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Entry version 159 (07 Apr 2021)
Sequence version 3 (01 Nov 1997)
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Protein

Acetyl esterase

Gene

aes

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity.3 Publications

Miscellaneous

Not essential for cell growth.

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius)1 Publication
  2. KM=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees Celsius)1 Publication
  3. KM=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees Celsius)1 Publication
  4. KM=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees Celsius)1 Publication
  5. KM=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees Celsius)1 Publication
  6. KM=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees Celsius)1 Publication
  1. Vmax=34.2 µmol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6 and 30 degrees Celsius)1 Publication
  2. Vmax=3.67 µmol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and 30 degrees Celsius)1 Publication
  3. Vmax=0.22 µmol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei165Curated1
Active sitei262Curated1
Active sitei292Curated1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11101-MONOMER
MetaCyc:EG11101-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.6, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P23872

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...
ESTHERi
ecoli-Aes, Hormone-sensitive_lipase_like

MEROPS protease database

More...
MEROPSi
S09.A47

MoonProt database of moonlighting proteins

More...
MoonProti
P23872

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Acetyl esterase (EC:3.1.1.-)
Alternative name(s):
EcE
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:aes
Synonyms:ybaC
Ordered Locus Names:b0476, JW0465
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi103H → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi128E → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi163G → A: Diminishes catalytic efficiency. 1 Publication1
Mutagenesisi164D → A: Strongly reduces enzymatic activity. 1 Publication1
Mutagenesisi165S → A: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi167G → A: Diminishes substrate affinity. 1 Publication1
Mutagenesisi262D → A: Strongly reduces enzymatic activity. 1 Publication1
Mutagenesisi266D → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi292H → A: Abolishes enzymatic activity. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000715551 – 319Acetyl esteraseAdd BLAST319

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P23872

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P23872

PRoteomics IDEntifications database

More...
PRIDEi
P23872

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with MalT and MelA.

2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263164, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-9062N

Protein interaction database and analysis system

More...
IntActi
P23872, 8 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0476

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P23872

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi91 – 93Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0657, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012494_6_4_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23872

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23872

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1820, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01958, Acetyl_esterase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR013094, AB_hydrolase_3
IPR023508, Acetyl_esterase
IPR002168, Lipase_GDXG_HIS_AS
IPR033140, Lipase_GDXG_put_SER_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07859, Abhydrolase_3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53474, SSF53474, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01173, LIPASE_GDXG_HIS, 1 hit
PS01174, LIPASE_GDXG_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P23872-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF
60 70 80 90 100
WNAGAPEMAT RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL
110 120 130 140 150
DTHDRIMRLL ASYSQCTVIG IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE
160 170 180 190 200
DYQINMSRIG FAGDSAGAML ALASALWLRD KQIDCGKVAG VLLWYGLYGL
210 220 230 240 250
RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY CLFNNDLTRE
260 270 280 290 300
VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
310
MKTADEALRD GAQFFTAQL
Length:319
Mass (Da):36,034
Last modified:November 1, 1997 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F9E234E23CCE7D0
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence L35149 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18K → N in D00798 (Ref. 8) Curated1
Sequence conflicti275 – 319LAAHQ…FTAQL → VSCASAAL in BAA14305 (PubMed:2051480).CuratedAdd BLAST45

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D90259 Genomic DNA Translation: BAA14305.2
U82664 Genomic DNA Translation: AAB40230.1
U00096 Genomic DNA Translation: AAC73578.1
AP009048 Genomic DNA Translation: BAE76255.1
D00798 Genomic DNA No translation available.
L35149 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
C64778

NCBI Reference Sequences

More...
RefSeqi
NP_415009.1, NC_000913.3
WP_000801813.1, NZ_SSZK01000009.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73578; AAC73578; b0476
BAE76255; BAE76255; BAE76255

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947514

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0465
eco:b0476

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1800

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90259 Genomic DNA Translation: BAA14305.2
U82664 Genomic DNA Translation: AAB40230.1
U00096 Genomic DNA Translation: AAC73578.1
AP009048 Genomic DNA Translation: BAE76255.1
D00798 Genomic DNA No translation available.
L35149 Genomic DNA No translation available.
PIRiC64778
RefSeqiNP_415009.1, NC_000913.3
WP_000801813.1, NZ_SSZK01000009.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4KRXX-ray1.80A/B/C1-319[»]
4KRYX-ray2.30A/B/C/D/E/F1-319[»]
SMRiP23872
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263164, 4 interactors
DIPiDIP-9062N
IntActiP23872, 8 interactors
STRINGi511145.b0476

Protein family/group databases

ESTHERiecoli-Aes, Hormone-sensitive_lipase_like
MEROPSiS09.A47
MoonProtiP23872

Proteomic databases

jPOSTiP23872
PaxDbiP23872
PRIDEiP23872

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
947514

Genome annotation databases

EnsemblBacteriaiAAC73578; AAC73578; b0476
BAE76255; BAE76255; BAE76255
GeneIDi947514
KEGGiecj:JW0465
eco:b0476
PATRICifig|1411691.4.peg.1800

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1093

Phylogenomic databases

eggNOGiCOG0657, Bacteria
HOGENOMiCLU_012494_6_4_6
InParanoidiP23872
PhylomeDBiP23872

Enzyme and pathway databases

BioCyciEcoCyc:EG11101-MONOMER
MetaCyc:EG11101-MONOMER
BRENDAi3.1.1.6, 2026
SABIO-RKiP23872

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P23872

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
HAMAPiMF_01958, Acetyl_esterase, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR013094, AB_hydrolase_3
IPR023508, Acetyl_esterase
IPR002168, Lipase_GDXG_HIS_AS
IPR033140, Lipase_GDXG_put_SER_AS
PfamiView protein in Pfam
PF07859, Abhydrolase_3, 1 hit
SUPFAMiSSF53474, SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS01173, LIPASE_GDXG_HIS, 1 hit
PS01174, LIPASE_GDXG_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAES_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23872
Secondary accession number(s): P77282, Q2MBV1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 159 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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