HIVEP3

Jump to navigation Jump to search
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Transcription factor HIVEP3 is a protein that in humans is encoded by the HIVEP3 gene.[1][2]

Function

Members of the ZAS family, such as ZAS3 (HIVEP3), are large proteins that contain a ZAS domain, a modular protein structure consisting of a pair of C2H2 zinc fingers with an acidic-rich region and a serine/threonine -rich sequence. These proteins bind specific DNA sequences, including the kappa-B motif (GGGACTTTCC), in the promoters and enhancer regions of several genes and viruses, including human immunodeficiency virus (HIV). ZAS genes span more than 150 kb and contain at least 10 exons, one of which is longer than 5.5 kb (Allen and Wu, 2004).[supplied by OMIM][2]

It regulates osteoblasts.[3]

Interactions

HIVEP3 has been shown to interact with TRAF1[4] and TRAF2.[4]

References

  1. Hicar MD, Liu Y, Allen CE, Wu LC (Jan 2001). "Structure of the human zinc finger protein HIVEP3: molecular cloning, expression, exon-intron structure, and comparison with paralogous genes HIVEP1 and HIVEP2". Genomics. 71 (1): 89–100. doi:10.1006/geno.2000.6425. PMID 11161801.
  2. 2.0 2.1 "Entrez Gene: HIVEP3 human immunodeficiency virus type I enhancer binding protein 3".
  3. Glimcher, LH; Jones, DC; Wein, MN (November 2007). "Control of postnatal bone mass by the zinc finger adapter protein Schnurri-3". Annals of the New York Academy of Sciences. 1116: 174–81. doi:10.1196/annals.1402.044. PMID 18083927.
  4. 4.0 4.1 Oukka M, Kim ST, Lugo G, Sun J, Wu LC, Glimcher LH (Jan 2002). "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF receptor-driven responses and interacts with TRAF2". Molecular Cell. 9 (1): 121–31. doi:10.1016/S1097-2765(01)00434-8. PMID 11804591.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.