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Protein

Cyclic AMP-responsive element-binding protein 3

Gene

CREB3

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

Endoplasmic reticulum (ER)-bound sequence-specific transcription factor that directly binds DNA and activates transcription (PubMed:9271389, PubMed:19779205, PubMed:10984507, PubMed:15845366, PubMed:16940180). Plays a role in the unfolded protein response (UPR), promoting cell survival versus ER stress-induced apoptotic cell death (PubMed:15845366, PubMed:16940180). Also involved in cell proliferation, migration and differentiation, tumor suppression and inflammatory gene expression. Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration (PubMed:19779205, PubMed:15001559, PubMed:17296613). Associates with chromatin to the HERPUD1 promoter (PubMed:16940180). Also induces transcriptional activation of chemokine receptors (PubMed:18587271, PubMed:17296613).8 Publications
Processed cyclic AMP-responsive element-binding protein 3: This is the transcriptionally active form that translocates to the nucleus and activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many promoters to activate transcription of the genes. Binds to the unfolded protein response element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3').1 Publication
Isoform 2: Functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells.1 Publication
(Microbial infection) Plays a role in human immunodeficiency virus type 1 (HIV-1) virus protein expression.1 Publication
(Microbial infection) Isoform 1: Plays a role in herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestering host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection.2 Publications
(Microbial infection) Isoform 1: May play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HCV) core protein.1 Publication
(Microbial infection) Processed cyclic AMP-responsive element-binding protein 3: Activates transcription of genes required for reactivation of the latent HSV-1 virus. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral promoters.1 Publication
(Microbial infection) Processed cyclic AMP-responsive element-binding protein 3: It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator HCV core protein.1 Publication

Caution

All experiments concerning the proteolytic cleavage are done with isoform 1.Curated

<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, Repressor
Biological processChemotaxis, Host-virus interaction, Transcription, Transcription regulation, Unfolded protein response

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8874211 CREB3 factors activate genes

SIGNOR Signaling Network Open Resource

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SIGNORi
O43889

<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 3
Short name:
CREB-3
Short name:
cAMP-responsive element-binding protein 3
Alternative name(s):
Leucine zipper protein
Luman
Transcription factor LZIP-alpha
Cleaved into the following chain:
Processed cyclic AMP-responsive element-binding protein 3
Short name:
N-terminal Luman
Short name:
Transcriptionally active form
<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:CREB3
Synonyms:LZIP
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000107175.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2347 CREB3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606443 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43889

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 230Cytoplasmic1 PublicationAdd BLAST230
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei231 – 247Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini248 – 371Lumenal1 PublicationAdd BLAST124

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, 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

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>Mutagenesisi12 – 13LL → AA: Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 56-A-A-57 and 78-A--A-81 (isoform 1). 1 Publication2
Mutagenesisi16 – 17LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 2). 2 Publications2
Mutagenesisi57 – 58LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 2). 1 Publication2
Mutagenesisi57 – 58LL → AA: Does not inhibit interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 78-A--A-81 (isoform 1). 1 Publication2
Mutagenesisi78 – 81DHTY → AAAA: Inhibits interaction with HCFC1. Reduces transcriptional activation. Inhibits strongly transcriptional activation; when associated with 12-A-A-13 and 56-A-A-57. Colocalizes with HCFC1 in the nucleus (isoform 1). 2 Publications4
Mutagenesisi81Y → A: Does not retain HCFC1 in the cytoplasm, does not interact with HCFC1, does not activate promoter and fail to protect cells from a productive infection by HSV-1. 1 Publication1
Mutagenesisi160N → G: Does not bind to DNA but retains its ability to interact with HCFC1. Reduces transcriptional activation of unfolded protein response elements (UPRE)-containing promoter. Colocalizes with HCFC1 in the ER membrane. 1 Publication1
Mutagenesisi252R → A: Does not inhibit proteolytic cleavage and transcriptional activation. 1 Publication1
Mutagenesisi264R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication1
Mutagenesisi267R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10488

Open Targets

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OpenTargetsi
ENSG00000107175

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26865

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CREB3

<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_00000766021 – 371Cyclic AMP-responsive element-binding protein 3Add BLAST371
ChainiPRO_00002962041 – ?Processed cyclic AMP-responsive element-binding protein 3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi348N-linked (GlcNAc...) asparagineSequence analysis1

<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

First proteolytically cleaved by site-1 protease (S1P) that generates membrane-associated N-terminus and a luminal C-terminus forms. The membrane-associated N-terminus form is further proteolytically processed probably by the site-2 protease (S2P) through a regulated intramembrane proteolysis (RIP), releasing the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form, which is transported to the nucleus. The proteolytic cleavage is strongly induced during dendritic cell (DC) maturation and inhibited by DCSTAMP. That form is rapidly degraded.5 Publications
N-glycosylated.2 Publications

