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O43889 (CREB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. Processed cyclic AMP-responsive element-binding protein 3
    Short name=N-terminal Luman
    Short name=Transcriptionally active form
Gene names
Name:CREB3
Synonyms:LZIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR). Involved in cell proliferation and migration, tumor suppression and inflammatory gene expression. Plays also a role in the human immunodeficiency virus type 1 (HIV-1) virus protein expression and in the herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Isoform 2 plays a role in the unfolded protein response (UPR). Isoform 2 acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Isoform 2 may play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HSV) core protein. Isoform 2 represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestring host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection. Isoform 3 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). Isoform 3 decreases the acetylation level of histone H4. Isoform 3 does not promote the chemotactic activity of leukocyte cells. Ref.1 Ref.3 Ref.4 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Processed cyclic AMP-responsive element-binding protein 3: acts as a transcription factor that activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Promotes cell survival against ER stress-induced apoptotic cell death during UPR. Activates transcription from CRE and C/EBP-containing reporter genes. Induces transcriptional activation of chemokine receptors. Activates transcription of genes required for reactivation of the latent HSV-1 virus. Down-regulates Tat-dependent transcription of the HIV-1 LTR by interacting with HIV-1 Tat. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16 and by the HCV core protein. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral and cellular promoters. Binds to the unfolded protein respons element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3'). Associates with chromatin to the HERPUD1 promoter. Ref.1 Ref.3 Ref.4 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Subunit structure

Homodimer; homodimerization is prevented by the HCV core protein. Interacts with HCFC1; the interaction is required to stimulate CREB3 transcriptional activity. Isoform 2 interacts with CREBZF; the interaction occurs only in combination with HCFC1. Isoform 2 interacts (via central part and transmembrane region) with TM7SF4 (via C-terminus cytoplasmic domain). Isoform 2 interacts with OS9. Isoform 2 interacts (via leucine-zipper domain) with CREBRF (via leucine-zipper domain); the interaction occurs only after CREB3 activation and promotes CREB3 degradation. Isoform 2 interacts (via C-terminal domain) with CCR1. Isoform 2 interacts (via leucine-zipper and transmembrane domains) with HIV-1 ENV (via cytoplasmic domain). Isoform 2 interacts (via leucine-zipper and transmembrane domains) with HIV-1 TMgp41 (via cytoplasmic domain); the interaction reduces CREB3 stability. Interacts with the HCV core protein. Processed cyclic AMP-responsive element-binding protein 3 interacts with HIV-1 Tat. Ref.2 Ref.3 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.20 Ref.21

Subcellular location

Isoform 2: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Membrane. Note: Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia By similarity. Colocalizes with TM7SF4 in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. Sequestred into the cytoplasm by the HCV core protein. Ref.3 Ref.4 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.20 Ref.21

Isoform 3: Nucleus. Cytoplasm. Note: Predominantly in the nucleus. Ref.3 Ref.4 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.20 Ref.21

Processed cyclic AMP-responsive element-binding protein 3: Nucleus. Note: Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB). Ref.3 Ref.4 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.20 Ref.21

Tissue specificity

Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level). Ubiquitous. Ref.1 Ref.2 Ref.3 Ref.4 Ref.21

Induction

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. Ref.14 Ref.17 Ref.18 Ref.20 Ref.21

Post-translational modification

The ER membrane embedded cyclic AMP-responsive element-binding protein 3 form is 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 TM7SF4. Ref.12 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21

The processed cyclic AMP-responsive element-binding protein 3 is rapidly degraded.

N-glycosylated. Ref.12 Ref.17

Sequence similarities

Belongs to the bZIP family. ATF subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Caution

All experiments concerning the proteolytic cleavage are done with isoform 2.

Ontologies

Keywords
   Biological processChemotaxis
Host-virus interaction
Transcription
Transcription regulation
Unfolded protein response
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal-anchor
Transmembrane
Transmembrane helix
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic sequestering of transcription factor

Inferred from direct assay PubMed 20091349. Source: UniProtKB

establishment of viral latency

Inferred from direct assay PubMed 20091349. Source: UniProtKB

induction of positive chemotaxis

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of cell cycle

Non-traceable author statement Ref.9. Source: UniProtKB

negative regulation of ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of calcium ion transport

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of cell migration

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of deacetylase activity

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of defense response to virus by host

Inferred from direct assay PubMed 20091349. Source: UniProtKB

positive regulation of monocyte chemotaxis

Inferred from direct assay Ref.18. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.18PubMed 98051186Ref.14PubMed 20091349PubMed 20141198PubMed 97415590. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response

Inferred from direct assay Ref.17Ref.20. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of cell growth

Inferred from direct assay PubMed 20141198. Source: UniProtKB

regulation of cell proliferation

Inferred from mutant phenotype Ref.3. Source: UniProtKB

release from viral latency

Inferred from direct assay PubMed 20091349. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from direct assay Ref.17Ref.20. Source: UniProtKB

response to unfolded protein

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from mutant phenotype Ref.9. Source: UniProtKB

Golgi membrane

Inferred from direct assay PubMed 20091349. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.20Ref.4PubMed 20091349. Source: UniProtKB

cytosol

Inferred from mutant phenotype Ref.13. Source: UniProtKB

endoplasmic reticulum

Inferred from mutant phenotype Ref.9. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay PubMed 20091349. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.21. Source: UniProtKB

integral component of membrane

Inferred from direct assay Ref.9. Source: UniProtKB

membrane

Inferred from direct assay Ref.4. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 20091349. Source: UniProtKB

nuclear body

Inferred from direct assay Ref.20. Source: UniProtKB

nucleus

Inferred from direct assay Ref.21Ref.3PubMed 20141198Ref.4. Source: UniProtKB

   Molecular_functionCCR1 chemokine receptor binding

Inferred from direct assay Ref.13. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.3Ref.1. Source: UniProtKB

RNA polymerase II regulatory region sequence-specific DNA binding

Inferred from direct assay Ref.14Ref.17. Source: UniProtKB

cAMP response element binding protein binding

Inferred from direct assay Ref.1. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.15Ref.20PubMed 98051186Ref.3Ref.13Ref.21Ref.1PubMed 97415590. Source: UniProtKB

protein dimerization activity

Traceable author statement Ref.9. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.3PubMed 20141198. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.3PubMed 20091349PubMed 20141198PubMed 97415590. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43889-1)

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.
Isoform 2 (identifier: O43889-2)

Also known as: LZIP;

The sequence of this isoform differs from the canonical sequence as follows:
     93-116: Missing.
Isoform 3 (identifier: O43889-3)

Also known as: smal LZIP; sLZIP;

The sequence of this isoform differs from the canonical sequence as follows:
     93-116: Missing.
     253-269: Missing.
Note: Does not contain a helical transmembrane domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Cyclic AMP-responsive element-binding protein 3
PRO_0000076602
Chain1 – ?Processed cyclic AMP-responsive element-binding protein 3PRO_0000296204

Regions

Topological domain1 – 254254Cytoplasmic Potential
Transmembrane255 – 27117Helical; Signal-anchor for type II membrane protein; Potential
Topological domain272 – 395124Lumenal Potential
Domain174 – 23764bZIP
Region1 – 9292Transcription activation (acidic)
Region176 – 20833Basic motif By similarity
Region216 – 23722Leucine-zipper By similarity
Motif13 – 175LXXLL motif 1
Motif54 – 585LXXLL motif 2
Motif78 – 814HCFC1-binding-motif (HBM)
Compositional bias340 – 38546Pro-rich

Sites

Site287 – 2882Cleavage; by PS1 Probable
Site290 – 2912Cleavage; by PS1 Probable

Amino acid modifications

Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence93 – 11624Missing in isoform 2 and isoform 3.
VSP_011838
Alternative sequence253 – 26917Missing in isoform 3.
VSP_043805

Experimental info

Mutagenesis12 – 132LL → 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 2). Ref.4
Mutagenesis16 – 172LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 3). Ref.4
Mutagenesis57 – 582LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 3). Ref.4
Mutagenesis57 – 582LL → 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 2). Ref.4
Mutagenesis78 – 814DHTY → 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 2). Ref.4 Ref.9 Ref.11 Ref.15
Mutagenesis811Y → 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. Ref.4 Ref.9
Mutagenesis1841N → G: Does not bind to DNA but retains its ability to interact with HCFC1. Reduces transcriptional activation of unfolded protein respons elements (UPRE)-containing promoter. Colocalizes with HCFC1 in the ER membrane. Ref.4 Ref.15
Mutagenesis2761R → A: Does not inhibit proteolytic cleavage and transcriptional activation. Ref.4 Ref.12
Mutagenesis2881R → G: Inhibits proteolytic cleavage and transcriptional activation. Ref.4 Ref.12
Mutagenesis2911R → G: Inhibits proteolytic cleavage and transcriptional activation. Ref.4 Ref.12
Sequence conflict211G → E in AAG43527. Ref.6
Sequence conflict2541C → G in AAD09210. Ref.3
Sequence conflict2701M → I in AAH09402. Ref.8
Sequence conflict2861L → C in AAD09210. Ref.3
Sequence conflict3571F → S in AAB69652. Ref.1
Sequence conflict3621C → V in AAD09210. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1C412AA0D51CB7B2

FASTA39543,917
        10         20         30         40         50         60 
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV DDLLCSLLSP 

        70         80         90        100        110        120 
PASLNILSSS NPCLVHHDHT YSLPRETVSM DLGECEISLT GRTGFMGLAI HTFPFAESES 

       130        140        150        160        170        180 
CRKEGTQMTP QHMEELAEQE IARLVLTDEE KSLLEKEGLI LPETLPLTKT EEQILKRVRR 

       190        200        210        220        230        240 
KIRNKRSAQE SRRKKKVYVG GLESRVLKYT AQNMELQNKV QLLEEQNLSL LDQLRKLQAM 

       250        260        270        280        290        300 
VIEISNKTSS SSTCILVLLV SFCLLLVPAM YSSDTRGSLP AEHGVLSRQL RALPSEDPYQ 

       310        320        330        340        350        360 
LELPALQSEV PKDSTHQWLD GSDCVLQAPG NTSCLLHYMP QAPSAEPPLE WPFPDLFSEP 

       370        380        390 
LCRGPILPLQ ANLTRKGGWL PTGSPSVILQ DRYSG 

« Hide

Isoform 2 (LZIP) [UniParc].

Checksum: 82152E496B924EEC
Show »

FASTA37141,379
Isoform 3 (smal LZIP) (sLZIP) [UniParc].

Checksum: BC8F014103A52111
Show »

FASTA35439,580

References

« Hide 'large scale' references
[1]"Luman, a new member of the CREB/ATF family, binds to herpes simplex virus VP16-associated host cellular factor."
Lu R., Yang P., O'Hare P., Misra V.
Mol. Cell. Biol. 17:5117-5126(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEAR FUNCTION IN TRANSCRIPTIONAL REGULATION, DNA-BINDING, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[2]"Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP."
Freiman R.N., Herr W.
Genes Dev. 11:3122-3127(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH HCFC1, TISSUE SPECIFICITY.
Tissue: Cervix carcinoma.
[3]"Hepatitis C virus core protein-induced loss of LZIP function correlates with cellular transformation."
Jin D.-Y., Wang H.-L., Zhou Y., Chun A.C.S., Kibler K.V., Hou Y.-D., Kung H.-F., Jeang K.-T.
EMBO J. 19:729-740(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), FUNCTION IN CELL PROLIFERATION, HOMODIMERIZATION, INTERACTION WITH HCV CORE PROTEIN, DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal liver.
[4]"A novel isoform of human LZIP negatively regulates the transactivation of the glucocorticoid receptor."
Kang H., Kim Y.S., Ko J.
Mol. Endocrinol. 23:1746-1757(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING (ISOFORM 2), FUNCTION IN GLUCOCORTICOID-INDUCED TRANSCRIPTIONAL REPRESSION (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 16-LEU-LEU-17 AND 57-LEU-LEU-58.
[5]"Novel activation and inhibitory domains of LZIP isoforms, retinoic acid-inducible genes in P19 embryonal carcinoma cell, differentially activate transcription in mouse development."
Hayashi M., Tanaka T.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"Complete nucleotide sequence and genomic structure of the human cAMP responsive element binding protein 3 (Luman) gene (CREB3)."
Ben-Yosef T., Francomano C.A.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
[7]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas and Skin.
[9]"Potential role for luman, the cellular homologue of herpes simplex virus VP16 (alpha gene trans-inducing factor), in herpesvirus latency."
Lu R., Misra V.
J. Virol. 74:934-943(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HSV-1 INFECTION (ISOFORM 2), MUTAGENESIS OF TYR-81, SUBCELLULAR LOCATION.
[10]"Mutations in host cell factor 1 separate its role in cell proliferation from recruitment of VP16 and LZIP."
Mahajan S.S., Wilson A.C.
Mol. Cell. Biol. 20:919-928(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCFC1.
[11]"N-terminal transcriptional activation domain of LZIP comprises two LxxLL motifs and the host cell factor-1 binding motif."
Luciano R.L., Wilson A.C.
Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION (ISOFORM 2), INTERACTION WITH HCFC1, TRANSCRIPTIONAL ACTIVATION DOMAIN, MUTAGENESIS OF 12-LEU-LEU-13; 16-LEU-LEU-17 AND 78-ASP--TYR-81.
[12]"Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis."
Raggo C., Rapin N., Stirling J., Gobeil P., Smith-Windsor E., O'Hare P., Misra V.
Mol. Cell. Biol. 22:5639-5649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, CLEAVAGE SITE, MUTAGENESIS OF ARG-276; ARG-288 AND ARG-291.
[13]"Human LZIP binds to CCR1 and differentially affects the chemotactic activities of CCR1-dependent chemokines."
Ko J., Jang S.W., Kim Y.S., Kim I.S., Sung H.J., Kim H.-H., Park J.Y., Lee Y.H., Kim J., Na D.S.
FASEB J. 18:890-892(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING (ISOFORM 2), INTERACTION WITH CCR1, SUBCELLULAR LOCATION.
[14]"Luman is capable of binding and activating transcription from the unfolded protein response element."
DenBoer L.M., Hardy-Smith P.W., Hogan M.R., Cockram G.P., Audas T.E., Lu R.
Biochem. Biophys. Res. Commun. 331:113-119(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE UNFOLDED PROTEIN RESPONSE (ISOFORM 2), DNA-BINDING, ABSENCE OF PROTEOLYTIC CLEAVAGE, INDUCTION.
[15]"Zhangfei is a potent and specific inhibitor of the host cell factor-binding transcription factor Luman."
Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.
J. Biol. Chem. 280:15257-15266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 2), INTERACTION WITH CREBZF AND HCFC1, SUBCELLULAR LOCATION, MUTAGENESIS OF 78-ASP--TYR-81 AND ASN-184.
[16]"Luman, a new partner of HIV-1 TMgp41, interferes with Tat-mediated transcription of the HIV-1 LTR."
Blot G., Lopez-Verges S., Treand C., Kubat N.J., Delcroix-Genete D., Emiliani S., Benarous R., Berlioz-Torrent C.
J. Mol. Biol. 364:1034-1047(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 INFECTIVITY (ISOFORM 2), INTERACTION WITH HIV-1 ENV, INTERACTION WITH HIV-1 TMGP41, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
[17]"Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element."
Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C., Kokame K., Lu R.
Mol. Cell. Biol. 26:7999-8010(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE UNFOLDED PROTEIN RESPONSE (ISOFORM 2), DNA-BINDING, GLYCOSYLATION, PROTEOLYTIC PROCESSING, INDUCTION.
[18]"Regulation of human LZIP expression by NF-kappaB and its involvement in monocyte cell migration induced by Lkn-1."
Jang S.W., Kim Y.S., Kim Y.R., Sung H.J., Ko J.
J. Biol. Chem. 282:11092-11100(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING (ISOFORM 2), INDUCTION.
[19]"Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration."
Sung H.J., Kim Y.S., Kang H., Ko J.
Exp. Mol. Med. 40:332-338(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION AND IN PROMOTING CHEMOTAXIS, DNA-BINDING.
[20]"A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response."
Audas T.E., Li Y., Liang G., Lu R.
Mol. Cell. Biol. 28:3952-3966(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CREBRF, PROTEOLYTIC PROCESSING, INDUCTION, SUBCELLULAR LOCATION.
[21]"DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation."
Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W., Hendriks I.A., Jansen B.J., Adema G.J.
Mol. Immunol. 47:1963-1973(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH OS9 AND TM7SF4, PROTEOLYTIC PROCESSING, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AF211847 Genomic DNA. Translation: AAG43527.1.
AF211848 mRNA. Translation: AAG43528.1.
AL133410 Genomic DNA. Translation: CAI10980.1.
BC009402 mRNA. Translation: AAH09402.1.
BC010158 mRNA. Translation: AAH10158.1.
CCDSCCDS6588.1. [O43889-2]
RefSeqNP_006359.3. NM_006368.4. [O43889-2]
UniGeneHs.522110.

3D structure databases

ProteinModelPortalO43889.
SMRO43889. Positions 180-225.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115751. 25 interactions.
IntActO43889. 123 interactions.
MINTMINT-1446829.
STRING9606.ENSP00000342136.

PTM databases

PhosphoSiteO43889.

Proteomic databases

PaxDbO43889.
PRIDEO43889.

Protocols and materials databases

DNASU10488.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneID10488.
KEGGhsa:10488.
UCSCuc003zxv.3. human. [O43889-2]
uc010mla.3. human. [O43889-1]

Organism-specific databases

CTD10488.
GeneCardsGC09P035722.
HGNCHGNC:2347. CREB3.
MIM606443. gene.
neXtProtNX_O43889.
PharmGKBPA26865.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254445.
HOGENOMHOG000133026.
HOVERGENHBG051114.
InParanoidO43889.
KOK09048.
OMAPSDWEVD.
OrthoDBEOG7KM5SZ.
PhylomeDBO43889.
TreeFamTF316079.

Gene expression databases

ArrayExpressO43889.
BgeeO43889.
CleanExHS_CREB3.
GenevestigatorO43889.

Family and domain databases

InterProIPR004827. bZIP.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCREB3. human.
GeneWikiCREB3.
GenomeRNAi10488.
NextBio39796.
PROO43889.
SOURCESearch...

Entry information

Entry nameCREB3_HUMAN
AccessionPrimary (citable) accession number: O43889
Secondary accession number(s): D0PTW6 expand/collapse secondary AC list , O14671, O14919, Q5TCV1, Q96GK8, Q9H2W3, Q9UE77
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant 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