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Protein

Cyclic AMP-responsive element-binding protein 1

Gene

CREB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei314Required for binding TORCs1

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processBiological rhythms, Differentiation, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-111931 PKA-mediated phosphorylation of CREB
R-HSA-111932 CaMK IV-mediated phosphorylation of CREB
R-HSA-198693 AKT phosphorylates targets in the nucleus
R-HSA-199920 CREB phosphorylation
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-2197563 NOTCH2 intracellular domain regulates transcription
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-400253 Circadian Clock
R-HSA-442717 CREB phosphorylation through the activation of CaMKK
R-HSA-442720 CREB phosphorylation through the activation of Adenylate Cyclase
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9022702 MECP2 regulates transcription of neuronal ligands
R-HSA-9022707 MECP2 regulates transcription factors

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P16220

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P16220

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cyclic AMP-responsive element-binding protein 1
Short name:
CREB-1
Short name:
cAMP-responsive element-binding protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CREB1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000118260.14

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2345 CREB1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
123810 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P16220

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Angiomatoid fibrous histiocytoma (AFH)
The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving CREB1 is found in a patient with angiomatoid fibrous histiocytoma. Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type.
Disease descriptionA distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis.
See also OMIM:612160
A CREB1 mutation has been found in a patient with multiple congenital anomalies consisting of agenesis of the corpus callosum, cerebellar hypoplasia, severe neonatal respiratory distress refractory to surfactant, thymus hypoplasia, and thyroid follicular hypoplasia.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi133S → A: Does not interact with TOX3 and inhibits induction of transcription by TOX3. Loss of phosphorylation by CaMK4. Loss of phosphorylation by TSSK4. 3 Publications1
Mutagenesisi155K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi271S → A: Impaired phosphorylation by HIPK2 and subsequent transactivation. 1 Publication1
Mutagenesisi271S → E: Potentiated transactivation. 1 Publication1
Mutagenesisi285K → R: Decreased sumoylation, in vivo and in vitro. 1 Publication1
Mutagenesisi304K → R: Decreased sumoylation, in vivo and in vitro. Loss of nuclear localization. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
1385

MalaCards human disease database

More...
MalaCardsi
CREB1
MIMi612160 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000118260

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
97338 Melanoma of soft tissue

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA26864

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5587

Drug and drug target database

More...
DrugBanki
DB00131 Adenosine monophosphate
DB01183 Naloxone

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CREB1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
117434

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000765971 – 341Cyclic AMP-responsive element-binding protein 1Add BLAST341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei133Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5, SGK1 and TSSK4PROSITE-ProRule annotation6 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei142PhosphoserineCombined sources1
Modified residuei271Phosphoserine; by HIPK2PROSITE-ProRule annotation1 Publication1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Stimulated by phosphorylation. Phosphorylation of both Ser-133 and Ser-142 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylation of Ser-133 allows CREBBP binding. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion (By similarity). CREBL2 positively regulates phosphorylation at Ser-133 thereby stimulating CREB1 transcriptional activity (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 (By similarity). 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. Phosphorylated by TSSK4 on Ser-133 (PubMed:15964553).By similarity7 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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P16220

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P16220

PeptideAtlas

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PeptideAtlasi
P16220

PRoteomics IDEntifications database

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PRIDEi
P16220

ProteomicsDB human proteome resource

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ProteomicsDBi
53324
53325 [P16220-2]
53326 [P16220-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P16220

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P16220

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P16220

<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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000118260 Expressed in 242 organ(s), highest expression level in lung

CleanEx database of gene expression profiles

More...
CleanExi
HS_CREB1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P16220 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P16220 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB003803
HPA019150

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. When phosphorylated on Ser-133, binds CREBBP (By similarity). Interacts with CREBL2; regulates CREB1 phosphorylation, stability and transcriptional activity (By similarity). Interacts (phosphorylated form) with TOX3. Interacts with ARRB1. Binds to HIPK2. Interacts with SGK1. Interacts with TSSK4; this interaction facilitates phosphorylation on Ser-133 (PubMed:15964553).By similarity9 Publications
(Microbial infection) Interacts with hepatitis B virus/HBV protein X.1 Publication
(Microbial infection) Interacts with HTLV-1 protein Tax.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107775, 145 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-8 ATF4-CREB1 transcription factor complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P16220

Database of interacting proteins

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DIPi
DIP-765N

Protein interaction database and analysis system

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IntActi
P16220, 80 interactors

Molecular INTeraction database

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MINTi
P16220

STRING: functional protein association networks

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STRINGi
9606.ENSP00000387699

<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

1341
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P16220

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P16220

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini101 – 160KIDPROSITE-ProRule annotationAdd BLAST60
Domaini283 – 341bZIPPROSITE-ProRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni284 – 309Basic motifPROSITE-ProRule annotationAdd BLAST26
Regioni311 – 332Leucine-zipperPROSITE-ProRule annotationAdd BLAST22

<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

Belongs to the bZIP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3584 Eukaryota
ENOG410ZZJZ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155408

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007365

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG011077

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P16220

KEGG Orthology (KO)

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KOi
K05870

Identification of Orthologs from Complete Genome Data

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OMAi
QXISTIA

Database of Orthologous Groups

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OrthoDBi
EOG091G0FTJ

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P16220

TreeFam database of animal gene trees

More...
TreeFami
TF106464

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004827 bZIP
IPR003102 Coactivator_CBP_pKID
IPR029802 CREB1
IPR001630 Leuzip_CREB

The PANTHER Classification System

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PANTHERi
PTHR22952:SF200 PTHR22952:SF200, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00170 bZIP_1, 1 hit
PF02173 pKID, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00041 LEUZIPPRCREB

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit
PS50953 KID, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform CREB-A (identifier: P16220-1) [UniParc]FASTAAdd 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
MTMESGAENQ 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):36,688
Last modified:May 1, 1992 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD5E989AE40BF69AF
GO
Isoform CREB-B (identifier: P16220-2) [UniParc]FASTAAdd to basket

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

Show »
Length:327
Mass (Da):35,136
Checksum:iF5BA8200EE5184B7
GO
Isoform 3 (identifier: P16220-3) [UniParc]FASTAAdd to basket
Also known as: htCREB

The sequence of this isoform differs from the canonical sequence as follows:
     162-272: Missing.

Note: Highly expressed in adult testis and sperm.
Show »
Length:230
Mass (Da):25,445
Checksum:i9FD8CA28F7632FBD
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J896C9J896_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
251Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JBT4C9JBT4_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
170Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EWP8E7EWP8_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
182Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J4L5C9J4L5_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
131Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C3I0H7C3I0_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
181Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C1R5H7C1R5_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
140Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J276C9J276_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
132Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JCI4C9JCI4_HUMAN
Cyclic AMP-responsive element-bindi...
CREB1
79Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti4E → D in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti8E → D in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti160T → A in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti167T → A in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti169T → A in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti176Q → R in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti184A → T in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti188G → R in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti195N → S in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti210T → A in CAA42620 (PubMed:1831258).Curated1
Sequence conflicti292K → E in AAQ24858 (PubMed:15579595).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068077116D → G Found in a patient with multiple congenital anomalies; does not affect CREB1 phosphorylation at S-133; fails to interact with CREBBP. 1 PublicationCorresponds to variant dbSNP:rs387906617EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00059688 – 101Missing in isoform CREB-B. 2 PublicationsAdd BLAST14
Alternative sequenceiVSP_043914162 – 272Missing in isoform 3. 1 PublicationAdd BLAST111

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S72459 Genomic DNA Translation: AAB20597.1
X55545 mRNA Translation: CAA39151.1
M34356 mRNA Translation: AAA35717.1
M34356 mRNA Translation: AAA35716.1
M27691 mRNA Translation: AAA35715.1
X60003 mRNA Translation: CAA42620.1
AY347527 mRNA Translation: AAQ24858.1
BC010636 mRNA Translation: AAH10636.1
S53724 Genomic DNA Translation: AAD13869.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2374.1 [P16220-2]
CCDS2375.1 [P16220-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A37340 A35769
B37340 B35769
S22298

NCBI Reference Sequences

More...
RefSeqi
NP_004370.1, NM_004379.4 [P16220-2]
NP_604391.1, NM_134442.4 [P16220-1]
XP_011508947.1, XM_011510645.1 [P16220-1]
XP_011508949.1, XM_011510647.2 [P16220-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.516646
Hs.717136

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000353267; ENSP00000236995; ENSG00000118260 [P16220-2]
ENST00000430624; ENSP00000405539; ENSG00000118260 [P16220-2]
ENST00000432329; ENSP00000387699; ENSG00000118260 [P16220-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1385

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1385

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S72459 Genomic DNA Translation: AAB20597.1
X55545 mRNA Translation: CAA39151.1
M34356 mRNA Translation: AAA35717.1
M34356 mRNA Translation: AAA35716.1
M27691 mRNA Translation: AAA35715.1
X60003 mRNA Translation: CAA42620.1
AY347527 mRNA Translation: AAQ24858.1
BC010636 mRNA Translation: AAH10636.1
S53724 Genomic DNA Translation: AAD13869.1
CCDSiCCDS2374.1 [P16220-2]
CCDS2375.1 [P16220-1]
PIRiA37340 A35769
B37340 B35769
S22298
RefSeqiNP_004370.1, NM_004379.4 [P16220-2]
NP_604391.1, NM_134442.4 [P16220-1]
XP_011508947.1, XM_011510645.1 [P16220-1]
XP_011508949.1, XM_011510647.2 [P16220-2]
UniGeneiHs.516646
Hs.717136

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 entryMethodResolution (Å)ChainPositionsPDBsum
2LXTNMR-C116-149[»]
5ZK1X-ray3.05A283-341[»]
5ZKOX-ray3.05A/C283-341[»]
ProteinModelPortaliP16220
SMRiP16220
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107775, 145 interactors
ComplexPortaliCPX-8 ATF4-CREB1 transcription factor complex
CORUMiP16220
DIPiDIP-765N
IntActiP16220, 80 interactors
MINTiP16220
STRINGi9606.ENSP00000387699

Chemistry databases

ChEMBLiCHEMBL5587
DrugBankiDB00131 Adenosine monophosphate
DB01183 Naloxone

PTM databases

iPTMnetiP16220
PhosphoSitePlusiP16220

Polymorphism and mutation databases

BioMutaiCREB1
DMDMi117434

Proteomic databases

EPDiP16220
PaxDbiP16220
PeptideAtlasiP16220
PRIDEiP16220
ProteomicsDBi53324
53325 [P16220-2]
53326 [P16220-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1385
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353267; ENSP00000236995; ENSG00000118260 [P16220-2]
ENST00000430624; ENSP00000405539; ENSG00000118260 [P16220-2]
ENST00000432329; ENSP00000387699; ENSG00000118260 [P16220-1]
GeneIDi1385
KEGGihsa:1385

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1385
DisGeNETi1385
EuPathDBiHostDB:ENSG00000118260.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CREB1
HGNCiHGNC:2345 CREB1
HPAiCAB003803
HPA019150
MalaCardsiCREB1
MIMi123810 gene
612160 phenotype
neXtProtiNX_P16220
OpenTargetsiENSG00000118260
Orphaneti97338 Melanoma of soft tissue
PharmGKBiPA26864

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3584 Eukaryota
ENOG410ZZJZ LUCA
GeneTreeiENSGT00940000155408
HOGENOMiHOG000007365
HOVERGENiHBG011077
InParanoidiP16220
KOiK05870
OMAiQXISTIA
OrthoDBiEOG091G0FTJ
PhylomeDBiP16220
TreeFamiTF106464

Enzyme and pathway databases

ReactomeiR-HSA-111931 PKA-mediated phosphorylation of CREB
R-HSA-111932 CaMK IV-mediated phosphorylation of CREB
R-HSA-198693 AKT phosphorylates targets in the nucleus
R-HSA-199920 CREB phosphorylation
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-2197563 NOTCH2 intracellular domain regulates transcription
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-400253 Circadian Clock
R-HSA-442717 CREB phosphorylation through the activation of CaMKK
R-HSA-442720 CREB phosphorylation through the activation of Adenylate Cyclase
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
R-HSA-9022692 Regulation of MECP2 expression and activity
R-HSA-9022699 MECP2 regulates neuronal receptors and channels
R-HSA-9022702 MECP2 regulates transcription of neuronal ligands
R-HSA-9022707 MECP2 regulates transcription factors
SignaLinkiP16220
SIGNORiP16220

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CREB1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CREB1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1385
PMAP-CutDBiP16220

Protein Ontology

More...
PROi
PR:P16220

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000118260 Expressed in 242 organ(s), highest expression level in lung
CleanExiHS_CREB1
ExpressionAtlasiP16220 baseline and differential
GenevisibleiP16220 HS

Family and domain databases

InterProiView protein in InterPro
IPR004827 bZIP
IPR003102 Coactivator_CBP_pKID
IPR029802 CREB1
IPR001630 Leuzip_CREB
PANTHERiPTHR22952:SF200 PTHR22952:SF200, 1 hit
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
PF02173 pKID, 1 hit
PRINTSiPR00041 LEUZIPPRCREB
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit
PS50953 KID, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCREB1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16220
Secondary accession number(s): P21934, Q6V963, Q9UMA7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: May 1, 1992
Last modified: December 5, 2018
This is version 225 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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