Ataxin-3 - Homo sapiens (Human)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Ataxin-3
EC=3.4.19.12

Alternative name(s):
Machado-Joseph disease protein 1
Spinocerebellar ataxia type 3 protein

Gene names

Name:	ATXN3
Synonyms:	ATX3, MJD, MJD1, SCA3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates. Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins. Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. In response to misfolded substrate ubiquitination, mediates deubiquitination of monoubiquitinated STUB1/CHIP. Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription. Ref.9 Ref.10 Ref.14
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Ref.10
Subunit structure	Interacts with STUB1/CHIP (when monoubiquitinated) By similarity. Interacts with DNA repair proteins RAD23A and RAD23B.
Subcellular location	Nucleus matrix. Note: Predominantly nuclear, but not exclusively, inner nuclear matrix. Ref.8
Tissue specificity	Ubiquitous.
Domain	The UIM domains bind ubiquitin and interact with various E3 ubiquitin-protein ligase, such as STUB1/CHIP. They are essential to limit the length of ubiquitin chains By similarity.
Post-translational modification	Monoubiquitinated by UBE2W, possibly leading to activate the deubiquitinating enzyme activity By similarity.
Polymorphism	The poly-Gln region of ATXN3 is highly polymorphic (14 to 41 repeats) in the normal population and is expanded to about 55-82 repeats in spinocerebellar ataxia 3 (SCA3) patients. The MJD1a allele carries a single nucleotide substitution in codon 349 generating a stop codon instead of a Tyr. In the Japanese population, the MJD1a allele seems to be significantly associated with Gln expansion.
Involvement in disease	Spinocerebellar ataxia 3 (SCA3) [MIM:109150]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to cerebellum degeneration with variable involvement of the brainstem and spinal cord. SCA3 belongs to the autosomal dominant cerebellar ataxias type I (ADCA I) which are characterized by cerebellar ataxia in combination with additional clinical features like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs, peripheral neuropathy and dementia. The molecular defect in SCA3 is the a CAG repeat expansion in ATX3 coding region. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1
Sequence similarities	Contains 1 Josephin domain. Contains 3 UIM (ubiquitin-interacting motif) repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Neurodegeneration Spinocerebellar ataxia
Domain	Repeat
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from mutant phenotype PubMed 20637808. Source: MGI cell death Inferred from electronic annotation. Source: UniProtKB-KW cellular response to heat Inferred from electronic annotation. Source: Compara cellular response to misfolded protein Inferred from sequence or structural similarity. Source: UniProtKB exploration behavior Inferred from electronic annotation. Source: Compara histone H3 deacetylation Inferred from electronic annotation. Source: Compara intermediate filament cytoskeleton organization Inferred from mutant phenotype PubMed 20637808. Source: MGI microtubule cytoskeleton organization Inferred from mutant phenotype PubMed 20637808. Source: MGI misfolded or incompletely synthesized protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB monoubiquitinated protein deubiquitination Inferred from sequence or structural similarity. Source: UniProtKB nervous system development Traceable author statement PubMed 9124802. Source: ProtInc nucleotide-excision repair Traceable author statement PubMed 10915768. Source: ProtInc proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell-substrate adhesion Inferred from mutant phenotype PubMed 20637808. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission Traceable author statement PubMed 7655453. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Traceable author statement PubMed 9124802. Source: ProtInc mitochondrial matrix Inferred from electronic annotation. Source: Compara mitochondrial membrane Inferred from electronic annotation. Source: Compara nuclear inclusion body Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement Ref.8. Source: ProtInc
Molecular_function	RNA polymerase II regulatory region DNA binding Inferred from electronic annotation. Source: Compara omega peptidase activity Inferred from electronic annotation. Source: InterPro ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin thiolesterase activity Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-specific protease activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C16orf70	Q9BSU1	2	EBI-946046,EBI-946080
VCP	P55072	10	EBI-946068,EBI-355164

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P54252-1) 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: P54252-2) The sequence of this isoform differs from the canonical sequence as follows: 332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK

Isoform 3 (identifier: P54252-3) The sequence of this isoform differs from the canonical sequence as follows: 10-64: Missing. 332-364: KACSPFIMFATFTLYLTYELHVIFALHYSSFPL → DAMSEEDMLQAAVTMSLETVRNDLKTEGKK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

Ataxin-3

PRO_0000053831

Regions

Domain

1 – 180

180

Josephin

Repeat

224 – 243

20

UIM 1

Repeat

244 – 263

20

UIM 2

Repeat

331 – 348

18

UIM 3

Compositional bias

292 – 305

14

Poly-Gln

Sites

Active site

14

1

Nucleophile

Active site

119

1

Proton acceptor Probable

Active site

134

1

Probable

Amino acid modifications

Modified residue

219

1

Phosphoserine By similarity

Natural variations

Alternative sequence

10 – 64

55

Missing in isoform 3.

VSP_002783

Alternative sequence

332 – 364

33

KACSP…SSFPL → DAMSEEDMLQAAVTMSLETV RNDLKTEGKK in isoform 2 and isoform 3.

VSP_002784

Natural variant

212

1

V → M. Ref.1 Ref.2 Ref.4
Corresponds to variant rs1048755 [ dbSNP | Ensembl ].

VAR_013688

Natural variant

306

1

G → QQQQQQQQQQQQR.

VAR_013689

Natural variant

349 – 364

16

Missing in allele MJD1a.

VAR_013690

Experimental info

Mutagenesis

14

1

C → A: Loss of ubiquitinated protein retention. Ref.14

Mutagenesis

236

1

S → A: Inhibits substrate trapping. Ref.14

Mutagenesis

256

1

S → A: Inhibits substrate trapping. Ref.14

Mutagenesis

335

1

S → A: No effect on ubiquitination. Ref.14

Sequence conflict

252

1

A → T in AAB63352. Ref.2

Sequence conflict

252

1

A → T in AAB63353. Ref.2

Sequence conflict

252

1

A → T in AAB63354. Ref.2

Secondary structure

1

.

364

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified March 2, 2010. Version 4. Checksum: 4B2477EB67C30EFF Show »	FASTA	364	41,781
10 20 30 40 50 60 MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT 70 80 90 100 110 120 FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLRIDPINER SFICNYKEHW 130 140 150 160 170 180 FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM 190 200 210 220 230 240 IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI 250 260 270 280 290 300 DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ 310 320 330 340 350 360 QQQQQGDLSG QSSHPCERPA TSSGALGSDL GKACSPFIMF ATFTLYLTYE LHVIFALHYS SFPL « Hide
Isoform 2 [UniParc]. Checksum: 90C3EF73BB26CAFD Show »	FASTA	361	41,250
10 20 30 40 50 60 MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT 70 80 90 100 110 120 FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLRIDPINER SFICNYKEHW 130 140 150 160 170 180 FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM 190 200 210 220 230 240 IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI 250 260 270 280 290 300 DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ 310 320 330 340 350 360 QQQQQGDLSG QSSHPCERPA TSSGALGSDL GDAMSEEDML QAAVTMSLET VRNDLKTEGK K « Hide
Isoform 3 [UniParc]. Checksum: D2103044A948A525 Show »	FASTA	306	35,006
10 20 30 40 50 60 MESIFHEKQP SGNMDDSGFF SIQVISNALK VWGLELILFN SPEYQRLRID PINERSFICN 70 80 90 100 110 120 YKEHWFTVRK LGKQWFNLNS LLTGPELISD TYLALFLAQL QQEGYSIFVV KGDLPDCEAD 130 140 150 160 170 180 QLLQMIRVQQ MHRPKLIGEE LAQLKEQRVH KTDLERVLEA NDGSGMLDED EEDLQRALAL 190 200 210 220 230 240 SRQEIDMEDE EADLRRAIQL SMQGSSRNIS QDMTQTSGTN LTSEELRKRR EAYFEKQQQK 250 260 270 280 290 300 QQQQQQQQQQ GDLSGQSSHP CERPATSSGA LGSDLGDAMS EEDMLQAAVT MSLETVRNDL KTEGKK « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1." Kawaguchi Y., Okamoto T., Taniwaki M., Aizawa M., Inoue M., Katayama S., Kawakami H., Nakamura S., Nishimura M., Akiguchi I., Kimura J., Narumiya S., Kakizuka A. Nat. Genet. 8:221-228(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-212; GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG AND 349-TYR--LEU-364 DEL, INVOLVEMENT IN SCA3. Tissue: Brain.
[2]	"Machado-Joseph disease gene products carrying different carboxyl termini." Goto J., Watanabe M., Ichikawa Y., Yee S.-B., Ihara N., Endo K., Igarashi S., Takiyama Y., Gaspar C., Maciel P., Tsuji S., Rouleau G.A., Kanazawa I. Neurosci. Res. 28:373-377(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS MET-212; GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG AND 349-TYR--LEU-364 DEL.
[3]	"The genomic structure and expression of MJD, the Machado-Joseph disease gene." Ichikawa Y., Goto J., Hattori M., Toyoda A., Ishii K., Jeong S.-Y., Hashida H., Masuda N., Ogata K., Kasai F., Hirai M., Maciel P., Rouleau G.A., Sakaki Y., Kanazawa I. J. Hum. Genet. 46:413-422(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), VARIANT 349-TYR--LEU-364 DEL.
[4]	NIEHS SNPs program Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-212.
[5]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 2), VARIANT GLY-306 DELINS GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-GLN-ARG. Tissue: Mammary gland.
[8]	"Ataxin-3 is transported into the nucleus and associates with the nuclear matrix." Tait D., Riccio M., Sittler A., Scherzinger E., Santi S., Ognibene A., Maraldi N.M., Lehrach H., Wanker E.E. Hum. Mol. Genet. 7:991-997(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities." Li F., Macfarlan T., Pittman R.N., Chakravarti D. J. Biol. Chem. 277:45004-45012(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes." Tzvetkov N., Breuer P. Biol. Chem. 388:973-978(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION.
[11]	"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].
[12]	"Structural modeling of ataxin-3 reveals distant homology to adaptins." Albrecht M., Hoffmann D., Evert B.O., Schmitt I., Wuellner U., Lengauer T. Proteins 50:355-370(2003) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[13]	"The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition." Nicastro G., Menon R.P., Masino L., Knowles P.P., McDonald N.Q., Pastore A. Proc. Natl. Acad. Sci. U.S.A. 102:10493-10498(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-182.
[14]	"Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain." Mao Y., Senic-Matuglia F., Di Fiore P.P., Polo S., Hodsdon M.E., De Camilli P. Proc. Natl. Acad. Sci. U.S.A. 102:12700-12705(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-185, FUNCTION, MUTAGENESIS OF CYS-14; SER-236; SER-256 AND SER-335.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S75313 mRNA. Translation: AAB33571.1.
U64820 mRNA. Translation: AAB63352.1.
U64821 mRNA. Translation: AAB63353.1.
U64822 mRNA. Translation: AAB63354.1.
AB050194 mRNA. Translation: BAB18798.1.
AB038653 Genomic DNA. Translation: BAB55645.1.
AB038653 Genomic DNA. Translation: BAB55646.1.
EU009923 Genomic DNA. Translation: ABS29269.1.
AL049872 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81472.1.
BC033711 mRNA. Translation: AAH33711.1.

IPI

IPI00219863.
IPI00219864.
IPI00979068.

PIR

S50830.

RefSeq

NP_001121168.1. NM_001127696.1.
NP_004984.2. NM_004993.5.
NP_109376.1. NM_030660.4.

UniGene

Hs.532632.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZB	NMR	-	A	1-182	[»]
2AGA	NMR	-	A	1-185	[»]
2DOS	NMR	-	A	1-171	[»]
2JRI	NMR	-	A	1-182	[»]
2KLZ	NMR	-	A	222-263	[»]

ProteinModelPortal

P54252.

SMR

P54252. Positions 1-185, 220-264.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54252. 14 interactions.

MINT

MINT-272839.

Protein family/group databases

MEROPS

C86.001.

PTM databases

PhosphoSite

P54252.

Polymorphism databases

DMDM

290457685.

Proteomic databases

PaxDb

P54252.

PRIDE

P54252.

Protocols and materials databases

DNASU

4287.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340660; ENSP00000339110; ENSG00000066427.
ENST00000393287; ENSP00000376965; ENSG00000066427.
ENST00000532032; ENSP00000437157; ENSG00000066427.

GeneID

4287.

KEGG

hsa:4287.

UCSC

uc001yac.4. human.
uc001yad.4. human.
uc021rzo.1. human.

Organism-specific databases

CTD

4287.

GeneCards

GC14M092524.

HGNC

HGNC:7106. ATXN3.

HPA

CAB021976.
HPA024123.

MIM

109150. phenotype.
607047. gene.

neXtProt

NX_P54252.

Orphanet

276238. Machado-Joseph disease type 1.
276241. Machado-Joseph disease type 2.
276244. Machado-Joseph disease type 3.

PharmGKB

PA134971833.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327234.

HOVERGEN

HBG025648.

KO

K11863.

Gene expression databases

ArrayExpress

P54252.

Bgee

P54252.

Genevestigator

P54252.

Family and domain databases

InterPro

IPR006155. Josephin.
IPR003903. Ubiquitin-int_motif.
[Graphical view]

Pfam

PF02099. Josephin. 1 hit.
PF02809. UIM. 2 hits.
[Graphical view]

PRINTS

PR01233. JOSEPHIN.

SMART

SM00726. UIM. 2 hits.
[Graphical view]

PROSITE

PS50957. JOSEPHIN. 1 hit.
PS50330. UIM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P54252.

GenomeRNAi

4287.

NextBio

16875.

PMAP-CutDB

A7LFZ5.

SOURCE

Search...

Entry information

Entry name

ATX3_HUMAN

Accession

Primary (citable) accession number: P54252
Secondary accession number(s): A7LFZ5

Q9H3N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 2, 2010
Last modified:	May 1, 2013
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 14

Human chromosome 14: 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents