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Cyclic AMP-responsive element-binding protein 1 (CREB-1) (cAMP-responsive element-binding protein 1) (Cyclic AMP-responsive DNA-binding protein)

 CREB1_BOVIN             Reviewed;         325 AA.
P27925; A5PK02; O18957;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
10-OCT-2018, entry version 146.
RecName: Full=Cyclic AMP-responsive element-binding protein 1;
Short=CREB-1;
Short=cAMP-responsive element-binding protein 1;
AltName: Full=Cyclic AMP-responsive DNA-binding protein;
Name=CREB1; Synonyms=CREB, CREB2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1837490; DOI=10.3109/10425179109020800;
Willems L., Kettmann R., Chen G., Portetelle D., Burny A., Derse D.;
"Nucleotide sequence of the bovine cyclic-AMP responsive DNA binding
protein (CREB2) cDNA.";
DNA Seq. 1:415-417(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Adam E., Twizere J.C., Burny A., Kettmann R., Willems L.;
"Nucleotide sequence of the CREB protein involved in bovine leukemia
virus expression.";
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=1309910;
Willems L., Kettmann R., Chen G., Portetelle D., Burny A., Derse D.;
"A cyclic AMP-responsive DNA-binding protein (CREB2) is a cellular
transactivator of the bovine leukemia virus long terminal repeat.";
J. Virol. 66:766-772(1992).
[5]
FUNCTION.
PubMed=8057465;
Adam E., Kerkhofs P., Mammerickx M., Kettmann R., Burny A.,
Droogmans L., Willems L.;
"Involvement of the cyclic AMP-responsive element binding protein in
bovine leukemia virus expression in vivo.";
J. Virol. 68:5845-5853(1994).
[6]
FUNCTION.
PubMed=8627725;
Adam E., Kerkhofs P., Mammerickx M., Burny A., Kettman R., Willems L.;
"The CREB, ATF-1, and ATF-2 transcription factors from bovine leukemia
virus-infected B lymphocytes activate viral expression.";
J. Virol. 70:1990-1999(1996).
[7]
PHOSPHORYLATION AT SER-117.
PubMed=11752053; DOI=10.1046/j.1471-4159.2001.00666.x;
Cammarota M., Bevilaqua L.R., Dunkley P.R., Rostas J.A.;
"Angiotensin II promotes the phosphorylation of cyclic AMP-responsive
element binding protein (CREB) at Ser133 through an ERK1/2-dependent
mechanism.";
J. Neurochem. 79:1122-1128(2001).
-!- FUNCTION: Phosphorylation-dependent transcription factor that
stimulates transcription upon binding to the DNA cAMP response
element (CRE), a sequence present in many viral and cellular
promoters. Transcription activation is enhanced by the TORC
coactivators which act independently of Ser-117 phosphorylation.
Involved in different cellular processes including the
synchronization of circadian rhythmicity and the differentiation
of adipose cells. {ECO:0000269|PubMed:1309910,
ECO:0000269|PubMed:8057465, ECO:0000269|PubMed:8627725}.
-!- SUBUNIT: Interacts with PPRC1. Binds DNA as a dimer. This dimer is
stabilized by magnesium ions. Interacts, through the bZIP domain,
with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3.
When phosphorylated on Ser-117, binds CREBBP. Interacts
(phosphorylated form) with TOX3. Binds to HIPK2 (By similarity).
Interacts with SGK1 (By similarity). Interacts with CREBL2;
regulates CREB1 phosphorylation, stability and transcriptional
activity (By similarity). Interacts with TSSK4; this interaction
facilitates phosphorylation on Ser-117 (By similarity).
{ECO:0000250|UniProtKB:P16220}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Sumoylated with SUMO1. Sumoylation on Lys-288, but not on
Lys-269, is required for nuclear localization of this protein.
Sumoylation is enhanced under hypoxia, promoting nuclear
localization and stabilization (By similarity). {ECO:0000250}.
-!- PTM: Stimulated by phosphorylation. Phosphorylation of both Ser-
117 and Ser-126 in the SCN regulates the activity of CREB and
participates in circadian rhythm generation. Phosphorylation of
Ser-117 allows CREBBP binding. Phosphorylated upon calcium influx
by CaMK4 and CaMK2 on Ser-117. CaMK4 is much more potent than
CaMK2 in activating CREB. Phosphorylated by CaMK2 on Ser-126.
