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UniProtKB - Q06507 (ATF4_MOUSE)

Entry version 157 (17 Jun 2020)
Sequence version 2 (27 Jul 2011)
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Protein

Cyclic AMP-dependent transcription factor ATF-4

Gene

Atf4

Organism
Mus musculus (Mouse)
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

Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and acts both as a regulator of normal metabolic and redox processes, and as a master transcription factor during the integrated stress response (ISR) (PubMed:8506317, PubMed:11106749, PubMed:12667446, PubMed:23624402). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (PubMed:8506317, PubMed:23624402). Core effector of the ISR, which is required for adaptation to various stress, such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress (PubMed:11106749, PubMed:12667446). During the ISR, ATF4 protein is translated in response to eIF-2-alpha/EIF2S1 phosphorylation caused by stress, and acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:11106749, PubMed:12667446). Protects cells against metabolic consequences of ER oxidation by promoting expression of genes linked to amino acid sufficiency and resistance to oxidative stress (PubMed:12667446). Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to amino acid deprivation or endoplasmic reticulum (ER) stress (PubMed:15775988, PubMed:21159964). Together with DDIT3/CHOP, mediates ER-mediated cell death by promoting expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the unfolded protein response (UPR) in response to ER stress (PubMed:23624402). ATF4 and DDIT3/CHOP activate the transcription of TRIB3 and promote ER stress-induced neuronal cell-death by regulating the expression of BBC3/PUMA (PubMed:15775988, PubMed:17369260, PubMed:21159964). During ER stress response, activates the transcription of NLRP1, possibly in concert with other factors (By similarity). Activates expression of genes required to promote cell recovery in response to mitochondrial stress (By similarity). Independently of the ISR, also required for normal metabolic processes: plays a key role in embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (PubMed:10096021, PubMed:10885750, PubMed:11806972, PubMed:12925279, PubMed:15109498, PubMed:22298775). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (PubMed:15109498). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (PubMed:22298775). Activates transcription of SIRT4 (PubMed:23663782). Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (PubMed:21768648, PubMed:22572884). Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (PubMed:21768648, PubMed:22572884). Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (PubMed:12925279). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471).By similarity17 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionActivator, DNA-binding, Repressor
Biological processBiological rhythms, Transcription, 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%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:
Cyclic AMP-dependent transcription factor ATF-4Curated
Short name:
cAMP-dependent transcription factor ATF-4Curated
Alternative name(s):
Activating transcription factor 41 Publication
C/EBP-related ATF1 Publication
Short name:
C/ATF1 Publication
Cyclic AMP-responsive element-binding protein 21 Publication
Short name:
CREB-21 Publication
Short name:
cAMP-responsive element-binding protein 21 Publication
<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:Atf41 PublicationImported
Synonyms:Creb21 Publication
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 15

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:88096 Atf4

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<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

Mice were born at a much lower rate than predicted by the Mendelian ratio (PubMed:10096021, PubMed:10885750). Homozygous pups generally die during the first hour after birth, although excess mortality occurrs throughout the first 3 weeks of life (PubMed:10096021, PubMed:11806972). Embryos are severely anemic during fetal development, due to an impairment in definitive hematopoiesis (PubMed:11806972). Surviving mice display defects in embryonic lens formation leading to severe microphthalmia in adults (PubMed:10096021, PubMed:10885750). Embryos show delayed bone formation and surviving mice display low bone mass throughout postnatal life (PubMed:15109498). Surviving null mice exhibit an increase in serum insulin levels and low blood glucose levels (PubMed:22298775). There is a decrease in total fat content, gonadal fat, lean mass and body weight (PubMed:22298775). Serum levels of osteocalcin/BGLAP are decreased (PubMed:22298775). PBK/AKT1-mediated phosphorylation of FOXO1 at 'Ser-258' is increased with a subsequent decrease of FOXO1-mediated transcriptional activity (PubMed:22298775).5 Publications

