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P17544

- ATF7_HUMAN

UniProt

P17544 - ATF7_HUMAN

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Protein

Cyclic AMP-dependent transcription factor ATF-7

Gene

ATF7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.
Isoform 4/ATF-A0 acts as a dominant repressor of the E-selectin/NF-ELAM1/delta-A promoter.
Isoform 5/ATF-4 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. enzyme binding Source: UniProt
  2. metal ion binding Source: UniProtKB-KW
  3. mitogen-activated protein kinase binding Source: UniProtKB
  4. sequence-specific DNA binding Source: InterPro
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB
  2. transcription, DNA-templated Source: UniProtKB-KW
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, 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
Synonyms:ATFA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:792. ATF7.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation. Nucleusnucleoplasm 1 Publication
Note: Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuclear periphery.
Isoform 5 : Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear periphery Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → A: Severely reduced TAF12-mediated enhancement of transcriptional activity. 1 Publication
Mutagenesisi14 – 141C → A: Greatly reduced JNK2- or adenovirus E1A-mediated transactivation. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-51; A-53 and G-112. 1 Publication
Mutagenesisi22 – 221D → K: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. 1 Publication
Mutagenesisi27 – 271H → N: No effect on binding adenovirus 2 E1A. Abolishes ATF7-mediated E1A responsiveness. 1 Publication
Mutagenesisi33 – 331M → D: Severely reduced TAF12-induced transcriptional activity; when associated with S-35. 1 Publication
Mutagenesisi35 – 351L → S: Severely reduced TAF12-induced transcriptional activity; when associated with D-33. 1 Publication
Mutagenesisi51 – 511T → 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-112. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-53 and G-112. 3 Publications
Mutagenesisi51 – 511T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-53. 3 Publications
Mutagenesisi53 – 531T → 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-112. Abolishes adenovirus 2 E1A-mediated transactivation; when associated with A-14; A-51 and G-112. 3 Publications
Mutagenesisi53 – 531T → D: Completely abolishes MAPK9- and adenovirus E1A-mediated transactivation; when associated with D-51. 3 Publications
Mutagenesisi112 – 1121T → 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 Publications
Mutagenesisi118 – 1181K → R: Abolishes sumoylation. Exclusive nucleoplasmic location. Increase in binding the E-selectin promoter. 1 Publication
Mutagenesisi156 – 1561T → A: No effect on transactivation; when associated with A-158. 1 Publication
Mutagenesisi158 – 1581T → A: No effect on transactivation; when associated with A-156. 1 Publication

Organism-specific databases

PharmGKBiPA25092.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Cyclic AMP-dependent transcription factor ATF-7PRO_0000076592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511Phosphothreonine; by MAPK111 Publication
Modified residuei53 – 531Phosphothreonine1 Publication
Modified residuei112 – 1121Phosphothreonine1 Publication
Cross-linki118 – 118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
Modified residuei424 – 4241Phosphoserine1 Publication

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.2 Publications
Sumoylation delays nuclear localization and inhibits transactivation activity through preventing binding to TAF12. RANBP2 appears to be the specific E3 ligase.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17544.
PaxDbiP17544.
PRIDEiP17544.

PTM databases

PhosphoSiteiP17544.

Expressioni

Tissue specificityi

Expressed in heart, lung and skeletal muscle. Isoform 4 is expressed in various tissues including heart, brain, placenta, lung and skeletal muscle. Highest levels in skeletal muscle. Lowest in lung and placenta.1 Publication

Gene expression databases

BgeeiP17544.
CleanExiHS_ATF7.
ExpressionAtlasiP17544. baseline and differential.
GenevestigatoriP17544.

Organism-specific databases

HPAiHPA003384.

Interactioni

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 adenovirus 2 E1A; the interaction enhances the ATF7-mediated viral transactivation activity which requires the zinc-binding domains of both E1A and ATF7. Interacts with MAPK9; the interaction does not phosphorylate ATF7 but acts as a docking site for ATF7-associated partners such as JUN.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OCIAD1Q9NX402EBI-765623,EBI-2683029

Protein-protein interaction databases

BioGridi116206. 19 interactions.
IntActiP17544. 9 interactions.
MINTiMINT-194321.
STRINGi9606.ENSP00000329212.

