Poly(A) polymerase alpha

Details

Name
Poly(A) polymerase alpha
Synonyms
  • 2.7.7.19
  • PAP
  • PAP-alpha
  • Polynucleotide adenylyltransferase alpha
Gene Name
PAPOLA
Organism
Humans
Amino acid sequence
>lcl|BSEQ0009436|Poly(A) polymerase alpha
MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQR
RILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVA
PRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPE
DLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNI
LGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVW
DPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSK
LFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQS
FPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVD
MKIAAMHVKRKQLHQLLPNHVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTS
ATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTAT
QPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEES
PKKTKTEEDETSEDANCLALSGHDKTEAKEQLDTETSTTQSETIQTAASLLASQKTSSTD
LSDIPALPANPIPVIKNSIKLRLNR
Number of residues
745
Molecular Weight
82841.78
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / magnesium ion binding / manganese ion binding / polynucleotide adenylyltransferase activity / RNA binding
Processes
gene expression / mRNA 3'-end processing / mRNA polyadenylation / mRNA splicing, via spliceosome / regulation of mRNA 3'-end processing / RNA polyadenylation / RNA splicing / termination of RNA polymerase II transcription / transcription from RNA polymerase II promoter
Components
cytoplasm / nucleoplasm / nucleus
General Function
Rna binding
Specific Function
Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0013158|Poly(A) polymerase alpha (PAPOLA)
ATGCCGTTTCCAGTTACAACACAGGGATCACAACAAACACAACCGCCACAGAAGCACTAT
GGCATTACTTCTCCTATCAGCTTAGCAGCCCCCAAGGAGACTGACTGCGTACTTACACAG
AAACTAATTGAGACATTGAAACCCTTTGGGGTTTTTGAAGAGGAAGAGGAACTGCAGCGC
AGGATTTTAATTTTGGGAAAACTAAATAACCTGGTAAAAGAGTGGATACGAGAAATCAGT
GAAAGCAAGAATCTTCCACAATCTGTAATTGAAAATGTTGGAGGAAAAATTTTTACATTT
GGATCTTACAGATTAGGAGTGCATACAAAAGGTGCTGATATTGATGCGTTGTGTGTTGCA
CCAAGACATGTTGATCGAAGTGACTTTTTCACCTCATTCTATGATAAGTTGAAATTACAG
GAAGAAGTAAAAGATTTAAGAGCTGTTGAAGAGGCATTCGTACCAGTTATTAAACTCTGT
TTTGATGGGATAGAGATTGATATTTTGTTTGCAAGATTAGCACTGCAGACAATTCCTGAA
GATTTGGATCTACGAGATGACAGTCTGCTAAAAAATTTAGATATAAGATGTATAAGAAGT
CTTAACGGTTGCAGGGTAACCGATGAAATTTTACATCTAGTACCAAACATTGACAACTTC
AGGTTAACTCTGAGAGCTATCAAACTATGGGCCAAACGCCACAACATCTATTCCAATATA
TTAGGTTTCCTCGGTGGTGTTTCCTGGGCTATGCTAGTAGCAAGAACTTGCCAGCTTTAT
CCAAATGCAATAGCATCAACTCTTGTACATAAATTTTTCTTGGTATTTTCTAAATGGTAT
GTGTTTAGATTATATTAA
Chromosome Location
14
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP51003
UniProtKB Entry NamePAPOA_HUMAN
HGNC IDHGNC:14981
General References
  1. 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. [PubMed:15489334]
  2. Thuresson AC, Astrom J, Astrom A, Gronvik KO, Virtanen A: Multiple forms of poly(A) polymerases in human cells. Proc Natl Acad Sci U S A. 1994 Feb 1;91(3):979-83. [PubMed:8302877]
  3. Dettwiler S, Aringhieri C, Cardinale S, Keller W, Barabino SM: Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. J Biol Chem. 2004 Aug 20;279(34):35788-97. Epub 2004 May 28. [PubMed:15169763]
  4. Kaufmann I, Martin G, Friedlein A, Langen H, Keller W: Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase. EMBO J. 2004 Feb 11;23(3):616-26. Epub 2004 Jan 29. [PubMed:14749727]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648]
  6. Kiefer H, Mizutani A, Iemura S, Natsume T, Ando H, Kuroda Y, Mikoshiba K: Inositol 1,4,5-triphosphate receptor-binding protein released with inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA 3' processing machinery in a phosphorylation-dependent manner and inhibits polyadenylation. J Biol Chem. 2009 Apr 17;284(16):10694-705. doi: 10.1074/jbc.M807136200. Epub 2009 Feb 18. [PubMed:19224921]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332]
  8. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [PubMed:20068231]
  9. 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. [PubMed:21269460]
  10. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [PubMed:22223895]
  11. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01860Cordycepin TriphosphateexperimentalunknownDetails
DB021533-sulfino-L-alanineexperimentalunknownDetails
DB03896Triphosphoric acidexperimentalunknownDetails