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A2A884 (ZEP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Hivep3
Synonyms:KBP1, Kiaa1555, Krc, Rc, shn3, Zas3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2348 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1. Ref.9 Ref.12 Ref.14

Subcellular location

Cytoplasm. Nucleus Ref.9.

Tissue specificity

Expressed in macrophages, lymphocytes, brain, thymus, spleen and bone marrow. Expressed in osteoblasts, whole bone and, to a lesser extend, in osteoclasts. Ref.2 Ref.4 Ref.11 Ref.14

Developmental stage

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. Ref.4 Ref.10

Induction

Upon CD3/CD28 stimulation in CD4 T-cells. Induced by LPS in pre-B-cells. Ref.10 Ref.12

Domain

ZAS2 domain binds DNA as dimers, tetramers, and multiple of tetramers and readily forms highly ordred DNA-protein structures. Ref.2 Ref.4 Ref.8

Post-translational modification

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. Ref.5

Disruption phenotype

Mice display adult-onset osteosclerosis with increased bone mass due to increased osteoblast activity; the osteoblasts contain elevated levels of Runx2. Ref.14

Miscellaneous

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

Sequence similarities

Contains 5 C2H2-type zinc fingers.

Sequence caution

The sequence AAA40039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23482348Transcription factor HIVEP3
PRO_0000331628

Regions

Repeat1897 – 190041
Repeat1927 – 193042
Repeat1933 – 193643
Repeat1961 – 196444
Repeat2024 – 202745
Zinc finger185 – 20723C2H2-type 1
Zinc finger213 – 23523C2H2-type 2
Zinc finger636 – 65823C2H2-type 3; degenerate
Zinc finger1720 – 174223C2H2-type 4
Zinc finger1748 – 177225C2H2-type 5
Region185 – 23551ZAS1
Region204 – 1055852No DNA binding activity or transactivation activity, but complete prevention of TRAF-dependent NF-Kappa-B activation; associates with TRAF2 and JUN
Region257 – 28024Acidic 1
Region844 – 86522Acidic 2
Region1720 – 177253ZAS2
Region1783 – 184159Acidic 3
Region2053 – 2148965 X 4 AA tandem repeats of [ST]-P-X-[RK]
Coiled coil1409 – 143325 Potential
Motif885 – 8917Nuclear localization signal Potential
Compositional bias301 – 32727Ser-rich
Compositional bias371 – 40737Ser-rich
Compositional bias780 – 80223Ser-rich
Compositional bias826 – 86237Glu/Pro-rich
Compositional bias898 – 93033Ser-rich
Compositional bias1873 – 190230Ser-rich

Experimental info

Sequence conflict1311L → S in AAR88090. Ref.2
Sequence conflict583 – 5842QP → HA in AAR88090. Ref.2
Sequence conflict721 – 7222GS → AC in AAR88090. Ref.2
Sequence conflict8721S → T in AAR88090. Ref.2
Sequence conflict11291E → Q in AAR88090. Ref.2
Sequence conflict15071K → F in AAA40039. Ref.4
Sequence conflict16601L → V in AAR88090. Ref.2
Sequence conflict16601L → V in AAA40039. Ref.4
Sequence conflict18801Q → E in AAR88090. Ref.2
Sequence conflict18801Q → E in AAA40039. Ref.4
Sequence conflict19441L → V in AAR88090. Ref.2
Sequence conflict19441L → V in AAA40039. Ref.4
Sequence conflict19941L → P in AAR88090. Ref.2
Sequence conflict19941L → P in AAA40039. Ref.4
Sequence conflict19981C → R in AAR88090. Ref.2
Sequence conflict19981C → R in AAA40039. Ref.4
Sequence conflict20141R → P in AAA40039. Ref.4
Sequence conflict21051A → G in AAR88090. Ref.2
Sequence conflict21051A → G in AAA40039. Ref.4

Sequences

Sequence LengthMass (Da)Tools
A2A884 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: E226133774AD50C8

FASTA2,348253,413
        10         20         30         40         50         60 
MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT QELLATQPFS 

        70         80         90        100        110        120 
GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP GKPEHLLEGS TWQLVDPMRP 

       130        140        150        160        170        180 
GPSGSFVAPG LHPQSQLLPS HASILPPEEL PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ 

       190        200        210        220        230        240 
KPGKYICQYC SRPCAKPSVL QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK 

       250        260        270        280        290        300 
AGLASGSSSE MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL 

       310        320        330        340        350        360 
SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT HTIKQKLALR 

       370        380        390        400        410        420 
LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP NTNAKSYAEI IFGKCGRIGQ 

       430        440        450        460        470        480 
RTSMLASTST QPLLPLSSED KPSLVPLSVP RTQVIEHITK LITINEAVVD TSEIDSVKPR 

       490        500        510        520        530        540 
RSSLTRRSSV ESPKSSLYRD SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA 

       550        560        570        580        590        600 
CTISTHHHTF RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG 

       610        620        630        640        650        660 
PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN YEAHKKYYCS 

       670        680        690        700        710        720 
ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT PLRKRRKEKS LGDEEEPPAF 

