Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cyclic AMP-dependent transcription factor ATF-4 (cAMP-dependent transcription factor ATF-4) (Activating transcription factor 4) (Cyclic AMP-responsive element-binding protein 2) (CREB-2) (cAMP-responsive element-binding protein 2) (DNA-binding protein TAXREB67) (Tax-responsive enhancer element-binding protein 67) (TaxREB67)

 ATF4_HUMAN              Reviewed;         351 AA.
P18848; Q96AQ3; Q9UH31;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
22-NOV-2017, entry version 196.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-4;
Short=cAMP-dependent transcription factor ATF-4;
AltName: Full=Activating transcription factor 4;
AltName: Full=Cyclic AMP-responsive element-binding protein 2;
Short=CREB-2;
Short=cAMP-responsive element-binding protein 2;
AltName: Full=DNA-binding protein TAXREB67;
AltName: Full=Tax-responsive enhancer element-binding protein 67;
Short=TaxREB67;
Name=ATF4; Synonyms=CREB2, TXREB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-22.
TISSUE=Fibroblast;
PubMed=1847461;
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;
PubMed=1534408; DOI=10.1073/pnas.89.11.4820;
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 MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-22.
TISSUE=Colon, Lung, Placenta, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 274-341.
PubMed=2516827; DOI=10.1101/gad.3.12b.2083;
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).
[8]
ERRATUM.
Hai T., Liu F., Coukos W.J., Green M.R.;
Genes Dev. 4:682-682(1990).
[9]
FUNCTION.
PubMed=15775988; DOI=10.1038/sj.emboj.7600596;
Ohoka N., Yoshii S., Hattori T., Onozaki K., Hayashi H.;
"TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP
pathway and is involved in cell death.";
EMBO J. 24:1243-1255(2005).
[10]
INTERACTION WITH TXLNG.
PubMed=15911876; DOI=10.1083/jcb.200412139;
Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J.,
Gauthier C., Roughley P.J., St-Arnaud R.;
"FIAT represses ATF4-mediated transcription to regulate bone mass in
transgenic mice.";
J. Cell Biol. 169:591-601(2005).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP290.
PubMed=16682973; DOI=10.1038/ng1786;
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).
[12]
FUNCTION, AND INTERACTION WITH DDIT3.
PubMed=18940792; DOI=10.1074/jbc.M806874200;
Su N., Kilberg M.S.;
"C/EBP homology protein (CHOP) interacts with activating transcription
factor 4 (ATF4) and negatively regulates the stress-dependent
induction of the asparagine synthetase gene.";
J. Biol. Chem. 283:35106-35117(2008).
[13]
SUBCELLULAR LOCATION, INTERACTION WITH NEK6, AND PHOSPHORYLATION.
PubMed=20873783; DOI=10.1021/pr100562w;
Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C.,
Santana Bernachi J., Paes Leme A.F., Kobarg J.;
"Characterization of hNek6 interactome reveals an important role for
its short N-terminal domain and colocalization with proteins at the
centrosome.";
J. Proteome Res. 9:6298-6316(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
INTERACTION WITH DAPK2 AND ZIPK/DAPK3.
PubMed=21408167; DOI=10.1371/journal.pone.0017344;
Shoval Y., Berissi H., Kimchi A., Pietrokovski S.;
"New modularity of DAP-kinases: alternative splicing of the DRP-1 gene
produces a ZIPk-like isoform.";
PLoS ONE 6:E17344-E17344(2011).
[16]
INTERACTION WITH ABRAXAS2, AND SUBCELLULAR LOCATION.
PubMed=22974638; DOI=10.1016/j.bbamcr.2012.08.020;
Ambivero C.T., Cilenti L., Zervos A.S.;
"ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates
in a cytoprotective pathway.";
Biochim. Biophys. Acta 1823:2149-2156(2012).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
FUNCTION.
PubMed=26086088; DOI=10.1371/journal.pone.0130635;
D'Osualdo A., Anania V.G., Yu K., Lill J.R., Kaufman R.J.,
Matsuzawa S., Reed J.C.;
"Transcription factor ATF4 induces NLRP1 inflammasome expression
during endoplasmic reticulum stress.";
PLoS ONE 10:E0130635-E0130635(2015).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-259; LYS-267 AND
LYS-272, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 279-341 IN COMPLEX WITH MOUSE
CEBPB, INTERACTION WITH CEBPB, AND DNA-BINDING.
PubMed=11018027; DOI=10.1074/jbc.M005594200;
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).
-!- FUNCTION: 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 endoplasmic reticulum (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. During ER stress response,
activates the transcription of NLRP1, possibly in concert with
other factors (PubMed:26086088). {ECO:0000250,
ECO:0000269|PubMed:15775988, ECO:0000269|PubMed:16682973,
ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:26086088}.