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>Sitei263 – 264Cleavage; by PS11 Publication2
Sitei266 – 267Cleavage; by PS11 Publication2

Keywords - PTMi

Glycoprotein

Proteomic databases

PeptideAtlas

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PeptideAtlasi
O43889

PRoteomics IDEntifications database

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PRIDEi
O43889

ProteomicsDB human proteome resource

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ProteomicsDBi
49216
49217 [O43889-2]
49218 [O43889-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43889

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

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PhosphoSitePlusi
O43889

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed (PubMed:9271389, PubMed:19779205). Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level) (PubMed:20546900).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated upon differentiation of monocytes towards immature dendritic cells (DC). Down-regulated upon DC maturation. Up-regulated by endoplasmic reticulum stress triggered by thapsigargin (Tg) or tunicamycin (Tm). Up-regulated by CCR1-dependent chemokines in an immediate early response and biphasic manner and by NF-kappa-B.5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000107175 Expressed in 219 organ(s), highest expression level in adenohypophysis

CleanEx database of gene expression profiles

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CleanExi
HS_CREB3

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43889 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA030978

<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

Homodimer (PubMed:10675342). Isoform 1 interacts with HCFC1; the interaction is required to stimulate CREB3 transcriptional activity (PubMed:9271389, PubMed:9389645, PubMed:10629049, PubMed:10984507). Isoform 1 interacts with CREBZF; the interaction occurs only in combination with HCFC1 (PubMed:15705566). Isoform 1 interacts (via central part and transmembrane region) with DCSTAMP (via C-terminus cytoplasmic domain) (PubMed:20546900). Isoform 1 interacts with OS9 (PubMed:20546900). Isoform 1 interacts (via leucine-zipper domain) with CREBRF (via leucine-zipper domain); the interaction occurs only after CREB3 activation and promotes CREB3 degradation (PubMed:18391022). Isoform 1 interacts (via C-terminal domain) with CCR1 (PubMed:15001559).9 Publications
(Microbial infection) Interacts with the HCV core protein; homodimerization is prevented by the HCV core protein (PubMed:10675342). Isoform 1 interacts (via leucine-zipper and transmembrane domains) with HIV-1 TMgp41 (via cytoplasmic domain); the interaction reduces CREB3 stability (PubMed:17054986). Processed cyclic AMP-responsive element-binding protein 3 interacts with HIV-1 Tat (PubMed:17054986).2 Publications

<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
115751, 191 interactors

Database of interacting proteins

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DIPi
DIP-33935N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O43889

Protein interaction database and analysis system

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IntActi
O43889, 169 interactors

Molecular INTeraction database

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MINTi
O43889

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O43889

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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>Domaini150 – 213bZIPPROSITE-ProRule annotationAdd BLAST64

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>Regioni1 – 92Transcription activation (acidic)1 PublicationAdd BLAST92
Regioni152 – 184Basic motifPROSITE-ProRule annotationAdd BLAST33
Regioni192 – 213Leucine-zipperPROSITE-ProRule annotationAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi13 – 17LXXLL motif 15
Motifi54 – 58LXXLL motif 25
Motifi78 – 81HCFC1-binding-motif (HBM)4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi316 – 361Pro-richAdd BLAST46

<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. ATF subfamily.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000160343

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000133026

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051114

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43889

KEGG Orthology (KO)

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KOi
K09048

Identification of Orthologs from Complete Genome Data

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OMAi
HVSIDLD

Database for complete collections of gene phylogenies

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PhylomeDBi
O43889

TreeFam database of animal gene trees

More...
TreeFami
TF316079

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004827 bZIP
IPR029808 Luman

The PANTHER Classification System

More...
PANTHERi
PTHR22952:SF100 PTHR22952:SF100, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00170 bZIP_1, 1 hit

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

<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 (2)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <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
Isoform 1 (identifier: O43889-2) [UniParc]FASTAAdd to basket
Also known as: LZIP

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
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV
60 70 80 90 100
DDLLCSLLSP PASLNILSSS NPCLVHHDHT YSLPRETVSM DLESESCRKE
110 120 130 140 150
GTQMTPQHME ELAEQEIARL VLTDEEKSLL EKEGLILPET LPLTKTEEQI
160 170 180 190 200
LKRVRRKIRN KRSAQESRRK KKVYVGGLES RVLKYTAQNM ELQNKVQLLE
210 220 230 240 250
EQNLSLLDQL RKLQAMVIEI SNKTSSSSTC ILVLLVSFCL LLVPAMYSSD
260 270 280 290 300
TRGSLPAEHG VLSRQLRALP SEDPYQLELP ALQSEVPKDS THQWLDGSDC
310 320 330 340 350
VLQAPGNTSC LLHYMPQAPS AEPPLEWPFP DLFSEPLCRG PILPLQANLT
360 370
RKGGWLPTGS PSVILQDRYS G
Length:371
Mass (Da):41,379
Last modified:March 28, 2018 - 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:i82152E496B924EEC
GO
Isoform 2 (identifier: O43889-3) [UniParc]FASTAAdd to basket
Also known as: small LZIP, sLZIP

The sequence of this isoform differs from the canonical sequence as follows:
     229-245: Missing.