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>Mutagenesisi212T → A: Promotes stabilization due to impaired ubiquitination; when associated with A-223; A-230; A-234 and A-247. 1 Publication1
Mutagenesisi218S → A: Promotes stabilization due to impaired ubiquitination. 1 Publication1
Mutagenesisi223S → A: Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-230; A-234 and A-247. 1 Publication1
Mutagenesisi230S → A: Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-234 and A-247. 1 Publication1
Mutagenesisi234S → A: Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-230 and A-247. 1 Publication1
Mutagenesisi247S → A: Promotes stabilization due to impaired ubiquitination; when associated with A-212; A-223; A-230 and A-234. Does not affect phosphorylation by RPS6KA3/RSK2. 2 Publications1
Mutagenesisi251S → A, R or D: Abolished phosphorylation by RPS6KA3/RSK2. 1 Publication1
Mutagenesisi254S → A: Does not affect phosphorylation by RPS6KA3/RSK2. 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_00000765851 – 349Cyclic AMP-dependent transcription factor ATF-4Add BLAST349

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 residuei604-hydroxyproline1 Publication1
Modified residuei212Phosphothreonine1 Publication1
Modified residuei214PhosphoserineBy similarity1
Modified residuei218Phosphoserine1 Publication1
Modified residuei223Phosphoserine1 Publication1
Modified residuei230Phosphoserine1 Publication1
Modified residuei234Phosphoserine1 Publication1
Modified residuei2354-hydroxyproline1 Publication1
Modified residuei247Phosphoserine1 Publication1
Modified residuei251Phosphoserine; by RPS6KA31 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei309N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated by SCF(BTRC) in response to mTORC1 signal, followed by proteasomal degradation and leading to down-regulate expression of SIRT4 (PubMed:23663782). Interaction with EP300/p300 inhibits ubiquitination by SCF(BTRC) (By similarity).By similarity1 Publication
Phosphorylation at Ser-251 by RPS6KA3/RSK2 in osteoblasts enhances transactivation activity and promotes osteoblast differentiation (PubMed:15109498). Phosphorylated on the betaTrCP degron motif at Ser-218, followed by phosphorylation at Thr-212, Ser-223, Ser-230, Ser-234 and Ser-247, promoting interaction with BTRC and ubiquitination (PubMed:23663782). Phosphorylation is promoted by mTORC1 (PubMed:23663782). Phosphorylation at Ser-214 by CK2 decreases its stability (By similarity). Phosphorylated by NEK6 (By similarity).By similarity2 Publications
Hydroxylated by PHD3, leading to decreased protein stability.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q06507

PRoteomics IDEntifications database

More...PRIDEi		Q06507

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06507

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q06507

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed in adults.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

During embryonic development, expressed at high levels in anterior epithelial lens cells at E14.5 (PubMed:10885750). At 16.5 dpc, expressed in osteoblasts surrounding newly formed trabecular bone (PubMed:19232401). At postnatal day 2, detected in most osteoblasts and lining cells (PubMed:19232401). By postnatal week 4, is detected in fewer osteoblasts, but remains present in lining cells (at protein level) (PubMed:19232401).2 Publications

<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

Specifically produced in response to various stress, such as endoplasmic reticulum (ER) stress, amino acid starvation, or oxidative stress (PubMed:21159964, PubMed:11106749, PubMed:12667446, PubMed:15277680). In absence of stress, some upstream open reading frame (uORF) of this transcript is translated, thereby preventing its translation (PubMed:11106749, PubMed:15277680). In response to stress and subsequent eIF-2-alpha/EIF2S1 phosphorylation, preferentially translated (PubMed:15277680). Expressed in a circadian manner in the liver with an increased expression seen during the light phase (PubMed:21768648, PubMed:22572884). Expressed in a circadian manner in the midbrain with an increased expression seen during the dark phase (at protein level) (PubMed:21768648, PubMed:22572884). Expressed in a circadian manner also in the suprachiasmatic nucleus (SCN) of the brain, cerebral cortex, kidney and small intestine (PubMed:21768648, PubMed:22572884).6 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000042406 Expressed in retina and 333 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q06507 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q06507 MM

<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

Binds DNA as a homodimer and as a heterodimer (PubMed:23624402). Heterodimer; heterodimerizes with CEBPB (PubMed:11018027). Heterodimer; heterodimerizes with DDIT3/CHOP (PubMed:23624402).