Structurei

3D structure databases

ProteinModelPortaliP17544.
SMRiP17544. Positions 1-38, 345-405.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini343 – 40664bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 296296Transactivation domainAdd
BLAST
Regioni336 – 494159Essential for binding adenovirus 2 E1AAdd
BLAST
Regioni345 – 36521Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni371 – 39929Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri7 – 3125C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG306955.
GeneTreeiENSGT00390000020106.
HOGENOMiHOG000220894.
HOVERGENiHBG004300.
InParanoidiP17544.
KOiK09045.
OMAiTPDVKIK.
PhylomeDBiP17544.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR004827. bZIP.
IPR016378. TF_cAMP-dep.
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]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 3 (identifier: P17544-1) [UniParc]FASTAAdd to Basket

Also known as: ATF-A1

This isoform has been chosen as the 'canonical' 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 AADEDEKKAR SRTVAKKLVA
110 120 130 140 150
AAGPLDMSLP STPDIKIKEE EPVEVDSSPP DSPASSPCSP PLKEKEVTPK
160 170 180 190 200
PVLISTPTPT IVRPGSLPLH LGYDPLHPTL PSPTSVITQA PPSNRQMGSP
210 220 230 240 250
TGSLPLVMHL ANGQTMPVLP GPPVQMPSVI SLARPVSMVP NIPGIPGPPV
260 270 280 290 300
NSSGSISPSG HPIPSEAKMR LKATLTHQVS SINGGCGMVV GTASTMVTAR
310 320 330 340 350
PEQSQILIQH PDAPSPAQPQ VSPAQPTPST GGRRRRTVDE DPDERRQRFL
360 370 380 390 400
ERNRAAASRC RQKRKLWVSS LEKKAEELTS QNIQLSNEVT LLRNEVAQLK
410 420 430 440 450
QLLLAHKDCP VTALQKKTQG YLESPKESSE PTGSPAPVIQ HSSATAPSNG
460 470 480 490
LSVRSAAEAV ATSVLTQMAS QRTELSMPIQ SHVIMTPQSQ SAGR
Length:494
Mass (Da):52,967
Last modified:January 24, 2001 - v2
Checksum:i511EAF79C6503300
GO
Isoform 1 (identifier: P17544-2) [UniParc]FASTAAdd to Basket

Also known as: ATF-A

The sequence of this isoform differs from the canonical sequence as follows:
     89-99: Missing.
     125-145: Missing.

Show »
Length:462
Mass (Da):49,650
Checksum:i92AB6DF8D2A954CD
GO
Isoform 2 (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:
     125-145: 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:
     89-99: Missing.
     146-321: 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:
     100-494: AAAGPLDMSL...MTPQSQSAGR → VFRPRLFLLCFGIIFLIG

Show »
Length:117
Mass (Da):13,278
Checksum:i15298D193695ACED
GO
Isoform 6 (identifier: P17544-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     89-99: Missing.

Note: No experimental confirmation available.

Show »
Length:483
Mass (Da):51,757
Checksum:i07080BC24FED635B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → T in AAH42363. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 9911Missing in isoform 1, isoform 4 and isoform 6. 3 PublicationsVSP_000594Add
BLAST
Alternative sequencei100 – 494395AAAGP…QSAGR → VFRPRLFLLCFGIIFLIG in isoform 5. 1 PublicationVSP_042469Add
BLAST
Alternative sequencei125 – 14521Missing in isoform 1 and isoform 2. 1 PublicationVSP_000595Add
BLAST
Alternative sequencei146 – 321176Missing in isoform 4. 1 PublicationVSP_034543Add
BLAST

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_005268587.1. [P17544-6]
XP_006719265.1. XM_006719202.1. [P17544-6]
UniGeneiHs.12286.
Hs.633602.

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.3. human. [P17544-6]
uc001sea.4. human. [P17544-5]
uc010sol.2. human. [P17544-2]

Polymorphism databases

DMDMi12643393.

Keywords - Coding sequence diversityi

Alternative splicing

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 .
CCDSi CCDS44906.1. [P17544-6 ]
CCDS58238.1. [P17544-5 ]
PIRi S12741.
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_005268587.1. [P17544-6 ]
XP_006719265.1. XM_006719202.1. [P17544-6 ]
UniGenei Hs.12286.
Hs.633602.

3D structure databases

ProteinModelPortali P17544.
SMRi P17544. Positions 1-38, 345-405.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116206. 19 interactions.
IntActi P17544. 9 interactions.
MINTi MINT-194321.
STRINGi 9606.ENSP00000329212.

Chemistry

DrugBanki DB00852. Pseudoephedrine.

PTM databases

PhosphoSitei P17544.

Polymorphism databases

DMDMi 12643393.

Proteomic databases

MaxQBi P17544.
PaxDbi P17544.
PRIDEi P17544.

Protocols and materials databases

DNASUi 11016.
Structural Biology Knowledgebase Search...

