Welcome! Click here to login or here to register.
Home
Pathways
Proteins
Catalytic RNA molecules
Enzymatic complexes
Structures
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

Poly(A) polymerase alpha

 
Known also as: Polynucleotide adenylyltransferase alpha, PAP-alpha

Known abbreviations: PAPOLA, PAP

 

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.
 
CATALYTIC ACTIVITY:
 
ATP + RNA(n) = diphosphate + RNA(n+1).
 
COFACTOR:
 
Binds 2 magnesium ions. Also active with manganese (By similarity.)
 
SUBUNIT STRUCTURE:
 
Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1 By similarity. Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP By similarity.
 
CELLULAR LOCALIZATION:
 
Cytoplasm. Nucleus. Note: The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic.
 
POST-TRANSLATIONAL MODIFICATION:
 
Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity.)
Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity.)
Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex (By similarity.)



Activities in which Poly(A) polymerase alpha is involved: Pathways in which Poly(A) polymerase alpha is involved:

NCBI GI number(s): 354681991
354681990
354681993
354681992
32490557
354681989
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P51003 P51003
BRENDA - -
KEGG hsa:10914 hsa:10914
PFAM: PF01909
PF04928
PF04926
PF01909
PF04928
PF04926
InterPro: IPR002934
IPR011068
IPR007012
IPR007010
IPR014492
IPR002934
IPR011068
IPR007012
IPR007010
IPR014492
CATH: - -
SCOP: - -


Protein sequence:
MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFG
VFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTF
GSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVE
EAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRS
LNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWA
MLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVW
DPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDE
ILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRI
LVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSE
NLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNH
VLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSS
GSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTAT
QPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVK
RTSSPHKEESPKKTKTEEDETSEDANCLALSGHDKTEAKEQLDTETSTTQ
SETIQTAASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR

Poly(A) polymerase alpha (Homo sapiens) is product of expression of PAPOLA gene.

References:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). 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, K Genome Res 2004-10-01 (14) 15489334
Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. Dettwiler S, Aringhieri C, Cardinale S, Keller W, Barabino SM J Biol Chem 2004-08-20 (279) 15169763
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A 2004-08-17 (101) 15302935
Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD J Proteome Res 2007-11-01 (6) 17924679
Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase. Kaufmann I, Martin G, Friedlein A, Langen H, Keller W EMBO J 2004-01-11 (23) 14749727
Multiple forms of poly(A) polymerases in human cells. Thuresson AC, Astrom J, Astrom A, Gronvik KO, Virtanen A Proc Natl Acad Sci U S A 1994-01-01 (91) 8302877



Add your own comment!


There are no comments yet.

Last modification of this entry: Sept. 25, 2012.

Welcome stranger! Click here to login or here to register.