Interacts with CEP290 (via an N-terminal region) (By similarity).

Interacts with NEK6, DAPK2 (isoform 2) and ZIPK/DAPK3 (By similarity).

Interacts (via its leucine zipper domain) with GABBR1 and GABBR2 (via their C-termini) (By similarity).

Forms a heterodimer with TXLNG in osteoblasts (PubMed:15911876).

Interacts (via its DNA binding domain) with FOXO1 (C-terminal half); the interaction occurs in osteoblasts and regulates glucose homeostasis through suppression of beta-cell proliferation and a decrease in insulin production (PubMed:22298775).

Interacts with SATB2; the interaction results in enhanced DNA binding and transactivation by these transcription factors (PubMed:16751105).

Interacts with ABRAXAS2 (PubMed:22974638).

Interacts with TRIB3, inhibiting the transactivation activity of ATF4 (PubMed:17369260).

Interacts with DISC1; which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471).

Interacts with EP300/p300; EP300/p300 stabilizes ATF4 and increases its transcriptional activity independently of its catalytic activity by preventing its ubiquitination (By similarity).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		198235, 11 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-6 ATF4-CREB1 transcription factor complex
CPX-7 ATF1-ATF4 transcription factor complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q06507

Database of interacting proteins

More...DIPi		DIP-30969N

Protein interaction database and analysis system

More...IntActi		Q06507, 9 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000105234

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q06507 protein

<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

1349
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		Q06507

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini276 – 339bZIPPROSITE-ProRule annotationAdd BLAST64

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>Regioni278 – 298Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni303 – 339Interaction with GABBR1By similarityAdd BLAST37
Regioni304 – 332Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

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>Motifi214 – 223BetaTrCP degron motif1 Publication10

<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 BetaTrCP degron motif promotes binding to BTRC when phosphorylated.1 Publication

<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 bZIP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4571 Eukaryota
ENOG4111ZXT LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063801

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_055748_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06507

KEGG Orthology (KO)

More...KOi		K04374

Identification of Orthologs from Complete Genome Data

More...OMAi		IVNPIGH

Database of Orthologous Groups

More...OrthoDBi		1524842at2759

TreeFam database of animal gene trees

More...TreeFami		TF316136

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029811 ATF4
IPR004827 bZIP

The PANTHER Classification System

More...PANTHERi		PTHR13044:SF32 PTHR13044:SF32, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00170 bZIP_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q06507-1 [UniParc]FASTAAdd to basket
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MTEMSFLNSE VLAGDLMSPF DQSGLGAEES LGLLDDYLEV AKHLKPHGFS 
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SDKAGSSEWP AMDDGLASAS DTGKEDAFSG TDWMLEKMDL KEFDFDALFR 
       110        120        130        140        150
MDDLETMPDE LLTTLDDTCD LFAPLVQETN KEPPQTVNPI GHLPESLIKV 
       160        170        180        190        200
DQVAPFTFLQ PFPCSPGVLS STPEHSFSLE LGSEVDISEG DRKPDSAAYI 
       210        220        230        240        250
TLIPPCVKEE DTPSDNDSGI CMSPESYLGS PQHSPSTSRA PPDNLPSPGG 
       260        270        280        290        300
SRGSPRPKPY DPPGVSLTAK VKTEKLDKKL KKMEQNKTAA TRYRQKKRAE 
       310        320        330        340 
QEALTGECKE LEKKNEALKE KADSLAKEIQ YLKDLIEEVR KARGKKRVP
Length:349
Mass (Da):38,355
Last modified:July 27, 2011 - 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:i0C3F895755B1C7B9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8VI82A0A2R8VI82_MOUSE
Cyclic AMP-dependent transcription ...
Atf4
116Annotation score:

Annotation score:1 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>

<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 AAA53043 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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 conflicti345K → Q in AAA40476 (PubMed:8506317).Curated1

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
L13791 mRNA Translation: AAA40476.1
M94087 mRNA Translation: AAA53043.1 Different initiation.
AK138657 mRNA Translation: BAE23736.1
AK144777 mRNA Translation: BAE26060.1
AK146193 mRNA Translation: BAE26967.1
AK156298 mRNA Translation: BAE33662.1
CH466550 Genomic DNA Translation: EDL04604.1
CH466550 Genomic DNA Translation: EDL04605.1
BC085169 mRNA Translation: AAH85169.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS37145.1

NCBI Reference Sequences

More...RefSeqi		NP_001274109.1, NM_001287180.1
NP_033846.2, NM_009716.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000109605; ENSMUSP00000105234; ENSMUSG00000042406

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11911

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:11911

UCSC genome browser

More...UCSCi		uc007wvl.2 mouse

<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
L13791 mRNA Translation: AAA40476.1
M94087 mRNA Translation: AAA53043.1 Different initiation.
AK138657 mRNA Translation: BAE23736.1
AK144777 mRNA Translation: BAE26060.1
AK146193 mRNA Translation: BAE26967.1
AK156298 mRNA Translation: BAE33662.1
CH466550 Genomic DNA Translation: EDL04604.1
CH466550 Genomic DNA Translation: EDL04605.1
BC085169 mRNA Translation: AAH85169.1
CCDSiCCDS37145.1
RefSeqiNP_001274109.1, NM_001287180.1
NP_033846.2, NM_009716.3

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
6IRRNMR-A314-349[»]
SMRiQ06507
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi198235, 11 interactors
ComplexPortaliCPX-6 ATF4-CREB1 transcription factor complex
CPX-7 ATF1-ATF4 transcription factor complex
CORUMiQ06507
DIPiDIP-30969N
IntActiQ06507, 9 interactors
STRINGi10090.ENSMUSP00000105234

PTM databases

iPTMnetiQ06507
PhosphoSitePlusiQ06507

Proteomic databases

PaxDbiQ06507
PRIDEiQ06507

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		12687 1050 antibodies

Genome annotation databases

EnsembliENSMUST00000109605; ENSMUSP00000105234; ENSMUSG00000042406
GeneIDi11911
KEGGimmu:11911
UCSCiuc007wvl.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		468
MGIiMGI:88096 Atf4

Phylogenomic databases

eggNOGiKOG4571 Eukaryota
ENOG4111ZXT LUCA
GeneTreeiENSGT00530000063801
HOGENOMiCLU_055748_1_0_1
InParanoidiQ06507
KOiK04374
OMAiIVNPIGH
OrthoDBi1524842at2759
TreeFamiTF316136

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		11911 10 hits in 16 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Atf4 mouse

Protein Ontology

More...PROi		PR:Q06507
RNActiQ06507 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000042406 Expressed in retina and 333 other tissues
ExpressionAtlasiQ06507 baseline and differential
GenevisibleiQ06507 MM

Family and domain databases

InterProiView protein in InterPro
IPR029811 ATF4
IPR004827 bZIP
PANTHERiPTHR13044:SF32 PTHR13044:SF32, 1 hit
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 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 nameiATF4_MOUSE
<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: Q06507
Secondary accession number(s): Q5U4B2, Q61906
<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: February 1, 1996
Last sequence update: July 27, 2011
Last modified: June 17, 2020
This is version 157 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, 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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