Keratin, type II cytoskeletal 8 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P05787 (K2C8_HUMAN)

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

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

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Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Coiled coil
PTM	Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cytoskeleton organization Non-traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	keratin filament Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Ref.15 Ref.20 Inferred from physical interaction. Source: UniProtKB structural molecule activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CLN5	O75503	1	EBI-297852,EBI-1043514
HSPA4L	O95757	1	EBI-297852,EBI-358652
KRT18	P05783	2	EBI-297852,EBI-297888
MDM2	Q00987	1	EBI-297852,EBI-389668

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 483

482

Keratin, type II cytoskeletal 8

PRO_0000063740

Regions

Region

2 – 90

Head

Region

91 – 398

308

Rod

Region

91 – 126

Coil 1A

Region

127 – 143

Linker 1

Region

144 – 235

Coil 1B

Region

236 – 259

Linker 12

Region

260 – 398

139

Coil 2

Region

261 – 382

122

Necessary for interaction with PNN

Region

399 – 483

Tail

Compositional bias

9 – 49

Ser-rich

Sites

Site

342

Stutter

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.16 Ref.26

Modified residue

Phosphoserine Ref.16

Modified residue

Phosphoserine Ref.16 Ref.26 Ref.4 Ref.24

Modified residue

Phosphothreonine Ref.24

Modified residue

Phosphoserine Ref.26 Ref.21

Modified residue

Phosphoserine Ref.26

Modified residue

Phosphoserine Ref.26

Modified residue

Phosphoserine Ref.16 Ref.26 Ref.25

Modified residue

Phosphoserine Ref.16 Ref.26 Ref.25

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by MAPK Ref.25 Ref.13 Ref.14

Modified residue

204

Phosphotyrosine Ref.23

Modified residue

251

Phosphoserine Ref.26

Modified residue

253

Phosphoserine Ref.26 Ref.25 Ref.19

Modified residue

258

Phosphoserine Ref.26 Ref.25

Modified residue

267

Phosphotyrosine Ref.23

Modified residue

274

Phosphoserine Ref.26 Ref.25

Modified residue

330

Phosphoserine Ref.26 Ref.19

Modified residue

400

Phosphoserine Ref.26

Modified residue

410

Phosphoserine Ref.26

Modified residue

417

Phosphoserine By similarity

Modified residue

424

Phosphoserine By similarity

Modified residue

432

Phosphoserine; by CaMK2 and MAPK Ref.26 Ref.4

Modified residue

451

Phosphoserine Ref.22

Modified residue

475

Phosphoserine Ref.26

Modified residue

478

Phosphoserine Ref.26

Natural variations

Natural variant

G → V in cryptogenic cirrhosis. Ref.28

VAR_023058

Natural variant

Y → C in cryptogenic cirrhosis. Ref.28

VAR_023059

Natural variant

G → C in cryptogenic cirrhosis. Ref.28 Ref.6

VAR_023060

Natural variant

I → V Ref.28

VAR_023061

Natural variant

401

R → W: dbSNP rs2277330.

VAR_049805

Experimental info

Mutagenesis

L → P: Increases phosphorylation. Ref.14

Mutagenesis

S → A: Generates normal-appearing filaments, that remain stable after okadaic acid treatment. Ref.14

Mutagenesis

S → D: Generates normal-appearing filaments, that are destabilized by okadaic acid. Ref.14

Sequence conflict

V → S in AAA35748. Ref.2

Sequence conflict

201

D → DVD in CAA52882. Ref.3

Sequence conflict

232

I → L in CAA67203. Ref.8

Sequence conflict

257

D → E in AAA35748. Ref.2

Sequence conflict

324

L → F in BAD96661. Ref.5

Sequence conflict

384

L → M in CAA67203. Ref.8

Sequence conflict

387

E → D in AAA35748. Ref.2

Sequence conflict

401

R → P in AAA35748. Ref.2

Sequence conflict

417

S → G in AAA35763. Ref.1

Sequence conflict

417

S → G in AAA35748. Ref.2

Sequence conflict

417

S → G in CAA67203. Ref.8

Sequence conflict

417

S → G Ref.9

Sequence conflict

429

G → D in AAA35748. Ref.2

Sequence conflict

429

G → D Ref.8

Sequence conflict

430 – 433

LTSP → SQA in AAA35763. Ref.1

Sequence conflict

431

T → A in CAA67203. Ref.8

Sequence conflict

432

S → D in AAA35748. Ref.2

Sequence conflict

432

S → D in CAA67203. Ref.8

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Sequences

Sequence

Length

Mass (Da)

Tools

P05787-1 [UniParc].

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

483

53,704

        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

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References

	« Hide 'large scale' referencesShow '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. 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.

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Web resources

Human Intermediate Filament Mutation Database

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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.
IPI	IPI00554648.
PIR	A34720.
RefSeq	NP_002264.1.
UniGene	Hs.533782 Hs.708445
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:424N.
IntAct	P05787. 12 interactions.
PTM databases
GlycoSuiteDB	P05787.
PhosphoSite	P05787.
2-D gel databases
SWISS-2DPAGE	P05787.
Siena-2DPAGE	P05787.
Proteomic databases
PeptideAtlas	P05787.
PRIDE	P05787.
Genome annotation databases
Ensembl	ENSG00000170421. Homo sapiens. [Contig view]
GeneID	3856.
KEGG	hsa:3856.
Organism-specific databases
GeneCards	GC12M051577.
H-InvDB	HIX0010658. HIX0035240.
HGNC	HGNC:6446. KRT8.
HPA	CAB000131. CAB001696.
MIM	148060. gene. 215600. phenotype.
PharmGKB	PA30234.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P05787.
OMA	P05787. DEINFYR.
Enzyme and pathway databases
Pathway_Interaction_DB	p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.
Gene expression databases
ArrayExpress	P05787.
Bgee	P05787.
GermOnline	ENSG00000170421. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR003054. Keratin_II. [Graphical view]
PANTHER	PTHR23239. IF. 1 hit. PTHR23239:SF18. Keratin_II. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01276. TYPE2KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
NextBio	15173.
PMAP-CutDB	P05787.
SOURCE	Search...

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Entry information

Entry name

K2C8_HUMAN

Accession

Primary (citable) accession number: P05787
Secondary accession number(s): Q14099

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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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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

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents