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-5 (cAMP-dependent transcription factor ATF-5) (Activating transcription factor 5) (Transcription factor ATFx)

 ATF5_HUMAN              Reviewed;         282 AA.
Q9Y2D1; B3KND3; Q9BSA1; Q9UNQ3;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
25-OCT-2017, entry version 154.
RecName: Full=Cyclic AMP-dependent transcription factor ATF-5;
Short=cAMP-dependent transcription factor ATF-5;
AltName: Full=Activating transcription factor 5;
AltName: Full=Transcription factor ATFx;
Name=ATF5; Synonyms=ATFX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=11087824; DOI=10.1073/pnas.240452197;
White J.H., McIllhinney R.A.J., Wise A., Ciruela F., Chan W.-Y.,
Emson P.C., Billinton A., Marshall F.H.;
"The GABAB receptor interacts directly with the related transcription
factors CREB2 and ATFx.";
Proc. Natl. Acad. Sci. U.S.A. 97:13967-13972(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-121.
TISSUE=Hepatoblastoma;
PubMed=15221005; DOI=10.1038/sj.onc.1207782;
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y.,
Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
Nakagawara A.;
"Expression profiling and differential screening between
hepatoblastomas and the corresponding normal livers: identification of
high expression of the PLK1 oncogene as a poor-prognostic indicator of
hepatoblastomas.";
Oncogene 23:5901-5911(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Kohroki J., Tanaka K.;
"cDNA clone encoding leucine-zipper protein.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-121.
TISSUE=Placenta;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 161-282, FUNCTION, AND UBIQUITINATION.
PubMed=10373550; DOI=10.1128/MCB.19.7.5001;
Pati D., Meistrich M.L., Plon S.E.;
"Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors
of cyclic AMP-induced transcription for proteolysis.";
Mol. Cell. Biol. 19:5001-5013(1999).
[9]
INTERACTION WITH CCND3, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15358120; DOI=10.1016/j.bbrc.2004.07.053;
Liu W., Sun M., Jiang J., Shen X., Sun Q., Liu W., Shen H., Gu J.;
"Cyclin D3 interacts with human activating transcription factor 5 and
potentiates its transcription activity.";
Biochem. Biophys. Res. Commun. 321:954-960(2004).
[10]
FUNCTION, AND DNA-BINDING.
PubMed=18701499; DOI=10.1158/0008-5472.CAN-07-6469;
Gho J.W., Ip W.K., Chan K.Y., Law P.T., Lai P.B., Wong N.;
"Re-expression of transcription factor ATF5 in hepatocellular
carcinoma induces G2-M arrest.";
Cancer Res. 68:6743-6751(2008).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18332083; DOI=10.1124/dmd.107.019380;
Pascual M., Gomez-Lechon M.J., Castell J.V., Jover R.;
"ATF5 is a highly abundant liver-enriched transcription factor that
cooperates with constitutive androstane receptor in the
transactivation of CYP2B6: implications in hepatic stress responses.";
Drug Metab. Dispos. 36:1063-1072(2008).
[12]
UBIQUITINATION, AND INDUCTION BY CISPLATIN.
PubMed=18458088; DOI=10.1074/jbc.M707879200;
Wei Y., Jiang J., Liu D., Zhou J., Chen X., Zhang S., Zong H., Yun X.,
Gu J.;
"Cdc34-mediated degradation of ATF5 is blocked by cisplatin.";
J. Biol. Chem. 283:18773-18781(2008).
[13]
FUNCTION.
PubMed=20654631; DOI=10.1016/j.lfs.2010.07.006;
Yamazaki T., Ohmi A., Kurumaya H., Kato K., Abe T., Yamamoto H.,
Nakanishi N., Okuyama R., Umemura M., Kaise T., Watanabe R., Okawa Y.,
Takahashi S., Takahashi Y.;
"Regulation of the human CHOP gene promoter by the stress response
transcription factor ATF5 via the AARE1 site in human hepatoma HepG2
cells.";
Life Sci. 87:294-301(2010).
[14]
FUNCTION, AND INDUCTION BY PRO-APOPTOTIC STIMULI.
PubMed=21212266; DOI=10.1074/jbc.M110.207639;
Dluzen D., Li G., Tacelosky D., Moreau M., Liu D.X.;
"BCL-2 is a downstream target of ATF5 that mediates the prosurvival
function of ATF5 in a cell type-dependent manner.";
J. Biol. Chem. 286:7705-7713(2011).
[15]
FUNCTION.
PubMed=21791614; DOI=10.1128/MCB.05887-11;
Liu D.X., Qian D., Wang B., Yang J.M., Lu Z.;
"p300-Dependent ATF5 acetylation is essential for Egr-1 gene
activation and cell proliferation and survival.";
Mol. Cell. Biol. 31:3906-3916(2011).
[16]
FUNCTION, INTERACTION WITH HSPA1A; HSPA1B AND NPM1, SUBCELLULAR
LOCATION, POLYUBIQUITINATION, AND MUTAGENESIS OF ASP-157.
PubMed=22528486; DOI=10.1074/jbc.M112.363622;
Liu X., Liu D., Qian D., Dai J., An Y., Jiang S., Stanley B., Yang J.,
Wang B., Liu X., Liu D.X.;
"Nucleophosmin (NPM1/B23) interacts with activating transcription
factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent
ATF5 degradation in hepatocellular carcinoma cells.";
J. Biol. Chem. 287:19599-19609(2012).
[17]
FUNCTION.
PubMed=22442021; DOI=10.1002/jcb.24150;
Leong D.T., Abraham M.C., Gupta A., Lim T.C., Chew F.T.,
Hutmacher D.W.;
"ATF5, a possible regulator of osteogenic differentiation in human
adipose-derived stem cells.";
J. Cell. Biochem. 113:2744-2753(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION, INDUCTION BY IL1B, INTERACTION WITH HSPA1A; HSPA1B AND NPM1,
AND MUTAGENESIS OF 3-LEU--VAL-25; 3-LEU-LEU-4; LEU-7; 9-LEU--LEU-11;
15-LEU-LEU-16 AND 21-LEU--VAL-25.
PubMed=24379400; DOI=10.1074/jbc.M113.491217;
Abe T., Kojima M., Akanuma S., Iwashita H., Yamazaki T., Okuyama R.,
Ichikawa K., Umemura M., Nakano H., Takahashi S., Takahashi Y.;
"N-terminal hydrophobic amino acids of activating transcription factor
5 (ATF5) protein confer interleukin 1beta (IL-1beta)-induced
stabilization.";
J. Biol. Chem. 289:3888-3900(2014).
[20]
FUNCTION.
PubMed=24216764; DOI=10.1128/MCB.00956-13;
Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F.,
Guo L., Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.;
"p300-dependent acetylation of activating transcription factor 5
enhances C/EBPbeta transactivation of C/EBPalpha during 3T3-L1
differentiation.";
Mol. Cell. Biol. 34:315-324(2014).
[21]
FUNCTION, INTERACTION WITH ALPHA-TUBULIN; GAMMA-TUBULIN; PCNT; TUBGCP2
AND TUBGCP4, AND SUBCELLULAR LOCATION.
PubMed=26213385; DOI=10.1016/j.cell.2015.06.055;
Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J.,
Liu X., Lu Z., Liu D.X.;
"ATF5 Connects the Pericentriolar Materials to the Proximal End of the
Mother Centriole.";
Cell 162:580-592(2015).
[22]
FUNCTION, INTERACTION WITH NLK, PHOSPHORYLATION, UBIQUITINATION, AND
MUTAGENESIS OF 92-SER--THR-94; SER-126 AND SER-190.
PubMed=25512613; DOI=10.1128/MCB.01228-14;
Zhang Z.Y., Li S.Z., Zhang H.H., Wu Q.R., Gong J., Liang T., Gao L.,
Xing N.N., Liu W.B., Du R.L., Zhang X.D.;
"Stabilization of ATF5 by TAK1-Nemo-like kinase critically regulates
the interleukin-1beta-stimulated C/EBP signaling pathway.";
Mol. Cell. Biol. 35:778-788(2015).
