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Entry version 52 (11 Dec 2019)
Sequence version 1 (16 May 2012)
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Protein

ECF RNA polymerase sigma factor SigR

Gene

sigR

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor (RsrA) until released. Responds to thiol-oxidative stress, involved in regulation of about 30 genes and operons, including the thioredoxin system (trxB-trxA, trxC), ribosomal protein L31, RNA polymerase-binding protein RbpA and mycothiol (MSH) biosynthetic (mshA) and recycling genes (mca). In conjunction with its cognate anti-sigma factor RsrA may sense the intracellular level of reduced MSH.4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi173 – 192H-T-H motifBy similarityAdd BLAST20

<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

  • DNA binding Source: UniProtKB-KW
  • DNA-binding transcription factor activity Source: InterPro
  • sigma factor activity Source: UniProtKB

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, Sigma factor
Biological processTranscription, Transcription regulation

<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:
ECF RNA polymerase sigma factor SigR
Short name:
ECF sigma factor SigR
Alternative name(s):
Alternative RNA polymerase sigma factor SigR
RNA polymerase sigma-R factor
Short name:
Sigma-R factor
<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:sigR
Ordered Locus Names:SCO5216
<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>OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
<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 identifieri100226 [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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
<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
  • UP000001973 <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

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Increased sensitivity to redox-cycling compounds menadione and plumbagin, and to diamide. Loss of expression of mycothiol biosynthetic and recycling genes.2 Publications

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004236491 – 227ECF RNA polymerase sigma factor SigRAdd BLAST227

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

SigR is present in multiple forms of different pI, suggesting other unknown post-translational modifications.
SigR prime is probably partially degraded by ClpP1-ClpP2.

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q7AKG9

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expressed from 2 promoters, 1 of which (sigRp2) positively regulates its own expression. The same promoter is transiently induced (about 70-fold) by the thiol-oxiding agent diamide. Also induced when mycothiol is oxidized or conjugated.3 Publications

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts transiently with the RNA polymerase catalytic core formed by RpoA, RpoB, RpoC and RpoZ (2 alpha, 1 beta, 1 beta' and 1 omega subunit) to form the RNA polymerase holoenzyme that can initiate transcription.

Interacts with cognate anti-sigma factor RsrA under reducing but not oxiding conditions, which prevents it binding to RNA polymerase. Treatment with the thiol-oxidzing agent diamide inhibits the interaction.

4 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
100226.SCO5216

<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

1227
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
Q7AKG9

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni43 – 106Sigma-70 factor domain-2Add BLAST64
Regioni148 – 198Sigma-70 factor domain-4Add BLAST51

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>Motifi63 – 66Polymerase core bindingSequence analysis4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity). Interactions between sigma-70 factor domain-2 and anti-sigma factors prevents interaction of sigma factors with the RNA polymerase catalytic core (Probable).By similarityCurated
The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA (By similarity).By similarity

<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 sigma-70 factor family. ECF subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105EMN Bacteria
COG1595 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000094755

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q7AKG9

KEGG Orthology (KO)

More...
KOi
K03088

Identification of Orthologs from Complete Genome Data

More...
OMAi
RGMLEDY

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q7AKG9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039425 RNA_pol_sigma-70-like
IPR014284 RNA_pol_sigma-70_dom
IPR014293 RNA_pol_sigma70_actinobac
IPR000838 RNA_pol_sigma70_ECF_CS
IPR007627 RNA_pol_sigma70_r2
IPR013249 RNA_pol_sigma70_r4_t2
IPR013325 RNA_pol_sigma_r2
IPR013324 RNA_pol_sigma_r3/r4-like
IPR036388 WH-like_DNA-bd_sf

The PANTHER Classification System

More...
PANTHERi
PTHR43133 PTHR43133, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04542 Sigma70_r2, 1 hit
PF08281 Sigma70_r4_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF88659 SSF88659, 1 hit
SSF88946 SSF88946, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02947 SigH_actino, 1 hit
TIGR02937 sigma70-ECF, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01063 SIGMA70_ECF, 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>. 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform SigR (identifier: Q7AKG9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGPVTGTDAG TEHGQAEQPE GRGTGAESTA ERSARFERDA LEFLDQMYSA
60 70 80 90 100
ALRMTRNPAD AEDLVQETYA KAYASFHQFR EGTNLKAWLY RILTNTFINS
110 120 130 140 150
YRKKQREPQR SAAEEIEDWQ LARAESHMST GLRSAESQAL DHLPDSDVKQ
160 170 180 190 200
ALQAIPEEFR IAVYLADVEG FAYKEIADIM GTPIGTVMSR LHRGRRQLRG
210 220
MLEDYARDRG LVPAGAGESN EAKGSGS
Note: Constitutively expressed major isoform, not induced by diamide (at protein level), contributes about half of the diamide-induced expression of the regulon.
Length:227
Mass (Da):25,218
Last modified:May 16, 2012 - v1
<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:iAE89C2EF0ED4F366
GO
Isoform SigR prime (identifier: Q7AKG9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGSAFCPSRSSRADLDWTVLHAAKTAPIRAAGGPDRRLSSDSSETGLGFTTTSEEM

Note: Present in low amounts in unstressed cells, strongly but transiently produced upon diamide induction. Functions as a sigma factor, contributes about half of the diamide-induced expression of the regulon. Unstable, half-life of about 10 minutes.Curated
Show »
Length:282
Mass (Da):30,956
Checksum:i482A1917C58C9858
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0532311M → MGSAFCPSRSSRADLDWTVL HAAKTAPIRAAGGPDRRLSS DSSETGLGFTTTSEEM in isoform SigR prime. Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ010320 Genomic DNA Translation: CAA09088.1
AL939122 Genomic DNA Translation: CAB94601.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T42015

NCBI Reference Sequences

More...
RefSeqi
NP_629363.1, NC_003888.3 [Q7AKG9-1]
WP_003973756.1, NC_003888.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB94601; CAB94601; CAB94601

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1100657

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sco:SCO5216

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|100226.15.peg.5300

Keywords - Coding sequence diversityi

Alternative initiation

<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
AJ010320 Genomic DNA Translation: CAA09088.1
AL939122 Genomic DNA Translation: CAB94601.1
PIRiT42015
RefSeqiNP_629363.1, NC_003888.3 [Q7AKG9-1]
WP_003973756.1, NC_003888.3

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
1H3LX-ray2.38A/B23-109[»]
5FGMX-ray2.60A143-207[»]
SMRiQ7AKG9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5216

Proteomic databases

PRIDEiQ7AKG9

Genome annotation databases

EnsemblBacteriaiCAB94601; CAB94601; CAB94601
GeneIDi1100657
KEGGisco:SCO5216
PATRICifig|100226.15.peg.5300

Phylogenomic databases

eggNOGiENOG4105EMN Bacteria
COG1595 LUCA
HOGENOMiHOG000094755
InParanoidiQ7AKG9
KOiK03088
OMAiRGMLEDY
PhylomeDBiQ7AKG9

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR039425 RNA_pol_sigma-70-like
IPR014284 RNA_pol_sigma-70_dom
IPR014293 RNA_pol_sigma70_actinobac
IPR000838 RNA_pol_sigma70_ECF_CS
IPR007627 RNA_pol_sigma70_r2
IPR013249 RNA_pol_sigma70_r4_t2
IPR013325 RNA_pol_sigma_r2
IPR013324 RNA_pol_sigma_r3/r4-like
IPR036388 WH-like_DNA-bd_sf
PANTHERiPTHR43133 PTHR43133, 1 hit
PfamiView protein in Pfam
PF04542 Sigma70_r2, 1 hit
PF08281 Sigma70_r4_2, 1 hit
SUPFAMiSSF88659 SSF88659, 1 hit
SSF88946 SSF88946, 1 hit
TIGRFAMsiTIGR02947 SigH_actino, 1 hit
TIGR02937 sigma70-ECF, 1 hit
PROSITEiView protein in PROSITE
PS01063 SIGMA70_ECF, 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 nameiSIGR_STRCO
<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: Q7AKG9
Secondary accession number(s): O87834
<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 16, 2013
Last sequence update: May 16, 2012
Last modified: December 11, 2019
This is version 52 of the entry and version 1 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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