Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O43889

- CREB3_HUMAN

UniProt

O43889 - CREB3_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 binding Source: UniProtKB
    6. protein dimerization activity Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity Source: NTNU_SB
    10. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    11. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
    12. 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

    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
    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

    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).
    Mutagenesisi16 – 172LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 57-A-A-58 (isoform 3).
    Mutagenesisi57 – 582LL → AA: Does not affect the transcriptional activation of the glucocorticoid receptor NR3C1; when associated with 16-A-A-17 (isoform 3).
    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).
    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).
    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

    ArrayExpressiO43889.
    BgeeiO43889.
    CleanExiHS_CREB3.
    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. 25 interactions.
    DIPiDIP-33935N.
    IntActiO43889. 124 interactions.
    MINTiMINT-1446829.
    STRINGi9606.ENSP00000342136.

    Structurei

    3D structure databases

    ProteinModelPortaliO43889.
    SMRiO43889. Positions 180-225.
    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.
    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

    MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV    50
    DDLLCSLLSP PASLNILSSS NPCLVHHDHT YSLPRETVSM DLGECEISLT 100
    GRTGFMGLAI HTFPFAESES CRKEGTQMTP QHMEELAEQE IARLVLTDEE 150
    KSLLEKEGLI LPETLPLTKT EEQILKRVRR KIRNKRSAQE SRRKKKVYVG 200
    GLESRVLKYT AQNMELQNKV QLLEEQNLSL LDQLRKLQAM VIEISNKTSS 250
    SSTCILVLLV SFCLLLVPAM YSSDTRGSLP AEHGVLSRQL RALPSEDPYQ 300
    LELPALQSEV PKDSTHQWLD GSDCVLQAPG NTSCLLHYMP QAPSAEPPLE 350
    WPFPDLFSEP LCRGPILPLQ ANLTRKGGWL PTGSPSVILQ DRYSG 395
    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 180-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115751. 25 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.
    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

    ArrayExpressi O43889.
    Bgeei O43889.
    CleanExi HS_CREB3.
    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

    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 1, 2014
    This is version 136 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