-!- FUNCTION: Transcription factor that either stimulates or represses
gene transcription through binding of different DNA regulatory
elements such as cAMP response element (CRE) (consensus: 5'-
GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE)
(consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid
response element (AARE), present in many viral and cellular
promoters. Critically involved, often in a cell type-dependent
manner, in cell survival, proliferation, and differentiation
(PubMed:10373550, PubMed:15358120, PubMed:21212266,
PubMed:20654631). Its transcriptional activity is enhanced by
CCND3 and slightly inhibited by CDK4 (PubMed:15358120). Important
regulator of the cerebral cortex formation, functions in cerebral
cortical neuroprogenitor cells to maintain proliferation and to
block differentiation into neurons. Must be down-regulated in
order for such cells to exit the cycle and differentiate (By
similarity). Participates in the pathways by which SHH promotes
cerebellar granule neuron progenitor cells proliferation (By
similarity). Critical for survival of mature olfactory sensory
neurons (OSN), directs expression of OSN-specific genes (By
similarity). May be involved in osteogenic differentiation
(PubMed:22442021). Promotes cell proliferation and survival by
inducing the expression of EGR1 sinergistically with ELK1. Once
acetylated by EP300, binds to ARE sequences on target genes
promoters, such as BCL2 and EGR1 (PubMed:21791614). Plays an anti-
apoptotic role through the transcriptional regulation of BCL2,
this function seems to be cell type-dependent (By similarity).
Cooperates with NR1I3/CAR in the transcriptional activation of
CYP2B6 in liver (PubMed:18332083). In hepatic cells, represses
CRE-dependent transcription and inhibits proliferation by blocking
at G2/M phase (PubMed:22528486, PubMed:18701499). May act as a
negative regulator of IL1B transduction pathway in liver
(PubMed:24379400). Upon IL1B stimulus, cooperates with NLK to
activate the transactivation activity of C/EBP subfamily members
(PubMed:25512613). Besides its function of transcription factor,
acts as a cofactor of CEBPB to activate CEBPA and promote
adipocyte differentiation (PubMed:24216764). Regulates centrosome
dynamics in a cell-cycle- and centriole-age-dependent manner.
Forms 9-foci symmetrical ring scaffold around the mother centriole
to control centrosome function and the interaction between
centrioles and pericentriolar material (PubMed:26213385).
{ECO:0000250|UniProtKB:O70191, ECO:0000250|UniProtKB:Q6P788,
ECO:0000269|PubMed:10373550, ECO:0000269|PubMed:15358120,
ECO:0000269|PubMed:18332083, ECO:0000269|PubMed:18701499,
ECO:0000269|PubMed:20654631, ECO:0000269|PubMed:21212266,
ECO:0000269|PubMed:21791614, ECO:0000269|PubMed:22442021,
ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:24216764,
ECO:0000269|PubMed:24379400, ECO:0000269|PubMed:25512613,
ECO:0000269|PubMed:26213385}.
-!- SUBUNIT: Binds DNA as a dimer. Interacts with PTP4A1/PRL-1 (By
similarity). Interacts with CCND3, but not with CCND1 or CCND2
(PubMed:15358120). Interacts with HSPA1A or HSPA1B; the
interaction protects ATF5 from degradation via proteasome-
dependent and caspase-dependent processes. Interacts (via C-
terminal region) with NPM1 (via C-terminal region); the
interaction leads to loss of association between HSPA1A or HSPA1B
and ATF5 and promotes ATF5 degradation via proteasome-dependent
and caspase-dependent processes (PubMed:22528486,
PubMed:24379400). Interacts with NLK; the interaction stabilizes
ATF5 at the protein level in a kinase-independent manner
(PubMed:25512613). Interacts with alpha-tubulin, gamma-tubulin
members TUBGCP2 and TUBGCP4, PCNT; the ATF5:PCNT:polyglutamylated
tubulin (PGT) tripartite unites the mother centriole and the
pericentriolar material (PCM) in the centrosome (PubMed:26213385).
