Creb1

Functionⁱ

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-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	314	Required for binding TORCsBy similarity		1

GO - Molecular functionⁱ

arrestin family protein binding Source: MGI
cAMP response element binding Source: MGI
DNA binding
Source: MGI
Inferred from direct assayⁱ
- 11354513
- 14594818
DNA-binding transcription activator activity, RNA polymerase II-specific
Source: ARUK-UCL
Inferred from mutant phenotypeⁱ
- 20876357
DNA-binding transcription factor activity
Source: MGI
Inferred from direct assayⁱ
- 12220541
double-stranded DNA binding Source: MGI
enzyme binding Source: MGI
histone acetyltransferase binding Source: MGI
Hsp70 protein binding Source: MGI
identical protein binding Source: MGI
RNA polymerase II activating transcription factor binding Source: MGI
RNA polymerase II distal enhancer sequence-specific DNA binding Source: MGI
RNA polymerase II proximal promoter sequence-specific DNA binding Source: MGI
RNA polymerase II transcription coactivator binding Source: MGI
sequence-specific DNA binding
Source: MGI
Inferred from direct assayⁱ
- 15030764
transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: MGI
transcription factor binding Source: MGI
transcription regulatory region DNA binding Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aging Source: Ensembl
axonogenesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 11988169
cellular response to fatty acid Source: Ensembl
cellular response to growth factor stimulus
Source: BHF-UCL
Inferred from direct assayⁱ
- 16427017
cellular response to hepatocyte growth factor stimulus
Source: MGI
Inferred from direct assayⁱ
- 21072211
cellular response to insulin-like growth factor stimulus Source: Ensembl
cellular response to leukemia inhibitory factor
Source: MGI
Inferred from expression patternⁱ
- 20439489
cellular response to nerve growth factor stimulus Source: Ensembl
cellular response to platelet-derived growth factor stimulus Source: Ensembl
cellular response to retinoic acid
Source: ARUK-UCL
Inferred from mutant phenotypeⁱ
- 20876357
cellular response to zinc ion
Source: MGI
Inferred from direct assayⁱ
- 23716681
chemotaxis to arachidonic acid Source: MGI
circadian rhythm
Source: UniProtKB
Inferred from direct assayⁱ
- 20852621
lactation
Source: MGI
Inferred from mutant phenotypeⁱ
- 16141355
lung epithelium development
Source: MGI
Inferred from mutant phenotypeⁱ
- 21408140
lung saccule development
Source: MGI
Inferred from mutant phenotypeⁱ
- 21408140
mammary gland development
Source: MGI
Inferred from mutant phenotypeⁱ
- 16141355
memory
Source: MGI
Inferred from mutant phenotypeⁱ
- 23223304
negative regulation of gene expression Source: MGI
negative regulation of neuron death Source: MGI
negative regulation of transcription by competitive promoter binding Source: MGI
pituitary gland development
Source: MGI
Inferred from mutant phenotypeⁱ
- 16141355
positive regulation of apoptotic process Source: MGI
positive regulation of cardiac muscle tissue development
Source: MGI
Inferred from mutant phenotypeⁱ
- 24364879
positive regulation of fat cell differentiation
Source: UniProtKB
Inferred from genetic interactionⁱ
- 21728997
positive regulation of hormone secretion
Source: MGI
Inferred from mutant phenotypeⁱ
- 16141355
positive regulation of lipid biosynthetic process
Source: UniProtKB
Inferred from genetic interactionⁱ
- 21728997
positive regulation of long-term synaptic potentiation Source: MGI
positive regulation of multicellular organism growth
Source: MGI
Inferred from mutant phenotypeⁱ
- 16141355
positive regulation of osteoclast differentiation
Source: MGI
Inferred from direct assayⁱ
- 23395171
positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: MGI
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from genetic interactionⁱ
- 21728997
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 20852621
positive regulation of transforming growth factor beta3 production Source: MGI
protein phosphorylation
Source: MGI
Inferred from sequence orthologyⁱ
- 8798441
protein stabilization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 21728997
regulation of apoptotic process Source: MGI
regulation of cell size
Source: MGI
Inferred from genetic interactionⁱ
- 12015964
regulation of circadian rhythm Source: MGI
regulation of fibroblast proliferation Source: MGI
regulation of glial cell proliferation Source: MGI
regulation of transcription, DNA-templated
Source: MGI
Inferred from direct assayⁱ
- 12220541
response to activity Source: Ensembl
response to drug
Source: MGI
Inferred from direct assayⁱ
- 9098922
response to glucagon
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20852621
response to hypoxia Source: Ensembl
response to L-glutamate Source: Ensembl
response to nicotine Source: Ensembl
response to organic substance
Source: MGI
Inferred from sequence orthologyⁱ
- 8798441
secretory granule organization
Source: MGI
Inferred from mutant phenotypeⁱ
- 21408140
transcription by RNA polymerase II Source: MGI
transforming growth factor beta receptor signaling pathway Source: MGI
type I pneumocyte differentiation
Source: MGI
Inferred from mutant phenotypeⁱ
- 21408140
visual learning Source: MGI

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	Biological rhythms, Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactomeⁱ	R-MMU-198693 AKT phosphorylates targets in the nucleus R-MMU-199920 CREB phosphorylation R-MMU-375165 NCAM signaling for neurite out-growth R-MMU-442717 CREB phosphorylation through the activation of CaMKK R-MMU-442720 CREB phosphorylation through the activation of Adenylate Cyclase R-MMU-442729 CREB phosphorylation through the activation of CaMKII R-MMU-442742 CREB phosphorylation through the activation of Ras R-MMU-881907 Gastrin-CREB signalling pathway via PKC and MAPK

Reactomeⁱ

R-MMU-198693 AKT phosphorylates targets in the nucleus
R-MMU-199920 CREB phosphorylation
R-MMU-375165 NCAM signaling for neurite out-growth
R-MMU-442717 CREB phosphorylation through the activation of CaMKK
R-MMU-442720 CREB phosphorylation through the activation of Adenylate Cyclase
R-MMU-442729 CREB phosphorylation through the activation of CaMKII
R-MMU-442742 CREB phosphorylation through the activation of Ras
R-MMU-881907 Gastrin-CREB signalling pathway via PKC and MAPK

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cyclic AMP-responsive element-binding protein 1 Short name: CREB-1 Short name: cAMP-responsive element-binding protein 1
Gene namesⁱ	Name:Creb1 Synonyms:Creb-1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 1

Organism-specific databases

MGIⁱ	MGI:88494 Creb1

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	133	S → A: Loss of phosphorylation by RPS6KA4 and RPS6KA5. 1 Publication	1
Mutagenesisⁱ	137 – 138	IL → AA: Abolishes CREBBP binding. 1 Publication	2
Mutagenesisⁱ	142	S → A: Attenuates light-induced phase shifts of locomotion and expression of c-Fos and mPer1 in the SCN. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076598	1 – 341	Cyclic AMP-responsive element-binding protein 1Add BLAST		341

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	133	Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK1PROSITE-ProRule annotation3 Publications	1
Cross-linkⁱ	136	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	142	Phosphoserine; by CaMK2PROSITE-ProRule annotationBy similarity	1
Modified residueⁱ	271	Phosphoserine; by HIPK2PROSITE-ProRule annotationBy similarity	1
Cross-linkⁱ	285	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linkⁱ	304	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationⁱ

Phosphorylation of Ser-133 allows CREBBP binding. Stimulated by phosphorylation. Phosphorylated Ser-142 can be detected in the suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the hippocampus but not in the striatum nor in the cerebellum. In the SCN, phosphorylation of Ser-142 and Ser-133 are stimulated by light exposure and submitted to circadian oscillations. In the retina, only phosphorylation of Ser-133 can be detected upon light exposure. Phosphorylation of both Ser-133 and Ser-142 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. 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 (By similarity). Phosphorylated at Ser-133 by RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. 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. Phosphorylated by TSSK4 on Ser-133 (By similarity).By similarity4 Publications

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).By similarity

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q01147
PaxDbⁱ	Q01147
PeptideAtlas More...PeptideAtlasⁱ	Q01147
PRIDEⁱ	Q01147

PTM databases

iPTMnetⁱ	Q01147
PhosphoSitePlusⁱ	Q01147

Expressionⁱ

Tissue specificityⁱ

Ubiquitously expressed.1 Publication

Gene expression databases

Bgeeⁱ	ENSMUSG00000025958 Expressed in 282 organ(s), highest expression level in mesenteric lymph node
CleanExⁱ	MM_CREB1
ExpressionAtlasⁱ	Q01147 baseline and differential
Genevisibleⁱ	Q01147 MM

