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Protein

Keratin, type II cytoskeletal 8

Gene

Krt8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

  • protein complex binding Source: RGD
  • structural molecule activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type II cytoskeletal 8
Alternative name(s):
Cytokeratin endo A
Cytokeratin-8
Short name:
CK-8
Keratin-8
Short name:
K8
Type-II keratin Kb8
Gene namesi
Name:Krt8
Synonyms:Krt2-8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi2984. Krt8.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • costamere Source: RGD
  • dystrophin-associated glycoprotein complex Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • keratin filament Source: RGD
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB-SubCell
  • sarcolemma Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 483483Keratin, type II cytoskeletal 8PRO_0000063742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by PKC/PRKCE1 Publication
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei24 – 241Phosphoserine; by PKC/PRKCE1 Publication
Modified residuei26 – 261PhosphothreonineCombined sources
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei43 – 431PhosphoserineCombined sources1 Publication
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei51 – 511PhosphoserineCombined sources1 Publication
Modified residuei101 – 1011N6-malonyllysineBy similarity
Modified residuei207 – 2071N6-acetyllysineBy similarity
Modified residuei253 – 2531PhosphoserineCombined sources
Modified residuei258 – 2581PhosphoserineCombined sources
Modified residuei274 – 2741PhosphoserineBy similarity
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei295 – 2951N6-acetyllysineBy similarity
Cross-linki304 – 304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei325 – 3251N6-acetyllysineBy similarity
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei410 – 4101PhosphoserineBy similarity
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei424 – 4241Phosphoserine1 Publication
Modified residuei426 – 4261Phosphoserine1 Publication
Modified residuei432 – 4321PhosphoserineCombined sources
Cross-linki472 – 472Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei475 – 4751PhosphoserineCombined sources
Modified residuei478 – 4781PhosphoserineCombined sources
Modified residuei482 – 4821PhosphoserineCombined sources

Post-translational modificationi

O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity).By similarity
O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ10758.
PRIDEiQ10758.

PTM databases

iPTMnetiQ10758.
PhosphoSiteiQ10758.

Expressioni

Tissue specificityi

Expressed in cardiac and striated muscle. Expressed at Z-lines within the muscle fibers and at Z-line and M-line domains at costameres at the sarcolemmal membrane (at protein level). Observed in coagulating gland, bladder, salivary gland, kidney, spleen, thymus, lung and heart. Also observed in ventral prostate, seminal vesicle and liver where expression increases following castration.2 Publications

Gene expression databases

GenevisibleiQ10758. RN.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. KRT8 associates with KRT18. Associates with KRT20. Interacts with PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Interacts with APEX1 (By similarity). Interacts with GPER1 (By similarity).By similarity

GO - Molecular functioni

  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi247655. 1 interaction.
IntActiQ10758. 3 interactions.
MINTiMINT-4596966.
STRINGi10116.ENSRNOP00000029068.

Structurei

3D structure databases

ProteinModelPortaliQ10758.
SMRiQ10758. Positions 89-126.
ModBaseiSearch...
MobiDBiSearch...

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 PNNBy similarityAdd
BLAST
Regioni399 – 48385TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 5143Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ10758.
KOiK07605.
OMAiXRASLEA.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ10758.
TreeFamiTF317854.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRVTQKSY KMSTSGPRAF SSRSFTSGPG ARISSSSFSR VGSSSSSFRG
60 70 80 90 100
SLGGFGGAGV GGITAVTVNQ SLLNPLKLEV DPNIQAVRTQ EKEQIKTLNN
110 120 130 140 150
KFASFIDKVR FLEQQNKMLE TKWSLLQQQK TSRSNMDNMF ESYINNLRRQ
160 170 180 190 200
LEALGQEKLK LEVELGNMQG LVEDFKNKYE DEINKRTEME NEFVLIKKDV
210 220 230 240 250
DEAYMNKVEL ESRLEGLTDE INFLRQIHEE EIRELQSQIS DTSVVLSMDN
260 270 280 290 300
SRSLDMDSII AEVRAQYEEI ANRSRAEAET MYQIKYEELQ TLAGKHGDDL
310 320 330 340 350
RRSKTEISEM NRNISRLQAE IDALKGQRAT LEAAIADAEQ RGELAVKDAN
360 370 380 390 400
AKLEDLKNAL QKAKQDMARQ LREYQELMNV KLALDIEIAT YRKLLEGEES
410 420 430 440 450
RLESGMQNMS IHTKTTSGYA GGLSSSYGGL TSPGFSYGMS SFQPGFGSVG
460 470 480
GSSTYSRTKA VVVKKIETRD GKLVSESSDI MSK
Length:483
Mass (Da):54,019
Last modified:January 23, 2007 - v3
Checksum:iF52521FFFD972C2A
GO

Sequence cautioni

The sequence AAA19668.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63482 mRNA. Translation: AAA19667.1.
M63482 mRNA. Translation: AAA19668.1. Different initiation.
S76054 mRNA. No translation available.
AY464139 mRNA. Translation: AAR36875.1.
BC091106 mRNA. Translation: AAH91106.1.
BC097497 mRNA. Translation: AAH97497.1.
RefSeqiNP_955402.1. NM_199370.1.
UniGeneiRn.11083.

