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Protein

Cyclic AMP-dependent transcription factor ATF-7

Gene

Atf7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays important functions in early cell signaling. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3'), a sequence present in many viral and cellular promoters. Activator of the NF-ELAM1/delta-A site of the E-selectin promoter. Has no intrinsic transcriptional activity, but activates transcription on formation of JUN or FOS heterodimers. Also can bind TRE promoter sequences when heterodimerized with members of the JUN family (By similarity).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

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
Gene namesi
Name:Atf7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2443472. Atf7.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Nucleusnucleoplasm By similarity

  • Note: Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear peiphery (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765931 – 413Cyclic AMP-dependent transcription factor ATF-7Add BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei51Phosphothreonine; by MAPK11By similarity1
Modified residuei53PhosphothreonineBy similarity1
Modified residuei101PhosphothreonineBy similarity1
Cross-linki107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

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 (By similarity).By similarity
Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8R0S1.
MaxQBiQ8R0S1.
PaxDbiQ8R0S1.
PRIDEiQ8R0S1.

PTM databases

iPTMnetiQ8R0S1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000099083.
CleanExiMM_ATF7.
ExpressionAtlasiQ8R0S1. baseline and differential.
GenevisibleiQ8R0S1. MM.

Interactioni

Subunit structurei

Homodimer; binds DNA as homodimer (By similarity). Heterodimer; heterodimerizes with other members of ATF family and with JUN family members (By similarity). 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 the interaction potentiates the transactivation activity 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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230215. 2 interactors.
IntActiQ8R0S1. 1 interactor.
MINTiMINT-7557949.
STRINGi10090.ENSMUSP00000104456.

Structurei

3D structure databases

ProteinModelPortaliQ8R0S1.
SMRiQ8R0S1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini332 – 395bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 285Transactivation domainBy similarityAdd BLAST285
Regioni334 – 354Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni360 – 388Leucine-zipperPROSITE-ProRule annotationAdd BLAST29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi118 – 253Pro-richAdd BLAST136
Compositional biasi322 – 325Poly-Arg4

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation
Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOVERGENiHBG004300.
InParanoidiQ8R0S1.
PhylomeDBiQ8R0S1.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR004827. bZIP.
IPR016378. TF_CRE-BP1-typ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8R0S1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDDRPFVCS APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ
60 70 80 90 100
TPTPTRFLKN CEEVGLFNEL ASSFEHEFKK ASDDDEKKGA AGPLDMSLPS
110 120 130 140 150
TPDIKIKEEE PVEVDSSPPD SPASSPCSPP LKEKEVTTKP VVISTPTPTI
160 170 180 190 200
VRPGSLPLHL GYDPLHPTLP SPTSVITQAP PSNRQIGSPT GSLPLVMHLA
210 220 230 240 250
NGQTMPMLPG PPVQMPSVIS LARPVSMVPN IPGIPGPPVN NSGSISPSGH
260 270 280 290 300
PMPSEAKMRL KATLTHQVSS INGGCGMVVG TASTMVTARP EQNQILIQHP
310 320 330 340 350
DAPSPAQPQV SPAQPTPSTG GRRRRTVDED PDERRQRFLE RNRAAASRCR
360 370 380 390 400
QKRKLWVSSL EKKAEELTSQ NIQLSNEVTL LRNEVAQLKQ LLLAHKDCPV
410
TALQKKTQGY LGK
Length:413
Mass (Da):44,608
Last modified:June 1, 2002 - v1
Checksum:iAFF4D1A7BFE71AF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026483 mRNA. Translation: AAH26483.1.
UniGeneiMm.208714.
Mm.475149.

Genome annotation databases

EnsembliENSMUST00000108828; ENSMUSP00000104456; ENSMUSG00000099083.
ENSMUST00000169033; ENSMUSP00000130130; ENSMUSG00000099083.
UCSCiuc007xwo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC026483 mRNA. Translation: AAH26483.1.
UniGeneiMm.208714.
Mm.475149.

3D structure databases

ProteinModelPortaliQ8R0S1.
SMRiQ8R0S1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230215. 2 interactors.
IntActiQ8R0S1. 1 interactor.
MINTiMINT-7557949.
STRINGi10090.ENSMUSP00000104456.

PTM databases

iPTMnetiQ8R0S1.

Proteomic databases

EPDiQ8R0S1.
MaxQBiQ8R0S1.
PaxDbiQ8R0S1.
PRIDEiQ8R0S1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108828; ENSMUSP00000104456; ENSMUSG00000099083.
ENSMUST00000169033; ENSMUSP00000130130; ENSMUSG00000099083.
UCSCiuc007xwo.1. mouse.

Organism-specific databases

MGIiMGI:2443472. Atf7.

Phylogenomic databases

eggNOGiKOG1414. Eukaryota.
ENOG4111CH5. LUCA.
GeneTreeiENSGT00390000020106.
HOVERGENiHBG004300.
InParanoidiQ8R0S1.
PhylomeDBiQ8R0S1.

Miscellaneous databases

ChiTaRSiAtf7. mouse.
PROiQ8R0S1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000099083.
CleanExiMM_ATF7.
ExpressionAtlasiQ8R0S1. baseline and differential.
GenevisibleiQ8R0S1. MM.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR004827. bZIP.
IPR016378. TF_CRE-BP1-typ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATF7_MOUSE
AccessioniPrimary (citable) accession number: Q8R0S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.