CREB3

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

GO - Molecular functionⁱ

cAMP response element binding Source: InterPro
cAMP response element binding protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9271389
CCR1 chemokine receptor binding
Source: UniProtKB
Inferred from direct assayⁱ
- 15001559
chromatin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 16940180
DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10675342
- 9271389
DNA-binding transcription factor activity
Source: UniProtKB
Inferred from direct assayⁱ
DNA-binding transcription factor activity, RNA polymerase II-specific Source: NTNU_SB
protein dimerization activity
Source: UniProtKB
Traceable author statementⁱ
- 10623756
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10675342
- 20141198
proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific
Source: NTNU_SB
Inferred from mutant phenotypeⁱ
- 16940180
RNA polymerase II proximal promoter sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 16940180
RNA polymerase II regulatory region sequence-specific DNA binding
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 16940180
transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding
Source: NTNU_SB
Inferred from direct assayⁱ
- 16940180

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chemotaxis Source: UniProtKB-KW
cytoplasmic sequestering of transcription factor
Source: UniProtKB
Inferred from direct assayⁱ
- 20091349
endoplasmic reticulum unfolded protein response Source: Reactome
establishment of viral latency
Source: UniProtKB
Inferred from direct assayⁱ
- 20091349
induction of positive chemotaxis
Source: UniProtKB
Inferred from direct assayⁱ
- 19779205
negative regulation of cell cycle
Source: UniProtKB
Non-traceable author statementⁱ
- 10623756
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 16940180
negative regulation of nuclear receptor transcription coactivator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19779205
positive regulation of calcium ion transport
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15001559
positive regulation of cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15001559
positive regulation of deacetylase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19779205
positive regulation of defense response to virus by host
Source: UniProtKB
Inferred from direct assayⁱ
- 20091349
positive regulation of monocyte chemotaxis
Source: UniProtKB
Inferred from direct assayⁱ
- 17296613
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 9271389
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response
Source: ParkinsonsUK-UCL
Inferred from direct assayⁱ
- 16940180
regulation of apoptotic process
Source: UniProtKB
Inferred from direct assayⁱ
- 16940180
regulation of cell growth
Source: UniProtKB
Inferred from direct assayⁱ
- 20141198
regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10675342
release from viral latency
Source: UniProtKB
Inferred from direct assayⁱ
- 20091349
response to endoplasmic reticulum stress
Source: UniProtKB
Inferred from direct assayⁱ
- 16940180
- 18391022
transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 9271389
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding, Repressor
Biological process	Chemotaxis, Host-virus interaction, Transcription, Transcription regulation, Unfolded protein response

Enzyme and pathway databases

Reactomeⁱ	R-HSA-8874211 CREB3 factors activate genes
SIGNORⁱ	O43889

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:CREB3 Synonyms:LZIP
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000107175.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:2347 CREB3
MIMⁱ	606443 gene
neXtProtⁱ	NX_O43889

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 230	Cytoplasmic1 PublicationAdd BLAST	230
Transmembraneⁱ	231 – 247	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	17
Topological domainⁱ	248 – 371	Lumenal1 PublicationAdd BLAST	124

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	12 – 13	LL → 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 Publication	2
Mutagenesisⁱ	16 – 17	LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 2). 2 Publications	2
Mutagenesisⁱ	57 – 58	LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 2). 1 Publication	2
Mutagenesisⁱ	57 – 58	LL → 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 Publication	2
Mutagenesisⁱ	78 – 81	DHTY → 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 Publications	4
Mutagenesisⁱ	81	Y → 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 Publication	1
Mutagenesisⁱ	160	N → 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 Publication	1
Mutagenesisⁱ	252	R → A: Does not inhibit proteolytic cleavage and transcriptional activation. 1 Publication	1
Mutagenesisⁱ	264	R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication	1
Mutagenesisⁱ	267	R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	10488
Open Targets More...OpenTargetsⁱ	ENSG00000107175
PharmGKBⁱ	PA26865

Polymorphism and mutation databases

BioMutaⁱ	CREB3

BioMutaⁱ

CREB3

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000076602	1 – 371	Cyclic AMP-responsive element-binding protein 3Add BLAST		371
ChainⁱPRO_0000296204	1 – ?	Processed cyclic AMP-responsive element-binding protein 3

