PBX3

Protein found in humans
PBX3
Identifiers
AliasesPBX3, PBX homeobox 3
External IDsOMIM: 176312; MGI: 97496; HomoloGene: 21243; GeneCards: PBX3; OMA:PBX3 - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for PBX3
Genomic location for PBX3
Band9q33.3Start125,747,345 bp[1]
End125,967,377 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for PBX3
Genomic location for PBX3
Band2 B|2 22.84 cMStart34,061,469 bp[2]
End34,263,154 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left ovary

  • right adrenal cortex

  • right ovary

  • left adrenal cortex

  • muscle layer of sigmoid colon

  • right auricle

  • internal globus pallidus

  • C1 segment

  • gallbladder

  • vena cava
Top expressed in
  • substantia nigra

  • olfactory bulb

  • ciliary body

  • retinal pigment epithelium

  • dorsal tegmental nucleus

  • adrenal gland

  • external carotid artery

  • habenula

  • fossa

  • abdominal wall
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • RNA polymerase II cis-regulatory region sequence-specific DNA binding
  • DNA binding
  • sequence-specific DNA binding
  • DNA-binding transcription activator activity, RNA polymerase II-specific
  • DNA-binding transcription factor activity, RNA polymerase II-specific
  • protein binding
Cellular component
  • nucleus
  • transcription regulator complex
Biological process
  • regulation of respiratory gaseous exchange by nervous system process
  • adult locomotory behavior
  • anterior compartment pattern formation
  • dorsal spinal cord development
  • neuron development
  • regulation of transcription, DNA-templated
  • transcription by RNA polymerase II
  • posterior compartment specification
  • respiratory gaseous exchange by respiratory system
  • positive regulation of transcription by RNA polymerase II
  • transcription, DNA-templated
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5090

18516

Ensembl

ENSG00000167081

ENSMUSG00000038718

UniProt

P40426
Q96AL5

O35317

RefSeq (mRNA)

NM_001134778
NM_006195
NM_001330782

NM_001290576
NM_016768

RefSeq (protein)

NP_001128250
NP_001317711
NP_006186
NP_006186.1

NP_001277505
NP_058048

Location (UCSC)Chr 9: 125.75 – 125.97 MbChr 2: 34.06 – 34.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Pre-B-cell leukemia transcription factor 3 is a protein that in humans is encoded by the PBX3 gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167081 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000038718 – 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. ^ Monica K, Galili N, Nourse J, Saltman D, Cleary ML (Dec 1991). "PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1". Mol Cell Biol. 11 (12): 6149–57. doi:10.1128/mcb.11.12.6149. PMC 361792. PMID 1682799.
  6. ^ "Entrez Gene: PBX3 pre-B-cell leukemia homeobox 3".

Further reading

  • Lu Q, Wright DD, Kamps MP (1994). "Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation". Mol. Cell. Biol. 14 (6): 3938–48. doi:10.1128/mcb.14.6.3938. PMC 358760. PMID 7910944.
  • Shen WF, Rozenfeld S, Kwong A, et al. (1999). "HOXA9 Forms Triple Complexes with PBX2 and MEIS1 in Myeloid Cells". Mol. Cell. Biol. 19 (4): 3051–61. doi:10.1128/mcb.19.4.3051. PMC 84099. PMID 10082572.
  • Fujino T, Yamazaki Y, Largaespada DA, et al. (2001). "Inhibition of myeloid differentiation by Hoxa9, Hoxb8, and Meis homeobox genes". Exp. Hematol. 29 (7): 856–63. doi:10.1016/S0301-472X(01)00655-5. PMID 11438208.
  • Knoepfler PS, Sykes DB, Pasillas M, Kamps MP (2001). "HoxB8 requires its Pbx-interaction motif to block differentiation of primary myeloid progenitors and of most cell line models of myeloid differentiation". Oncogene. 20 (39): 5440–8. doi:10.1038/sj.onc.1204710. PMID 11571641.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. Bibcode:2004Natur.429..369H. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
  • Rhee JW, Arata A, Selleri L, et al. (2004). "Pbx3 Deficiency Results in Central Hypoventilation". Am. J. Pathol. 165 (4): 1343–50. doi:10.1016/S0002-9440(10)63392-5. PMC 1618620. PMID 15466398.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

  • v
  • t
  • e
  • 1b72: PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX
    1b72: PBX1, HOMEOBOX PROTEIN HOX-B1/DNA TERNARY COMPLEX
  • 1b8i: STRUCTURE OF THE HOMEOTIC UBX/EXD/DNA TERNARY COMPLEX
    1b8i: STRUCTURE OF THE HOMEOTIC UBX/EXD/DNA TERNARY COMPLEX
  • 1du6: SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN
    1du6: SOLUTION STRUCTURE OF THE TRUNCATED PBX HOMEODOMAIN
  • 1lfu: NMR solution structure of the extended PBX homeodomain bound to DNA
    1lfu: NMR solution structure of the extended PBX homeodomain bound to DNA
  • 1puf: Crystal structure of HoxA9 and Pbx1 homeodomains bound to DNA
    1puf: Crystal structure of HoxA9 and Pbx1 homeodomains bound to DNA
  • v
  • t
  • e
(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

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


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