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P18848

- ATF4_HUMAN

UniProt

P18848 - ATF4_HUMAN

Protein

Cyclic AMP-dependent transcription factor ATF-4

Gene

ATF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production By similarity. It binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to ER stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes.By similarity3 Publications

    GO - Molecular functioni

    1. core promoter sequence-specific DNA binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular amino acid metabolic process Source: UniProtKB
    3. cellular protein metabolic process Source: Reactome
    4. circadian regulation of gene expression Source: UniProtKB
    5. endoplasmic reticulum unfolded protein response Source: Reactome
    6. gamma-aminobutyric acid signaling pathway Source: Ensembl
    7. gluconeogenesis Source: UniProtKB
    8. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    9. negative regulation of potassium ion transport Source: Ensembl
    10. positive regulation of neuron apoptotic process Source: UniProtKB
    11. positive regulation of transcription, DNA-templated Source: UniProtKB
    12. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    13. regulation of transcription, DNA-templated Source: UniProtKB
    14. response to endoplasmic reticulum stress Source: BHF-UCL
    15. transcription from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18277. PERK regulates gene expression.
    REACT_18355. ATF4 activates genes.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP-dependent transcription factor ATF-4
    Short name:
    cAMP-dependent transcription factor ATF-4
    Alternative name(s):
    Activating transcription factor 4
    Cyclic AMP-responsive element-binding protein 2
    Short name:
    CREB-2
    Short name:
    cAMP-responsive element-binding protein 2
    DNA-binding protein TAXREB67
    Tax-responsive enhancer element-binding protein 67
    Short name:
    TaxREB67
    Gene namesi
    Name:ATF4
    Synonyms:CREB2, TXREB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:786. ATF4.

    Subcellular locationi

    Cytoplasm. Cell membrane. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Colocalizes with GABBR1 in hippocampal neuron dendritic membranes By similarity. Co- localizes with NEK6 in the centrosome.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. dendrite membrane Source: Ensembl
    3. microtubule organizing center Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25086.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Cyclic AMP-dependent transcription factor ATF-4PRO_0000076584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei213 – 2131PhosphothreonineBy similarity
    Modified residuei219 – 2191PhosphoserineBy similarity
    Modified residuei224 – 2241PhosphoserineBy similarity
    Modified residuei231 – 2311PhosphoserineBy similarity
    Modified residuei235 – 2351PhosphoserineBy similarity
    Modified residuei248 – 2481PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated by SCF(BTRC) in response to mTORC1 signal, followed by proteasomal degradation and leading to down-regulate expression of SIRT4.By similarity
    Phosphorylated by NEK6 By similarity. Phosphorylated on the betaTrCP degron motif at Ser-219, followed by phosphorylation at Thr-213, Ser-224, Ser-231, Ser-235 and Ser-248, promoting interaction with BTRC and ubiquitination. Phosphorylation is promoted by mTORC1 By similarity.By similarity
    Phosphorylated by NEK6.1 Publication

    Keywords - PTMi

    Lipoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP18848.
    PaxDbiP18848.
    PRIDEiP18848.

    PTM databases

    PhosphoSiteiP18848.

    Expressioni

    Gene expression databases

    BgeeiP18848.
    CleanExiHS_ATF4.
    GenevestigatoriP18848.

    Organism-specific databases

    HPAiCAB011596.
    HPA036934.

    Interactioni

    Subunit structurei

    Binds DNA as a homo- or heterodimer. Interacts (via its leucine zipper domain) with GABBR1 and GABBR2 (via their C-termini). Interacts (via its DNA binding domain) with FOXO1 (C-terminal half); the interaction occurs in osteoblasts and regulates glucose homeostasis through suppression of beta-cell proliferation and a decrease in insulin production. Interacts with SATB2; the interaction results in enhanced DNA binding and transactivation by these transcription factors By similarity. Interacts with CEP290 (via an N-terminal region). Interacts with NEK6, DAPK2 (isoform 2) and ZIPK/DAPK3. Forms a heterodimer with TXLNG in osteoblasts. Interacts with DDIT3/CHOP.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTRCQ9Y2974EBI-492498,EBI-307461
    BTRCQ9Y297-25EBI-492498,EBI-8826333
    CREBZFQ9NS375EBI-492498,EBI-632965
    DISC1Q9NRI53EBI-492498,EBI-529989
    JUNP054122EBI-492498,EBI-852823
    TRIB3Q96RU72EBI-492498,EBI-492476

    Protein-protein interaction databases

    BioGridi106958. 66 interactions.
    DIPiDIP-207N.
    DIP-354N.
    IntActiP18848. 25 interactions.
    MINTiMINT-146610.
    STRINGi9606.ENSP00000336790.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi288 – 34053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CI6X-ray2.60A280-341[»]
    ProteinModelPortaliP18848.
    SMRiP18848. Positions 286-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18848.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini278 – 34164bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni280 – 30021Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni305 – 34137Interaction with GABBR1By similarityAdd
    BLAST
    Regioni306 – 33429Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili280 – 34061Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi215 – 22410BetaTrCP degron motif

    Domaini

    The BetaTrCP degron motif promotes binding to BTRC when phosphorylated.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG325856.
    HOGENOMiHOG000004844.
    HOVERGENiHBG004301.
    InParanoidiP18848.
    KOiK04374.
    OMAiGECRELE.
    OrthoDBiEOG72JWGW.
    PhylomeDBiP18848.
    TreeFamiTF316136.

    Family and domain databases

    InterProiIPR004827. bZIP.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P18848-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEMSFLSSE VLVGDLMSPF DQSGLGAEES LGLLDDYLEV AKHFKPHGFS    50
    SDKAKAGSSE WLAVDGLVSP SNNSKEDAFS GTDWMLEKMD LKEFDLDALL 100
    GIDDLETMPD DLLTTLDDTC DLFAPLVQET NKQPPQTVNP IGHLPESLTK 150
    PDQVAPFTFL QPLPLSPGVL SSTPDHSFSL ELGSEVDITE GDRKPDYTAY 200
    VAMIPQCIKE EDTPSDNDSG ICMSPESYLG SPQHSPSTRG SPNRSLPSPG 250
    VLCGSARPKP YDPPGEKMVA AKVKGEKLDK KLKKMEQNKT AATRYRQKKR 300
    AEQEALTGEC KELEKKNEAL KERADSLAKE IQYLKDLIEE VRKARGKKRV 350
    P 351
    Length:351
    Mass (Da):38,590
    Last modified:October 17, 2006 - v3
    Checksum:i3BBB7379DC3B0D07
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti284 – 2841K → R no nucleotide entry (PubMed:2516827)Curated
    Sequence conflicti290 – 2901T → R no nucleotide entry (PubMed:2516827)Curated
    Sequence conflicti329 – 3313KEI → REK no nucleotide entry (PubMed:2516827)Curated
    Sequence conflicti338 – 3381I → L no nucleotide entry (PubMed:2516827)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221Q → P.3 Publications
    Corresponds to variant rs4894 [ dbSNP | Ensembl ].
    VAR_028253
    Natural varianti258 – 2581P → A.
    Corresponds to variant rs1803323 [ dbSNP | Ensembl ].
    VAR_029259
    Natural varianti322 – 3221E → D.
    Corresponds to variant rs1803324 [ dbSNP | Ensembl ].
    VAR_014768

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90209 mRNA. Translation: BAA14234.1.
    M86842 mRNA. Translation: AAA52071.1.
    AL022312 Genomic DNA. Translation: CAB45284.1.
    BC008090 mRNA. Translation: AAH08090.1.
    BC011994 mRNA. Translation: AAH11994.1.
    BC024775 mRNA. Translation: AAH24775.1.
    BC073990 mRNA. Translation: AAH73990.1.
    CCDSiCCDS13996.1.
    PIRiA45377.
    RefSeqiNP_001666.2. NM_001675.4.
    NP_877962.1. NM_182810.2.
    UniGeneiHs.496487.

    Genome annotation databases

    EnsembliENST00000337304; ENSP00000336790; ENSG00000128272.
    ENST00000396680; ENSP00000379912; ENSG00000128272.
    ENST00000404241; ENSP00000384587; ENSG00000128272.
    GeneIDi468.
    KEGGihsa:468.
    UCSCiuc003axz.3. human.

    Polymorphism databases

    DMDMi116241262.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90209 mRNA. Translation: BAA14234.1 .
    M86842 mRNA. Translation: AAA52071.1 .
    AL022312 Genomic DNA. Translation: CAB45284.1 .
    BC008090 mRNA. Translation: AAH08090.1 .
    BC011994 mRNA. Translation: AAH11994.1 .
    BC024775 mRNA. Translation: AAH24775.1 .
    BC073990 mRNA. Translation: AAH73990.1 .
    CCDSi CCDS13996.1.
    PIRi A45377.
    RefSeqi NP_001666.2. NM_001675.4.
    NP_877962.1. NM_182810.2.
    UniGenei Hs.496487.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CI6 X-ray 2.60 A 280-341 [» ]
    ProteinModelPortali P18848.
    SMRi P18848. Positions 286-341.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106958. 66 interactions.
    DIPi DIP-207N.
    DIP-354N.
    IntActi P18848. 25 interactions.
    MINTi MINT-146610.
    STRINGi 9606.ENSP00000336790.

    Chemistry

    DrugBanki DB00852. Pseudoephedrine.

    PTM databases

    PhosphoSitei P18848.

    Polymorphism databases

    DMDMi 116241262.

    Proteomic databases

    MaxQBi P18848.
    PaxDbi P18848.
    PRIDEi P18848.

    Protocols and materials databases

    DNASUi 468.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337304 ; ENSP00000336790 ; ENSG00000128272 .
    ENST00000396680 ; ENSP00000379912 ; ENSG00000128272 .
    ENST00000404241 ; ENSP00000384587 ; ENSG00000128272 .
    GeneIDi 468.
    KEGGi hsa:468.
    UCSCi uc003axz.3. human.

    Organism-specific databases

    CTDi 468.
    GeneCardsi GC22P039916.
    HGNCi HGNC:786. ATF4.
    HPAi CAB011596.
    HPA036934.
    MIMi 604064. gene.
    neXtProti NX_P18848.
    PharmGKBi PA25086.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325856.
    HOGENOMi HOG000004844.
    HOVERGENi HBG004301.
    InParanoidi P18848.
    KOi K04374.
    OMAi GECRELE.
    OrthoDBi EOG72JWGW.
    PhylomeDBi P18848.
    TreeFami TF316136.

    Enzyme and pathway databases

    Reactomei REACT_18277. PERK regulates gene expression.
    REACT_18355. ATF4 activates genes.
    REACT_18423. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi ATF4. human.
    EvolutionaryTracei P18848.
    GeneWikii ATF4.
    GenomeRNAii 468.
    NextBioi 1935.
    PROi P18848.
    SOURCEi Search...

    Gene expression databases

    Bgeei P18848.
    CleanExi HS_ATF4.
    Genevestigatori P18848.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I."
      Tsujimoto A., Nyunoya H., Morita T., Sato T., Shimotohno K.
      J. Virol. 65:1420-1426(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-22.
      Tissue: Fibroblast.
    2. "Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element."
      Karpinski B.A., Morle G.D., Huggenvik J., Uhler M.D., Leiden J.M.
      Proc. Natl. Acad. Sci. U.S.A. 89:4820-4824(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-22.
      Tissue: Leukemic T-cell.
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT PRO-22.
      Tissue: Lung and Placenta.
    5. "Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers."
      Hai T., Liu F., Coukos W.J., Green M.R.
      Genes Dev. 3:2083-2090(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 274-341.
    6. Erratum
      Hai T., Liu F., Coukos W.J., Green M.R.
      Genes Dev. 4:682-682(1990)
    7. "TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death."
      Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.
      EMBO J. 24:1243-1255(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "FIAT represses ATF4-mediated transcription to regulate bone mass in transgenic mice."
      Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J., Gauthier C., Roughley P.J., St-Arnaud R.
      J. Cell Biol. 169:591-601(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXLNG.
    9. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CEP290.
    10. "C/EBP homology protein (CHOP) interacts with activating transcription factor 4 (ATF4) and negatively regulates the stress-dependent induction of the asparagine synthetase gene."
      Su N., Kilberg M.S.
      J. Biol. Chem. 283:35106-35117(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DDIT3.
    11. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
      Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
      J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "New modularity of DAP-kinases: alternative splicing of the DRP-1 gene produces a ZIPk-like isoform."
      Shoval Y., Berissi H., Kimchi A., Pietrokovski S.
      PLoS ONE 6:E17344-E17344(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAPK2 AND ZIPK/DAPK3.
    14. "Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA."
      Podust L.M., Krezel A.M., Kim Y.
      J. Biol. Chem. 276:505-513(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 279-341 IN COMPLEX WITH MOUSE CEBPB.

    Entry informationi

    Entry nameiATF4_HUMAN
    AccessioniPrimary (citable) accession number: P18848
    Secondary accession number(s): Q9UH31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3