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UniProtKB - P18848 (ATF4_HUMAN)

Entry version 227 (23 Feb 2022)
Sequence version 3 (17 Oct 2006)
Previous versions | rss
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Protein

Cyclic AMP-dependent transcription factor ATF-4

Gene

ATF4

Organism
Homo sapiens (Human)
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 displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (PubMed:17684156, PubMed:16682973, PubMed:31444471, PubMed:32132707).

Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (By similarity).

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:32132707).

During ISR, ATF4 translation is induced via an alternative ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:32132706, PubMed:32132707).

Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (By similarity).

Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress (PubMed:26086088).

Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress (PubMed:11960987).

However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (PubMed:18940792).

Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (By similarity).

Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress (PubMed:15775988).

May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (PubMed:33384352).

In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (By similarity).

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 (By similarity).

Activates transcription of SIRT4 (By similarity).

Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (By similarity).

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 (By similarity).

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 (By similarity).

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 similarity11 Publications

(Microbial infection) Binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I.

1 Publication

<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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P18848

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-380994, ATF4 activates genes in response to endoplasmic reticulum stress
R-HSA-381042, PERK regulates gene expression
R-HSA-381183, ATF6 (ATF6-alpha) activates chaperone genes
R-HSA-9633012, Response of EIF2AK4 (GCN2) to amino acid deficiency
R-HSA-9648895, Response of EIF2AK1 (HRI) to heme deficiency

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P18848

SIGNOR Signaling Network Open Resource

More...SIGNORi		P18848

<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
Cyclic AMP-responsive element-binding protein 21 Publication
Short name:
CREB-21 Publication
Short name:
cAMP-responsive element-binding protein 21 Publication
Tax-responsive enhancer element-binding protein 671 Publication
Short name:
TaxREB671 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, TXREB1 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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 22

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:786, ATF4

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		604064, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P18848

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000128272

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

Keywords - Cellular componenti

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

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>Mutagenesisi156P → A: Increased stability in low oxygen conditions; when associated with A-162, A-164, A-167 and A-174. 1 Publication1
Mutagenesisi162P → A: Increased stability in low oxygen conditions; when associated with A-156, A-164, A-167 and A-174. 1 Publication1
Mutagenesisi164P → A: Increased stability in low oxygen conditions; when associated with A-156, A-162, A-167 and A-174. 1 Publication1
Mutagenesisi167P → A: Increased stability in low oxygen conditions; when associated with A-156, A-162, A-164 and A-174. 1 Publication1
Mutagenesisi174P → A: Increased stability in low oxygen conditions; when associated with A-156, A-162, A-164 and A-167. 1 Publication1
Mutagenesisi213T → A: Does not affect phosphorylation by CK2. 1 Publication1
Mutagenesisi215S → A: Abolished phosphorylation by CK2 leading to increased stability. 1 Publication1
Mutagenesisi219S → N: Abolished phosphorylation on the betaTrCP degron motif, interaction with BTRC and subsequent ubiquitination. 1 Publication1
Mutagenesisi245S → A: Abolished phosphorylation by RPS6KA3/RSK2. 1 Publication1
Mutagenesisi311K → R: Decreased acetylation without affecting ubiquitination by SCF(BTRC). 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		468

Open Targets

More...OpenTargetsi		ENSG00000128272

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA25086

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P18848, Tbio

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00852, Pseudoephedrine

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ATF4

Domain mapping of disease mutations (DMDM)

More...DMDMi		116241262

<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_00000765841 – 351Cyclic AMP-dependent transcription factor ATF-4Add BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei213PhosphothreonineBy similarity1
Modified residuei215Phosphoserine; by CK21 Publication1
Modified residuei219PhosphoserineBy similarity1
Modified residuei224PhosphoserineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei235PhosphoserineBy similarity1
Modified residuei2364-hydroxyprolineBy similarity1
Modified residuei245Phosphoserine; by RPS6KA31 Publication1
Modified residuei248PhosphoserineBy similarity1
Cross-linki259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei311N6-acetyllysine1 Publication1

