RNA polymerase II subunit B4

Protein-coding gene in the species Homo sapiens

POLR2D
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2C35, 5IYD, 5IY8, 5IYC, 5IY6, 5IY7, 5IYA, 5IY9, 5IYB

Identifiers
AliasesPOLR2D, HSRBP4, HSRPB4, RBP4, RPB16, RNA polymerase II subunit B4, polymerase (RNA) II subunit D, RNA polymerase II subunit D, RPB4
External IDsOMIM: 606017; MGI: 1916491; HomoloGene: 37968; GeneCards: POLR2D; OMA:POLR2D - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for POLR2D
Genomic location for POLR2D
Band2q14.3Start127,843,553 bp[1]
End127,858,155 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for POLR2D
Genomic location for POLR2D
Band18|18 B1Start31,922,212 bp[2]
End31,929,754 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • left testis

  • right testis

  • pancreatic ductal cell

  • tibialis anterior muscle

  • ganglionic eminence

  • ventricular zone

  • islet of Langerhans

  • gastrocnemius muscle

  • quadriceps femoris muscle
Top expressed in
  • primary oocyte

  • yolk sac

  • ventricular zone

  • embryo

  • embryo

  • secondary oocyte

  • epiblast

  • endocardial cushion

  • medial ganglionic eminence

  • morula
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • DNA-directed 5'-3' RNA polymerase activity
  • single-stranded DNA binding
  • catalytic activity
  • single-stranded RNA binding
  • translation initiation factor binding
Cellular component
  • P-body
  • RNA polymerase II, core complex
  • nucleus
  • nucleoplasm
  • cytosol
  • nuclear speck
  • nuclear DNA-directed RNA polymerase complex
  • RNA polymerase complex
Biological process
  • mRNA splicing, via spliceosome
  • recruitment of 3'-end processing factors to RNA polymerase II holoenzyme complex
  • transcription elongation from RNA polymerase II promoter
  • 7-methylguanosine mRNA capping
  • transcription by RNA polymerase II
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
  • cell metabolism
  • transcription-coupled nucleotide-excision repair
  • transcription initiation from RNA polymerase II promoter
  • positive regulation of translational initiation
  • mRNA export from nucleus in response to heat stress
  • fibroblast growth factor receptor signaling pathway
  • snRNA transcription by RNA polymerase II
  • RNA metabolic process
  • regulation of gene silencing by miRNA
  • DNA-templated transcription, initiation
  • transcription, DNA-templated
  • somatic stem cell population maintenance
  • positive regulation of viral transcription
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5433

69241

Ensembl

ENSG00000144231

ENSMUSG00000024258

UniProt

O15514

Q9D7M8

RefSeq (mRNA)

NM_004805

NM_027002
NM_001357480

RefSeq (protein)

NP_004796

NP_081278
NP_001344409

Location (UCSC)Chr 2: 127.84 – 127.86 MbChr 18: 31.92 – 31.93 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA-directed RNA polymerase II subunit RPB4 is an enzyme that in humans is encoded by the POLR2D gene.[5]

This gene encodes the fourth-largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. In yeast, this polymerase subunit is associated with the polymerase under suboptimal growth conditions and may have a stress protective role. A sequence for a ribosomal pseudogene is contained within the 3' untranslated region of the transcript from this gene.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000144231 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024258 – 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. ^ Khazak V, Estojak J, Cho H, Majors J, Sonoda G, Testa JR, Golemis EA (May 1998). "Analysis of the interaction of the novel RNA polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and with pol II". Mol Cell Biol. 18 (4): 1935–45. doi:10.1128/mcb.18.4.1935. PMC 121423. PMID 9528765.
  6. ^ "Entrez Gene: POLR2D polymerase (RNA) II (DNA directed) polypeptide D".

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447–9. Bibcode:1998CBio....8.R447Y. doi:10.1016/S0960-9822(98)70289-1. PMID 9651670. S2CID 15480646.
  • Romano G, Kasten M, De Falco G, et al. (2000). "Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression". J. Cell. Biochem. 75 (3): 357–68. doi:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. PMID 10536359. S2CID 43685090.
  • Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator". IUBMB Life. 51 (3): 175–81. doi:10.1080/152165401753544241. PMID 11547919. S2CID 10931640.
  • Stevens M, De Clercq E, Balzarini J (2007). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention". Med Res Rev. 26 (5): 595–625. doi:10.1002/med.20081. PMC 7168390. PMID 16838299.
  • Harrich D, McMillan N, Munoz L, et al. (2007). "Will diverse Tat interactions lead to novel antiretroviral drug targets?". Current Drug Targets. 7 (12): 1595–606. doi:10.2174/138945006779025338. PMID 17168834.
  • Kato H, Sumimoto H, Pognonec P, et al. (1992). "HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors". Genes Dev. 6 (4): 655–66. doi:10.1101/gad.6.4.655. PMID 1559613.
  • Southgate C, Zapp ML, Green MR (1990). "Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein". Nature. 345 (6276): 640–2. Bibcode:1990Natur.345..640S. doi:10.1038/345640a0. PMID 2190099. S2CID 4233742.
  • Wu-Baer F, Sigman D, Gaynor RB (1995). "Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat". Proc. Natl. Acad. Sci. U.S.A. 92 (16): 7153–7. Bibcode:1995PNAS...92.7153W. doi:10.1073/pnas.92.16.7153. PMC 41297. PMID 7638159.
  • Herrmann CH, Rice AP (1995). "Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor". J. Virol. 69 (3): 1612–20. doi:10.1128/JVI.69.3.1612-1620.1995. PMC 188757. PMID 7853496.
  • Keen NJ, Gait MJ, Karn J (1996). "Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex". Proc. Natl. Acad. Sci. U.S.A. 93 (6): 2505–10. Bibcode:1996PNAS...93.2505K. doi:10.1073/pnas.93.6.2505. PMC 39827. PMID 8637904.
  • Yang X, Herrmann CH, Rice AP (1996). "The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function". J. Virol. 70 (7): 4576–84. doi:10.1128/JVI.70.7.4576-4584.1996. PMC 190394. PMID 8676484.
  • Agostini I, Navarro JM, Rey F, et al. (1996). "The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB". J. Mol. Biol. 261 (5): 599–606. doi:10.1006/jmbi.1996.0485. PMID 8800208.
  • Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat". Science. 274 (5287): 605–10. Bibcode:1996Sci...274..605Z. doi:10.1126/science.274.5287.605. PMID 8849451. S2CID 13266489.
  • Okamoto H, Sheline CT, Corden JL, et al. (1996). "Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11575–9. Bibcode:1996PNAS...9311575O. doi:10.1073/pnas.93.21.11575. PMC 38099. PMID 8876177.
  • Chun RF, Jeang KT (1996). "Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1". J. Biol. Chem. 271 (44): 27888–94. doi:10.1074/jbc.271.44.27888. PMID 8910388.
  • Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain". Nature. 384 (6607): 375–8. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526. S2CID 4278432.
  • García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes". J. Biol. Chem. 272 (11): 6951–8. doi:10.1074/jbc.272.11.6951. PMID 9054383.
  • Cujec TP, Cho H, Maldonado E, et al. (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme". Mol. Cell. Biol. 17 (4): 1817–23. doi:10.1128/mcb.17.4.1817. PMC 232028. PMID 9121429.
  • García-Martínez LF, Mavankal G, Neveu JM, et al. (1997). "Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription". EMBO J. 16 (10): 2836–50. doi:10.1093/emboj/16.10.2836. PMC 1169892. PMID 9184228.
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  • 2c35: SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II
    2c35: SUBUNITS RPB4 AND RPB7 OF HUMAN RNA POLYMERASE II
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