Interacts with CEBPB and EP300; EP300 is required for ATF5 and
CEBPB interaction and DNA binding (By similarity).
{ECO:0000250|UniProtKB:O70191, ECO:0000269|PubMed:15358120,
ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:24379400,
ECO:0000269|PubMed:25512613, ECO:0000269|PubMed:26213385}.
-!- INTERACTION:
P53567:CEBPG; NbExp=4; IntAct=EBI-492509, EBI-740209;
Q9NRI5:DISC1; NbExp=8; IntAct=EBI-492509, EBI-529989;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15358120}.
Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
ECO:0000269|PubMed:15358120, ECO:0000269|PubMed:22528486}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:26213385}. Note=Actively transported to the
centrosome and accumulated in the pericentriolar material (PCM)
during G1 to M phase via a microtubule-dependent mechanism. During
late telophase and cytokinesis, translocates from the centrosome
to the midbody. {ECO:0000269|PubMed:26213385}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression levels
in liver. {ECO:0000269|PubMed:18332083}.
-!- INDUCTION: Down-regulated by pro-apoptotic stimuli
(PubMed:21212266). However, the pro-apoptotic cisplatin increases
protein levels by inhibiting polyubiquitination (PubMed:18458088).
IL1B increases protein levels through protein stabilization and
increase of translation efficiency (PubMed:24379400).
{ECO:0000269|PubMed:18458088, ECO:0000269|PubMed:21212266,
ECO:0000269|PubMed:24379400}.
-!- PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by
the proteasome. Cisplatin inhibits ubiquitination and proteasome-
mediated degradation by inhibiting the interaction with CDC34
(PubMed:18458088). Ubiquitination and degradation by the
proteasome are inhibited by NLK in a kinase-independent manner
(PubMed:25512613). {ECO:0000269|PubMed:10373550,
ECO:0000269|PubMed:18458088, ECO:0000269|PubMed:22528486,
ECO:0000269|PubMed:25512613}.
-!- PTM: Phosphorylated by NLK, probably at Ser-92, Thr-94, Ser-126
and Ser-190. {ECO:0000269|PubMed:25512613}.
-!- PTM: Acetylated at Lys-29 by EP300, the acetylation enhances the
interaction with CEBPB, DNA-binding and transactivation activity.
{ECO:0000250|UniProtKB:O70191, ECO:0000250|UniProtKB:Q6P788}.
-!- 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/ATF5ID50361ch19q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF305687; AAG22558.1; -; mRNA.
EMBL; AB073613; BAD38650.1; -; mRNA.
EMBL; AB021663; BAA78477.2; -; mRNA.
EMBL; AK024402; BAG51295.1; -; mRNA.
EMBL; AC011452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52581.1; -; Genomic_DNA.
EMBL; BC005174; AAH05174.1; -; mRNA.
EMBL; AF101388; AAD28370.1; -; mRNA.
CCDS; CCDS12789.1; -.
RefSeq; NP_001180575.1; NM_001193646.1.
RefSeq; NP_001277675.1; NM_001290746.1.
RefSeq; NP_036200.2; NM_012068.5.
RefSeq; XP_011524931.1; XM_011526629.2.
UniGene; Hs.9754; -.
ProteinModelPortal; Q9Y2D1; -.
SMR; Q9Y2D1; -.
BioGrid; 116487; 10.
IntAct; Q9Y2D1; 14.
STRING; 9606.ENSP00000396954; -.
DrugBank; DB00852; Pseudoephedrine.
iPTMnet; Q9Y2D1; -.
PhosphoSitePlus; Q9Y2D1; -.
BioMuta; ATF5; -.
DMDM; 308153647; -.
PaxDb; Q9Y2D1; -.
PeptideAtlas; Q9Y2D1; -.
PRIDE; Q9Y2D1; -.
TopDownProteomics; Q9Y2D1; -.
DNASU; 22809; -.
Ensembl; ENST00000423777; ENSP00000396954; ENSG00000169136.
Ensembl; ENST00000595125; ENSP00000470633; ENSG00000169136.
