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UniProtKB/Swiss-Prot entry P18848


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATF4_HUMAN
Primary accession number P18848
Secondary accession number Q9UH31
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on October 17, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 104)
Name and origin of the protein
Protein name Cyclic AMP-dependent transcription factor ATF-4
Synonyms cAMP-dependent transcription factor ATF-4
Activating transcription factor 4
DNA-binding protein TAXREB67
Cyclic AMP-responsive element-binding protein 2
cAMP-responsive element-binding protein 2
CREB-2
Gene name
Name: ATF4
Synonyms: CREB2, TXREB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-22.
TISSUE=Fibroblast;
PubMed=1847461 [NCBI, ExPASy, EBI, Israel, Japan]
Tsujimoto A., Nyunoya H., Morita T., Sato T., Shimotohno K.;
"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.";
J. Virol. 65:1420-1426(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-22.
TISSUE=Leukemic T-cell;
DOI=10.1073/pnas.89.11.4820; PubMed=1534408 [NCBI, ExPASy, EBI, Israel, Japan]
Karpinski B.A., Morle G.D., Huggenvik J., Uhler M.D., Leiden J.M.;
"Molecular cloning of human CREB-2: an ATF/CREB transcription factor that can negatively regulate transcription from the cAMP response element.";
Proc. Natl. Acad. Sci. U.S.A. 89:4820-4824(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-22.
TISSUE=Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 274-341.
PubMed=2516827 [NCBI, ExPASy, EBI, Israel, Japan]
Hai T., Liu F., Coukos W.J., Green M.R.;
"Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers.";
Genes Dev. 3:2083-2090(1989).
[6]
ERRATUM.
Hai T., Liu F., Coukos W.J., Green M.R.;
Genes Dev. 4:682-682(1990).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP290.
DOI=10.1038/ng1786; PubMed=16682973 [NCBI, ExPASy, EBI, Israel, Japan]
Sayer J.A., Otto E.A., O'toole J.F., Nurnberg G., Kennedy M.A., Becker C., Hennies H.C., Helou J., Attanasio M., Fausett B.V., Utsch B., Khanna H., Liu Y., Drummond I., Kawakami I., Kusakabe T., Tsuda M., Ma L., Lee H., Larson R.G., Allen S.J., Wilkinson C.J., Nigg E.A., Shou C., Lillo C., Williams D.S., Hoppe B., Kemper M.J., Neuhaus T., Parisi M.A., Glass I.A., Petry M., Kispert A., Gloy J., Ganner A., Walz G., Zhu X., Goldman D., Nurnberg P., Swaroop A., Leroux M.R., Hildebrandt F.;
"The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and activates transcription factor ATF4.";
Nat. Genet. 38:674-681(2006).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 279-341 IN COMPLEX WITH MOUSE CEBPB.
DOI=10.1074/jbc.M005594200; PubMed=11018027 [NCBI, ExPASy, EBI, Israel, Japan]
Podust L.M., Krezel A.M., Kim Y.;
"Crystal structure of the CCAAT box/enhancer-binding protein beta activating transcription factor-4 basic leucine zipper heterodimer in the absence of DNA.";
J. Biol. Chem. 276:505-513(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D90209; BAA14234.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M86842; AAA52071.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022312; CAB45284.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008090; AAH08090.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011994; AAH11994.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024775; AAH24775.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073990; AAH73990.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00002503; -.
PIR A45377; A45377.
RefSeq NP_001666.2; -.
NP_877962.1; -.
UniGene Hs.496487
3D structure databases
PDB
1CI6; X-ray; 2.60 A; A=280-341.[ExPASy / RCSB / EBI]
PDBsum 1CI6; -.
ModBase P18848.
Protein-protein interaction databases
DIP DIP:207N; -.
DIP:354N; -.
IntAct P18848; 6.
PTM databases
PhosphoSite P18848; -.
Organism-specific databases
GeneCards GC17M071736; -.
GC22P038241; -.
HGNC HGNC:786; ATF4.
GenAtlas ATF4.
MIM 604064; gene. [NCBI / EBI]
PharmGKB PA25086; -.
Gene expression databases
ArrayExpress P18848; -.
Bgee P18848; -.
CleanEx HS_ATF4; -.
GermOnline ENSG00000128272; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from electronic annotation from InterPro).
GO:0003704; Molecular function: specific RNA polymerase II transcription factor activity (inferred from sequence or structural similarity from UniProtKB).
GO:0016563; Molecular function: transcription activator activity (inferred from mutant phenotype from UniProtKB).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from UniProtKB).
GO:0006520; Biological process: cellular amino acid metabolic process (traceable author statement from UniProtKB).
GO:0006094; Biological process: gluconeogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0045944; Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from UniProtKB).
GO:0006950; Biological process: response to stress (inferred from expression pattern from UniProtKB).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR004827; TF_bZIP.
Graphical view of domain structure.
Pfam PF00170; bZIP_1; 1.
Pfam graphical view of domain structure.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P18848; -.
Genome annotation databases
Ensembl ENSG00000128272; Homo sapiens. [Contig view]
GeneID 468; -.
KEGG hsa:468; -.
Phylogenomic databases
HOGENOM P18848; -.
HOVERGEN P18848; -.
OMA P18848; SYLGSPQ.
Other
NextBio 1935; -.
SOURCE ATF4; Homo sapiens.
ProtoNet P18848.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Cell membrane; Coiled coil; Cytoplasm; DNA-binding; Membrane; Nucleus; Polymorphism; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   351  351     Cyclic AMP-dependent transcription factor ATF-4. PRO_0000076584
DOMAIN   306   334  29     Leucine-zipper. 
DNA_BIND   280   300  21     Basic motif. 
REGION   305   341  37     Interaction with GABBR1 (By similarity). 
COILED   280   340  61      
VARIANT   22    22  1     Q -> P (in dbSNP:rs4894 [NCBI]). VAR_028253 
VARIANT   258   258  1     P -> A (in dbSNP:rs1803323 [NCBI]). VAR_029259 
VARIANT   322   322  1     E -> D (in dbSNP:rs1803324 [NCBI]). VAR_014768 
CONFLICT   284   284        K -> R (in Ref. 2). 
CONFLICT   290   290        T -> R (in Ref. 5). 
CONFLICT   329   331        KEI -> REK (in Ref. 5). 
CONFLICT   338   338        I -> L (in Ref. 5). 
HELIX   288   340  53      
Sequence information
Length: 351 AA [This is the length of the unprocessed precursor] Molecular weight: 38590 Da [This is the MW of the unprocessed precursor] CRC64: 3BBB7379DC3B0D07 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTEMSFLSSE VLVGDLMSPF DQSGLGAEES LGLLDDYLEV AKHFKPHGFS SDKAKAGSSE 

        70         80         90        100        110        120 
WLAVDGLVSP SNNSKEDAFS GTDWMLEKMD LKEFDLDALL GIDDLETMPD DLLTTLDDTC 

       130        140        150        160        170        180 
DLFAPLVQET NKQPPQTVNP IGHLPESLTK PDQVAPFTFL QPLPLSPGVL SSTPDHSFSL 

       190        200        210        220        230        240 
ELGSEVDITE GDRKPDYTAY VAMIPQCIKE EDTPSDNDSG ICMSPESYLG SPQHSPSTRG 

       250        260        270        280        290        300 
SPNRSLPSPG VLCGSARPKP YDPPGEKMVA AKVKGEKLDK KLKKMEQNKT AATRYRQKKR 

       310        320        330        340        350 
AEQEALTGEC KELEKKNEAL KERADSLAKE IQYLKDLIEE VRKARGKKRV P 

P18848 in FASTA format

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