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Reviewed, UniProtKB/Swiss-Prot P05787 (K2C8_HUMAN)

Last modified June 16, 2009. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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
Gene names
Name: KRT8
Synonyms: CYK8
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.17

Subunit structure

Heterotetramer of two type I and two type II keratins. keratin-8 associates with keratin-18. Associates with KRT20. Interacts with HCV core protein and PNN. When associated with KRT19, interacts with DMD. Interacts with TCHP. Ref.17 Ref.11 Ref.12 Ref.15 Ref.18 Ref.20

Subcellular location

Cytoplasm. Ref.11

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.17 Ref.11

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 at multiple sites; glycans consist of single N-acetylglucosamine residues. Ref.10

Involvement in disease

Defects in KRT8 are a cause of cryptogenic cirrhosis [MIM:215600]. Ref.28

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
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainCoiled coil
   PTMGlycoprotein
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcytoskeleton organization

Non-traceable author statement. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentkeratin filament

Inferred from electronic annotation. Source: InterPro

   Molecular functionprotein binding Ref.15 Ref.20

Inferred from physical interaction. Source: UniProtKB

structural molecule activity

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 483482Keratin, type II cytoskeletal 8
PRO_0000063740

Regions

Region2 – 9089Head
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 similarity
Modified residue131Phosphoserine By similarity
Modified residue211Phosphoserine Ref.16 Ref.26
Modified residue221Phosphoserine Ref.16
Modified residue241Phosphoserine Ref.16 Ref.26 Ref.4 Ref.24
Modified residue261Phosphothreonine Ref.24
Modified residue271Phosphoserine Ref.26 Ref.21
Modified residue341Phosphoserine Ref.26
Modified residue361Phosphoserine Ref.26
Modified residue371Phosphoserine Ref.16 Ref.26 Ref.25
Modified residue431Phosphoserine Ref.16 Ref.26 Ref.25
Modified residue441Phosphoserine By similarity
Modified residue741Phosphoserine; by MAPK Ref.25 Ref.13 Ref.14
Modified residue2041Phosphotyrosine Ref.23
Modified residue2511Phosphoserine Ref.26
Modified residue2531Phosphoserine Ref.26 Ref.25 Ref.19
Modified residue2581Phosphoserine Ref.26 Ref.25
Modified residue2671Phosphotyrosine Ref.23
Modified residue2741Phosphoserine Ref.26 Ref.25
Modified residue3301Phosphoserine Ref.26 Ref.19
Modified residue4001Phosphoserine Ref.26
Modified residue4101Phosphoserine Ref.26
Modified residue4171Phosphoserine By similarity
Modified residue4241Phosphoserine By similarity
Modified residue4321Phosphoserine; by CaMK2 and MAPK Ref.26 Ref.4
Modified residue4511Phosphoserine Ref.22
Modified residue4751Phosphoserine Ref.26
Modified residue4781Phosphoserine Ref.26

Natural variations

Natural variant531G → V in cryptogenic cirrhosis. Ref.28
VAR_023058
Natural variant541Y → C in cryptogenic cirrhosis. Ref.28
VAR_023059
Natural variant621G → C in cryptogenic cirrhosis. Ref.28 Ref.6
VAR_023060
Natural variant631I → V Ref.28
VAR_023061
Natural variant4011R → W: dbSNP rs2277330.
VAR_049805

Experimental info

Mutagenesis721L → P: Increases phosphorylation. Ref.14
Mutagenesis741S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. Ref.14
Mutagenesis741S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. Ref.14
Sequence conflict771V → S in AAA35748. Ref.2
Sequence conflict2011D → DVD in CAA52882. Ref.3
Sequence conflict2321I → L in CAA67203. Ref.8
Sequence conflict2571D → E in AAA35748. Ref.2
Sequence conflict3241L → F in BAD96661. Ref.5
Sequence conflict3841L → M in CAA67203. Ref.8
Sequence conflict3871E → D in AAA35748. Ref.2
Sequence conflict4011R → P in AAA35748. Ref.2
Sequence conflict4171S → G in AAA35763. Ref.1
Sequence conflict4171S → G in AAA35748. Ref.2
Sequence conflict4171S → G in CAA67203. Ref.8
Sequence conflict4171S → G Ref.9
Sequence conflict4291G → D in AAA35748. Ref.2
Sequence conflict4291G → D Ref.8
Sequence conflict430 – 4334LTSP → SQA in AAA35763. Ref.1
Sequence conflict4311T → A in CAA67203. Ref.8
Sequence conflict4321S → D in AAA35748. Ref.2
Sequence conflict4321S → D in CAA67203. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P05787-1 [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