GeneID; 22809; -.
KEGG; hsa:22809; -.
UCSC; uc002prd.4; human.
CTD; 22809; -.
DisGeNET; 22809; -.
EuPathDB; HostDB:ENSG00000169136.8; -.
GeneCards; ATF5; -.
H-InvDB; HIX0015352; -.
HGNC; HGNC:790; ATF5.
HPA; HPA030187; -.
MIM; 606398; gene.
neXtProt; NX_Q9Y2D1; -.
OpenTargets; ENSG00000169136; -.
PharmGKB; PA25090; -.
eggNOG; KOG4571; Eukaryota.
eggNOG; ENOG4111ZXT; LUCA.
GeneTree; ENSGT00530000063801; -.
HOGENOM; HOG000004844; -.
HOVERGEN; HBG003535; -.
InParanoid; Q9Y2D1; -.
KO; K09044; -.
OMA; LAIYCRG; -.
OrthoDB; EOG091G0SPB; -.
PhylomeDB; Q9Y2D1; -.
TreeFam; TF316136; -.
SIGNOR; Q9Y2D1; -.
ChiTaRS; ATF5; human.
GeneWiki; ATF5; -.
GenomeRNAi; 22809; -.
PRO; PR:Q9Y2D1; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000169136; -.
CleanEx; HS_ATF5; -.
ExpressionAtlas; Q9Y2D1; baseline and differential.
Genevisible; Q9Y2D1; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0021930; P:cerebellar granule cell precursor proliferation; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0021891; P:olfactory bulb interneuron development; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0046605; P:regulation of centrosome cycle; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
InterPro; IPR029855; ATF-5.
InterPro; IPR004827; bZIP.
PANTHER; PTHR13044:SF3; PTHR13044:SF3; 3.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm; Cytoskeleton;
DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 282 Cyclic AMP-dependent transcription factor
ATF-5.
/FTId=PRO_0000076586.
DOMAIN 208 271 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 21 Required for protein stabilization
induced by IL1B.
{ECO:0000269|PubMed:24379400}.
REGION 119 217 Interaction with PTP4A1.
REGION 210 230 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 236 250 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
COMPBIAS 123 139 Poly-Pro.
COMPBIAS 186 194 Poly-Pro.
MOD_RES 29 29 N6-acetyllysine; by EP300.
{ECO:0000250|UniProtKB:O70191}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 121 121 P -> L (in dbSNP:rs283526).
{ECO:0000269|PubMed:15221005,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_022786.
MUTAGEN 3 25 LLATLGLELDRALLPASGLGWLV->AAATAGAEADRAAAPA
SGAGWAA: Highly increases protein levels.
No effect on protein stability enhanced
by IL1B. {ECO:0000269|PubMed:24379400}.
MUTAGEN 3 4 LL->AA: Increases protein levels. No
effect on protein stability enhanced by
IL1B. {ECO:0000269|PubMed:24379400}.
MUTAGEN 3 4 LL->II: Decreases protein levels.
{ECO:0000269|PubMed:24379400}.
MUTAGEN 3 4 LL->VV: No effect on protein levels. No
effect on protein stability enhanced by
IL1B. {ECO:0000269|PubMed:24379400}.
MUTAGEN 7 7 L->A: Increases protein levels.
{ECO:0000269|PubMed:24379400}.
MUTAGEN 9 11 LEL->AEA: Increases protein levels.
{ECO:0000269|PubMed:24379400}.
MUTAGEN 15 16 LL->AA: Increases protein levels.
{ECO:0000269|PubMed:24379400}.
MUTAGEN 21 25 LGWLV->AGWAA: Increases protein levels.
{ECO:0000269|PubMed:24379400}.
MUTAGEN 92 94 SPT->APA: Not phosphorylated; when
associated with A-126 and A-190.
MUTAGEN 126 126 S->A: Not phosphorylated; when associated
with 92-A--A-94 and A-190.
MUTAGEN 157 157 D->A: Resistant to cleavage by CASP3.
{ECO:0000269|PubMed:22528486}.