-!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
(PubMed:11018027). Interacts with CEBPB and binds DNA as a
heterodimer with CEBPB (PubMed:11018027). 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)
(PubMed:16682973). Interacts with NEK6, DAPK2 (isoform 2) and
ZIPK/DAPK3 (PubMed:20873783, PubMed:21408167). Forms a heterodimer
with TXLNG in osteoblasts (PubMed:15911876). Interacts with
DDIT3/CHOP (PubMed:18940792). Interacts with ABRAXAS2
(PubMed:22974638). {ECO:0000250|UniProtKB:Q06507,
ECO:0000250|UniProtKB:Q9ES19, ECO:0000269|PubMed:11018027,
ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:16682973,
ECO:0000269|PubMed:18940792, ECO:0000269|PubMed:20873783,
ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:22974638}.
-!- INTERACTION:
P18847:ATF3; NbExp=7; IntAct=EBI-492498, EBI-712767;
Q13515:BFSP2; NbExp=8; IntAct=EBI-492498, EBI-10229433;
Q9Y297:BTRC; NbExp=12; IntAct=EBI-492498, EBI-307461;
Q9Y297-2:BTRC; NbExp=5; IntAct=EBI-492498, EBI-8826333;
Q9BWC9:CCDC106; NbExp=9; IntAct=EBI-492498, EBI-711501;
P49715:CEBPA; NbExp=2; IntAct=EBI-492498, EBI-1172054;
P17676:CEBPB; NbExp=2; IntAct=EBI-492498, EBI-969696;
P49716:CEBPD; NbExp=2; IntAct=EBI-492498, EBI-7962058;
P53567:CEBPG; NbExp=10; IntAct=EBI-492498, EBI-740209;
Q9NS37:CREBZF; NbExp=6; IntAct=EBI-492498, EBI-632965;
Q9UIK4-2:DAPK2; NbExp=2; IntAct=EBI-492498, EBI-9693115;
O54784:Dapk3 (xeno); NbExp=2; IntAct=EBI-492498, EBI-77359;
P35638:DDIT3; NbExp=3; IntAct=EBI-492498, EBI-742651;
Q9NRI5:DISC1; NbExp=3; IntAct=EBI-492498, EBI-529989;
P01100:FOS; NbExp=3; IntAct=EBI-492498, EBI-852851;
Q96CN9:GCC1; NbExp=5; IntAct=EBI-492498, EBI-746252;
Q92805:GOLGA1; NbExp=8; IntAct=EBI-492498, EBI-6164177;
Q0D2H9:GOLGA8DP; NbExp=5; IntAct=EBI-492498, EBI-10181276;
Q08AF8:GOLGA8G; NbExp=6; IntAct=EBI-492498, EBI-10181260;
Q08AF8-2:GOLGA8G; NbExp=4; IntAct=EBI-492498, EBI-11956781;
Q13227:GPS2; NbExp=9; IntAct=EBI-492498, EBI-713355;
Q99871:HAUS7; NbExp=3; IntAct=EBI-492498, EBI-395719;
P05412:JUN; NbExp=2; IntAct=EBI-492498, EBI-852823;
O95751:LDOC1; NbExp=7; IntAct=EBI-492498, EBI-740738;
O14777:NDC80; NbExp=5; IntAct=EBI-492498, EBI-715849;
P19387:POLR2C; NbExp=6; IntAct=EBI-492498, EBI-394729;
Q86UD0:SAPCD2; NbExp=4; IntAct=EBI-492498, EBI-2561646;
Q96RU7:TRIB3; NbExp=14; IntAct=EBI-492498, EBI-492476;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ES19}.
Cell membrane {ECO:0000250|UniProtKB:Q9ES19}. Nucleus
{ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:22974638}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:20873783}. Note=Colocalizes with GABBR1 in
hippocampal neuron dendritic membranes (By similarity).
Colocalizes with NEK6 at the centrosome (PubMed:20873783).
{ECO:0000250|UniProtKB:Q9ES19, ECO:0000269|PubMed:20873783}.
-!- DOMAIN: The BetaTrCP degron motif promotes binding to BTRC when
phosphorylated. {ECO:0000250}.
-!- PTM: Ubiquitinated by SCF(BTRC) in response to mTORC1 signal,
followed by proteasomal degradation and leading to down-regulate
expression of SIRT4. {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Phosphorylated by NEK6. {ECO:0000269|PubMed:20873783}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ATF4ID44413ch22q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D90209; BAA14234.1; -; mRNA.
EMBL; M86842; AAA52071.1; -; mRNA.
EMBL; CR456384; CAG30270.1; -; mRNA.
EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60341.1; -; Genomic_DNA.
EMBL; CH471095; EAW60342.1; -; Genomic_DNA.
EMBL; BC008090; AAH08090.1; -; mRNA.
