HIVEP3

Protein-coding gene in the species Homo sapiens
HIVEP3
Identifiers
AliasesHIVEP3, Hivep3, 2900056N03Rik, A130075N07, AI848000, E030045D18Rik, KBP-1, KBP1, Rc, Schnurri-3, Shn3, Zas3, ZNF40C, human immunodeficiency virus type I enhancer binding protein 3, Kappa Recognition Component (Krc), KRC, HIVEP zinc finger 3
External IDsOMIM: 606649; MGI: 106589; HomoloGene: 7803; GeneCards: HIVEP3; OMA:HIVEP3 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for HIVEP3
Genomic location for HIVEP3
Band1p34.2Start41,506,365 bp[1]
End42,035,925 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for HIVEP3
Genomic location for HIVEP3
Band4|4 D2.1Start119,590,981 bp[2]
End119,995,242 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • endothelial cell

  • Brodmann area 23

  • cartilage tissue

  • parietal pleura

  • primary visual cortex

  • granulocyte

  • middle temporal gyrus

  • entorhinal cortex

  • germinal epithelium
Top expressed in
  • gastrula

  • medial geniculate nucleus

  • Rostral migratory stream

  • subiculum

  • medial dorsal nucleus

  • lateral geniculate nucleus

  • substantia nigra

  • trigeminal ganglion

  • anterior amygdaloid area

  • submandibular gland
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • sequence-specific DNA binding
  • DNA binding
  • metal ion binding
  • nucleic acid binding
  • DNA-binding transcription factor activity, RNA polymerase II-specific
Cellular component
  • cytoplasm
  • nucleus
Biological process
  • multicellular organism development
  • skeletal muscle cell differentiation
  • positive regulation of transcription, DNA-templated
  • regulation of transcription, DNA-templated
  • transcription by RNA polymerase II
  • signal transduction
  • transcription, DNA-templated
  • regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

59269

16656

Ensembl

ENSG00000127124

ENSMUSG00000028634

UniProt

Q5T1R4

A2A884

RefSeq (mRNA)

NM_001127714
NM_024503

NM_010657

RefSeq (protein)

NP_001121186
NP_078779

NP_034787

Location (UCSC)Chr 1: 41.51 – 42.04 MbChr 4: 119.59 – 120 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Transcription factor HIVEP3 is a protein that in humans is encoded by the HIVEP3 gene.[5][6]

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][6]

It regulates osteoblasts.[7]

Interactions

HIVEP3 has been shown to interact with TRAF1[8] and TRAF2.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000127124 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028634 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ a b "Entrez Gene: HIVEP3 human immunodeficiency virus type I enhancer binding protein 3".
  7. ^ 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 (1): 174–81. Bibcode:2007NYASA1116..174G. doi:10.1196/annals.1402.044. PMID 18083927. S2CID 25260678.
  8. ^ a b 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

  • Rustgi AK, Van 't Veer LJ, Bernards R (Nov 1990). "Two genes encode factors with NF-kappa B- and H2TF1-like DNA-binding properties". Proceedings of the National Academy of Sciences of the United States of America. 87 (22): 8707–10. Bibcode:1990PNAS...87.8707R. doi:10.1073/pnas.87.22.8707. PMC 55028. PMID 2247438.
  • Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O (Aug 2000). "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 7 (4): 273–81. doi:10.1093/dnares/7.4.271. PMID 10997877.
  • 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.
  • Oukka M, Wein MN, Glimcher LH (Jan 2004). "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T cells". The Journal of Experimental Medicine. 199 (1): 15–24. doi:10.1084/jem.20030421. PMC 1887724. PMID 14707112.
  • Qin H, Wang J, Liang Y, Taniguchi Y, Tanigaki K, Han H (2004). "RING1 inhibits transactivation of RBP-J by Notch through interaction with LIM protein KyoT2". Nucleic Acids Research. 32 (4): 1492–501. doi:10.1093/nar/gkh295. PMC 390284. PMID 14999091.
  • Hong JW, Wu LC (Jan 2005). "Structural characterization of the gene encoding the large zinc finger protein ZAS3: implication to the origin of multiple promoters in eukaryotic genes". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1681 (2–3): 74–87. doi:10.1016/j.bbaexp.2004.10.004. PMID 15627499.
  • Bettelli E, Dastrange M, Oukka M (Apr 2005). "Foxp3 interacts with nuclear factor of activated T cells and NF-kappa B to repress cytokine gene expression and effector functions of T helper cells". Proceedings of the National Academy of Sciences of the United States of America. 102 (14): 5138–43. Bibcode:2005PNAS..102.5138B. doi:10.1073/pnas.0501675102. PMC 555574. PMID 15790681.
  • Li YJ, Deng J, Mayhew GM, Grimsley JW, Huo X, Vance JM (Sep 2007). "Investigation of the PARK10 gene in Parkinson disease". Annals of Human Genetics. 71 (Pt 5): 639–47. doi:10.1111/j.1469-1809.2007.00353.x. PMID 17388942. S2CID 22122597.

External links

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

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(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
(1.2) Basic helix-loop-helix (bHLH)
Group A
Group B
Group C
bHLH-PAS
Group D
Group E
Group F
bHLH-COE
(1.3) bHLH-ZIP
(1.4) NF-1
(1.5) RF-X
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1
subfamily 2
subfamily 3
subfamily 4
subfamily 5
subfamily 6
subfamily 0
(2.2) Other Cys4
(2.3) Cys2His2
(2.4) Cys6
(2.5) Alternating composition
(2.6) WRKY
(3) Helix-turn-helix domains
(3.1) Homeodomain
Antennapedia
ANTP class
protoHOX
Hox-like
metaHOX
NK-like
other
(3.2) Paired box
(3.3) Fork head / winged helix
(3.4) Heat shock factors
(3.5) Tryptophan clusters
(3.6) TEA domain
  • transcriptional enhancer factor
(4) β-Scaffold factors with minor groove contacts
(4.1) Rel homology region
(4.2) STAT
(4.3) p53-like
(4.4) MADS box
(4.6) TATA-binding proteins
(4.7) High-mobility group
(4.9) Grainyhead
(4.10) Cold-shock domain
(4.11) Runt
(0) Other transcription factors
(0.2) HMGI(Y)
(0.3) Pocket domain
(0.5) AP-2/EREBP-related factors
(0.6) Miscellaneous
see also transcription factor/coregulator deficiencies
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