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

 CREB1_RAT               Reviewed;         341 AA.
P15337;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-SEP-2018, entry version 190.
RecName: Full=Cyclic AMP-responsive element-binding protein 1;
Short=CREB-1;
Short=cAMP-responsive element-binding protein 1;
Name=Creb1; Synonyms=Creb-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2521922; DOI=10.1038/337749a0;
Gonzalez G.A., Yamamoto K.K., Fischer W.H., Karr D., Menzel P.,
Biggs W. III, Vale W.W., Montminy M.R.;
"A cluster of phosphorylation sites on the cyclic AMP-regulated
nuclear factor CREB predicted by its sequence.";
Nature 337:749-752(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=1831258; DOI=10.1093/nar/19.15.4290;
Short M.L., Manohar C.F., Furtado M.R., Ghadge G.D., Wolinsky S.M.,
Thimmapaya B., Jungmann R.A.;
"Nucleotide and derived amino-acid sequences of the CRE-binding
proteins from rat C6 glioma and HeLa cells.";
Nucleic Acids Res. 19:4290-4290(1991).
[3]
PHOSPHORYLATION AT SER-133, AND PHOSPHORYLATION BY CAMK1 AND CAMK4.
PubMed=1646483; DOI=10.1126/science.1646483;
Sheng M., Thompson M.A., Greenberg M.E.;
"CREB: a Ca(2+)-regulated transcription factor phosphorylated by
calmodulin-dependent kinases.";
Science 252:1427-1430(1991).
[4]
PHOSPHORYLATION AT SER-133 AND SER-142, AND MUTAGENESIS OF SER-133 AND
SER-142.
PubMed=7958915; DOI=10.1101/gad.8.21.2527;
Sun P., Enslen H., Myung P.S., Maurer R.A.;
"Differential activation of CREB by Ca2+/calmodulin-dependent protein
kinases type II and type IV involves phosphorylation of a site that
negatively regulates activity.";
Genes Dev. 8:2527-2539(1994).
[5]
PHOSPHORYLATION AT SER-133, AND PHOSPHORYLATION BY CAMK1.
PubMed=8621702; DOI=10.1074/jbc.271.6.3066;
Sun P., Lou L., Maurer R.A.;
"Regulation of activating transcription factor-1 and the cAMP response
element-binding protein by Ca2+/calmodulin-dependent protein kinases
type I, II, and IV.";
J. Biol. Chem. 271:3066-3073(1996).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
STRUCTURE BY NMR OF 119-146 IN COMPLEX WITH CREBBP.
PubMed=10222196; DOI=10.1006/jmbi.1999.2658;
Radhakrishnan I., Perez-Alvarado G.C., Parker D., Dyson H.J.,
Montminy M.R., Wright P.E.;
"Structural analyses of CREB-CBP transcriptional activator-coactivator
complexes by NMR spectroscopy: implications for mapping the boundaries
of structural domains.";
J. Mol. Biol. 287:859-865(1999).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PPRC1. Binds DNA as a dimer. Interacts,
through the bZIP domain, with the coactivators TORC1/CRTC1,
TORC2/CRTC2 and TORC3/CRTC3 (By similarity). When phosphorylated
on Ser-133, binds CREBBP. Interacts with ARRB1. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha;
IsoId=P15337-1; Sequence=Displayed;
Name=2; Synonyms=Delta;
IsoId=P15337-2; Sequence=VSP_000598;
-!- PTM: Phosphorylation of Ser-133 allows CREBBP binding. Stimulated
by phosphorylation. Phosphorylation of both Ser-142 and Ser-133 in
the SCN regulates the activity of CREB and participate in
circadian rhythm generation (By similarity). Phosphorylated upon
calcium influx by CaMK4 and CaMK2 on Ser-133. CaMK4 is much more
potent than CaMK2 in activating CREB. Phosphorylated by CaMK2 on
Ser-142. Phosphorylation of Ser-142 blocks CREB-mediated
transcription even when Ser-133 is phosphorylated. Phosphorylated
by CaMK1. Phosphorylation of Ser-271 by HIPK2 in response to
genotoxic stress promotes CREB1 activity, facilitating the
recruitment of the coactivator CBP. Phosphorylated at Ser-133 by
RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress
stimuli (By similarity). CREBL2 positively regulates
phosphorylation at Ser-133 thereby stimulating CREB1
transcriptional activity. In liver, phosphorylation is induced by
fasting or glucagon in a circadian fashion (By similarity).
{ECO:0000250}.
-!- PTM: Sumoylated with SUMO1. Sumoylation on Lys-304, but not on
Lys-285, is required for nuclear localization of this protein.
Sumoylation is enhanced under hypoxia, promoting nuclear
localization and stabilization (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X14788; CAA32890.1; -; mRNA.
EMBL; X60002; CAA42619.1; -; mRNA.
PIR; A35663; A35663.
PIR; S03343; S03343.
PIR; S22299; S22299.
RefSeq; NP_112279.1; NM_031017.1. [P15337-1]
RefSeq; NP_604392.1; NM_134443.1.
RefSeq; XP_006245127.1; XM_006245065.3. [P15337-1]
RefSeq; XP_006245128.1; XM_006245066.3. [P15337-2]
UniGene; Rn.90061; -.
PDB; 1KDX; NMR; -; B=119-146.