EMBL; BC011994; AAH11994.1; -; mRNA.
EMBL; BC016855; AAH16855.1; -; mRNA.
EMBL; BC022088; AAH22088.1; -; mRNA.
EMBL; BC024775; AAH24775.1; -; mRNA.
EMBL; BC044895; AAH44895.1; -; mRNA.
EMBL; BC073754; AAH73754.1; -; mRNA.
EMBL; BC073990; AAH73990.1; -; mRNA.
CCDS; CCDS13996.1; -.
PIR; A45377; A45377.
RefSeq; NP_001666.2; NM_001675.4.
RefSeq; NP_877962.1; NM_182810.2.
RefSeq; XP_016884296.1; XM_017028807.1.
UniGene; Hs.496487; -.
PDB; 1CI6; X-ray; 2.60 A; A=280-341.
PDBsum; 1CI6; -.
ProteinModelPortal; P18848; -.
SMR; P18848; -.
BioGrid; 106958; 75.
CORUM; P18848; -.
DIP; DIP-354N; -.
ELM; P18848; -.
IntAct; P18848; 55.
MINT; MINT-146610; -.
STRING; 9606.ENSP00000336790; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; P18848; -.
PhosphoSitePlus; P18848; -.
BioMuta; ATF4; -.
DMDM; 116241262; -.
EPD; P18848; -.
PaxDb; P18848; -.
PeptideAtlas; P18848; -.
PRIDE; P18848; -.
DNASU; 468; -.
Ensembl; ENST00000337304; ENSP00000336790; ENSG00000128272.
Ensembl; ENST00000396680; ENSP00000379912; ENSG00000128272.
Ensembl; ENST00000404241; ENSP00000384587; ENSG00000128272.
GeneID; 468; -.
KEGG; hsa:468; -.
UCSC; uc003axz.4; human.
CTD; 468; -.
DisGeNET; 468; -.
EuPathDB; HostDB:ENSG00000128272.14; -.
GeneCards; ATF4; -.
HGNC; HGNC:786; ATF4.
HPA; CAB011596; -.
MIM; 604064; gene.
neXtProt; NX_P18848; -.
OpenTargets; ENSG00000128272; -.
PharmGKB; PA25086; -.
eggNOG; KOG4571; Eukaryota.
eggNOG; ENOG4111ZXT; LUCA.
GeneTree; ENSGT00530000063801; -.
HOGENOM; HOG000004844; -.
HOVERGEN; HBG004301; -.
InParanoid; P18848; -.
KO; K04374; -.
OMA; AFSGMDW; -.
OrthoDB; EOG091G0FNW; -.
PhylomeDB; P18848; -.
TreeFam; TF316136; -.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-381042; PERK regulates gene expression.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
SIGNOR; P18848; -.
ChiTaRS; ATF4; human.
EvolutionaryTrace; P18848; -.
GeneWiki; ATF4; -.
GenomeRNAi; 468; -.
PRO; PR:P18848; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000128272; -.
CleanEx; HS_ATF4; -.
ExpressionAtlas; P18848; baseline and differential.
Genevisible; P18848; HS.
GO; GO:1990590; C:ATF1-ATF4 transcription factor complex; IDA:ParkinsonsUK-UCL.
GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IDA:ParkinsonsUK-UCL.
GO; GO:1990617; C:CHOP-ATF4 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
GO; GO:1990037; C:Lewy body core; IDA:ParkinsonsUK-UCL.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
GO; GO:0034399; C:nuclear periphery; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0043522; F:leucine zipper domain binding; IDA:ParkinsonsUK-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; NAS:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001076; F:transcription factor activity, RNA polymerase II transcription factor binding; IC:ParkinsonsUK-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:UniProtKB.
GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
GO; GO:1903351; P:cellular response to dopamine; IMP:CAFA.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:ParkinsonsUK-UCL.
GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl.
GO; GO:0032057; P:negative regulation of translational initiation in response to stress; ISS:UniProtKB.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; IMP:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:0061395; P:positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; TAS:ParkinsonsUK-UCL.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IC:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:ParkinsonsUK-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:BHF-UCL.
GO; GO:1990737; P:response to manganese-induced endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISS:UniProtKB.
InterPro; IPR029811; ATF4.
InterPro; IPR004827; bZIP.
PANTHER; PTHR13044:SF2; PTHR13044:SF2; 1.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Activator; Biological rhythms; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding;
Isopeptide bond; Lipoprotein; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 351 Cyclic AMP-dependent transcription factor
ATF-4.
/FTId=PRO_0000076584.
DOMAIN 278 341 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 280 300 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 305 341 Interaction with GABBR1. {ECO:0000250}.
REGION 306 334 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COILED 280 340
MOTIF 215 224 BetaTrCP degron motif.
MOD_RES 213 213 Phosphothreonine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000250|UniProtKB:Q06507}.
