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P18848

- ATF4_HUMAN

UniProt

P18848 - ATF4_HUMAN

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Protein

Cyclic AMP-dependent transcription factor ATF-4

Gene
ATF4, CREB2, TXREB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 SIRT4.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. sequence-specific DNA binding Source: InterPro
  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. endoplasmic reticulum unfolded protein response Source: Reactome
  5. gamma-aminobutyric acid signaling pathway Source: Ensembl
  6. gluconeogenesis Source: UniProtKB
  7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  8. negative regulation of potassium ion transport Source: Ensembl
  9. positive regulation of neuron apoptotic process Source: UniProtKB
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. regulation of transcription, DNA-templated Source: UniProtKB
  13. response to endoplasmic reticulum stress Source: BHF-UCL
  14. transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

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.2 Publications

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
Complete GO annotation...

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 – 2131Phosphothreonine By similarity
Modified residuei219 – 2191Phosphoserine By similarity
Modified residuei224 – 2241Phosphoserine By similarity
Modified residuei231 – 2311Phosphoserine By similarity
Modified residuei235 – 2351Phosphoserine By similarity
Modified residuei248 – 2481Phosphoserine By 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.1 Publication
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.5 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106958. 66 interactions.
DIPiDIP-207N.
DIP-354N.
IntActiP18848. 23 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.

Miscellaneous databases

EvolutionaryTraceiP18848.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 34164bZIPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 30021Basic motif By similarityAdd
BLAST
Regioni305 – 34137Interaction with GABBR1 By similarityAdd
BLAST
Regioni306 – 33429Leucine-zipper By similarityAdd
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.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841K → R no nucleotide entry 1 Publication
Sequence conflicti290 – 2901T → R no nucleotide entry 1 Publication
Sequence conflicti329 – 3313KEI → REK no nucleotide entry 1 Publication
Sequence conflicti338 – 3381I → L no nucleotide entry 1 Publication

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. 23 interactions.
MINTi MINT-146610.
STRINGi 9606.ENSP00000336790.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 159 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

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