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A2A884

- ZEP3_MOUSE

UniProt

A2A884 - ZEP3_MOUSE

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Protein

Transcription factor HIVEP3

Gene

Hivep3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
  2. nucleus Source: MGI
Complete GO annotation...

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

BgeeiA2A884.
ExpressionAtlasiA2A884. baseline and differential.
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

« Hide

        10         20         30         40         50
MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT
60 70 80 90 100
QELLATQPFS GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP
110 120 130 140 150
GKPEHLLEGS TWQLVDPMRP GPSGSFVAPG LHPQSQLLPS HASILPPEEL
160 170 180 190 200
PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ KPGKYICQYC SRPCAKPSVL
210 220 230 240 250
QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK AGLASGSSSE
260 270 280 290 300
MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL
310 320 330 340 350
SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT
360 370 380 390 400
HTIKQKLALR LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP
410 420 430 440 450
NTNAKSYAEI IFGKCGRIGQ RTSMLASTST QPLLPLSSED KPSLVPLSVP
460 470 480 490 500
RTQVIEHITK LITINEAVVD TSEIDSVKPR RSSLTRRSSV ESPKSSLYRD
510 520 530 540 550
SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA CTISTHHHTF
560 570 580 590 600
RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG
610 620 630 640 650
PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN
660 670 680 690 700
YEAHKKYYCS ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT
710 720 730 740 750
PLRKRRKEKS LGDEEEPPAF GSPGPSETAH NRPLGSTKSP AEASKSAPSL
760 770 780 790 800
EGPTSFQPRT PKPGAGSEPG KERRTMSKEI SVIQHTSSFE KSDPPEQPSG
810 820 830 840 850
LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI LVTEEPDRPD
860 870 880 890 900
TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG
910 920 930 940 950
ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS
960 970 980 990 1000
KTLGSHMLTV PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL
1010 1020 1030 1040 1050
SPTGPSLAVP AAPPPPAAPP ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE
1060 1070 1080 1090 1100
SSEEPAASKP STKSSVPQIS VGTTQGGPSG GKSQMQDRPP LGSSPPYTEA
1110 1120 1130 1140 1150
LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM AGLLSSPYSM
1160 1170 1180 1190 1200
PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC
1210 1220 1230 1240 1250
PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST
1260 1270 1280 1290 1300
EYSSDIQLPP VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS
1310 1320 1330 1340 1350
YGSAMYTTLS QILVTQSPGS PASTALTKYE EPSSKSMTVC EADVYEAEPG
1360 1370 1380 1390 1400
PSSISKEQNR GYQTPYLRVP ERKGTSLSSE GILSLEGCSS TASGSKRVLS
1410 1420 1430 1440 1450
PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT STEDRKKTEK
1460 1470 1480 1490 1500
PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE
1510 1520 1530 1540 1550
YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL
1560 1570 1580 1590 1600
QEGTDSKKVL QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS
1610 1620 1630 1640 1650
LYNPNLPGVS TKAALSLLRS KQKVSKETYT MATAPHPEAG RLVPSNSRKP
1660 1670 1680 1690 1700
RMTEVHLPSL VSPESQKDPA RVEKEEKQGK AEEGTPTSKR GEPARVKIFE
1710 1720 1730 1740 1750
GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR THTDVRPYVC
1760 1770 1780 1790 1800
KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE
1810 1820 1830 1840 1850
GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA
1860 1870 1880 1890 1900
PPCLPPTLQE NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR
1910 1920 1930 1940 1950
GTQGLPRLGL APLEKDMSSA PSPKATSPRR PWSPSKEAGS RPSLTRKHSL
1960 1970 1980 1990 2000
TKNDSSPQQC SPAREAQASV TSTPGPQMGP GRDLGPHLCG SPRLELSCLT
2010 2020 2030 2040 2050
PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT VLPGKWALAG
2060 2070 2080 2090 2100
PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP
2110 2120 2130 2140 2150
SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP
2160 2170 2180 2190 2200
IGGIQMVQAR PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP
2210 2220 2230 2240 2250
TESPSASVSP VAKVSKFTLS SELEEERTGR GPGRPPDWEP HRAEAPPGPM
2260 2270 2280 2290 2300
GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL ANLKASSFPP LDRSSSMDCL
2310 2320 2330 2340
AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP KGSGPPSI
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

Bgeei A2A884.
ExpressionAtlasi A2A884. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 72 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