DNA-directed RNA polymerases I, II, and III subunit RPABC5

NameDNA-directed RNA polymerases I, II, and III subunit RPABC5
SynonymsDNA-directed RNA polymerase III subunit L RNA polymerase II 7.6 kDa subunit RNA polymerases I, II, and III subunit ABC5 RPB10 homolog RPB7.6
Gene NamePOLR2L
OrganismHuman
Amino acid sequence
>lcl|BSEQ0013576|DNA-directed RNA polymerases I, II, and III subunit RPABC5
MIIPVRCFTCGKIVGNKWEAYLGLLQAEYTEGDALDALGLKRYCCRRMLLAHVDLIEKLL
NYAPLEK
Number of residues67
Molecular Weight7645.02
Theoretical pINone
GO Classification
Functions
    zinc ion binding
DNA binding
DNA-directed RNA polymerase activity
Processes
    gene expression
7-methylguanosine mRNA capping
transcription elongation from RNA polymerase I promoter
transcription initiation from RNA polymerase II promoter
gene silencing by RNA
transcription elongation from RNA polymerase III promoter
mRNA splicing, via spliceosome
transcription from RNA polymerase I promoter
piRNA metabolic process
transcription from RNA polymerase III promoter
innate immune response
positive regulation of viral transcription
transcription initiation from RNA polymerase I promoter
somatic stem cell population maintenance
RNA splicing
DNA repair
regulation of transcription from RNA polymerase I promoter
transcription-coupled nucleotide-excision repair
transcription elongation from RNA polymerase II promoter
viral process
nucleotide-excision repair
negative regulation of gene expression, epigenetic
transcription from RNA polymerase II promoter
regulation of gene expression, epigenetic
termination of RNA polymerase I transcription
positive regulation of type I interferon production
termination of RNA polymerase III transcription
Components
    cytosol
nucleoplasm
nucleus
DNA-directed RNA polymerase I complex
DNA-directed RNA polymerase III complex
DNA-directed RNA polymerase II, core complex
General FunctionZinc ion binding
Specific FunctionDNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and a small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2L/RBP10 is part of the core element with the central large cleft (By similarity).
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP62875
UniProtKB Entry NameRPAB5_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0013577|DNA-directed RNA polymerases I, II, and III subunit RPABC5 (POLR2L)
ATGATCATCCCTGTACGCTGCTTCACTTGTGGCAAGATCGTCGGCAACAAGTGGGAGGCT
TACCTGGGGCTGCTGCAGGCCGAGTACACCGAGGGGGATGCGCTGGATGCCCTGGGCCTG
AAGCGCTACTGCTGCCGCCGGATGCTGCTGGCCCACGTGGACCTGATCGAGAAGCTGCTC
AATTATGCACCCCTGGAGAAGTGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:9199
Chromosome Location11
LocusNone
References
  1. McKune K, Moore PA, Hull MW, Woychik NA: Six human RNA polymerase subunits functionally substitute for their yeast counterparts. Mol Cell Biol. 1995 Dec;15(12):6895-900.[8524256 ]
  2. Shpakovski GV, Acker J, Wintzerith M, Lacroix JF, Thuriaux P, Vigneron M: Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae. Mol Cell Biol. 1995 Sep;15(9):4702-10.[7651387 ]
  3. Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53.[9852112 ]
  4. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48.[16809778 ]
  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17.[21269460 ]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21.[14702039 ]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]

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