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Glycosylationⁱ	307	N-linked (GlcNAc...) asparagineSequence analysis		1
Glycosylationⁱ	348	N-linked (GlcNAc...) asparagineSequence analysis		1

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 key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	263 – 264	Cleavage; by PS11 Publication		2
Siteⁱ	266 – 267	Cleavage; by PS11 Publication		2

Keywords - PTMⁱ

Glycoprotein

Proteomic databases

PeptideAtlas More...PeptideAtlasⁱ	O43889
PRIDEⁱ	O43889
ProteomicsDBⁱ	49216 49217 [O43889-2] 49218 [O43889-3]

PTM databases

iPTMnetⁱ	O43889
PhosphoSitePlusⁱ	O43889

Expressionⁱ

Tissue specificityⁱ

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

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

Bgeeⁱ	ENSG00000107175 Expressed in 219 organ(s), highest expression level in adenohypophysis
CleanExⁱ	HS_CREB3
Genevisibleⁱ	O43889 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA030978

HPAⁱ

HPA030978

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
	P29846	8	EBI-625022,EBI-909718	From Hepatitis C virus genotype 1b (isolate Taiwan).
AGER	Q15109	3	EBI-625022,EBI-1646426
ALG3	Q92685	3	EBI-625022,EBI-2848814
ALG8	Q9BVK2	3	EBI-625022,EBI-3921603
APOD	P05090	3	EBI-625022,EBI-715495
AQP1	P29972	3	EBI-625022,EBI-745213
AQP2	P41181	3	EBI-625022,EBI-12701138
AQP4	P55087	3	EBI-625022,EBI-10104898
C1S	P09871	3	EBI-625022,EBI-2810045
C2	P06681	3	EBI-625022,EBI-2835920
CCR1	P32246	7	EBI-625022,EBI-608322
CD207	Q9UJ71	3	EBI-625022,EBI-2873235
CFHR5	Q9BXR6	3	EBI-625022,EBI-11579371
CLDN19	Q8N6F1-2	3	EBI-625022,EBI-12256978
CREB3L3	Q68CJ9	2	EBI-625002,EBI-852194
CREBRF	Q8IUR6	4	EBI-625022,EBI-1042699
CYP4F2	P78329	3	EBI-625022,EBI-1752413
DCSTAMP	Q9H295	6	EBI-625022,EBI-6095316
EBP	Q15125	3	EBI-625022,EBI-3915253
EMD	P50402	3	EBI-625022,EBI-489887
FDFT1	P37268	3	EBI-625022,EBI-714550
FMO1	Q01740	3	EBI-625022,EBI-12701460
FMO3	P31513	3	EBI-625022,EBI-12361463
GJA1	P17302	3	EBI-625022,EBI-1103439
GYPA	A0A0C4DFT7	3	EBI-625022,EBI-12044847
HCFC1	P51610	5	EBI-625002,EBI-396176
IGFBP5	P24593	3	EBI-625022,EBI-720480
JUN	P05412	4	EBI-625002,EBI-852823
LHFPL5	Q8TAF8	3	EBI-625022,EBI-2820517
LTA	Q6FG55	3	EBI-625022,EBI-11984863
MGST2	Q99735	3	EBI-625022,EBI-11324706
NEU1	Q99519	3	EBI-625022,EBI-721517
PLN	P26678	3	EBI-625022,EBI-692836
PLP1	P60201-2	3	EBI-625022,EBI-12188331
PMP22	Q01453	3	EBI-625022,EBI-2845982
SERPING1	P05155	3	EBI-625022,EBI-1223454
SFTPC	P11686	3	EBI-625022,EBI-10197617
SLC29A3	Q9BZD2	3	EBI-625022,EBI-12701374
SLC2A1	P11166	3	EBI-625022,EBI-717153
SLC2A4	P14672	3	EBI-625022,EBI-367146
SLC30A2	Q9BRI3	3	EBI-625022,EBI-8644112
SLC7A9	P82251	3	EBI-625022,EBI-3936589
SYNGR1	O43759-2	3	EBI-625022,EBI-12187159
TAF4	O00268	2	EBI-625002,EBI-1034261
VANGL1	Q8TAA9	3	EBI-625022,EBI-682393
ZDHHC9	Q9Y397	3	EBI-625022,EBI-12690113