Note: Does not contain a helical transmembrane domain.
Show »
Length:354
Mass (Da):39,580
Checksum:iBC8F014103A52111
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC04325 differs from that shown. Probable cloning artifact.Curated

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 conflicti21G → E in AAG43527 (Ref. 6) Curated1
Sequence conflicti230C → G in AAD09210 (PubMed:10675342).Curated1
Sequence conflicti246M → I in AAH09402 (PubMed:15489334).Curated1
Sequence conflicti262L → C in AAD09210 (PubMed:10675342).Curated1
Sequence conflicti333F → S in AAB69652 (PubMed:9271389).Curated1
Sequence conflicti338C → V in AAD09210 (PubMed:10675342).Curated1

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_059386229 – 245Missing in isoform 2. Add BLAST17

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF009368 mRNA Translation: AAB69652.1
AF029674 mRNA Translation: AAB84166.1
U59629 Genomic DNA Translation: AAD09210.1
FJ263669 mRNA Translation: ACN32251.1
U88528 mRNA Translation: AAC04325.1 Sequence problems.
AF211847 Genomic DNA Translation: AAG43527.1
AF211848 mRNA Translation: AAG43528.1
AL133410 Genomic DNA No translation available.
BC009402 mRNA Translation: AAH09402.1
BC010158 mRNA Translation: AAH10158.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS6588.1 [O43889-2]

NCBI Reference Sequences

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RefSeqi
NP_006359.3, NM_006368.4 [O43889-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.522110

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000353704; ENSP00000342136; ENSG00000107175 [O43889-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
10488

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10488

UCSC genome browser

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UCSCi
uc003zxv.4 human [O43889-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF009368 mRNA Translation: AAB69652.1
AF029674 mRNA Translation: AAB84166.1
U59629 Genomic DNA Translation: AAD09210.1
FJ263669 mRNA Translation: ACN32251.1
U88528 mRNA Translation: AAC04325.1 Sequence problems.
AF211847 Genomic DNA Translation: AAG43527.1
AF211848 mRNA Translation: AAG43528.1
AL133410 Genomic DNA No translation available.
BC009402 mRNA Translation: AAH09402.1
BC010158 mRNA Translation: AAH10158.1
CCDSiCCDS6588.1 [O43889-2]
RefSeqiNP_006359.3, NM_006368.4 [O43889-2]
UniGeneiHs.522110

3D structure databases

ProteinModelPortaliO43889
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115751, 191 interactors
DIPiDIP-33935N
ELMiO43889
IntActiO43889, 169 interactors
MINTiO43889

PTM databases

iPTMnetiO43889
PhosphoSitePlusiO43889

Polymorphism and mutation databases

BioMutaiCREB3

Proteomic databases

PeptideAtlasiO43889
PRIDEiO43889
ProteomicsDBi49216
49217 [O43889-2]
49218 [O43889-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10488
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353704; ENSP00000342136; ENSG00000107175 [O43889-2]
GeneIDi10488
KEGGihsa:10488
UCSCiuc003zxv.4 human [O43889-2]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
10488
DisGeNETi10488
EuPathDBiHostDB:ENSG00000107175.10

GeneCards: human genes, protein and diseases

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GeneCardsi
CREB3
HGNCiHGNC:2347 CREB3
HPAiHPA030978
MIMi606443 gene
neXtProtiNX_O43889
OpenTargetsiENSG00000107175
PharmGKBiPA26865

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00940000160343
HOGENOMiHOG000133026
HOVERGENiHBG051114
InParanoidiO43889
KOiK09048
OMAiHVSIDLD
PhylomeDBiO43889
TreeFamiTF316079

Enzyme and pathway databases

ReactomeiR-HSA-8874211 CREB3 factors activate genes
SIGNORiO43889

Miscellaneous databases

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

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ChiTaRSi
CREB3 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CREB3

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

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GenomeRNAii
10488

Protein Ontology

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PROi
PR:O43889

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000107175 Expressed in 219 organ(s), highest expression level in adenohypophysis
CleanExiHS_CREB3
GenevisibleiO43889 HS

Family and domain databases

InterProiView protein in InterPro
IPR004827 bZIP
IPR029808 Luman
PANTHERiPTHR22952:SF100 PTHR22952:SF100, 1 hit
PfamiView protein in Pfam
PF00170 bZIP_1, 1 hit
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiCREB3_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: O43889
Secondary accession number(s): D0PTW6
, O14671, O14919, Q5TCV1, Q96GK8, Q9H2W3, Q9UE77
<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: November 9, 2004
Last sequence update: March 28, 2018
Last modified: December 5, 2018
This is version 176 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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