 hit.
[Graphical view ]
PRINTSi PR01276. TYPE2KERATIN.
SUPFAMi SSF46579. SSF46579. 1 hit.
PROSITEi PS00226. IF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. 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.

Entry informationi

Entry nameiK2C8_HUMAN
AccessioniPrimary (citable) accession number: P05787
Secondary accession number(s): A8K4H3
, B0AZN5, F8VXB4, Q14099, Q14716, Q14717, Q53GJ0, Q6DHW5, Q6GMY0, Q6P4C7, Q96J60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 179 of the entry and version 7 of the sequence. [Complete history]
Entry statusiReviewed (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.

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. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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