GO - Molecular functionⁱ

cAMP response element binding protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9271389
CCR1 chemokine receptor binding
Source: UniProtKB
Inferred from direct assayⁱ
- 15001559
protein dimerization activity
Source: UniProtKB
Traceable author statementⁱ
- 10623756
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10675342
- 20141198

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115751, 191 interactors
Database of interacting proteins More...DIPⁱ	DIP-33935N
ELMⁱ	O43889
IntActⁱ	O43889, 169 interactors
Molecular INTeraction database More...MINTⁱ	O43889

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	O43889
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	150 – 213	bZIPPROSITE-ProRule annotationAdd BLAST		64

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 92	Transcription activation (acidic)1 PublicationAdd BLAST	92
Regionⁱ	152 – 184	Basic motifPROSITE-ProRule annotationAdd BLAST	33
Regionⁱ	192 – 213	Leucine-zipperPROSITE-ProRule annotationAdd BLAST	22

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	13 – 17	LXXLL motif 1	5
Motifⁱ	54 – 58	LXXLL motif 2	5
Motifⁱ	78 – 81	HCFC1-binding-motif (HBM)	4

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	316 – 361	Pro-richAdd BLAST		46

Sequence similaritiesⁱ

Belongs to the bZIP family. ATF subfamily.Curated

Keywords - Domainⁱ

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00520000055538
HOGENOMⁱ	HOG000133026
HOVERGENⁱ	HBG051114
InParanoidⁱ	O43889
KEGG Orthology (KO) More...KOⁱ	K09048
OMAⁱ	HVSIDLD
PhylomeDBⁱ	O43889
TreeFamⁱ	TF316079

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR029808 Luman
PANTHERⁱ	PTHR22952:SF100 PTHR22952:SF100, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: O43889-2) [UniParc]FASTA Add 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

Checksum:ⁱ82152E496B924EEC

GO

Isoform 2 (identifier: O43889-3) [UniParc]FASTA Add to basket

Also known as: small LZIP, sLZIP

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

« 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 SNKTSSSSMY SSDTRGSLPA EHGVLSRQLR 
       260        270        280        290        300
ALPSEDPYQL ELPALQSEVP KDSTHQWLDG SDCVLQAPGN TSCLLHYMPQ 
       310        320        330        340        350
APSAEPPLEW PFPDLFSEPL CRGPILPLQA NLTRKGGWLP TGSPSVILQD 

RYSG

Note: Does not contain a helical transmembrane domain.

Show »

Length:354

Mass (Da):39,580

Checksum:ⁱBC8F014103A52111

GO

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	21	G → E in AAG43527 (Ref. 6) Curated	1
Sequence conflictⁱ	230	C → G in AAD09210 (PubMed:10675342).Curated	1
Sequence conflictⁱ	246	M → I in AAH09402 (PubMed:15489334).Curated	1
Sequence conflictⁱ	262	L → C in AAD09210 (PubMed:10675342).Curated	1
Sequence conflictⁱ	333	F → S in AAB69652 (PubMed:9271389).Curated	1
Sequence conflictⁱ	338	C → V in AAD09210 (PubMed:10675342).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_059386	229 – 245	Missing in isoform 2. Add BLAST		17

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6588.1 [O43889-2]
NCBI Reference Sequences More...RefSeqⁱ	NP_006359.3, NM_006368.4 [O43889-2]
UniGeneⁱ	Hs.522110

Genome annotation databases

Ensemblⁱ	ENST00000353704; ENSP00000342136; ENSG00000107175 [O43889-2]
GeneIDⁱ	10488
KEGGⁱ	hsa:10488
UCSC genome browser More...UCSCⁱ	uc003zxv.4 human [O43889-2]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O43889	cDNA FLJ57143, highly similar to Cyclic AMP-responsive element-binding protein 3		HUMAN		282	UniRef100_O43889

Protein	Similar proteins		Species	Score	Length	Source
O43889	cDNA FLJ57143, highly similar to Cyclic AMP-responsive element-binding protein 3		HUMAN		282	UniRef90_O43889
Uncharacterized protein		CERAT		372
Uncharacterized protein		MANLE		372
Uncharacterized protein		MACNE		372
Uncharacterized protein		PAPAN		372
+16
O43889-3	Uncharacterized protein		Cebus capucinus imitator		374	UniRef90_O43889-3
cAMP responsive element binding protein 3		SAIBB		371
Uncharacterized protein		AOTNA		371
cAMP responsive element binding protein 3		CALJA		370
Cyclic AMP-responsive element-binding protein 3-like protein (Fragment)		CALJA		193
+6