Phosphorylation of Ser-126 blocks CREB-mediated transcription even
when Ser-117 is phosphorylated. Phosphorylated by CaMK1.
Phosphorylation of Ser-255 by HIPK2 in response to genotoxic
stress promotes CREB1 activity, facilitating the recruitment of
the coactivator CBP. Phosphorylated at Ser-117 by RPS6KA3, RPS6KA4
and RPS6KA5 in response to mitogenic or stress stimuli. CREBL2
positively regulates phosphorylation at Ser-117 thereby
stimulating CREB1 transcriptional activity. In liver,
phosphorylation is induced by fasting or glucagon in a circadian
fashion (By similarity). Phosphorylated by TSSK4 on Ser-117 (By
similarity). {ECO:0000250|UniProtKB:P16220}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X57031; CAA40347.1; -; mRNA.
EMBL; AF006042; AAB62381.1; -; mRNA.
EMBL; BC142303; AAI42304.1; -; mRNA.
PIR; S23007; S23007.
RefSeq; NP_776710.1; NM_174285.1.
UniGene; Bt.4183; -.
ProteinModelPortal; P27925; -.
SMR; P27925; -.
STRING; 9913.ENSBTAP00000007201; -.
iPTMnet; P27925; -.
PaxDb; P27925; -.
PRIDE; P27925; -.
GeneID; 281713; -.
KEGG; bta:281713; -.
CTD; 1385; -.
eggNOG; KOG3584; Eukaryota.
eggNOG; ENOG410ZZJZ; LUCA.
HOVERGEN; HBG011077; -.
InParanoid; P27925; -.
KO; K05870; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0033762; P:response to glucagon; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR003102; Coactivator_CBP_pKID.
InterPro; IPR029802; CREB1.
InterPro; IPR001630; Leuzip_CREB.
PANTHER; PTHR22952:SF200; PTHR22952:SF200; 1.
Pfam; PF00170; bZIP_1; 1.
Pfam; PF02173; pKID; 1.
PRINTS; PR00041; LEUZIPPRCREB.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
PROSITE; PS50953; KID; 1.
1: Evidence at protein level;
Activator; Biological rhythms; Complete proteome; Differentiation;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 325 Cyclic AMP-responsive element-binding
protein 1.
/FTId=PRO_0000076600.
DOMAIN 85 144 KID. {ECO:0000255|PROSITE-
ProRule:PRU00312}.
DOMAIN 267 325 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 268 293 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 295 316 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
SITE 298 298 Required for binding TORCs.
{ECO:0000250}.
MOD_RES 117 117 Phosphoserine; by CaMK1, CaMK2, CaMK4,
PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4,
RPS6KA5 and SGK1. {ECO:0000255|PROSITE-
ProRule:PRU00312,
ECO:0000269|PubMed:11752053}.
MOD_RES 126 126 Phosphoserine; by CaMK2.
{ECO:0000250|UniProtKB:P15337,
ECO:0000255|PROSITE-ProRule:PRU00312}.
MOD_RES 255 255 Phosphoserine; by HIPK2.
{ECO:0000250|UniProtKB:P16220,
ECO:0000255|PROSITE-ProRule:PRU00312}.
CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 288 288 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
CONFLICT 60 61 QT -> TK (in Ref. 1; CAA40347).
{ECO:0000305}.
SEQUENCE 325 AA; 34877 MW; 61B4B4244FAB474B CRC64;
MESGAENQQS GDAAVTEAES QQMTVQAQPQ IATLAQVSMP AAHATSSAPT VTLVQLPNGQ
TVQVHGVIQA AQPSVIQSPQ VQTVQISTIA ESEDSQESVD SVTDSQKRRE ILSRRPSYRK
ILNDLSSDAP GVPRIEEEKS EEETSAPAIT TVTVPTPIYQ TSSGQYIAIT QGGAIQLANN
GTDGVQGLQT LTMTNAAATQ PGTTILQYAQ TTDGQQILVP SNQVVVQAAS GDVQTYQIRT
APTSTIAPGV VMASSPALPT QPAEEAARKR EVRLMKNREA ARECRRKKKE YVKCLENRVA
VLENQNKTLI EELKALKDLY CHKSD


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