Genome annotation databases

EnsembliENSRNOT00000038480; ENSRNOP00000029068; ENSRNOG00000009779.
GeneIDi25626.
KEGGirno:25626.
UCSCiRGD:2984. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63482 mRNA. Translation: AAA19667.1.
M63482 mRNA. Translation: AAA19668.1. Different initiation.
S76054 mRNA. No translation available.
AY464139 mRNA. Translation: AAR36875.1.
BC091106 mRNA. Translation: AAH91106.1.
BC097497 mRNA. Translation: AAH97497.1.
RefSeqiNP_955402.1. NM_199370.1.
UniGeneiRn.11083.

3D structure databases

ProteinModelPortaliQ10758.
SMRiQ10758. Positions 89-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247655. 1 interaction.
IntActiQ10758. 3 interactions.
MINTiMINT-4596966.
STRINGi10116.ENSRNOP00000029068.

PTM databases

iPTMnetiQ10758.
PhosphoSiteiQ10758.

Proteomic databases

PaxDbiQ10758.
PRIDEiQ10758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000038480; ENSRNOP00000029068; ENSRNOG00000009779.
GeneIDi25626.
KEGGirno:25626.
UCSCiRGD:2984. rat.

Organism-specific databases

CTDi3856.
RGDi2984. Krt8.

Phylogenomic databases

eggNOGiENOG410IG4R. Eukaryota.
ENOG410YY6B. LUCA.
GeneTreeiENSGT00760000118796.
HOGENOMiHOG000230976.
HOVERGENiHBG013015.
InParanoidiQ10758.
KOiK07605.
OMAiXRASLEA.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ10758.
TreeFamiTF317854.

Miscellaneous databases

PROiQ10758.

Gene expression databases

GenevisibleiQ10758. RN.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR032444. Keratin_2_head.
IPR003054. Keratin_II.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 2 hits.
PfamiPF00038. Filament. 1 hit.
PF16208. Keratin_2_head. 1 hit.
[Graphical view]
PRINTSiPR01276. TYPE2KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of basal and luminal cell-specific cytokeratin expression in rat accessory sex organs. Evidence for a new class of androgen-repressed genes and insight into their pairwise control."
    Hsieh J.-T., Zhau H.E., Wang X.-H., Liew C.-C., Chung L.W.K.
    J. Biol. Chem. 267:2303-2310(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Prostate.
  2. "Cloning and characterization of a specific cytokeratin-8 cDNA from rat prostatic epithelium."
    Wang X., Hsieh J.-T., Zhau H.E.
    Zhongguo Yi Xue Ke Xue Yuan Xue Bao 16:1-7(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Prostate.
  3. "Cloning and characterization of cytokeratins 8 and 19 in adult rat striated muscle. Interaction with the dystrophin glycoprotein complex."
    Ursitti J.A., Lee P.C., Resneck W.G., McNally M.M., Bowman A.L., O'Neill A., Stone M.R., Bloch R.J.
    J. Biol. Chem. 279:41830-41838(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DMD, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Heart muscle.
  4. "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].
    Tissue: Placenta and Thymus.
  5. "Keratin 8 phosphorylation in vitro by cAMP-dependent protein kinase occurs within the amino- and carboxyl-terminal end domains."
    Ando S., Tokui T., Yano T., Inagaki M.
    Biochem. Biophys. Res. Commun. 221:67-71(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-18; 24-75 AND 415-452, PHOSPHORYLATION AT SER-9; SER-13; SER-24; SER-34; SER-37; SER-43; SER-51; SER-417; SER-424 AND SER-426.
    Tissue: Liver.
  6. "Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space."
    Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K., Watanabe Y., Furukawa K., Horigome T.
    FEBS J. 272:4327-4338(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 265-273, SUBCELLULAR LOCATION.
    Tissue: Liver.
  7. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
    Moser K., White F.M.
    J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; THR-26; SER-27; SER-43; SER-44; SER-47; SER-51; SER-253; SER-258; SER-432; SER-475; SER-478 AND SER-482, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiK2C8_RAT
AccessioniPrimary (citable) accession number: Q10758
Secondary accession number(s): Q5WPB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 133 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.