Interactionⁱ

Subunit structureⁱ

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. Interacts (phosphorylated form) with TOX3 (By similarity). When phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1. Binds to HIPK2 (By similarity). Interacts with SGK1 (By similarity). Interacts with CREBL2; regulates CREB1 phosphorylation, stability and transcriptional activity. Interacts with TSSK4; this interaction facilitates phosphorylation on Ser-133 (By similarity).By similarity3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Crebbp	P45481	2	EBI-2291098,EBI-296306
Crebl2	Q32M00	4	EBI-2291098,EBI-5314489
EP300	Q09472	2	EBI-2291098,EBI-447295	From Homo sapiens.
Ncor1	Q60974	5	EBI-2291098,EBI-349004

GO - Molecular functionⁱ

arrestin family protein binding Source: MGI
enzyme binding Source: MGI
histone acetyltransferase binding Source: MGI
Hsp70 protein binding Source: MGI
identical protein binding Source: MGI
RNA polymerase II activating transcription factor binding Source: MGI
RNA polymerase II transcription coactivator binding Source: MGI
transcription factor binding Source: MGI

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	198873, 17 interactors
ComplexPortalⁱ	CPX-6 ATF4-CREB1 transcription factor complex
CORUMⁱ	Q01147
IntActⁱ	Q01147, 10 interactors
Molecular INTeraction database More...MINTⁱ	Q01147
STRINGⁱ	10090.ENSMUSP00000059973

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Helixⁱ	286 – 333	Combined sources		48

Show more details

3D structure databases

ProteinModelPortalⁱ	Q01147
SMRⁱ	Q01147
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q01147

EvolutionaryTraceⁱ

Q01147

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	101 – 160	KIDPROSITE-ProRule annotationAdd BLAST		60
Domainⁱ	283 – 341	bZIPPROSITE-ProRule annotationAdd BLAST		59

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	284 – 309	Basic motifPROSITE-ProRule annotationAdd BLAST		26
Regionⁱ	311 – 332	Leucine-zipperPROSITE-ProRule annotationAdd BLAST		22

Sequence similaritiesⁱ

Belongs to the bZIP family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3584 Eukaryota ENOG410ZZJZ LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008655
HOGENOMⁱ	HOG000007365
HOVERGENⁱ	HBG011077
InParanoidⁱ	Q01147
KEGG Orthology (KO) More...KOⁱ	K05870
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0FTJ
PhylomeDBⁱ	Q01147
TreeFamⁱ	TF106464

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR003102 Coactivator_CBP_pKID IPR029802 CREB1 IPR001630 Leuzip_CREB
PANTHERⁱ	PTHR22952:SF200 PTHR22952:SF200, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit PF02173 pKID, 1 hit
PRINTSⁱ	PR00041 LEUZIPPRCREB
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit PS50953 KID, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

Note: At least 6 isoforms are produced.

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: Q01147-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA 
        60         70         80         90        100
PTVTLVQLPN GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT 
       110        120        130        140        150
QISTIAESED SQESVDSVTD SQKRREILSR RPSYRKILND LSSDAPGVPR 
       160        170        180        190        200
IEEEKSEEET SAPAITTVTV PTPIYQTSSG QYIAITQGGA IQLANNGTDG 
       210        220        230        240        250
VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV VVQAASGDVQ 
       260        270        280        290        300
TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC 
       310        320        330        340 
RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D

Length:341

Mass (Da):36,674

Last modified:June 1, 1994 - v1

Checksum:ⁱCF2958DE9174968A

GO

Isoform 2 (identifier: Q01147-2) [UniParc]FASTA Add to basket

Also known as: CREB-delta

The sequence of this isoform differs from the canonical sequence as follows:
88-101: Missing.

« Hide

        10         20         30         40         50
MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA 
        60         70         80         90        100
PTVTLVQLPN GQTVQVHGVI QAAQPSVIQS PQVQTVQIST IAESEDSQES 
       110        120        130        140        150
VDSVTDSQKR REILSRRPSY RKILNDLSSD APGVPRIEEE KSEEETSAPA 
       160        170        180        190        200
ITTVTVPTPI YQTSSGQYIA ITQGGAIQLA NNGTDGVQGL QTLTMTNAAA 
       210        220        230        240        250
TQPGTTILQY AQTTDGQQIL VPSNQVVVQA ASGDVQTYQI RTAPTSTIAP 
       260        270        280        290        300
GVVMASSPAL PTQPAEEAAR KREVRLMKNR EAARECRRKK KEYVKCLENR 
       310        320 
VAVLENQNKT LIEELKALKD LYCHKSD

Show »

Length:327

Mass (Da):35,122

Checksum:ⁱ00D1F26B00D48442

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q62347	Q62347_MOUSE	Cyclic AMP-responsive element-bindi... Cyclic AMP-responsive element-binding protein 1 (M.musculus transcription factor/DNA binding protein)	Creb1	287	Annotation score:
A0A087WRI6	A0A087WRI6_MOUSE	Cyclic AMP-responsive element-bindi... Cyclic AMP-responsive element-binding protein 1	Creb1	317	Annotation score:
Q61441	Q61441_MOUSE	C-AMP-responsive-element binding pr... C-AMP-responsive-element binding protein gamma (Cyclic AMP-responsive element-binding protein 1)	Creb1 CREB	90	Annotation score:

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_000597	88 – 101	Missing in isoform 2. CuratedAdd BLAST		14

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X67719 X67728 Genomic DNA Translation: CAA47953.1 X67719 X67728 Genomic DNA Translation: CAA47954.1 M95106 mRNA Translation: AAA37456.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS15004.1 [Q01147-1] CCDS15005.1 [Q01147-2]
PIRⁱ	S20955 S42699
NCBI Reference Sequences More...RefSeqⁱ	NP_034082.1, NM_009952.2 [Q01147-1] NP_598589.2, NM_133828.2 [Q01147-2] XP_006495713.1, XM_006495650.3 [Q01147-1] XP_006495714.1, XM_006495651.3 [Q01147-2] XP_017169569.1, XM_017314080.1 [Q01147-1] XP_017169588.1, XM_017314099.1 [Q01147-2]
UniGeneⁱ	Mm.422634

Genome annotation databases

Ensemblⁱ	ENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958 [Q01147-1] ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958 [Q01147-2] ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958 [Q01147-2] ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958 [Q01147-1]
GeneIDⁱ	12912
KEGGⁱ	mmu:12912
UCSC genome browser More...UCSCⁱ	uc007bgr.1 mouse [Q01147-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q01147	cAMP response element binding protein		MOUSE		341	UniRef100_Q01147
Q01147-2	cAMP responsive element binding protein 1, isoform CRA_a		MOUSE		327	UniRef100_Q543W0

Protein	Similar proteins		Species	Score	Length	Source
Q01147	Cyclic AMP-responsive element-binding protein 1	)	HUMAN		341	UniRef90_P16220
Cyclic AMP-responsive element-binding protein 1	)	RAT		341
Cyclic AMP-responsive element-binding protein 1		BOVIN		325
Cyclic AMP-responsive element-binding protein 1		MYODS		353
CREB1 isoform 2		PANTR		341
+211

Protein	Similar proteins		Species	Score	Length	Source
Q01147	Cyclic AMP-responsive element-binding protein 1	)	HUMAN		341	UniRef50_P16220
Cyclic AMP-responsive element-binding protein 1	)	RAT		341
Cyclic AMP-responsive element-binding protein 1		BOVIN		325
Cyclic AMP-responsive element-binding protein 1		MYODS		353
CREB1 isoform 2		PANTR		341
+520

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X67719 X67728 Genomic DNA Translation: CAA47953.1 X67719 X67728 Genomic DNA Translation: CAA47954.1 M95106 mRNA Translation: AAA37456.1
CCDSⁱ	CCDS15004.1 [Q01147-1] CCDS15005.1 [Q01147-2]
PIRⁱ	S20955 S42699
RefSeqⁱ	NP_034082.1, NM_009952.2 [Q01147-1] NP_598589.2, NM_133828.2 [Q01147-2] XP_006495713.1, XM_006495650.3 [Q01147-1] XP_006495714.1, XM_006495651.3 [Q01147-2] XP_017169569.1, XM_017314080.1 [Q01147-1] XP_017169588.1, XM_017314099.1 [Q01147-2]
UniGeneⁱ	Mm.422634

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1DH3	X-ray	3.00	A/C	285-339	[»]
ProteinModelPortalⁱ	Q01147
SMRⁱ	Q01147
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	198873, 17 interactors
ComplexPortalⁱ	CPX-6 ATF4-CREB1 transcription factor complex
CORUMⁱ	Q01147
IntActⁱ	Q01147, 10 interactors
MINTⁱ	Q01147
STRINGⁱ	10090.ENSMUSP00000059973

PTM databases

iPTMnetⁱ	Q01147
PhosphoSitePlusⁱ	Q01147

Proteomic databases

EPDⁱ	Q01147
PaxDbⁱ	Q01147
PeptideAtlasⁱ	Q01147
PRIDEⁱ	Q01147

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958 [Q01147-1] ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958 [Q01147-2] ENSMUST00000185594; ENSMUSP00000139995; ENSMUSG00000025958 [Q01147-2] ENSMUST00000190348; ENSMUSP00000140112; ENSMUSG00000025958 [Q01147-1]
GeneIDⁱ	12912
KEGGⁱ	mmu:12912
UCSCⁱ	uc007bgr.1 mouse [Q01147-1]

Organism-specific databases

CTDⁱ	1385
MGIⁱ	MGI:88494 Creb1

Phylogenomic databases

eggNOGⁱ	KOG3584 Eukaryota ENOG410ZZJZ LUCA
GeneTreeⁱ	ENSGT00390000008655
HOGENOMⁱ	HOG000007365
HOVERGENⁱ	HBG011077
InParanoidⁱ	Q01147
KOⁱ	K05870
OrthoDBⁱ	EOG091G0FTJ
PhylomeDBⁱ	Q01147
TreeFamⁱ	TF106464

Enzyme and pathway databases

Reactomeⁱ	R-MMU-198693 AKT phosphorylates targets in the nucleus R-MMU-199920 CREB phosphorylation R-MMU-375165 NCAM signaling for neurite out-growth R-MMU-442717 CREB phosphorylation through the activation of CaMKK R-MMU-442720 CREB phosphorylation through the activation of Adenylate Cyclase R-MMU-442729 CREB phosphorylation through the activation of CaMKII R-MMU-442742 CREB phosphorylation through the activation of Ras R-MMU-881907 Gastrin-CREB signalling pathway via PKC and MAPK

Reactomeⁱ

R-MMU-198693 AKT phosphorylates targets in the nucleus
R-MMU-199920 CREB phosphorylation
R-MMU-375165 NCAM signaling for neurite out-growth
R-MMU-442717 CREB phosphorylation through the activation of CaMKK
R-MMU-442720 CREB phosphorylation through the activation of Adenylate Cyclase
R-MMU-442729 CREB phosphorylation through the activation of CaMKII
R-MMU-442742 CREB phosphorylation through the activation of Ras
R-MMU-881907 Gastrin-CREB signalling pathway via PKC and MAPK

Miscellaneous databases

ChiTaRSⁱ	Creb1 mouse
EvolutionaryTraceⁱ	Q01147
Protein Ontology More...PROⁱ	PR:Q01147
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000025958 Expressed in 282 organ(s), highest expression level in mesenteric lymph node
CleanExⁱ	MM_CREB1
ExpressionAtlasⁱ	Q01147 baseline and differential
Genevisibleⁱ	Q01147 MM

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR003102 Coactivator_CBP_pKID IPR029802 CREB1 IPR001630 Leuzip_CREB
PANTHERⁱ	PTHR22952:SF200 PTHR22952:SF200, 1 hit
Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit PF02173 pKID, 1 hit
PRINTSⁱ	PR00041 LEUZIPPRCREB
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit PS50953 KID, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CREB1_MOUSE
Accessionⁱ	Q01147Primary (citable) accession number: Q01147
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
	Last sequence update:	June 1, 1994
	Last modified:	November 7, 2018
	This is version 191 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - Q01147 (CREB1_MOUSE)

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Cyclic AMP-responsive element-binding protein 1

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

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Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

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Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

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Protocols and materials databases

Genome annotation databases

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Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