CREB1_MOUSE
ID CREB1_MOUSE Reviewed; 327 AA.
AC Q01147;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Cyclic AMP-responsive element-binding protein 1;
DE Short=CREB-1;
DE Short=cAMP-responsive element-binding protein 1;
GN Name=Creb1; Synonyms=Creb-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=1532935; DOI=10.1002/j.1460-2075.1992.tb05195.x;
RA Ruppert S., Cole T.J., Boshart M., Schmid E., Schuetz G.;
RT "Multiple mRNA isoforms of the transcription activator protein CREB:
RT generation by alternative splicing and specific expression in primary
RT spermatocytes.";
RL EMBO J. 11:1503-1512(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=1387109; DOI=10.1016/0888-7543(92)90010-p;
RA Cole T.J., Copeland N.G., Gilbert D.J., Jenkins N.A., Schuetz G.,
RA Ruppert R.;
RT "The mouse CREB (cAMP responsive element binding protein) gene: structure,
RT promoter analysis, and chromosomal localization.";
RL Genomics 13:974-982(1992).
RN [3]
RP INTERACTION WITH CREBBP, PHOSPHORYLATION AT SER-119, AND MUTAGENESIS OF
RP 123-ILE-LEU-124.
RX PubMed=8552098; DOI=10.1128/mcb.16.2.694;
RA Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C.,
RA Hoeger C., Montminy M.R.;
RT "Phosphorylation of CREB at Ser-133 induces complex formation with CREB-
RT binding protein via a direct mechanism.";
RL Mol. Cell. Biol. 16:694-703(1996).
RN [4]
RP PHOSPHORYLATION AT SER-119 AND SER-128, MUTAGENESIS OF SER-128, AND
RP FUNCTION.
RX PubMed=11970866; DOI=10.1016/s0896-6273(02)00656-6;
RA Gau D., Lemberger T., von Gall C., Kretz O., Le Minh N., Gass P.,
RA Schmid W., Schibler U., Korf H.W., Schuetz G.;
RT "Phosphorylation of CREB Ser142 regulates light-induced phase shifts of the
RT circadian clock.";
RL Neuron 34:245-253(2002).
RN [5]
RP PHOSPHORYLATION AT SER-119, AND MUTAGENESIS OF SER-119.
RX PubMed=18690222; DOI=10.1038/ni.1644;
RA Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M.,
RA Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.;
RT "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor
RT signaling.";
RL Nat. Immunol. 9:1028-1036(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=20852621; DOI=10.1038/nm.2214;
RA Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T.,
RA Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A., Montminy M.,
RA Kay S.A.;
RT "Cryptochrome mediates circadian regulation of cAMP signaling and hepatic
RT gluconeogenesis.";
RL Nat. Med. 16:1152-1156(2010).
RN [8]
RP FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREBL2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21728997; DOI=10.1042/bj20101475;
RA Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.;
RT "CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1
RT adipocytes.";
RL Biochem. J. 439:27-38(2011).
RN [9]
RP INTERACTION WITH TOX4.
RX PubMed=34914893; DOI=10.1016/j.cmet.2021.11.013;
RA Wang L., Yu J., Zhou Q., Wang X., Mukhanova M., Du W., Sun L.,
RA Pajvani U.B., Accili D.;
RT "TOX4, an insulin receptor-independent regulator of hepatic glucose
RT production, is activated in diabetic liver.";
RL Cell Metab. 34:158-170.e5(2022).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE SOMATOSTATIN CAMP
RP RESPONSE ELEMENT (SSCRE).
RX PubMed=10952992; DOI=10.1074/jbc.m007293200;
RA Schumacher M.A., Goodman R.H., Brennan R.G.;
RT "The structure of a CREB bZIP.somatostatin CRE complex reveals the basis
RT for selective dimerization and divalent cation-enhanced DNA binding.";
RL J. Biol. Chem. 275:35242-35247(2000).
CC -!- FUNCTION: Phosphorylation-dependent transcription factor that
CC stimulates transcription upon binding to the DNA cAMP response element
CC (CRE), a sequence present in many viral and cellular promoters.
CC Transcription activation is enhanced by the TORC coactivators which act
CC independently of Ser-119 phosphorylation. Involved in different
CC cellular processes including the synchronization of circadian
CC rhythmicity and the differentiation of adipose cells.
CC {ECO:0000269|PubMed:11970866, ECO:0000269|PubMed:21728997}.
CC -!- SUBUNIT: Interacts with PPRC1. Binds DNA as a dimer. This dimer is
CC stabilized by magnesium ions. Interacts, through the bZIP domain, with
CC the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3. Interacts
CC (phosphorylated form) with TOX3 (By similarity). When phosphorylated on
CC Ser-119, binds CREBBP. Interacts with ARRB1. Binds to HIPK2 (By
CC similarity). Interacts with SGK1 (By similarity). Interacts with
CC CREBL2; regulates CREB1 phosphorylation, stability and transcriptional
CC activity. Interacts with TSSK4; this interaction facilitates
CC phosphorylation on Ser-119 (By similarity). Forms a complex with KMT2A
CC and CREBBP (By similarity). Interacts with TOX4; CREB1 is required for
CC full induction of TOX4-dependent activity and the interaction is
CC increased by cAMP and inhibited by insulin (PubMed:34914893).
CC {ECO:0000250|UniProtKB:P16220, ECO:0000269|PubMed:10952992,
CC ECO:0000269|PubMed:21728997, ECO:0000269|PubMed:34914893,
CC ECO:0000269|PubMed:8552098}.
CC -!- INTERACTION:
CC Q01147; Q32M00: Crebl2; NbExp=4; IntAct=EBI-2291098, EBI-5314489;
CC Q01147; Q60974: Ncor1; NbExp=4; IntAct=EBI-2291098, EBI-349004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312,
CC ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:21728997}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=At least 6 isoforms may be produced.
CC {ECO:0000269|PubMed:1532935};
CC Name=1; Synonyms=Delta {ECO:0000303|PubMed:1532935};
CC IsoId=Q01147-2; Sequence=Displayed;
CC Name=2; Synonyms=Alpha {ECO:0000303|PubMed:1532935};
CC IsoId=Q01147-1; Sequence=VSP_060704;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:1387109}.
CC -!- PTM: Phosphorylation of Ser-119 allows CREBBP binding. Stimulated by
CC phosphorylation. Phosphorylated Ser-128 can be detected in the
CC suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the
CC hippocampus but not in the striatum nor in the cerebellum. In the SCN,
CC phosphorylation of Ser-128 and Ser-119 are stimulated by light exposure
CC and submitted to circadian oscillations. In the retina, only
CC phosphorylation of Ser-119 can be detected upon light exposure.
CC Phosphorylation of both Ser-119 and Ser-128 in the SCN regulates the
CC activity of CREB and participates in circadian rhythm generation.
CC Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-119. CaMK4
CC is much more potent than CAMK2 in activating CREB. Phosphorylated by
CC CaMK2 on Ser-128. Phosphorylation of Ser-128 blocks CREB-mediated
CC transcription even when Ser-119 is phosphorylated. Phosphorylated by
CC CaMK1. Phosphorylation of Ser-271 by HIPK2 in response to genotoxic
CC stress promotes CREB1 activity, facilitating the recruitment of the
CC coactivator CBP (By similarity). Phosphorylated at Ser-119 by RPS6KA3,
CC RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. CREBL2
CC positively regulates phosphorylation at Ser-119 thereby stimulating
CC CREB1 transcriptional activity. In liver, phosphorylation is induced by
CC fasting or glucagon in a circadian fashion. Phosphorylated by TSSK4 on
CC Ser-119 (By similarity). {ECO:0000250|UniProtKB:P16220,
CC ECO:0000269|PubMed:11970866, ECO:0000269|PubMed:18690222,
CC ECO:0000269|PubMed:20852621, ECO:0000269|PubMed:8552098}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation on Lys-290, but not on Lys-271,
CC is required for nuclear localization of this protein. Sumoylation is
CC enhanced under hypoxia, promoting nuclear localization and
CC stabilization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X67719; CAA47953.1; -; Genomic_DNA.
DR EMBL; X67721; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67724; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67725; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67726; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67727; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67728; CAA47953.1; JOINED; Genomic_DNA.
DR EMBL; X67719; CAA47954.1; -; Genomic_DNA.
DR EMBL; X67721; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67722; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67724; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67725; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67726; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67727; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; X67728; CAA47954.1; JOINED; Genomic_DNA.
DR EMBL; M95106; AAA37456.1; -; mRNA.
DR CCDS; CCDS15004.1; -. [Q01147-1]
DR CCDS; CCDS15005.1; -. [Q01147-2]
DR PIR; S20955; S20955.
DR PIR; S42699; S42699.
DR RefSeq; NP_034082.1; NM_009952.2. [Q01147-1]
DR RefSeq; NP_598589.2; NM_133828.2. [Q01147-2]
DR RefSeq; XP_006495713.1; XM_006495650.3. [Q01147-1]
DR RefSeq; XP_006495714.1; XM_006495651.3. [Q01147-2]
DR RefSeq; XP_017169569.1; XM_017314080.1. [Q01147-1]
DR RefSeq; XP_017169588.1; XM_017314099.1. [Q01147-2]
DR PDB; 1DH3; X-ray; 3.00 A; A/C=271-325.
DR PDBsum; 1DH3; -.
DR AlphaFoldDB; Q01147; -.
DR BMRB; Q01147; -.
DR SMR; Q01147; -.
DR BioGRID; 198873; 27.
DR ComplexPortal; CPX-6; bZIP transcription factor complex, Atf4-Creb1.
DR CORUM; Q01147; -.
DR IntAct; Q01147; 10.
DR MINT; Q01147; -.
DR STRING; 10090.ENSMUSP00000140112; -.
DR iPTMnet; Q01147; -.
DR PhosphoSitePlus; Q01147; -.
DR EPD; Q01147; -.
DR jPOST; Q01147; -.
DR PaxDb; Q01147; -.
DR PeptideAtlas; Q01147; -.
DR PRIDE; Q01147; -.
DR ProteomicsDB; 284119; -. [Q01147-2]
DR ProteomicsDB; 284120; -. [Q01147-2]
DR ABCD; Q01147; 1 sequenced antibody.
DR Antibodypedia; 3536; 2247 antibodies from 54 providers.
DR DNASU; 12912; -.
DR Ensembl; ENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958. [Q01147-1]
DR Ensembl; ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958. [Q01147-2]
DR Ensembl; ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958. [Q01147-2]
DR Ensembl; ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958. [Q01147-1]
DR GeneID; 12912; -.
DR KEGG; mmu:12912; -.
DR UCSC; uc007bgr.1; mouse. [Q01147-2]
DR CTD; 1385; -.
DR MGI; MGI:88494; Creb1.
DR VEuPathDB; HostDB:ENSMUSG00000025958; -.
DR eggNOG; KOG3584; Eukaryota.
DR GeneTree; ENSGT00940000155408; -.
DR InParanoid; Q01147; -.
DR OMA; QXISTIA; -.
DR PhylomeDB; Q01147; -.
DR TreeFam; TF106464; -.
DR Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-MMU-199920; CREB phosphorylation.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR Reactome; R-MMU-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR BioGRID-ORCS; 12912; 12 hits in 77 CRISPR screens.
DR ChiTaRS; Creb1; mouse.
DR EvolutionaryTrace; Q01147; -.
DR PRO; PR:Q01147; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q01147; protein.
DR Bgee; ENSMUSG00000025958; Expressed in medial ganglionic eminence and 237 other tissues.
DR ExpressionAtlas; Q01147; baseline and differential.
DR Genevisible; Q01147; MM.
DR GO; GO:1990589; C:ATF4-CREB1 transcription factor complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:1990763; F:arrestin family protein binding; ISO:MGI.
DR GO; GO:0035497; F:cAMP response element binding; IDA:ARUK-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0110148; P:biomineralization; ISO:MGI.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR GO; GO:1904322; P:cellular response to forskolin; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:ARUK-UCL.
DR GO; GO:0071294; P:cellular response to zinc ion; IDA:MGI.
DR GO; GO:0034670; P:chemotaxis to arachidonic acid; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
DR GO; GO:0046879; P:hormone secretion; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0060428; P:lung epithelium development; IMP:MGI.
DR GO; GO:0060430; P:lung saccule development; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:MGI.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
DR GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IMP:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IGI:UniProtKB.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IMP:MGI.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IGI:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0032916; P:positive regulation of transforming growth factor beta3 production; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008361; P:regulation of cell size; IGI:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISO:MGI.
DR GO; GO:0048145; P:regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0060251; P:regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0033762; P:response to glucagon; IMP:UniProtKB.
DR GO; GO:0010035; P:response to inorganic substance; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0014074; P:response to purine-containing compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0033363; P:secretory granule organization; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IMP:MGI.
DR GO; GO:0008542; P:visual learning; ISO:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR003102; Coactivator_CBP_pKID.
DR InterPro; IPR029802; CREB1.
DR InterPro; IPR001630; Leuzip_CREB.
DR PANTHER; PTHR45879; PTHR45879; 1.
DR PANTHER; PTHR45879:SF1; PTHR45879:SF1; 1.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF02173; pKID; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS50953; KID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Biological rhythms;
KW Differentiation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..327
FT /note="Cyclic AMP-responsive element-binding protein 1"
FT /id="PRO_0000076598"
FT DOMAIN 87..146
FT /note="KID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312"
FT DOMAIN 269..327
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..295
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 297..318
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT SITE 300
FT /note="Required for binding TORCs"
FT /evidence="ECO:0000250"
FT MOD_RES 119
FT /note="Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or
FT PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00312,
FT ECO:0000269|PubMed:11970866, ECO:0000269|PubMed:18690222,
FT ECO:0000269|PubMed:8552098"
FT MOD_RES 128
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P15337,
FT ECO:0000255|PROSITE-ProRule:PRU00312"
FT MOD_RES 257
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:P16220,
FT ECO:0000255|PROSITE-ProRule:PRU00312"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P16220"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P16220"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P16220"
FT VAR_SEQ 86
FT /note="V -> VQSSCKDLKRLFSGT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060704"
FT MUTAGEN 119
FT /note="S->A: Loss of phosphorylation by RPS6KA4 and
FT RPS6KA5."
FT /evidence="ECO:0000269|PubMed:18690222"
FT MUTAGEN 123..124
FT /note="IL->AA: Abolishes CREBBP binding."
FT /evidence="ECO:0000269|PubMed:8552098"
FT MUTAGEN 128
FT /note="S->A: Attenuates light-induced phase shifts of
FT locomotion and expression of c-Fos and mPer1 in the SCN."
FT /evidence="ECO:0000269|PubMed:11970866"
FT HELIX 272..319
FT /evidence="ECO:0007829|PDB:1DH3"
SQ SEQUENCE 327 AA; 35122 MW; 00D1F26B00D48442 CRC64;
MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA PTVTLVQLPN
GQTVQVHGVI QAAQPSVIQS PQVQTVQIST IAESEDSQES VDSVTDSQKR REILSRRPSY
RKILNDLSSD APGVPRIEEE KSEEETSAPA ITTVTVPTPI YQTSSGQYIA ITQGGAIQLA
NNGTDGVQGL QTLTMTNAAA TQPGTTILQY AQTTDGQQIL VPSNQVVVQA ASGDVQTYQI
RTAPTSTIAP GVVMASSPAL PTQPAEEAAR KREVRLMKNR EAARECRRKK KEYVKCLENR
VAVLENQNKT LIEELKALKD LYCHKSD