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: 1691124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 1692965] [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: 1705144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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: 9054461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-24 AND SER-432.
[5]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].
Tissue: Kidney.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-62.
Tissue: Colon, Liver, Lung and Placenta.
[7]"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: 2471065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-231.
[8]"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: 2434381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 205-483.
[9]"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: 9150948] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Colon carcinoma.
[10]"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: 1371281] [Abstract]
Cited for: GLYCOSYLATION.
[11]"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: 10973561] [Abstract]
Cited for: INTERACTION WITH KRT20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"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: 10809736] [Abstract]
Cited for: INTERACTION WITH PNN.
[13]"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: 11781324] [Abstract]
Cited for: PHOSPHORYLATION AT SER-74.
[14]"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: 11788583] [Abstract]
Cited for: PHOSPHORYLATION AT SER-74, MUTAGENESIS OF LEU-72 AND SER-74.
[15]"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: 15731013] [Abstract]
Cited for: INTERACTION WITH TCHP.
[16]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-22; SER-24; SER-37 AND SER-43, MASS SPECTROMETRY.
[17]"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: 16000376] [Abstract]
Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
[18]"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: 15846844] [Abstract]
Cited for: INTERACTION WITH HCV CORE PROTEIN.
[19]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND SER-330, MASS SPECTROMETRY.
Tissue: Epithelium.
[20]"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: 16608857] [Abstract]
Cited for: INTERACTION WITH KRT20.
[21]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY.
Tissue: Epithelium.
[22]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, MASS SPECTROMETRY.
Tissue: Epithelium.
[23]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204 AND TYR-267, MASS SPECTROMETRY.
[24]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND THR-26, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-43; SER-74; SER-253; SER-258 AND SER-274, MASS SPECTROMETRY.
[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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-27; SER-34; SER-36; SER-37; SER-43; SER-251; SER-253; SER-258; SER-274; SER-330; SER-400; SER-410; SER-432; SER-475 AND SER-478, MASS SPECTROMETRY.
[27]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[28]"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: 12724528] [Abstract]
Cited for: VARIANTS CRYPTOGENIC CIRRHOSIS VAL-53; CYS-54 AND CYS-62, VARIANT VAL-63.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
AK222941 mRNA. Translation: BAD96661.1.
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.
IPIIPI00554648.
PIRA34720.
RefSeqNP_002264.1.
UniGeneHs.533782
Hs.708445

3D structure databases

HSSPHSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:424N.
IntActP05787. 12 interactions.

PTM databases

GlycoSuiteDBP05787.
PhosphoSiteP05787.

2-D gel databases

SWISS-2DPAGEP05787.
Siena-2DPAGEP05787.

Proteomic databases

PeptideAtlasP05787.
PRIDEP05787.

Genome annotation databases

EnsemblENSG00000170421. Homo sapiens. [Contig view]
GeneID3856.
KEGGhsa:3856.

Organism-specific databases

GeneCardsGC12M051577.
H-InvDBHIX0010658.
HIX0035240.
HGNCHGNC:6446. KRT8.
HPACAB000131.
CAB001696.
MIM148060. gene.
215600. phenotype.
PharmGKBPA30234.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP05787.
OMAP05787. DEINFYR.

Enzyme and pathway databases

Pathway_Interaction_DBp38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Gene expression databases

ArrayExpressP05787.
BgeeP05787.
GermOnlineENSG00000170421. Homo sapiens.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR003054. Keratin_II.
[Graphical view]
PANTHERPTHR23239. IF. 1 hit.
PTHR23239:SF18. Keratin_II. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01276. TYPE2KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.
NextBio15173.
PMAP-CutDBP05787.
SOURCESearch...

Entry information

Entry nameK2C8_HUMAN
AccessionPrimary (citable) accession number: P05787
Secondary accession number(s): Q14099 expand/collapse secondary AC list , 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: June 16, 2009
This is version 121 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents