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Entry version 45 (08 May 2019)
Sequence version 2 (08 May 2019)
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Protein

Stimulator of interferon genes protein

Gene

TMEM173

Organism
Gallus gallus (Chicken)
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

Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (By similarity). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:30842659). Upon binding of c-di-GMP or cGAMP, TMEM173/STING oligomerizes and is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state (PubMed:30842659). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, TMEM173/STING buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei268Cyclic dinucleotideCombined sources1 Publication1

<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

Biological processAutophagy, Immunity, Innate immunity
LigandNucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-GGA-1834941 STING mediated induction of host immune responses
R-GGA-3134975 Regulation of innate immune responses to cytosolic DNA
R-GGA-3249367 STAT6-mediated induction of chemokines
R-GGA-6798695 Neutrophil degranulation

<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:
Stimulator of interferon genes protein1 Publication
Short name:
STING1 Publication
Alternative name(s):
Transmembrane protein 173By similarity
<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:TMEM173By similarity
Synonyms:STING1 Publication
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <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> Componentsi: Chromosome 13, Unplaced

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 23Cytoplasmic1 PublicationAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei24 – 40Helical; Name=11 PublicationAdd BLAST17
Topological domaini41 – 50Lumenal1 Publication10
Transmembranei51 – 75Helical; Name=21 PublicationAdd BLAST25
Topological domaini76 – 97Cytoplasmic1 PublicationAdd BLAST22
Transmembranei98 – 111Helical; Name=31 PublicationAdd BLAST14
Topological domaini112 – 121Lumenal1 Publication10
Transmembranei122 – 139Helical; Name=41 PublicationAdd BLAST18
Topological domaini140 – 379Cytoplasmic1 PublicationAdd BLAST240

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

<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_00004045881 – 379Stimulator of interferon genes proteinAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei366Phosphoserine; by TBK11 Publication1

<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

Phosphorylation by TBK1 leads to activation and production of IFN-beta (Probable). Following cyclic nucleotide (c-di-GMP or cGAMP)-binding, activation and translocation from the endoplasmic reticulum, TMEM173/STING is phosphorylated by TBK1 at Ser-366 in the pLxIS motif (Probable). The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines (Probable).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
E1C7U0

<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

Homodimer; forms a homodimer in absence of cyclic nucleotide (c-di-GMP or cGAMP) (PubMed:30842659). Homotetramer; in presence of cyclic nucleotide (c-di-GMP or cGAMP), forms tetramers and higher-order oligomers through side-by-side packing (PubMed:30842659). Interacts (when phosphorylated) with IRF3; following activation and phosphorylation on the pLxIS motif by TBK1, recruits IRF3 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000001248

<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

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
6NT6electron microscopy4.0A/B1-379[»]
6NT7electron microscopy4.0A/B1-379[»]
6NT8electron microscopy6.5A/B/C/D1-379[»]
6NT9electron microscopy3.3A/B1-379[»]

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

<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>Regioni158 – 345Cyclic dinucleotide-binding domain (CBD)Combined sources1 PublicationAdd BLAST188
Regioni167 – 172Cyclic dinucleotide bindingCombined sources1 Publication6
Regioni243 – 246Cyclic dinucleotide bindingCombined sources1 Publication4

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>Motifi363 – 366pLxIS motifBy similarity4

<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

In absence of cGAMP, the transmembrane and cytoplasmic regions interact to form an integrated, domain-swapped dimeric assembly (PubMed:30842659). In absence of cyclic nucleotide (c-di-GMP or cGAMP), the protein is autoinhibited by an intramolecular interaction between the cyclic dinucleotide-binding domain (CBD) and the C-terminal tail (CTT) (By similarity). Following cGAMP-binding, the cyclic dinucleotide-binding domain (CBD) is closed, leading to a 180 degrees rotation of the CBD domain relative to the transmembrane domain (PubMed:30842659). This rotation is coupled to a conformational change in a loop on the side of the CBD dimer, which leads to the formation of the TMEM173/STING tetramer and higher-order oligomers through side-by-side packing (PubMed:30842659). The N-terminal part of the CBD region was initially though to contain a fifth transmembrane region (TM5) but is part of the folded, soluble CBD (By similarity).By similarity1 Publication
The pLxIS motif constitutes an IRF3-binding motif: following phosphorylation by TBK1, the phosphorylated pLxIS motif of TMEM173/STING recruits IRF3. IRF3 is then phosphorylated and activated by TBK1 to induce type-I interferons and other cytokines.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 TMEM173 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IH2R Eukaryota
ENOG4111M85 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008582

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
E1C7U0

Identification of Orthologs from Complete Genome Data

More...
OMAi
YSNSVYE

Database of Orthologous Groups

More...
OrthoDBi
865174at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
E1C7U0

TreeFam database of animal gene trees

More...
TreeFami
TF324444

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12146 STING_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.12100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029158 STING
IPR033952 STING_C
IPR038623 STING_C_sf

The PANTHER Classification System

More...
PANTHERi
PTHR34339 PTHR34339, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15009 TMEM173, 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.

E1C7U0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPQDPSTRSS PARLLIPEPR AGRARHAACV LLAVCFVVLF LSGEPLAPII
60 70 80 90 100
RSVCTQLAAL QLGVLLKGCC CLAEEIFHLH SRHHGSLWQV LCSCFPPRWY
110 120 130 140 150
LALLLVGGSA YLDPPEDNGH SPRLALTLSC LCQLLVLALG LQKLSAVEVS
160 170 180 190 200
ELTESSKKNV AHGLAWSYYI GYLKVVLPRL KECMEELSRT NPMLRAHRDT
210 220 230 240 250
WKLHILVPLG CDIWDDLEKA DSNIQYLADL PETILTRAGI KRRVYKHSLY
260 270 280 290 300
VIRDKDNKLR PCVLEFASPL QTLCAMSQDD CAAFSREQRL EQARLFYRSL
310 320 330 340 350
RDILGSSKEC AGLYRLIAYE EPAEPESHFL SGLILWHLQQ QQREEYMVQE
360 370
ELPLGTSSVE LSLQVSSSDL PQPLRSDCP
Length:379
Mass (Da):42,596
Last modified:May 8, 2019 - v2
<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:i41E0232AE90E0D47
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
AADN02063745 Genomic DNA No translation available.
AADN02063746 Genomic DNA No translation available.
AADN04000430 Genomic DNA No translation available.

NCBI Reference Sequences

More...
RefSeqi
XP_001232171.2, XM_001232170.4
XP_015149009.1, XM_015293523.1
XP_015149010.1, XM_015293524.1
XP_015149011.1, XM_015293525.1
XP_015149012.1, XM_015293526.1
XP_015149013.1, XM_015293527.1
XP_015149014.1, XM_015293528.1
XP_015149015.1, XM_015293529.1
XP_015149016.1, XM_015293530.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSGALT00000071854; ENSGALP00000048751; ENSGALG00000041129

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
768990

<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
AADN02063745 Genomic DNA No translation available.
AADN02063746 Genomic DNA No translation available.
AADN04000430 Genomic DNA No translation available.
RefSeqiXP_001232171.2, XM_001232170.4
XP_015149009.1, XM_015293523.1
XP_015149010.1, XM_015293524.1
XP_015149011.1, XM_015293525.1
XP_015149012.1, XM_015293526.1
XP_015149013.1, XM_015293527.1
XP_015149014.1, XM_015293528.1
XP_015149015.1, XM_015293529.1
XP_015149016.1, XM_015293530.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6NT6electron microscopy4.0A/B1-379[»]
6NT7electron microscopy4.0A/B1-379[»]
6NT8electron microscopy6.5A/B/C/D1-379[»]
6NT9electron microscopy3.3A/B1-379[»]
ModBaseiSearch...
MobiDBiSearch...
SWISS-MODEL-WorkspaceiSubmit a new modelling project...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000001248

Proteomic databases

PaxDbiE1C7U0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000071854; ENSGALP00000048751; ENSGALG00000041129
GeneIDi768990

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
340061

Phylogenomic databases

eggNOGiENOG410IH2R Eukaryota
ENOG4111M85 LUCA
GeneTreeiENSGT00390000008582
InParanoidiE1C7U0
OMAiYSNSVYE
OrthoDBi865174at2759
PhylomeDBiE1C7U0
TreeFamiTF324444

Enzyme and pathway databases

ReactomeiR-GGA-1834941 STING mediated induction of host immune responses
R-GGA-3134975 Regulation of innate immune responses to cytosolic DNA
R-GGA-3249367 STAT6-mediated induction of chemokines
R-GGA-6798695 Neutrophil degranulation

Family and domain databases

CDDicd12146 STING_C, 1 hit
Gene3Di3.40.50.12100, 1 hit
InterProiView protein in InterPro
IPR029158 STING
IPR033952 STING_C
IPR038623 STING_C_sf
PANTHERiPTHR34339 PTHR34339, 1 hit
PfamiView protein in Pfam
PF15009 TMEM173, 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 nameiSTING_CHICK
<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: E1C7U0
Secondary accession number(s): A0A1D5P7Q9
<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: February 8, 2011
Last sequence update: May 8, 2019
Last modified: May 8, 2019
This is version 45 of the entry and version 2 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 programChordata 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, 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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