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P17544

- ATF7_HUMAN

UniProt

P17544 - ATF7_HUMAN

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
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    5. sequence-specific DNA binding Source: InterPro
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. 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

    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-SubCell
    2. nuclear periphery Source: UniProtKB
    3. nucleoplasm Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB

    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

    ArrayExpressiP17544.
    BgeeiP17544.
    CleanExiHS_ATF7.
    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. 15 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.
    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

    MGDDRPFVCN APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RTDSVIIADQ    50
    TPTPTRFLKN CEEVGLFNEL ASSFEHEFKK AADEDEKKAR SRTVAKKLVA 100
    AAGPLDMSLP STPDIKIKEE EPVEVDSSPP DSPASSPCSP PLKEKEVTPK 150
    PVLISTPTPT IVRPGSLPLH LGYDPLHPTL PSPTSVITQA PPSNRQMGSP 200
    TGSLPLVMHL ANGQTMPVLP GPPVQMPSVI SLARPVSMVP NIPGIPGPPV 250
    NSSGSISPSG HPIPSEAKMR LKATLTHQVS SINGGCGMVV GTASTMVTAR 300
    PEQSQILIQH PDAPSPAQPQ VSPAQPTPST GGRRRRTVDE DPDERRQRFL 350
    ERNRAAASRC RQKRKLWVSS LEKKAEELTS QNIQLSNEVT LLRNEVAQLK 400
    QLLLAHKDCP VTALQKKTQG YLESPKESSE PTGSPAPVIQ HSSATAPSNG 450
    LSVRSAAEAV ATSVLTQMAS QRTELSMPIQ SHVIMTPQSQ SAGR 494
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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. 15 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.
    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

    ArrayExpressi P17544.
    Bgeei P17544.
    CleanExi HS_ATF7.
    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

    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 1, 2014
    This is version 152 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