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UniProtKB - P17544 (ATF7_HUMAN)

Entry version 211 (02 Jun 2021)
Sequence version 3 (07 Oct 2020)
Previous versions | rss
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Protein

Cyclic AMP-dependent transcription factor ATF-7

Gene

ATF7

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

Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation (PubMed:29490055).

In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recruiting histone H3K9 tri- and di-methyltransferases thus silencing the transcription of target genes such as STAT1 in adipocytes, or genes involved in innate immunity in macrophages and adipocytes (By similarity).

Stress induces ATF7 phosphorylation that disrupts interactions with histone methyltransferase and enhances the association with coactivators containing histone acetyltransferase and/or histone demethylase, leading to disruption of the heterochromatin-like structure and subsequently transcriptional activation (By similarity).

In response to TNF-alpha, which is induced by various stresses, phosphorylated ATF7 and telomerase are released from telomeres leading to telomere shortening (PubMed:29490055).

Plays also a role in maintaining epithelial regenerative capacity and protecting against cell death during intestinal epithelial damage and repair (By similarity).

By similarity1 Publication

Acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter.

Acts as a negative regulator, inhibiting both ATF2 and ATF7 transcriptional activities. It may exert these effects by sequestrating in the cytoplasm the Thr-53 phosphorylating kinase, preventing activation.

1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri7 – 31C2H2-typePROSITE-ProRule annotationAdd BLAST25

<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
Biological processHost-virus interaction, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P17544

SIGNOR Signaling Network Open Resource

More...SIGNORi		P17544

<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-7
Short name:
cAMP-dependent transcription factor ATF-7
Alternative name(s):
Activating transcription factor 7
Transcription factor ATF-A
<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:ATF7
Synonyms:ATFA
<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 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:792, ATF7

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		606371, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P17544

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000170653.18

<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

Chromosome, Cytoplasm, Nucleus, Telomere

<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>Mutagenesisi9C → A: Severely reduced TAF12-mediated enhancement of transcriptional activity. 1 Publication1
Mutagenesisi14C → A: Greatly reduced JNK2- or adenovirus E1A-mediated transactivation. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-51; A-53 and G-101. 1 Publication1
Mutagenesisi22D → K: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. 1 Publication1
Mutagenesisi27H → N: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. 1 Publication1
Mutagenesisi33M → D: Severely reduced TAF12-induced transcriptional activity; when associated with S-35. 1 Publication1
Mutagenesisi35L → S: Severely reduced TAF12-induced transcriptional activity; when associated with D-33. 1 Publication1
Mutagenesisi51T → A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-53. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-53 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-53 and G-101. 3 Publications1
Mutagenesisi51T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53. 3 Publications1
Mutagenesisi53T → A: Severely reduced TAF12-induced transcriptional activity. No effect on MAPK9-mediated phosphorylation; when associated with A-51. Greatly reduces MAPK9- and adenovirus E1A-mediated transactivation; when associated with A-51 and G-101. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and G-101. 3 Publications1
Mutagenesisi53T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51. 3 Publications1
Mutagenesisi101T → G: Some reduction in transactivation but, completely abolishes MAPK9-mediated activation. Abolishes MAPK9-mediated and greatly reduces adenovirus E1A-mediated transactivation; when associated with A-51 and A-53. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and A-53. 2 Publications1
Mutagenesisi107K → R: Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter. 1 Publication1
Mutagenesisi145T → A: No effect on transactivation; when associated with A-147. 1 Publication1
Mutagenesisi147T → A: No effect on transactivation; when associated with A-145. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		11016

Open Targets

More...OpenTargetsi		ENSG00000170653

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA25092

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P17544, 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		ATF7

Domain mapping of disease mutations (DMDM)

More...DMDMi		12643393

<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_00000765921 – 483Cyclic AMP-dependent transcription factor ATF-7Add BLAST483

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 residuei51Phosphothreonine; by MAPK111 Publication1
Modified residuei53Phosphothreonine1 Publication1
Modified residuei101Phosphothreonine1 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-linki107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)2 Publications
Modified residuei413PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1

<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

On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity.1 Publication
Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase.
On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity (PubMed:18950637). Social isolation stress as well as TNF-alpha also induce the phosphorylation of ATF7 (PubMed:29490055). Phosphorylated in proliferating colonic and small intestinal epithelial cells (By similarity).By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P17544

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17544

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P17544

MaxQB - The MaxQuant DataBase

More...MaxQBi		P17544

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

More...PaxDbi		P17544

PeptideAtlas

More...PeptideAtlasi		P17544

PRoteomics IDEntifications database

More...PRIDEi		P17544

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53487 [P17544-1]
53488 [P17544-2]
53489 [P17544-3]
53490 [P17544-4]
53491 [P17544-5]
53492 [P17544-6]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P17544, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17544

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

More...PhosphoSitePlusi		P17544

<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

Expressed in various tissues including heart, brain, placenta, lung and skeletal muscle. Highest levels in skeletal muscle. Lowest in lung and placenta.1 Publication
Strongly expressed in skeletal muscle. Also expressed at lower levels in heart and lung.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000170653, Expressed in sural nerve and 207 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P17544, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17544, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000170653, 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

Homodimer; binds DNA as homodimer. Heterodimer; heterodimerizes with other members of ATF family and with JUN family members.

Interacts with JNK2; the interaction does not phosphorylate ATF7 but acts as a docking site for other ATF-associated partners such as JUN family members.

Interacts (via its transactivation domain) with TAF12 (isoforms TAFII15 and TAFII20); the interaction potentiates the transactivation activity (isoform TAFII20 only) and is inhibited by ATF7 sumoylation.

Interacts with TAF4; the interaction inhibits the TAF12-dependent transactivation.

Interacts with MAPK9; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN.

Interacts with Ku complex components XRCC6 and XRCC7 (PubMed:29490055).

Interacts with TERT (PubMed:29490055).

7 Publications

(Microbial infection) Interacts with adenovirus 2 E1A; the interaction enhances the ATF7-mediated viral transactivation activity which requires the zinc-binding domains of both E1A and ATF7.

2 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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		116206, 48 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P17544

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P17544

Protein interaction database and analysis system

More...IntActi		P17544, 37 interactors

Molecular INTeraction database

More...MINTi		P17544

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000399465

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P17544, 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

3D structure databases

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

More...SMRi		P17544

Database of comparative protein structure models

More...ModBasei		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>Domaini332 – 395bZIPPROSITE-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>Regioni1 – 285Transactivation domainAdd BLAST285
Regioni110 – 148DisorderedSequence analysisAdd BLAST39
Regioni299 – 345DisorderedSequence analysisAdd BLAST47
Regioni325 – 483Essential for binding adenovirus 2 E1AAdd BLAST159
Regioni334 – 354Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni360 – 388Leucine-zipperPROSITE-ProRule annotationAdd BLAST29
Regioni407 – 439DisorderedSequence analysisAdd BLAST33

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 biasi322 – 345Basic and acidic residuesSequence analysisAdd BLAST24

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri7 – 31C2H2-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1414, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155261

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021564_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17544

Identification of Orthologs from Complete Genome Data

More...OMAi		TELSMPM

Database of Orthologous Groups

More...OrthoDBi		978850at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17544

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004827, bZIP
IPR016378, TF_CRE-BP1-typ
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF003153, ATF2_CRE-BP1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00338, BRLZ, 1 hit
SM00355, ZnF_C2H2, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57667, SSF57667, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50217, BZIP, 1 hit
PS00036, BZIP_BASIC, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 1 hit
PS50157, ZINC_FINGER_C2H2_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%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>Sequences (6+)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 describes 6 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P17544-6) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ 
        60         70         80         90        100
TPTPTRFLKN CEEVGLFNEL ASSFEHEFKK AADEDEKKAA AGPLDMSLPS 
       110        120        130        140        150
TPDIKIKEEE PVEVDSSPPD SPASSPCSPP LKEKEVTPKP VLISTPTPTI 
       160        170        180        190        200
VRPGSLPLHL GYDPLHPTLP SPTSVITQAP PSNRQMGSPT GSLPLVMHLA 
       210        220        230        240        250
NGQTMPVLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN SSGSISPSGH 
       260        270        280        290        300
PIPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQSQILIQHP 
       310        320        330        340        350
DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR 
       360        370        380        390        400
QKRKLWVSSL EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV 
       410        420        430        440        450
TALQKKTQGY LESPKESSEP TGSPAPVIQH SSATAPSNGL SVRSAAEAVA 
       460        470        480 
TSVLTQMASQ RTELSMPIQS HVIMTPQSQS AGR
Length:483
Mass (Da):51,757
Last modified:October 7, 2020 - 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:i07080BC24FED635B
GO
Isoform 6 (identifier: P17544-1) [UniParc]FASTAAdd to basket
Also known as: ATF-A1

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: K → KARSRTVAKKLV

Show »
Length:494
Mass (Da):52,967
Checksum:i511EAF79C6503300
GO
Isoform 2 (identifier: P17544-2) [UniParc]FASTAAdd to basket
Also known as: ATF-A

The sequence of this isoform differs from the canonical sequence as follows:
     114-134: Missing.

Show »
Length:462
Mass (Da):49,650
Checksum:i92AB6DF8D2A954CD
GO
Isoform 3 (identifier: P17544-3) [UniParc]FASTAAdd to basket
Also known as: ATF-A-delta

The sequence of this isoform differs from the canonical sequence as follows:
     88-88: K → KARSRTVAKKLV
     114-134: Missing.

Show »
Length:473
Mass (Da):50,860
Checksum:i6CB9C4D7A0128AA9
GO
Isoform 4 (identifier: P17544-4) [UniParc]FASTAAdd to basket
Also known as: ATF-A0

The sequence of this isoform differs from the canonical sequence as follows:
     135-310: Missing.

Show »
Length:307
Mass (Da):33,681
Checksum:i01665BFA649C6CA1
GO
Isoform 5 (identifier: P17544-5) [UniParc]FASTAAdd to basket
Also known as: ATF-4

The sequence of this isoform differs from the canonical sequence as follows:
     89-117: AAAGPLDMSLPSTPDIKIKEEEPVEVDSS → ARSRTVAKKLVVFRPRLFLLCFGIIFLIG
     118-483: Missing.

Show »
Length:117
Mass (Da):13,278
Checksum:i15298D193695ACED
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7ESA4K7ESA4_HUMAN
Cyclic AMP-dependent transcription ...
ATF7
163Annotation 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>
F8VWG7F8VWG7_HUMAN
Cyclic AMP-dependent transcription ...
ATF7
78Annotation 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>
K7EKZ7K7EKZ7_HUMAN
Cyclic AMP-dependent transcription ...
ATF7
79Annotation 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 conflicti12P → T in AAH42363 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_06069788K → KARSRTVAKKLV in isoform 6 and isoform 3. Curated1
Alternative sequenceiVSP_06069889 – 117AAAGP…EVDSS → ARSRTVAKKLVVFRPRLFLL CFGIIFLIG in isoform 5. CuratedAdd BLAST29
Alternative sequenceiVSP_060699114 – 134Missing in isoform 2 and isoform 3. CuratedAdd BLAST21
Alternative sequenceiVSP_060700118 – 483Missing in isoform 5. CuratedAdd BLAST366
Alternative sequenceiVSP_060701135 – 310Missing in isoform 4. CuratedAdd BLAST176

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
X52943 mRNA Translation: CAA37118.1
X57197 mRNA Translation: CAA40483.1
AK298853 mRNA Translation: BAG60976.1
AC023509 Genomic DNA No translation available.
AC073594 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW96723.1
CH471054 Genomic DNA Translation: EAW96724.1
BC042363 mRNA Translation: AAH42363.1
BC136302 mRNA Translation: AAI36303.1
BC140006 mRNA Translation: AAI40007.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44906.1 [P17544-6]
CCDS58238.1 [P17544-5]

Protein sequence database of the Protein Information Resource

More...PIRi		S12741

NCBI Reference Sequences

More...RefSeqi		NP_001123532.1, NM_001130060.1 [P17544-2]
NP_001193611.1, NM_001206682.1 [P17544-5]
NP_001193612.1, NM_001206683.1 [P17544-5]
NP_006847.1, NM_006856.2 [P17544-6]
XP_005268644.1, XM_005268587.3
XP_016874211.1, XM_017018722.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000420353; ENSP00000399465; ENSG00000170653 [P17544-6]
ENST00000456903; ENSP00000387406; ENSG00000170653 [P17544-6]
ENST00000548118; ENSP00000456858; ENSG00000170653 [P17544-5]
ENST00000548446; ENSP00000449938; ENSG00000170653 [P17544-1]
ENST00000591397; ENSP00000465192; ENSG00000170653 [P17544-5]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		11016

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:11016

UCSC genome browser

More...UCSCi		uc001sdz.4, human [P17544-6]

Keywords - Coding sequence diversityi

Alternative splicing

<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
X52943 mRNA Translation: CAA37118.1
X57197 mRNA Translation: CAA40483.1
AK298853 mRNA Translation: BAG60976.1
AC023509 Genomic DNA No translation available.
AC073594 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW96723.1
CH471054 Genomic DNA Translation: EAW96724.1
BC042363 mRNA Translation: AAH42363.1
BC136302 mRNA Translation: AAI36303.1
BC140006 mRNA Translation: AAI40007.1
CCDSiCCDS44906.1 [P17544-6]
CCDS58238.1 [P17544-5]
PIRiS12741
RefSeqiNP_001123532.1, NM_001130060.1 [P17544-2]
NP_001193611.1, NM_001206682.1 [P17544-5]
NP_001193612.1, NM_001206683.1 [P17544-5]
NP_006847.1, NM_006856.2 [P17544-6]
XP_005268644.1, XM_005268587.3
XP_016874211.1, XM_017018722.1

3D structure databases

SMRiP17544
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi116206, 48 interactors
CORUMiP17544
ELMiP17544
IntActiP17544, 37 interactors
MINTiP17544
STRINGi9606.ENSP00000399465

Chemistry databases

DrugBankiDB00852, Pseudoephedrine

PTM databases

GlyGeniP17544, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP17544
PhosphoSitePlusiP17544

Genetic variation databases

BioMutaiATF7
DMDMi12643393

Proteomic databases

EPDiP17544
jPOSTiP17544
MassIVEiP17544
MaxQBiP17544
PaxDbiP17544
PeptideAtlasiP17544
PRIDEiP17544
ProteomicsDBi53487 [P17544-1]
53488 [P17544-2]
53489 [P17544-3]
53490 [P17544-4]
53491 [P17544-5]
53492 [P17544-6]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P17544, 6 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		931, 279 antibodies

The DNASU plasmid repository

More...DNASUi		11016

Genome annotation databases

EnsembliENST00000420353; ENSP00000399465; ENSG00000170653 [P17544-6]
ENST00000456903; ENSP00000387406; ENSG00000170653 [P17544-6]
ENST00000548118; ENSP00000456858; ENSG00000170653 [P17544-5]
ENST00000548446; ENSP00000449938; ENSG00000170653 [P17544-1]
ENST00000591397; ENSP00000465192; ENSG00000170653 [P17544-5]
GeneIDi11016
KEGGihsa:11016
UCSCiuc001sdz.4, human [P17544-6]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		11016
DisGeNETi11016

GeneCards: human genes, protein and diseases

More...GeneCardsi		ATF7
HGNCiHGNC:792, ATF7
HPAiENSG00000170653, Low tissue specificity
MIMi606371, gene
neXtProtiNX_P17544
OpenTargetsiENSG00000170653
PharmGKBiPA25092
VEuPathDBiHostDB:ENSG00000170653.18

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1414, Eukaryota
GeneTreeiENSGT00940000155261
HOGENOMiCLU_021564_0_0_1
InParanoidiP17544
OMAiTELSMPM
OrthoDBi978850at2759
PhylomeDBiP17544

Enzyme and pathway databases

PathwayCommonsiP17544
SIGNORiP17544

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		11016, 26 hits in 1015 CRISPR screens

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

More...ChiTaRSi		ATF7, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ATF7

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

More...GenomeRNAii		11016
PharosiP17544, Tbio

Protein Ontology

More...PROi		PR:P17544
RNActiP17544, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000170653, Expressed in sural nerve and 207 other tissues
ExpressionAtlasiP17544, baseline and differential
GenevisibleiP17544, HS

Family and domain databases

InterProiView protein in InterPro
IPR004827, bZIP
IPR016378, TF_CRE-BP1-typ
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type
PfamiView protein in Pfam
PF00170, bZIP_1, 1 hit
PIRSFiPIRSF003153, ATF2_CRE-BP1, 1 hit
SMARTiView protein in SMART
SM00338, BRLZ, 1 hit
SM00355, ZnF_C2H2, 1 hit
SUPFAMiSSF57667, SSF57667, 1 hit
PROSITEiView protein in PROSITE
PS50217, BZIP, 1 hit
PS00036, BZIP_BASIC, 1 hit
PS00028, ZINC_FINGER_C2H2_1, 1 hit
PS50157, ZINC_FINGER_C2H2_2, 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 nameiATF7_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: P17544
Secondary accession number(s): A5D6Y4
, B2RMP1, B4DQL4, Q13814, Q8IVR8, Q9UD83
<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: August 1, 1990
Last sequence update: October 7, 2020
Last modified: June 2, 2021
This is version 211 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

Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
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