<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:11238952). Interaction with EP300/p300 inhibits ubiquitination by SCF(BTRC) (PubMed:16219772).2 Publications
Phosphorylation at Ser-245 by RPS6KA3/RSK2 in osteoblasts enhances transactivation activity and promotes osteoblast differentiation (PubMed:15109498). Phosphorylated on the betaTrCP degron motif at Ser-219, followed by phosphorylation at Thr-213, Ser-224, Ser-231, Ser-235 and Ser-248, promoting interaction with BTRC and ubiquitination (By similarity). Phosphorylation is promoted by mTORC1 (By similarity). Phosphorylation at Ser-215 by CK2 decreases its stability (PubMed:23123191). Phosphorylated by NEK6 (PubMed:20873783).By similarity3 Publications
Hydroxylated by PHD3, leading to decreased protein stability.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P18848

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P18848

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P18848

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

More...PaxDbi		P18848

PeptideAtlas

More...PeptideAtlasi		P18848

PRoteomics IDEntifications database

More...PRIDEi		P18848

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53615

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P18848

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

More...PhosphoSitePlusi		P18848

<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

Regulated at the translational level in response to various stress such as endoplasmic reticulum stress, amino acid starvation or oxidative stress (PubMed:27629041, PubMed:33384352). In the absence of stress, ribosomes re-initiate translation at an inhibitory open reading frame (uORF) upstream of the ATF4 transcript, which precludes AFT4 translation. In response to stress and subsequent EIF2S1/eIF-2-alpha phosphorylation, ribosomes bypass the inhibitory uORF and re-initiate translation at the AFT4 coding sequence (PubMed:27629041).1 Publication1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000128272, Expressed in lower esophagus and 125 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P18848, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000128272, Low tissue specificity

<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:11018027). Heterodimer; heterodimerizes with CEBPB (PubMed:11018027). Heterodimer; heterodimerizes with DDIT3/CHOP (PubMed:18940792).

Interacts with CEP290 (via an N-terminal region) (PubMed:16682973).

Interacts with NEK6, DAPK2 (isoform 2) and ZIPK/DAPK3 (PubMed:20873783, PubMed:21408167).

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 (By similarity).

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

Interacts with ABRAXAS2 (PubMed:22974638).

Interacts with TRIB3, inhibiting the transactivation activity of ATF4 (By similarity).

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

Interacts with EP300/p300; EP300/p300 stabilizes ATF4 and increases its transcriptional activity independently of its catalytic activity by preventing its ubiquitination (PubMed:16219772).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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
P18848
With#Exp.IntAct
AP1M1 [Q9BXS5]3EBI-492498,EBI-541426
ATF2 [P15336]2EBI-492498,EBI-1170906
ATF3 [P18847]9EBI-492498,EBI-712767
itself2EBI-492498,EBI-492498
BATF [Q16520]3EBI-492498,EBI-749503
BATF3 [Q9NR55]2EBI-492498,EBI-10312707
BFSP2 [Q13515]11EBI-492498,EBI-10229433
BTRC [A0A0S2Z507]6EBI-492498,EBI-16429247
BTRC [B7Z3H4]3EBI-492498,EBI-16429269
BTRC [Q9Y297]21EBI-492498,EBI-307461
BTRC - isoform 2 [Q9Y297-2]5EBI-492498,EBI-8826333
CASP6 [P55212]3EBI-492498,EBI-718729
CCDC106 [Q9BWC9]14EBI-492498,EBI-711501
CEBPA [P49715]4EBI-492498,EBI-1172054
CEBPB [P17676]2EBI-492498,EBI-969696
CEBPD [P49716]2EBI-492498,EBI-7962058
CEBPE [Q15744]2EBI-492498,EBI-3907048
CEBPG [P53567]16EBI-492498,EBI-740209
CEP83 - isoform 2 [Q9Y592-2]3EBI-492498,EBI-11123098
CREBZF [Q9NS37]7EBI-492498,EBI-632965
DAPK2 - isoform 2 [Q9UIK4-2]2EBI-492498,EBI-9693115
DDIT3 [P35638]5EBI-492498,EBI-742651
DISC1 [Q9NRI5]4EBI-492498,EBI-529989
EXOC1 [Q9NV70]3EBI-492498,EBI-1045313
FOS [P01100]4EBI-492498,EBI-852851
FOSL1 [P15407]2EBI-492498,EBI-744510
GCC1 [Q96CN9]6EBI-492498,EBI-746252
GOLGA1 [Q92805]11EBI-492498,EBI-6164177
GOLGA8DP [Q0D2H9]3EBI-492498,EBI-10181276
GOLGA8G [Q08AF8]7EBI-492498,EBI-10181260
GPS2 [Q13227]13EBI-492498,EBI-713355
HAUS7 [Q99871]3EBI-492498,EBI-395719
JDP2 [Q8WYK2]3EBI-492498,EBI-1248415
JUN [P05412]4EBI-492498,EBI-852823
JUNB [P17275]3EBI-492498,EBI-748062
LAMP2 - isoform LAMP-2B [P13473-2]3EBI-492498,EBI-21591415
LDOC1 [O95751]10EBI-492498,EBI-740738
MAF [O75444]3EBI-492498,EBI-2805091
NAP1L5 [Q96NT1]3EBI-492498,EBI-713627
NDC80 [O14777]8EBI-492498,EBI-715849
NFE2L2 [Q16236]8EBI-492498,EBI-2007911
POLR2C [P19387]6EBI-492498,EBI-394729
PRPF40A - isoform 2 [O75400-2]3EBI-492498,EBI-5280197
SAPCD2 [Q86UD0]3EBI-492498,EBI-2561646
SH3GLB1 [Q9Y371]3EBI-492498,EBI-2623095
TARS3 [A2RTX5]3EBI-492498,EBI-1056629
TRIB3 [Q96RU7]16EBI-492498,EBI-492476
TTR [P02766]3EBI-492498,EBI-711909
Dapk3 [O54784] from Mus musculus.2EBI-492498,EBI-77359

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106958, 90 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-6385, bZIP transcription factor complex, ATF3-ATF4
CPX-6408, bZIP transcription factor complex, ATF2-ATF4
CPX-6521, bZIP transcription factor complex, ATF4-ATF4
CPX-6522, bZIP transcription factor complex, ATF4-BATF
CPX-6523, bZIP transcription factor complex, ATF4-BATF2
CPX-6524, bZIP transcription factor complex, ATF4-BATF3
CPX-6525, bZIP transcription factor complex, ATF4-CEBPA
CPX-6526, bZIP transcription factor complex, ATF4-CEBPB
CPX-6527, bZIP transcription factor complex, ATF4-CEBPG
CPX-6528, bZIP transcription factor complex, ATF4-CEBPD
CPX-6529, bZIP transcription factor complex, ATF4-CEBPE
CPX-6541, bZIP transcription factor complex, ATF4-CREB3
CPX-6542, bZIP transcription factor complex, ATF4-CREBZF
CPX-6543, bZIP transcription factor complex, ATF4-DDIT3
CPX-6562, bZIP transcription factor complex, ATF4-JUN
CPX-6563, bZIP transcription factor complex, ATF4-JUNB
CPX-6564, bZIP transcription factor complex, ATF4-FOS
CPX-6565, bZIP transcription factor complex, ATF4-FOSL1
CPX-6566, bZIP transcription factor complex, ATF4-MAF
CPX-6567, bZIP transcription factor complex, ATF4-MAFB
CPX-6568, bZIP transcription factor complex, ATF4-NFE2
CPX-6569, bZIP transcription factor complex, ATF4-NFE2L1
CPX-6570, bZIP transcription factor complex, ATF4-NFE2L2
CPX-6572, bZIP transcription factor complex, ATF4-NFE2L3
CPX-8, bZIP transcription factor complex, ATF4-CREB1
CPX-9, bZIP transcription factor complex, ATF1-ATF4

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P18848

Database of interacting proteins

More...DIPi		DIP-354N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P18848

Protein interaction database and analysis system

More...IntActi		P18848, 80 interactors

Molecular INTeraction database

More...MINTi		P18848

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000336790

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P18848, 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

1351
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		P18848

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P18848

<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>Domaini278 – 341bZIPPROSITE-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>Regioni210 – 268DisorderedSequence analysisAdd BLAST59
Regioni280 – 300Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni305 – 341Interaction with GABBR1By similarityAdd BLAST37
Regioni306 – 334Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili280 – 340Add BLAST61

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>Motifi215 – 224BetaTrCP degron motif1 Publication10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi217 – 245Polar residuesSequence analysisAdd BLAST29

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4571, Eukaryota

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		P18848

Identification of Orthologs from Complete Genome Data

More...OMAi		IVNPIGH

Database of Orthologous Groups

More...OrthoDBi		1524842at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P18848

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 7 potential isoforms that are computationally mapped.Show allAlign All

P18848-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTEMSFLSSE VLVGDLMSPF DQSGLGAEES LGLLDDYLEV AKHFKPHGFS 
        60         70         80         90        100
SDKAKAGSSE WLAVDGLVSP SNNSKEDAFS GTDWMLEKMD LKEFDLDALL 
       110        120        130        140        150
GIDDLETMPD DLLTTLDDTC DLFAPLVQET NKQPPQTVNP IGHLPESLTK 
       160        170        180        190        200
PDQVAPFTFL QPLPLSPGVL SSTPDHSFSL ELGSEVDITE GDRKPDYTAY 
       210        220        230        240        250
VAMIPQCIKE EDTPSDNDSG ICMSPESYLG SPQHSPSTRG SPNRSLPSPG 
       260        270        280        290        300
VLCGSARPKP YDPPGEKMVA AKVKGEKLDK KLKKMEQNKT AATRYRQKKR 
       310        320        330        340        350
AEQEALTGEC KELEKKNEAL KERADSLAKE IQYLKDLIEE VRKARGKKRV 

P
Length:351
Mass (Da):38,590
Last modified:October 17, 2006 - 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:i3BBB7379DC3B0D07
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 are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A6Q8PG17A0A6Q8PG17_HUMAN
Activating transcription factor 4
ATF4
322Annotation score:

Annotation score:2 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>
B4DJD4B4DJD4_HUMAN
Activating transcription factor 4
ATF4
267Annotation score:

Annotation score:2 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>
A0A6Q8PFH6A0A6Q8PFH6_HUMAN
Cyclic AMP-dependent transcription ...
ATF4
126Annotation 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>
A0A6Q8PGY1A0A6Q8PGY1_HUMAN
Cyclic AMP-dependent transcription ...
ATF4
189Annotation 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>
A0A6Q8PHB3A0A6Q8PHB3_HUMAN
Cyclic AMP-dependent transcription ...
ATF4
121Annotation 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>
A0A7P0Z4J5A0A7P0Z4J5_HUMAN
Cyclic AMP-dependent transcription ...
ATF4
97Annotation 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>
A0A6Q8PF56A0A6Q8PF56_HUMAN
Cyclic AMP-dependent transcription ...
ATF4
59Annotation 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>

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 conflicti284K → R no nucleotide entry (PubMed:2516827).Curated1
Sequence conflicti290T → R no nucleotide entry (PubMed:2516827).Curated1
Sequence conflicti329 – 331KEI → REK no nucleotide entry (PubMed:2516827).Curated3
Sequence conflicti338I → L no nucleotide entry (PubMed:2516827).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02825322Q → P3 PublicationsCorresponds to variant dbSNP:rs4894Ensembl.1
Natural variantiVAR_029259258P → A. Corresponds to variant dbSNP:rs1803323EnsemblClinVar.1
Natural variantiVAR_014768322E → D. Corresponds to variant dbSNP:rs1803324EnsemblClinVar.1

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
D90209 mRNA Translation: BAA14234.1
M86842 mRNA Translation: AAA52071.1
CR456384 mRNA Translation: CAG30270.1
AL022312 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60341.1
CH471095 Genomic DNA Translation: EAW60342.1
BC008090 mRNA Translation: AAH08090.1
BC011994 mRNA Translation: AAH11994.1
BC016855 mRNA Translation: AAH16855.1
BC022088 mRNA Translation: AAH22088.1
BC024775 mRNA Translation: AAH24775.1
BC044895 mRNA Translation: AAH44895.1
BC073754 mRNA Translation: AAH73754.1
BC073990 mRNA Translation: AAH73990.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13996.1

Protein sequence database of the Protein Information Resource

More...PIRi		A45377

NCBI Reference Sequences

More...RefSeqi		NP_001666.2, NM_001675.4
NP_877962.1, NM_182810.2
XP_016884296.1, XM_017028807.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000337304; ENSP00000336790; ENSG00000128272
ENST00000396680; ENSP00000379912; ENSG00000128272
ENST00000404241; ENSP00000384587; ENSG00000128272
ENST00000674568; ENSP00000501783; ENSG00000128272
ENST00000674835; ENSP00000502610; ENSG00000128272
ENST00000674920; ENSP00000501863; ENSG00000128272
ENST00000676346; ENSP00000502400; ENSG00000128272
ENST00000679776; ENSP00000505360; ENSG00000128272

Database of genes from NCBI RefSeq genomes

More...GeneIDi		468

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:468

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000674920.3; ENSP00000501863.1; NM_182810.3; NP_877962.1

UCSC genome browser

More...UCSCi		uc003axz.4, human

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90209 mRNA Translation: BAA14234.1
M86842 mRNA Translation: AAA52071.1
CR456384 mRNA Translation: CAG30270.1
AL022312 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60341.1
CH471095 Genomic DNA Translation: EAW60342.1
BC008090 mRNA Translation: AAH08090.1
BC011994 mRNA Translation: AAH11994.1
BC016855 mRNA Translation: AAH16855.1
BC022088 mRNA Translation: AAH22088.1
BC024775 mRNA Translation: AAH24775.1
BC044895 mRNA Translation: AAH44895.1
BC073754 mRNA Translation: AAH73754.1
BC073990 mRNA Translation: AAH73990.1
CCDSiCCDS13996.1
PIRiA45377
RefSeqiNP_001666.2, NM_001675.4
NP_877962.1, NM_182810.2
XP_016884296.1, XM_017028807.1

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
1CI6X-ray2.60A280-341[»]
SMRiP18848
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106958, 90 interactors
ComplexPortaliCPX-6385, bZIP transcription factor complex, ATF3-ATF4
CPX-6408, bZIP transcription factor complex, ATF2-ATF4
CPX-6521, bZIP transcription factor complex, ATF4-ATF4
CPX-6522, bZIP transcription factor complex, ATF4-BATF
CPX-6523, bZIP transcription factor complex, ATF4-BATF2
CPX-6524, bZIP transcription factor complex, ATF4-BATF3
CPX-6525, bZIP transcription factor complex, ATF4-CEBPA
CPX-6526, bZIP transcription factor complex, ATF4-CEBPB
CPX-6527, bZIP transcription factor complex, ATF4-CEBPG
CPX-6528, bZIP transcription factor complex, ATF4-CEBPD
CPX-6529, bZIP transcription factor complex, ATF4-CEBPE
CPX-6541, bZIP transcription factor complex, ATF4-CREB3
CPX-6542, bZIP transcription factor complex, ATF4-CREBZF
CPX-6543, bZIP transcription factor complex, ATF4-DDIT3
CPX-6562, bZIP transcription factor complex, ATF4-JUN
CPX-6563, bZIP transcription factor complex, ATF4-JUNB
CPX-6564, bZIP transcription factor complex, ATF4-FOS
CPX-6565, bZIP transcription factor complex, ATF4-FOSL1
CPX-6566, bZIP transcription factor complex, ATF4-MAF
CPX-6567, bZIP transcription factor complex, ATF4-MAFB
CPX-6568, bZIP transcription factor complex, ATF4-NFE2
CPX-6569, bZIP transcription factor complex, ATF4-NFE2L1
CPX-6570, bZIP transcription factor complex, ATF4-NFE2L2
CPX-6572, bZIP transcription factor complex, ATF4-NFE2L3
CPX-8, bZIP transcription factor complex, ATF4-CREB1
CPX-9, bZIP transcription factor complex, ATF1-ATF4
CORUMiP18848
DIPiDIP-354N
ELMiP18848
IntActiP18848, 80 interactors
MINTiP18848
STRINGi9606.ENSP00000336790

Chemistry databases

DrugBankiDB00852, Pseudoephedrine

PTM databases

iPTMnetiP18848
PhosphoSitePlusiP18848

Genetic variation databases

BioMutaiATF4
DMDMi116241262

Proteomic databases

EPDiP18848
jPOSTiP18848
MassIVEiP18848
PaxDbiP18848
PeptideAtlasiP18848
PRIDEiP18848
ProteomicsDBi53615

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P18848, 1 sequenced antibody

Antibodypedia a portal for validated antibodies

More...Antibodypediai		12687, 1126 antibodies from 46 providers

The DNASU plasmid repository

More...DNASUi		468

Genome annotation databases

EnsembliENST00000337304; ENSP00000336790; ENSG00000128272
ENST00000396680; ENSP00000379912; ENSG00000128272
ENST00000404241; ENSP00000384587; ENSG00000128272
ENST00000674568; ENSP00000501783; ENSG00000128272
ENST00000674835; ENSP00000502610; ENSG00000128272
ENST00000674920; ENSP00000501863; ENSG00000128272
ENST00000676346; ENSP00000502400; ENSG00000128272
ENST00000679776; ENSP00000505360; ENSG00000128272
GeneIDi468
KEGGihsa:468
MANE-SelectiENST00000674920.3; ENSP00000501863.1; NM_182810.3; NP_877962.1
UCSCiuc003axz.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		468
DisGeNETi468

GeneCards: human genes, protein and diseases

More...GeneCardsi		ATF4
HGNCiHGNC:786, ATF4
HPAiENSG00000128272, Low tissue specificity
MIMi604064, gene
neXtProtiNX_P18848
OpenTargetsiENSG00000128272
PharmGKBiPA25086
VEuPathDBiHostDB:ENSG00000128272

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4571, Eukaryota
GeneTreeiENSGT00530000063801
HOGENOMiCLU_055748_1_0_1
InParanoidiP18848
OMAiIVNPIGH
OrthoDBi1524842at2759
PhylomeDBiP18848
TreeFamiTF316136

Enzyme and pathway databases

PathwayCommonsiP18848
ReactomeiR-HSA-380994, ATF4 activates genes in response to endoplasmic reticulum stress
R-HSA-381042, PERK regulates gene expression
R-HSA-381183, ATF6 (ATF6-alpha) activates chaperone genes
R-HSA-9633012, Response of EIF2AK4 (GCN2) to amino acid deficiency
R-HSA-9648895, Response of EIF2AK1 (HRI) to heme deficiency
SignaLinkiP18848
SIGNORiP18848

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		468, 443 hits in 1039 CRISPR screens

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

More...ChiTaRSi		ATF4, human
EvolutionaryTraceiP18848

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ATF4

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		468
PharosiP18848, Tbio

Protein Ontology

More...PROi		PR:P18848
RNActiP18848, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000128272, Expressed in lower esophagus and 125 other tissues
GenevisibleiP18848, HS

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

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_HUMAN
<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: P18848
Secondary accession number(s): Q96AQ3, Q9UH31
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 17, 2006
Last modified: February 23, 2022
This is version 227 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 programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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