       730        740        750        760        770        780 
GSPGPSETAH NRPLGSTKSP AEASKSAPSL EGPTSFQPRT PKPGAGSEPG KERRTMSKEI 

       790        800        810        820        830        840 
SVIQHTSSFE KSDPPEQPSG LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI 

       850        860        870        880        890        900 
LVTEEPDRPD TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG 

       910        920        930        940        950        960 
ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS KTLGSHMLTV 

       970        980        990       1000       1010       1020 
PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL SPTGPSLAVP AAPPPPAAPP 

      1030       1040       1050       1060       1070       1080 
ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE SSEEPAASKP STKSSVPQIS VGTTQGGPSG 

      1090       1100       1110       1120       1130       1140 
GKSQMQDRPP LGSSPPYTEA LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM 

      1150       1160       1170       1180       1190       1200 
AGLLSSPYSM PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC 

      1210       1220       1230       1240       1250       1260 
PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST EYSSDIQLPP 

      1270       1280       1290       1300       1310       1320 
VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS YGSAMYTTLS QILVTQSPGS 

      1330       1340       1350       1360       1370       1380 
PASTALTKYE EPSSKSMTVC EADVYEAEPG PSSISKEQNR GYQTPYLRVP ERKGTSLSSE 

      1390       1400       1410       1420       1430       1440 
GILSLEGCSS TASGSKRVLS PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT 

      1450       1460       1470       1480       1490       1500 
STEDRKKTEK PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE 

      1510       1520       1530       1540       1550       1560 
YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL QEGTDSKKVL 

      1570       1580       1590       1600       1610       1620 
QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS LYNPNLPGVS TKAALSLLRS 

      1630       1640       1650       1660       1670       1680 
KQKVSKETYT MATAPHPEAG RLVPSNSRKP RMTEVHLPSL VSPESQKDPA RVEKEEKQGK 

      1690       1700       1710       1720       1730       1740 
AEEGTPTSKR GEPARVKIFE GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR 

      1750       1760       1770       1780       1790       1800 
THTDVRPYVC KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE 

      1810       1820       1830       1840       1850       1860 
GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA PPCLPPTLQE 

      1870       1880       1890       1900       1910       1920 
NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR GTQGLPRLGL APLEKDMSSA 

      1930       1940       1950       1960       1970       1980 
PSPKATSPRR PWSPSKEAGS RPSLTRKHSL TKNDSSPQQC SPAREAQASV TSTPGPQMGP 

      1990       2000       2010       2020       2030       2040 
GRDLGPHLCG SPRLELSCLT PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT 

      2050       2060       2070       2080       2090       2100 
VLPGKWALAG PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP 

      2110       2120       2130       2140       2150       2160 
SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP IGGIQMVQAR 

      2170       2180       2190       2200       2210       2220 
PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP TESPSASVSP VAKVSKFTLS 

      2230       2240       2250       2260       2270       2280 
SELEEERTGR GPGRPPDWEP HRAEAPPGPM GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL 

      2290       2300       2310       2320       2330       2340 
ANLKASSFPP LDRSSSMDCL AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP 


KGSGPPSI 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL607142 Genomic DNA. Translation: CAM27499.1.
AY454345 mRNA. Translation: AAR88090.1. Frameshift.
AK173200 mRNA. Translation: BAD32478.1.
L07911 mRNA. Translation: AAA40039.1. Sequence problems.
CCDSCCDS38863.1.
PIRS41479.
T42717.
RefSeqNP_034787.2. NM_010657.3.
XP_006502878.1. XM_006502815.1.
XP_006502879.1. XM_006502816.1.
XP_006502880.1. XM_006502817.1.
UniGeneMm.302758.
Mm.394479.
Mm.422538.
Mm.487430.
Mm.488325.

3D structure databases

ProteinModelPortalA2A884.
SMRA2A884. Positions 184-240, 1719-1775.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteA2A884.

Proteomic databases

PaxDbA2A884.
PRIDEA2A884.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000106307; ENSMUSP00000101914; ENSMUSG00000028634.
ENSMUST00000166542; ENSMUSP00000130249; ENSMUSG00000028634.
GeneID16656.
KEGGmmu:16656.
UCSCuc008una.1. mouse.

Organism-specific databases

CTD59269.
MGIMGI:106589. Hivep3.
RougeSearch...

Phylogenomic databases

eggNOGNOG296349.
GeneTreeENSGT00530000063161.
HOGENOMHOG000155774.
HOVERGENHBG095595.
InParanoidA2A884.
KOK09239.
OMAMERIPGE.
OrthoDBEOG7V1FPQ.
PhylomeDBA2A884.
TreeFamTF331837.

Gene expression databases

ArrayExpressA2A884.
BgeeA2A884.
GenevestigatorA2A884.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio290349.
PROA2A884.
SOURCESearch...

Entry information

Entry nameZEP3_MOUSE
AccessionPrimary (citable) accession number: A2A884
Secondary accession number(s): A2MZW0, Q69ZG6, Q6SNP9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot