RNA polymerase II subunit B4

POLR2D
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2C35, 5IYD, 5IY8, 5IYC, 5IY6, 5IY7, 5IYA, 5IY9, 5IYB
Identifiers
Aliases	POLR2D , HSRBP4, HSRPB4, RBP4, RPB16, RNA polymerase II subunit B4, polymerase (RNA) II subunit D, RNA polymerase II subunit D, RPB4
External IDs	OMIM: 606017 MGI: 1916491 HomoloGene: 37968 GeneCards: POLR2D
Gene location (Human) Chr. Chromosome 2 (human) [1] Band 2q14.3 Start 127,843,553 bp [1] End 127,858,155 bp [1]
Gene location (Mouse) Chr. Chromosome 18 (mouse) [2] Band 18|18 B1 Start 31,922,212 bp [2] End 31,929,754 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell pancreatic ductal cell tibialis anterior muscle ganglionic eminence islet of Langerhans gastrocnemius muscle quadriceps femoris muscle vastus lateralis muscle internal globus pallidus skeletal muscle tissue Top expressed in yolk sac secondary oocyte endocardial cushion medial ganglionic eminence morula neural tube primitive streak abdominal wall otic placode maxillary prominence 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 Species Human Mouse 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 Mb Chr 18: 31.92 – 31.93 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/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. GRCh38: Ensembl release 89: ENSG00000144231 - Ensembl, May 2017
2. 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.