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O43889

- CREB3_HUMAN

UniProt

O43889 - CREB3_HUMAN

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Protein

Cyclic AMP-responsive element-binding protein 3

Gene

CREB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei287 – 2882Cleavage; by PS1Curated
Sitei290 – 2912Cleavage; by PS1Curated

GO - Molecular functioni

  1. cAMP response element binding protein binding Source: UniProtKB
  2. CCR1 chemokine receptor binding Source: UniProtKB
  3. chromatin binding Source: UniProtKB
  4. DNA binding Source: UniProtKB
  5. protein dimerization activity Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: NTNU_SB
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  10. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  11. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. chemotaxis Source: UniProtKB-KW
  2. cytoplasmic sequestering of transcription factor Source: UniProtKB
  3. establishment of viral latency Source: UniProtKB
  4. induction of positive chemotaxis Source: UniProtKB
  5. negative regulation of cell cycle Source: UniProtKB
  6. negative regulation of ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  7. positive regulation of calcium ion transport Source: UniProtKB
  8. positive regulation of cell migration Source: UniProtKB
  9. positive regulation of deacetylase activity Source: UniProtKB
  10. positive regulation of defense response to virus by host Source: UniProtKB
  11. positive regulation of monocyte chemotaxis Source: UniProtKB
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  14. positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: UniProtKB
  15. regulation of cell growth Source: UniProtKB
  16. regulation of cell proliferation Source: UniProtKB
  17. release from viral latency Source: UniProtKB
  18. response to endoplasmic reticulum stress Source: UniProtKB
  19. response to unfolded protein Source: UniProtKB-KW
  20. transcription, DNA-templated Source: UniProtKB
  21. transcription from RNA polymerase II promoter Source: GOC
  22. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Chemotaxis, Host-virus interaction, Transcription, Transcription regulation, Unfolded protein response

Keywords - Ligandi

DNA-binding

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2347. CREB3.

Subcellular locationi

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.By similarity
Isoform 3 : Nucleus. Cytoplasm
Note: Predominantly in the nucleus.
Chain 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).

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. endoplasmic reticulum membrane Source: UniProtKB
  5. Golgi apparatus Source: UniProtKB
  6. Golgi membrane Source: UniProtKB
  7. integral component of endoplasmic reticulum membrane Source: UniProtKB
  8. integral component of membrane Source: UniProtKB
  9. membrane Source: UniProtKB
  10. neuronal cell body Source: UniProtKB
  11. nuclear body Source: UniProtKB
  12. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 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). 1 Publication
Mutagenesisi16 – 172LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 3). 2 Publications
Mutagenesisi57 – 582LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 3). 1 Publication
Mutagenesisi57 – 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). 1 Publication
Mutagenesisi78 – 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). 2 Publications
Mutagenesisi81 – 811Y → 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
Mutagenesisi184 – 1841N → 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. 1 Publication
Mutagenesisi276 – 2761R → A: Does not inhibit proteolytic cleavage and transcriptional activation. 1 Publication
Mutagenesisi288 – 2881R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication
Mutagenesisi291 – 2911R → G: Inhibits proteolytic cleavage and transcriptional activation. 1 Publication

Organism-specific databases

PharmGKBiPA26865.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Cyclic AMP-responsive element-binding protein 3PRO_0000076602Add
BLAST
Chaini1 – ?Processed cyclic AMP-responsive element-binding protein 3PRO_0000296204

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.
The processed cyclic AMP-responsive element-binding protein 3 is rapidly degraded.
N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO43889.
PRIDEiO43889.

PTM databases

PhosphoSiteiO43889.

Expressioni

Tissue specificityi

Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level). Ubiquitous.5 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

BgeeiO43889.
CleanExiHS_CREB3.
ExpressionAtlasiO43889. baseline and differential.
GenevestigatoriO43889.

Interactioni

Subunit structurei

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.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P298468EBI-625022,EBI-909718From a different organism.
CCR1P322467EBI-625022,EBI-608322
CREBRFQ8IUR64EBI-625022,EBI-1042699
DCSTAMPQ9H2956EBI-625022,EBI-6095316
HCFC1P516105EBI-625002,EBI-396176
JUNP054124EBI-625002,EBI-852823

Protein-protein interaction databases

BioGridi115751. 41 interactions.
DIPiDIP-33935N.
IntActiO43889. 124 interactions.
MINTiMINT-1446829.
STRINGi9606.ENSP00000342136.

Structurei

3D structure databases

ProteinModelPortaliO43889.
SMRiO43889. Positions 166-232.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 254254CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini272 – 395124LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei255 – 27117Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini174 – 23764bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9292Transcription activation (acidic)Add
BLAST
Regioni176 – 20833Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni216 – 23722Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi13 – 175LXXLL motif 1
Motifi54 – 585LXXLL motif 2
Motifi78 – 814HCFC1-binding-motif (HBM)

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi340 – 38546Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. ATF subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG254445.
GeneTreeiENSGT00520000055538.
HOGENOMiHOG000133026.
HOVERGENiHBG051114.
InParanoidiO43889.
KOiK09048.
OMAiPSDWEVD.
OrthoDBiEOG7KM5SZ.
PhylomeDBiO43889.
TreeFamiTF316079.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43889-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV
60 70 80 90 100
DDLLCSLLSP PASLNILSSS NPCLVHHDHT YSLPRETVSM DLGECEISLT
110 120 130 140 150
GRTGFMGLAI HTFPFAESES CRKEGTQMTP QHMEELAEQE IARLVLTDEE
160 170 180 190 200
KSLLEKEGLI LPETLPLTKT EEQILKRVRR KIRNKRSAQE SRRKKKVYVG
210 220 230 240 250
GLESRVLKYT AQNMELQNKV QLLEEQNLSL LDQLRKLQAM VIEISNKTSS
260 270 280 290 300
SSTCILVLLV SFCLLLVPAM YSSDTRGSLP AEHGVLSRQL RALPSEDPYQ
310 320 330 340 350
LELPALQSEV PKDSTHQWLD GSDCVLQAPG NTSCLLHYMP QAPSAEPPLE
360 370 380 390
WPFPDLFSEP LCRGPILPLQ ANLTRKGGWL PTGSPSVILQ DRYSG
Length:395
Mass (Da):43,917
Last modified:June 1, 1998 - v1
Checksum:i1C412AA0D51CB7B2
GO
Isoform 2 (identifier: O43889-2) [UniParc]FASTAAdd to Basket

Also known as: LZIP

The sequence of this isoform differs from the canonical sequence as follows:
     93-116: Missing.

Show »
Length:371
Mass (Da):41,379
Checksum:i82152E496B924EEC
GO
Isoform 3 (identifier: O43889-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:354
Mass (Da):39,580
Checksum:iBC8F014103A52111
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211G → E in AAG43527. 1 PublicationCurated
Sequence conflicti254 – 2541C → G in AAD09210. (PubMed:10675342)Curated
Sequence conflicti270 – 2701M → I in AAH09402. (PubMed:15489334)Curated
Sequence conflicti286 – 2861L → C in AAD09210. (PubMed:10675342)Curated
Sequence conflicti357 – 3571F → S in AAB69652. (PubMed:9271389)Curated
Sequence conflicti362 – 3621C → V in AAD09210. (PubMed:10675342)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei93 – 11624Missing in isoform 2 and isoform 3. 5 PublicationsVSP_011838Add
BLAST
Alternative sequencei253 – 26917Missing in isoform 3. 1 PublicationVSP_043805Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
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.
CCDSiCCDS6588.1. [O43889-2]
RefSeqiNP_006359.3. NM_006368.4. [O43889-2]
UniGeneiHs.522110.

Genome annotation databases

EnsembliENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneIDi10488.
KEGGihsa:10488.
UCSCiuc003zxv.3. human. [O43889-2]
uc010mla.3. human. [O43889-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
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 .
CCDSi CCDS6588.1. [O43889-2 ]
RefSeqi NP_006359.3. NM_006368.4. [O43889-2 ]
UniGenei Hs.522110.

3D structure databases

ProteinModelPortali O43889.
SMRi O43889. Positions 166-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115751. 41 interactions.
DIPi DIP-33935N.
IntActi O43889. 124 interactions.
MINTi MINT-1446829.
STRINGi 9606.ENSP00000342136.

PTM databases

PhosphoSitei O43889.

Proteomic databases

PaxDbi O43889.
PRIDEi O43889.

Protocols and materials databases

DNASUi 10488.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000353704 ; ENSP00000342136 ; ENSG00000107175 . [O43889-2 ]
GeneIDi 10488.
KEGGi hsa:10488.
UCSCi uc003zxv.3. human. [O43889-2 ]
uc010mla.3. human. [O43889-1 ]

Organism-specific databases

CTDi 10488.
GeneCardsi GC09P035722.
HGNCi HGNC:2347. CREB3.
MIMi 606443. gene.
neXtProti NX_O43889.
PharmGKBi PA26865.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG254445.
GeneTreei ENSGT00520000055538.
HOGENOMi HOG000133026.
HOVERGENi HBG051114.
InParanoidi O43889.
KOi K09048.
OMAi PSDWEVD.
OrthoDBi EOG7KM5SZ.
PhylomeDBi O43889.
TreeFami TF316079.

Miscellaneous databases

ChiTaRSi CREB3. human.
GeneWikii CREB3.
GenomeRNAii 10488.
NextBioi 39796.
PROi O43889.
SOURCEi Search...

Gene expression databases

Bgeei O43889.
CleanExi HS_CREB3.
ExpressionAtlasi O43889. baseline and differential.
Genevestigatori O43889.

Family and domain databases

InterProi IPR004827. bZIP.
[Graphical view ]
Pfami PF00170. bZIP_1. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCREB3_HUMAN
AccessioniPrimary (citable) accession number: O43889
Secondary accession number(s): D0PTW6
, O14671, O14919, Q5TCV1, Q96GK8, Q9H2W3, Q9UE77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: June 1, 1998
Last modified: October 29, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
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.

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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3