PDBsum; 1KDX; -.
DisProt; DP00080; -.
ProteinModelPortal; P15337; -.
SMR; P15337; -.
BioGrid; 249546; 3.
DIP; DIP-36407N; -.
IntAct; P15337; 3.
MINT; P15337; -.
STRING; 10116.ENSRNOP00000018326; -.
iPTMnet; P15337; -.
PhosphoSitePlus; P15337; -.
PaxDb; P15337; -.
PRIDE; P15337; -.
Ensembl; ENSRNOT00000018326; ENSRNOP00000018326; ENSRNOG00000013412. [P15337-1]
Ensembl; ENSRNOT00000049654; ENSRNOP00000049369; ENSRNOG00000013412. [P15337-2]
GeneID; 81646; -.
KEGG; rno:81646; -.
UCSC; RGD:620218; rat. [P15337-1]
CTD; 1385; -.
RGD; 620218; Creb1.
eggNOG; KOG3584; Eukaryota.
eggNOG; ENOG410ZZJZ; LUCA.
GeneTree; ENSGT00390000008655; -.
HOGENOM; HOG000007365; -.
HOVERGEN; HBG011077; -.
InParanoid; P15337; -.
KO; K05870; -.
OMA; QXISTIA; -.
OrthoDB; EOG091G0FTJ; -.
PhylomeDB; P15337; -.
TreeFam; TF106464; -.
Reactome; R-RNO-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-RNO-199920; CREB phosphorylation.
Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
Reactome; R-RNO-442720; CREB phosphorylation through the activation of Adenylate Cyclase.
Reactome; R-RNO-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-RNO-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
EvolutionaryTrace; P15337; -.
PRO; PR:P15337; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000013412; Expressed in 9 organ(s), highest expression level in testis.
Genevisible; P15337; RN.
GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IEA:Ensembl.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0000785; C:chromatin; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005719; C:nuclear euchromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IDA:RGD.
GO; GO:1990763; F:arrestin family protein binding; IPI:RGD.
GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:RGD.
GO; GO:0030544; F:Hsp70 protein binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001225; F:RNA polymerase II transcription coactivator binding; IPI:CAFA.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:RGD.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:RGD.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEP:RGD.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
GO; GO:0034670; P:chemotaxis to arachidonic acid; IMP:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0060430; P:lung saccule development; IEA:Ensembl.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IEA:Ensembl.
GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; IMP:RGD.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:RGD.
GO; GO:0048145; P:regulation of fibroblast proliferation; IMP:RGD.
GO; GO:0060251; P:regulation of glial cell proliferation; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0033762; P:response to glucagon; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:1902065; P:response to L-glutamate; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:RGD.
GO; GO:0060509; P:type I pneumocyte differentiation; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IMP:RGD.
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;
3D-structure; Activator; Alternative splicing; Biological rhythms;
Complete proteome; Differentiation; Direct protein sequencing;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 341 Cyclic AMP-responsive element-binding
protein 1.
/FTId=PRO_0000076599.
DOMAIN 101 160 KID. {ECO:0000255|PROSITE-
ProRule:PRU00312}.
DOMAIN 283 341 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 284 309 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 311 332 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 133 133 Phosphoserine; by CaMK1, CaMK2, CaMK4,
PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4,
RPS6KA5 and SGK1. {ECO:0000255|PROSITE-
ProRule:PRU00312,
ECO:0000269|PubMed:1646483,
ECO:0000269|PubMed:7958915,
ECO:0000269|PubMed:8621702}.
MOD_RES 142 142 Phosphoserine; by CaMK2.
{ECO:0000244|PubMed:22673903,
ECO:0000255|PROSITE-ProRule:PRU00312,
ECO:0000269|PubMed:7958915}.
MOD_RES 271 271 Phosphoserine; by HIPK2.
{ECO:0000250|UniProtKB:P16220,
ECO:0000255|PROSITE-ProRule:PRU00312}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
CROSSLNK 304 304 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P16220}.
VAR_SEQ 88 101 Missing (in isoform 2).
{ECO:0000303|PubMed:1831258}.
/FTId=VSP_000598.
MUTAGEN 133 133 S->A: Loss of activation by CaMK4.
{ECO:0000269|PubMed:7958915}.
MUTAGEN 142 142 S->A: Loss of phosphorylation by CaMK2.
Activation by CaMK2.
{ECO:0000269|PubMed:7958915}.
CONFLICT 135 135 R -> K (in Ref. 2; CAA42619).
{ECO:0000305}.
CONFLICT 319 319 E -> K (in Ref. 2; CAA42619).
{ECO:0000305}.
HELIX 120 128 {ECO:0000244|PDB:1KDX}.
HELIX 133 144 {ECO:0000244|PDB:1KDX}.
SEQUENCE 341 AA; 36633 MW; FC08AC5A335D4C2F CRC64;
MTMDSGADNQ QSGDAAVTEA ESQQMTVQAQ PQIATLAQVS MPAAHATSSA PTVTLVQLPN
GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT QISTIAESED SQESVDSVTD
SQKRREILSR RPSYRKILND LSSDAPGVPR IEEEKSEEET SAPAITTVTV PTPIYQTSSG
QYIAITQGGA IQLANNGTDG VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV
VVQAASGDVQ TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D


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