Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endonuclease 8

Gene

nei

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

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Acts on DNA bubble and 3'-fork structures, suggesting a role in replication-associated DNA repair. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. EC:4.2.99.18

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei2Schiff-base intermediate with DNA1
Active sitei3Proton donorCurated1
Active sitei53Proton donor; for beta-elimination activityCurated1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei70DNA1 Publication1
Binding sitei125DNA1 Publication1
Binding sitei169DNA1 Publication1
Active sitei253Proton donor; for delta-elimination activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri229 – 263FPG-typeAdd BLAST35

<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 functionDNA-binding, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6383-MONOMER
MetaCyc:G6383-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.2.23 2026
4.2.99.18 2026

<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_and_taxonomy_section">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:
Endonuclease 8
Alternative name(s):
DNA glycosylase/AP lyase Nei (EC:3.2.2.-, EC:4.2.99.18)
DNA-(apurinic or apyrimidinic site) lyase Nei
Endonuclease VIII
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:nei
Ordered Locus Names:b0714, JW0704
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG13237 nei

<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_and_biotech_section">'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>Mutagenesisi2P → T: Loss of glycosylase and AP lyase activity. 1 Publication1
Mutagenesisi3E → A or Q: Loss of glycosylase activity. No effect on AP lyase activity. 2 Publications1
Mutagenesisi3E → D: Much reduced glycosylase activity. No effect on AP lyase activity. 2 Publications1
Mutagenesisi6E → Q: Reduced glycosylase activity. No effect on AP lyase activity. 1 Publication1
Mutagenesisi53K → A: Loss of DNA cleavage at sites containing oxidized pyrimidine. No effect on AP lyase activity. 1 Publication1
Mutagenesisi129D → N: Reduced glycosylase activity. No effect on AP lyase activity. 1 Publication1
Mutagenesisi160D → N: No effect on glycosylase and AP lyase activity. 1 Publication1
Mutagenesisi174E → Q: Loss of glycosylase activity. No effect on AP lyase activity. 1 Publication1
Mutagenesisi213R → A: Slightly reduced activity. 1 Publication1
Mutagenesisi253R → A: Reduced DNA cleavage at sites containing oxidized pyrimidine. No effect on AP lyase 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001708932 – 263Endonuclease 8Add BLAST262

Proteomic databases

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

More...
PaxDbi
P50465

PRoteomics IDEntifications database

More...
PRIDEi
P50465

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259928, 110 interactors

Database of interacting proteins

More...
DIPi
DIP-10327N

Protein interaction database and analysis system

More...
IntActi
P50465, 13 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0781

<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

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00375

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P50465

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

More...
SMRi
P50465

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P50465

<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

<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 FPG family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri229 – 263FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4108S0J Bacteria
COG0266 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000020882

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P50465

KEGG Orthology (KO)

More...
KOi
K05522

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P50465

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.190.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01253 Endonuclease_8, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR023713 Endonuclease-VIII
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P50465-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKPYQSQL IGQHVTHVET
60 70 80 90 100
RGKALLTHFS NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT
110 120 130 140 150
ILLYSASDIE MLTPEQLTTH PFLQRVGPDV LDPNLTPEVV KERLLSPRFR
160 170 180 190 200
NRQFAGLLLD QAFLAGLGNY LRVEILWQVG LTGNHKAKDL NAAQLDALAH
210 220 230 240 250
ALLEIPRFSY ATRGQVDENK HHGALFRFKV FHRDGEPCER CGSIIEKTTL
260
SSRPFYWCPG CQH
Length:263
Mass (Da):29,845
Last modified:January 23, 2007 - 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:i7D10B79F58ADDA24
GO

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
U38616 Genomic DNA Translation: AAC45355.1
D89754 Genomic DNA Translation: BAA20414.1
U00096 Genomic DNA Translation: AAC73808.1
AP009048 Genomic DNA Translation: BAA35378.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A64807

NCBI Reference Sequences

More...
RefSeqi
NP_415242.1, NC_000913.3
WP_001113989.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73808; AAC73808; b0714
BAA35378; BAA35378; BAA35378

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945320

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0704
eco:b0714

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1559

<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
U38616 Genomic DNA Translation: AAC45355.1
D89754 Genomic DNA Translation: BAA20414.1
U00096 Genomic DNA Translation: AAC73808.1
AP009048 Genomic DNA Translation: BAA35378.1
PIRiA64807
RefSeqiNP_415242.1, NC_000913.3
WP_001113989.1, NZ_LN832404.1

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
1K3WX-ray1.42A2-263[»]
1K3XX-ray1.25A2-263[»]
1Q39X-ray2.80A2-263[»]
1Q3BX-ray2.05A2-263[»]
1Q3CX-ray2.30A2-263[»]
2EA0X-ray1.40A2-263[»]
2OPFX-ray1.85A2-263[»]
2OQ4X-ray2.60A/B2-263[»]
DisProtiDP00375
ProteinModelPortaliP50465
SMRiP50465
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259928, 110 interactors
DIPiDIP-10327N
IntActiP50465, 13 interactors
STRINGi316385.ECDH10B_0781

Proteomic databases

PaxDbiP50465
PRIDEiP50465

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73808; AAC73808; b0714
BAA35378; BAA35378; BAA35378
GeneIDi945320
KEGGiecj:JW0704
eco:b0714
PATRICifig|1411691.4.peg.1559

Organism-specific databases

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

More...
EchoBASEi
EB3026
EcoGeneiEG13237 nei

Phylogenomic databases

eggNOGiENOG4108S0J Bacteria
COG0266 LUCA
HOGENOMiHOG000020882
InParanoidiP50465
KOiK05522
PhylomeDBiP50465

Enzyme and pathway databases

BioCyciEcoCyc:G6383-MONOMER
MetaCyc:G6383-MONOMER
BRENDAi3.2.2.23 2026
4.2.99.18 2026

Miscellaneous databases

EvolutionaryTraceiP50465

Protein Ontology

More...
PROi
PR:P50465

Family and domain databases

Gene3Di3.20.190.10, 1 hit
HAMAPiMF_01253 Endonuclease_8, 1 hit
InterProiView protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR023713 Endonuclease-VIII
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit
SMARTiView protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit
PROSITEiView protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiEND8_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: P50465
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 163 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, Complete proteome, 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
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again