Genome annotation databases

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 ]
GeneIDi 11016.
KEGGi hsa:11016.
UCSCi uc001sdz.3. human. [P17544-6 ]
uc001sea.4. human. [P17544-5 ]
uc010sol.2. human. [P17544-2 ]

Organism-specific databases

CTDi 11016.
GeneCardsi GC12M053905.
H-InvDB HIX0201838.
HGNCi HGNC:792. ATF7.
HPAi HPA003384.
MIMi 606371. gene.
neXtProti NX_P17544.
PharmGKBi PA25092.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306955.
GeneTreei ENSGT00390000020106.
HOGENOMi HOG000220894.
HOVERGENi HBG004300.
InParanoidi P17544.
KOi K09045.
OMAi TPDVKIK.
PhylomeDBi P17544.

Miscellaneous databases

ChiTaRSi ATF7. human.
GeneWikii ATF7.
GenomeRNAii 11016.
NextBioi 41853.
PROi P17544.
SOURCEi Search...

Gene expression databases

Bgeei P17544.
CleanExi HS_ATF7.
ExpressionAtlasi P17544. baseline and differential.
Genevestigatori P17544.

Family and domain databases

Gene3Di 3.30.160.60. 1 hit.
InterProi IPR004827. bZIP.
IPR016378. TF_cAMP-dep.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00170. bZIP_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF003153. ATF2_CRE-BP1. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells."
    Gaire M., Chatton B., Kedinger C.
    Nucleic Acids Res. 18:3467-3473(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cervix carcinoma.
  2. "ATF-a1, a new member of the human ATF family."
    Chatton B., Gaire M., Goetz J., Hauss C., Kedinger C.
    Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "ATF-a0, a novel variant of the ATF/CREB transcription factor family, forms a dominant transcription inhibitor in ATF-a heterodimers."
    Pescini R., Kaszubska W., Whelan J., DeLamarter J.F., Hooft van Huijsduijnen R.
    J. Biol. Chem. 269:1159-1165(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, SUBUNIT.
    Tissue: Cervix carcinoma.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
    Tissue: Brain and Colon.
  8. "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity."
    Hai T., Curran T.
    Proc. Natl. Acad. Sci. U.S.A. 88:3720-3724(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
  9. "Transcriptional activation by the adenovirus larger E1a product is mediated by members of the cellular transcription factor ATF family which can directly associate with E1a."
    Chatton B., Bocco J.L., Gaire M., Hauss C., Reimund B., Goetz J., Kedinger C.
    Mol. Cell. Biol. 13:561-570(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ADENOVIRUS 2 E1A, ZINC-BINDING, MUTAGENESIS OF ASP-22 AND HIS-27.
  10. "Jun and Fos heterodimerize with ATFa, a member of the ATF/CREB family and modulate its transcriptional activity."
    Chatton B., Bocco J.L., Goetz J., Gaire M., Lutz Y., Kedinger C.
    Oncogene 9:375-385(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, FUNCTION.
  11. Cited for: INTERACTION WITH JUN; MAPK9 AND HUMAN ADENOVIRUS 2 E1A, SUBUNIT, FUNCTION, MUTAGENESIS OF CYS-14; THR-51; THR-53; THR-112; THR-156 AND THR-158.
  12. "A functional interaction between ATF7 and TAF12 that is modulated by TAF4."
    Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., Chatton B.
    Oncogene 24:3472-3483(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF4 AND TAF12, FUNCTION, TRANSACTIVATION DOMAIN, MUTAGENESIS OF CYS-9; MET-33; LEU-35; THR-51 AND THR-53.
  13. "Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity."
    Hamard P.J., Boyer-Guittaut M., Camuzeaux B., Dujardin D., Hauss C., Oelgeschlager T., Vigneron M., Kedinger C., Chatton B.
    Nucleic Acids Res. 35:1134-1144(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-118, SUBCELLULAR LOCATION, INTERACTION WITH TAF12, FUNCTION.
  14. "p38beta2-mediated phosphorylation and sumoylation of ATF7 are mutually exclusive."
    Camuzeaux B., Diring J., Hamard P.J., Oulad-Abdelghani M., Donzeau M., Vigneron M., Kedinger C., Chatton B.
    J. Mol. Biol. 384:980-991(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-51; THR-53 AND THR-112, SUMOYLATION AT LYS-118, FUNCTION, MUTAGENESIS OF THR-51; THR-53; THR-112 AND LYS-118.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and ATF2 phosphorylation and transcriptional activity."
    Diring J., Camuzeaux B., Donzeau M., Vigneron M., Rosa-Calatrava M., Kedinger C., Chatton B.
    PLoS ONE 6:E23351-E23351(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5).
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATF7_HUMAN
AccessioniPrimary (citable) accession number: P17544
Secondary accession number(s): A5D6Y4
, B2RMP1, B4DQL4, Q13814, Q8IVR8, Q9UD83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 24, 2001
Last modified: October 29, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

External Data

Dasty 3