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A2A884

- ZEP3_MOUSE

UniProt

A2A884 - ZEP3_MOUSE

Protein

Transcription factor HIVEP3

Gene

Hivep3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and proinflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri185 – 20723C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri213 – 23523C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri636 – 65823C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1720 – 174223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1748 – 177225C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: MGI
    2. skeletal muscle cell differentiation Source: MGI
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor HIVEP3
    Alternative name(s):
    Human immunodeficiency virus type I enhancer-binding protein 3 homolog
    KB-binding and recognition component
    Kappa-B and V(D)J recombination signal sequences-binding protein
    Kappa-binding protein 1
    Short name:
    KBP-1
    Recombinant component
    Schnurri-3
    Zinc finger protein ZAS3
    Gene namesi
    Name:Hivep3
    Synonyms:KBP1, Kiaa1555, Krc, Rc, shn3, Zas3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:106589. Hivep3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice display adult-onset osteosclerosis with increased bone mass due to increased osteoblast activity; the osteoblasts contain elevated levels of Runx2.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23482348Transcription factor HIVEP3PRO_0000331628Add
    BLAST

    Post-translational modificationi

    Phosphorylated on threonine and serine residues. Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3 DNA binding affinity, and by epidermal growth factor receptor kinase increases its DNA binding affinity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiA2A884.
    PRIDEiA2A884.

    PTM databases

    PhosphoSiteiA2A884.

    Expressioni

    Tissue specificityi

    Expressed in macrophages, lymphocytes, brain, thymus, spleen and bone marrow. Expressed in osteoblasts, whole bone and, to a lesser extend, in osteoclasts.4 Publications

    Developmental stagei

    Expressed in the thymus with increasing level, approximately 4-fold, from E15.5 to E16.5, constant level from E16.5 to birth, then decrease to a low level by P30. Expressed at E13.5 in the dorsal root ganglia of the peripheral nervous system and the trigeminal ganglion of the metencephalon and at relatively low levels in the cerebral cortex; no significant expression was observed prior to E13.5. Expressed in the spinal cord at E19, but weakly detected in the lung and the liver.2 Publications

    Inductioni

    Upon CD3/CD28 stimulation in CD4 T-cells. Induced by LPS in pre-B-cells.2 Publications

    Gene expression databases

    ArrayExpressiA2A884.
    BgeeiA2A884.
    GenevestigatoriA2A884.

    Interactioni

    Subunit structurei

    Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1.3 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliA2A884.
    SMRiA2A884. Positions 184-240, 1719-1775.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1897 – 1900411 Publication
    Repeati1927 – 1930421 Publication
    Repeati1933 – 1936431 Publication
    Repeati1961 – 1964441 Publication
    Repeati2024 – 2027451 Publication

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni185 – 23551ZAS1Add
    BLAST
    Regioni204 – 1055852No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUNAdd
    BLAST
    Regioni257 – 28024Acidic 1Add
    BLAST
    Regioni844 – 86522Acidic 2Add
    BLAST
    Regioni1720 – 177253ZAS2Add
    BLAST
    Regioni1783 – 184159Acidic 3Add
    BLAST
    Regioni2053 – 2148965 X 4 AA tandem repeats of [ST]-P-X-[RK]Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1409 – 143325Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi885 – 8917Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi301 – 32727Ser-richAdd
    BLAST
    Compositional biasi371 – 40737Ser-richAdd
    BLAST
    Compositional biasi780 – 80223Ser-richAdd
    BLAST
    Compositional biasi826 – 86237Glu/Pro-richAdd
    BLAST
    Compositional biasi898 – 93033Ser-richAdd
    BLAST
    Compositional biasi1873 – 190230Ser-richAdd
    BLAST

    Domaini

    ZAS2 domain binds DNA as dimers, tetramers, and multiple of tetramers and readily forms highly ordred DNA-protein structures.3 Publications

    Sequence similaritiesi

    Contains 5 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri185 – 20723C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri213 – 23523C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri636 – 65823C2H2-type 3; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1720 – 174223C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1748 – 177225C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG296349.
    GeneTreeiENSGT00530000063161.
    HOGENOMiHOG000155774.
    HOVERGENiHBG095595.
    InParanoidiA2A884.
    KOiK09239.
    OMAiMERIPGE.
    OrthoDBiEOG7V1FPQ.
    PhylomeDBiA2A884.
    TreeFamiTF331837.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 5 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A2A884-1 [UniParc]FASTAAdd to Basket

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    MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT     50
    QELLATQPFS GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP 100
    GKPEHLLEGS TWQLVDPMRP GPSGSFVAPG LHPQSQLLPS HASILPPEEL 150
    PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ KPGKYICQYC SRPCAKPSVL 200
    QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK AGLASGSSSE 250
    MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL 300
    SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT 350
    HTIKQKLALR LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP 400
    NTNAKSYAEI IFGKCGRIGQ RTSMLASTST QPLLPLSSED KPSLVPLSVP 450
    RTQVIEHITK LITINEAVVD TSEIDSVKPR RSSLTRRSSV ESPKSSLYRD 500
    SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA CTISTHHHTF 550
    RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG 600
    PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN 650
    YEAHKKYYCS ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT 700
    PLRKRRKEKS LGDEEEPPAF GSPGPSETAH NRPLGSTKSP AEASKSAPSL 750
    EGPTSFQPRT PKPGAGSEPG KERRTMSKEI SVIQHTSSFE KSDPPEQPSG 800
    LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI LVTEEPDRPD 850
    TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG 900
    ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS 950
    KTLGSHMLTV PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL 1000
    SPTGPSLAVP AAPPPPAAPP ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE 1050
    SSEEPAASKP STKSSVPQIS VGTTQGGPSG GKSQMQDRPP LGSSPPYTEA 1100
    LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM AGLLSSPYSM 1150
    PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC 1200
    PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST 1250
    EYSSDIQLPP VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS 1300
    YGSAMYTTLS QILVTQSPGS PASTALTKYE EPSSKSMTVC EADVYEAEPG 1350
    PSSISKEQNR GYQTPYLRVP ERKGTSLSSE GILSLEGCSS TASGSKRVLS 1400
    PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT STEDRKKTEK 1450
    PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE 1500
    YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL 1550
    QEGTDSKKVL QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS 1600
    LYNPNLPGVS TKAALSLLRS KQKVSKETYT MATAPHPEAG RLVPSNSRKP 1650
    RMTEVHLPSL VSPESQKDPA RVEKEEKQGK AEEGTPTSKR GEPARVKIFE 1700
    GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR THTDVRPYVC 1750
    KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE 1800
    GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA 1850
    PPCLPPTLQE NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR 1900
    GTQGLPRLGL APLEKDMSSA PSPKATSPRR PWSPSKEAGS RPSLTRKHSL 1950
    TKNDSSPQQC SPAREAQASV TSTPGPQMGP GRDLGPHLCG SPRLELSCLT 2000
    PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT VLPGKWALAG 2050
    PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP 2100
    SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP 2150
    IGGIQMVQAR PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP 2200
    TESPSASVSP VAKVSKFTLS SELEEERTGR GPGRPPDWEP HRAEAPPGPM 2250
    GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL ANLKASSFPP LDRSSSMDCL 2300
    AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP KGSGPPSI 2348
    Length:2,348
    Mass (Da):253,413
    Last modified:February 20, 2007 - v1
    Checksum:iE226133774AD50C8
    GO

    Sequence cautioni

    The sequence AAA40039.1 differs from that shown. Reason: Frameshift at positions 1502 and 2242.
    The sequence AAR88090.1 differs from that shown. Reason: Frameshift at positions 752, 781, 1045, 1054 and 2242.
    The sequence AAA40039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311L → S in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti583 – 5842QP → HA in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti721 – 7222GS → AC in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti872 – 8721S → T in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1129 – 11291E → Q in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1507 – 15071K → F in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti1660 – 16601L → V in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1660 – 16601L → V in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti1880 – 18801Q → E in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1880 – 18801Q → E in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti1944 – 19441L → V in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1944 – 19441L → V in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti1994 – 19941L → P in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1994 – 19941L → P in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti1998 – 19981C → R in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti1998 – 19981C → R in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti2014 – 20141R → P in AAA40039. (PubMed:8255760)Curated
    Sequence conflicti2105 – 21051A → G in AAR88090. (PubMed:8812474)Curated
    Sequence conflicti2105 – 21051A → G in AAA40039. (PubMed:8255760)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL607142 Genomic DNA. Translation: CAM27499.1.
    AY454345 mRNA. Translation: AAR88090.1. Frameshift.
    AK173200 mRNA. Translation: BAD32478.1.
    L07911 mRNA. Translation: AAA40039.1. Sequence problems.
    CCDSiCCDS38863.1.
    PIRiS41479.
    T42717.
    RefSeqiNP_034787.2. NM_010657.3.
    XP_006502878.1. XM_006502815.1.
    XP_006502879.1. XM_006502816.1.
    XP_006502880.1. XM_006502817.1.
    UniGeneiMm.302758.
    Mm.394479.
    Mm.422538.
    Mm.487430.
    Mm.488325.

    Genome annotation databases

    EnsembliENSMUST00000106307; ENSMUSP00000101914; ENSMUSG00000028634.
    ENSMUST00000166542; ENSMUSP00000130249; ENSMUSG00000028634.
    GeneIDi16656.
    KEGGimmu:16656.
    UCSCiuc008una.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL607142 Genomic DNA. Translation: CAM27499.1 .
    AY454345 mRNA. Translation: AAR88090.1 . Frameshift.
    AK173200 mRNA. Translation: BAD32478.1 .
    L07911 mRNA. Translation: AAA40039.1 . Sequence problems.
    CCDSi CCDS38863.1.
    PIRi S41479.
    T42717.
    RefSeqi NP_034787.2. NM_010657.3.
    XP_006502878.1. XM_006502815.1.
    XP_006502879.1. XM_006502816.1.
    XP_006502880.1. XM_006502817.1.
    UniGenei Mm.302758.
    Mm.394479.
    Mm.422538.
    Mm.487430.
    Mm.488325.

    3D structure databases

    ProteinModelPortali A2A884.
    SMRi A2A884. Positions 184-240, 1719-1775.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei A2A884.

    Proteomic databases

    PaxDbi A2A884.
    PRIDEi A2A884.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000106307 ; ENSMUSP00000101914 ; ENSMUSG00000028634 .
    ENSMUST00000166542 ; ENSMUSP00000130249 ; ENSMUSG00000028634 .
    GeneIDi 16656.
    KEGGi mmu:16656.
    UCSCi uc008una.1. mouse.

    Organism-specific databases

    CTDi 59269.
    MGIi MGI:106589. Hivep3.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG296349.
    GeneTreei ENSGT00530000063161.
    HOGENOMi HOG000155774.
    HOVERGENi HBG095595.
    InParanoidi A2A884.
    KOi K09239.
    OMAi MERIPGE.
    OrthoDBi EOG7V1FPQ.
    PhylomeDBi A2A884.
    TreeFami TF331837.

    Miscellaneous databases

    NextBioi 290349.
    PROi A2A884.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A2A884.
    Bgeei A2A884.
    Genevestigatori A2A884.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 5 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "The mouse DNA binding protein Rc for the kappa B motif of transcription and for the V(D)J recombination signal sequences contains composite DNA-protein interaction domains and belongs to a new family of large transcriptional proteins."
      Wu L.-C., Liu Y., Strandtmann J., Mak C.-H., Lee B., Li Z., Yu C.Y.
      Genomics 35:415-424(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2341, DOMAIN, FUNCTION, TISSUE SPECIFICITY.
      Strain: BALB/c.
      Tissue: Brain.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1281-2348.
      Tissue: Thymus.
    4. "Molecular cloning of a zinc finger protein which binds to the heptamer of the signal sequence for V(D)J recombination."
      Wu L.-C., Mak C.-H., Dear N., Boehm T., Foroni L., Rabbitts T.H.
      Nucleic Acids Res. 21:5067-5073(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1497-2295, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, REPEAT.
    5. "Regulation by phosphorylation of the zinc finger protein KRC that binds the kappaB motif and V(D)J recombination signal sequences."
      Bachmeyer C., Mak C.H., Yu C.Y., Wu L.-C.
      Nucleic Acids Res. 27:643-648(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    6. "Downregulation of KRC induces proliferation, anchorage independence, and mitotic cell death in HeLa cells."
      Allen C.E., Wu L.-C.
      Exp. Cell Res. 260:346-356(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "The kappaB and V(D)J recombination signal sequence binding protein KRC regulates transcription of the mouse metastasis-associated gene S100A4/mts1."
      Hjelmsoe I., Allen C.E., Cohn M.A., Tulchinsky E.M., Wu L.-C.
      J. Biol. Chem. 275:913-920(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The kappa B transcriptional enhancer motif and signal sequences of V(D)J recombination are targets for the zinc finger protein HIVEP3/KRC: a site selection amplification binding study."
      Allen C.E., Mak C.-H., Wu L.-C.
      BMC Immunol. 3:10-10(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN ZAS.
    9. "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-driven responses and interacts with TRAF2."
      Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.
      Mol. Cell 9:121-131(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TRAF1 AND TRAF2, REGION.
    10. "Embryonic expression and regulation of the large zinc finger protein KRC."
      Hicar M.D., Robinson M.L., Wu L.-C.
      Genesis 33:8-20(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, DEVELOPMENTAL STAGE.
    11. "Inhibition of NF-kappaB by ZAS3, a zinc-finger protein that also binds to the kappaB motif."
      Hong J.W., Allen C.E., Wu L.-C.
      Proc. Natl. Acad. Sci. U.S.A. 100:12301-12306(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T cells."
      Oukka M., Wein M.N., Glimcher L.H.
      J. Exp. Med. 199:15-24(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH JUN, INDUCTION.
    13. "Structural characterization of the gene encoding the large zinc finger protein ZAS3: implication to the origin of multiple promoters in eukaryotic genes."
      Hong J.-W., Wu L.-C.
      Biochim. Biophys. Acta 1681:74-87(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE.
    14. "Regulation of adult bone mass by the zinc finger adapter protein Schnurri-3."
      Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J., Glimcher L.H.
      Science 312:1223-1227(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INTERACTION WITH RUNX2 AND WWP1.

    Entry informationi

    Entry nameiZEP3_MOUSE
    AccessioniPrimary (citable) accession number: A2A884
    Secondary accession number(s): A2MZW0, Q69ZG6, Q6SNP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Hivep3 gene expression is probably controlled by a combination of differential promoter usage, alternative splicing, and possible intergenic splicing.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3