Protein	Similar proteins		Species	Score	Length	Source
O43889	cDNA FLJ57143, highly similar to Cyclic AMP-responsive element-binding protein 3		HUMAN		282	UniRef50_O43889
Cyclic AMP-responsive element-binding protein 3		MACMU		372
Cyclic AMP-responsive element-binding protein 3		MACFA		372
Uncharacterized protein		RHIRO		372
Uncharacterized protein		CHLSB		372
+19
O43889-3	Cyclic AMP-responsive element-binding protein 3		BOVIN		368	UniRef50_O43889-3
Cyclic AMP-responsive element-binding protein 3		MOUSE		404
Uncharacterized protein		Cebus capucinus imitator		374
Uncharacterized protein		AOTNA		371
cAMP responsive element binding protein 3		SAIBB		371
+157

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
CCDSⁱ	CCDS6588.1 [O43889-2]
RefSeqⁱ	NP_006359.3, NM_006368.4 [O43889-2]
UniGeneⁱ	Hs.522110

3D structure databases

ProteinModelPortalⁱ	O43889
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115751, 191 interactors
DIPⁱ	DIP-33935N
ELMⁱ	O43889
IntActⁱ	O43889, 169 interactors
MINTⁱ	O43889

PTM databases

iPTMnetⁱ	O43889
PhosphoSitePlusⁱ	O43889

Polymorphism and mutation databases

BioMutaⁱ	CREB3

BioMutaⁱ

CREB3

Proteomic databases

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

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	10488
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000353704; ENSP00000342136; ENSG00000107175 [O43889-2]
GeneIDⁱ	10488
KEGGⁱ	hsa:10488
UCSCⁱ	uc003zxv.4 human [O43889-2]

Organism-specific databases

CTDⁱ	10488
DisGeNETⁱ	10488
EuPathDBⁱ	HostDB:ENSG00000107175.10
GeneCardsⁱ	CREB3
HGNCⁱ	HGNC:2347 CREB3
HPAⁱ	HPA030978
MIMⁱ	606443 gene
neXtProtⁱ	NX_O43889
OpenTargetsⁱ	ENSG00000107175
PharmGKBⁱ	PA26865
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

GeneTreeⁱ	ENSGT00520000055538
HOGENOMⁱ	HOG000133026
HOVERGENⁱ	HBG051114
InParanoidⁱ	O43889
KOⁱ	K09048
OMAⁱ	HVSIDLD
PhylomeDBⁱ	O43889
TreeFamⁱ	TF316079

Enzyme and pathway databases

Reactomeⁱ	R-HSA-8874211 CREB3 factors activate genes
SIGNORⁱ	O43889

Miscellaneous databases

ChiTaRSⁱ	CREB3 human
GeneWikiⁱ	CREB3
GenomeRNAiⁱ	10488
Protein Ontology More...PROⁱ	PR:O43889
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000107175 Expressed in 219 organ(s), highest expression level in adenohypophysis
CleanExⁱ	HS_CREB3
Genevisibleⁱ	O43889 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR004827 bZIP IPR029808 Luman
PANTHERⁱ	PTHR22952:SF100 PTHR22952:SF100, 1 hit
Pfamⁱ	View protein in Pfam PF00170 bZIP_1, 1 hit
SMARTⁱ	View protein in SMART SM00338 BRLZ, 1 hit
PROSITEⁱ	View protein in PROSITE PS50217 BZIP, 1 hit PS00036 BZIP_BASIC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CREB3_HUMAN
Accessionⁱ	O43889Primary (citable) accession number: O43889 Secondary accession number(s): D0PTW6 Q9UE77
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
	Last sequence update:	March 28, 2018
	Last modified:	November 7, 2018
	This is version 175 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

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UniProtKB - O43889 (CREB3_HUMAN)

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Cyclic AMP-responsive element-binding protein 3

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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

Caution

<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

<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

Golgi apparatus

Endoplasmic reticulum

Nucleus

Other locations

Nucleus

Other locations

Cytosol

Endoplasmic reticulum

Golgi apparatus

Nucleus

Other locations

Topology

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

Organism-specific databases

Polymorphism and mutation databases

<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

Sites

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

Organism-specific 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

3D structure 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

Region

Motif

Compositional bias

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<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

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

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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 - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