MUTAGEN 190 190 S->A: Not phosphorylated; when associated
with 92-A--A-94 and A-126.
CONFLICT 161 163 LLA -> RHE (in Ref. 8; AAD28370).
{ECO:0000305}.
SEQUENCE 282 AA; 30674 MW; DDB2F907CA0215A0 CRC64;
MSLLATLGLE LDRALLPASG LGWLVDYGKL PPAPAPLAPY EVLGGALEGG LPVGGEPLAG
DGFSDWMTER VDFTALLPLE PPLPPGTLPQ PSPTPPDLEA MASLLKKELE QMEDFFLDAP
PLPPPSPPPL PPPPLPPAPS LPLSLPSFDL PQPPVLDTLD LLAIYCRNEA GQEEVGMPPL
PPPQQPPPPS PPQPSRLAPY PHPATTRGDR KQKKRDQNKS AALRYRQRKR AEGEALEGEC
QGLEARNREL KERAESVERE IQYVKDLLIE VYKARSQRTR SC


Related products :

Catalog number Product name Quantity
E1346h ELISA Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T
E1346h ELISA kit Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T
U1346h CLIA Activating transcription factor 1,ATF1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Homo sapiens,Human,Protein TREB36 96T
18-003-42999 Cyclic AMP-dependent transcription factor ATF-5 - Activating transcription factor 5; Transcription factor ATFx Polyclonal 0.05 mg Aff Pur
E1346b ELISA kit Activating transcription factor 1,ATF1,Bos taurus,Bovine,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1 96T
E1346b ELISA Activating transcription factor 1,ATF1,Bos taurus,Bovine,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1 96T
U1346b CLIA Activating transcription factor 1,ATF1,Bos taurus,Bovine,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1 96T
E1346m ELISA Activating transcription factor 1,Atf1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Mouse,Mus musculus,TCR-ATF1 96T
U1346m CLIA Activating transcription factor 1,Atf1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Mouse,Mus musculus,TCR-ATF1 96T
E1346m ELISA kit Activating transcription factor 1,Atf1,cAMP-dependent transcription factor ATF-1,Cyclic AMP-dependent transcription factor ATF-1,Mouse,Mus musculus,TCR-ATF1 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
18-003-43256 Cyclic AMP-dependent transcription factor ATF-7 - Activating transcription factor 7; Transcription factor ATF-A Polyclonal 0.1 mg Protein A
18-003-43222 Cyclic AMP-dependent transcription factor ATF-1 - Activating transcription factor 1; TREB36 protein Polyclonal 0.05 mg Aff Pur
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
27-359 TCFL5 is a new bHLH transcription factor that negatively regulates upstream transcription factor-dependent transcription. 0.05 mg
10-663-45549 Activating Transcription Factor-2 (ATF-2) Human - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 1 mg
10-663-45549 Activating Transcription Factor-2 (ATF-2) Human - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.01 mg
10-663-45549 Activating Transcription Factor-2 (ATF-2) Human - Activating transcription factor 2; cAMP response element-binding protein CRE-BP1; HB16 N_A 0.002 mg
EIAAB42084 Homo sapiens,Human,Mitochondrial transcription factor 1,MtTF1,mtTFA,TCF6,TCF-6,TCF6L2,TFAM,Transcription factor 6,Transcription factor 6-like 2,Transcription factor A, mitochondrial
18-003-42098 Ets domain transcription factor - ESE3 transcription factor; EHF protein; DJ875K15.1.2 (Ets homologous factor (Ets-domain transcription factor. ESE-3B (Isoform 2))); ETS-family transcription factor EH 0.1 mg Protein A
EIAAB42103 Immunoglobulin enhancer-binding factor E12_E47,Pan,Pancreas specific transcription factor 1c,Ptf1c,Rat,Rattus norvegicus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor E2-alpha,Transcri
EIAAB42104 Alf2,Immunoglobulin enhancer-binding factor E12_E47,Me2,Mouse,Mus musculus,Tcf3,TCF-3,Tcfe2a,Transcription factor 3,Transcription factor A1,Transcription factor E2-alpha


 

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