CROSSLNK 53 53 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 259 259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 267 267 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 272 272 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 22 22 Q -> P (in dbSNP:rs4894).
{ECO:0000269|PubMed:1534408,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1847461}.
/FTId=VAR_028253.
VARIANT 258 258 P -> A (in dbSNP:rs1803323).
/FTId=VAR_029259.
VARIANT 322 322 E -> D (in dbSNP:rs1803324).
/FTId=VAR_014768.
CONFLICT 284 284 K -> R (in Ref. 7; no nucleotide entry).
{ECO:0000305}.
CONFLICT 290 290 T -> R (in Ref. 7; no nucleotide entry).
{ECO:0000305}.
CONFLICT 329 331 KEI -> REK (in Ref. 7; no nucleotide
entry). {ECO:0000305}.
CONFLICT 338 338 I -> L (in Ref. 7; no nucleotide entry).
{ECO:0000305}.
HELIX 288 340 {ECO:0000244|PDB:1CI6}.
SEQUENCE 351 AA; 38590 MW; 3BBB7379DC3B0D07 CRC64;
MTEMSFLSSE VLVGDLMSPF DQSGLGAEES LGLLDDYLEV AKHFKPHGFS SDKAKAGSSE
WLAVDGLVSP SNNSKEDAFS GTDWMLEKMD LKEFDLDALL GIDDLETMPD DLLTTLDDTC
DLFAPLVQET NKQPPQTVNP IGHLPESLTK PDQVAPFTFL QPLPLSPGVL SSTPDHSFSL
ELGSEVDITE GDRKPDYTAY VAMIPQCIKE EDTPSDNDSG ICMSPESYLG SPQHSPSTRG
SPNRSLPSPG VLCGSARPKP YDPPGEKMVA AKVKGEKLDK KLKKMEQNKT AATRYRQKKR
AEQEALTGEC KELEKKNEAL KERADSLAKE IQYLKDLIEE VRKARGKKRV P


Related products :

Catalog number Product name Quantity
EIAAB09243 cAMP-responsive element-binding protein 3-like protein 3,CREB3L3,CREBH,Cyclic AMP-responsive element-binding protein 3-like protein 3,Homo sapiens,Human,HYST1481,Transcription factor CREB-H
EIAAB09244 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Crebh,Cyclic AMP-responsive element-binding protein 3-like protein 3,Mouse,Mus musculus,Transcription factor CREB-H
EIAAB09242 cAMP-responsive element-binding protein 3-like protein 3,Creb3l3,Cyclic AMP-responsive element-binding protein 3-like protein 3,Rat,Rattus norvegicus,Transcription factor CREB-H
EIAAB09320 cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Homo sapiens,Human,Luman,LZIP,Transcription factor LZIP-alpha
EIAAB09319 cAMP-responsive element-binding protein 3,Creb3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Lzip,Mouse,Mus musculus,Transcription factor LZIP
18-003-44064 Cyclic AMP-dependent transcription factor ATF-4 - Activating transcription factor 4; DNA-binding protein TAXREB67; Cyclic AMP response element-binding protein 2; CREB2 Polyclonal 0.1 mg Protein A
U1318b CLIA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
E1318b ELISA kit Bos taurus,Bovine,cAMP-responsive element-binding protein 1,CREB,CREB1,CREB-1,CREB2,Cyclic AMP-responsive DNA-binding protein,Cyclic AMP-responsive element-binding protein 1 96T
EIAAB09321 cAMP-responsive element-binding protein 5,CREB5,CREB-5,CREBPA,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Homo sapiens,Human
E1318h ELISA kit cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
E1318h ELISA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
U1318h CLIA cAMP-responsive element-binding protein 1,CREB1,CREB-1,Cyclic AMP-responsive element-binding protein 1,Homo sapiens,Human 96T
EIAAB09318 Bos taurus,Bovine,cAMP-responsive element-binding protein 3,CREB3,CREB-3,Cyclic AMP-responsive element-binding protein 3,Luman
EIAAB09322 cAMP-responsive element-binding protein 5,Creb5,CREB-5,CRE-BPa,Cyclic AMP-responsive element-binding protein 5,Mouse,Mus musculus
U1318r CLIA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
U1318m CLIA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
E1318r ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
E1318m ELISA kit cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
E1318r ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Rat,Rattus norvegicus 96T
E1318m ELISA cAMP-responsive element-binding protein 1,Creb1,CREB-1,Creb-1,Cyclic AMP-responsive element-binding protein 1,Mouse,Mus musculus 96T
10-782-55004 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.2 mg
10-782-55004 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.05 mg
18-662-20064 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 Polyclonal 0.1 ml
18-003-42489 Cyclic AMP-dependent transcription factor ATF-2 - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 Polyclonal 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur