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Protein

Poly(A) RNA polymerase protein 2

Gene

PAP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF4 is also required for proper nuclear division in mitosis, DNA damage repair and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.17 Publications

Catalytic activityi

ATP + RNA(n) = diphosphate + RNA(n+1).1 Publication

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi236 – 2361Magnesium or manganese; catalyticBy similarity
Metal bindingi238 – 2381Magnesium or manganese; catalyticBy similarity

GO - Molecular functioni

  • 5'-deoxyribose-5-phosphate lyase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • polynucleotide adenylyltransferase activity Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: SGD
  • cell division Source: UniProtKB-KW
  • histone mRNA catabolic process Source: SGD
  • meiotic DNA double-strand break formation Source: SGD
  • mitotic nuclear division Source: UniProtKB-KW
  • ncRNA polyadenylation Source: UniProtKB
  • negative regulation of DNA recombination Source: SGD
  • nuclear mRNA surveillance of mRNA 3'-end processing Source: SGD
  • nuclear polyadenylation-dependent antisense transcript catabolic process Source: SGD
  • nuclear polyadenylation-dependent CUT catabolic process Source: SGD
  • nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
  • nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
  • nuclear polyadenylation-dependent snoRNA catabolic process Source: SGD
  • nuclear polyadenylation-dependent snRNA catabolic process Source: SGD
  • nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
  • polyadenylation-dependent mRNA catabolic process Source: SGD
  • polyadenylation-dependent snoRNA 3'-end processing Source: SGD
  • snoRNA polyadenylation Source: SGD
  • tRNA modification Source: SGD
  • U4 snRNA 3'-end processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33512-MONOMER.
BRENDAi4.2.99.B1. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A) RNA polymerase protein 2 (EC:2.7.7.-)
Alternative name(s):
DNA polymerase kappa
DNA polymerase sigma
Topoisomerase 1-related protein TRF4
Gene namesi
Name:PAP2
Synonyms:TRF4
Ordered Locus Names:YOL115W
ORF Names:HRC584, O0716
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL115W.
SGDiS000005475. PAP2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleolus Source: SGD
  • nucleus Source: SGD
  • TRAMP complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1333EDE → AAA in TRF4-131; slow growth. 1 Publication
Mutagenesisi140 – 1423ERE → AAA in TRF4-140; slow growth. 1 Publication
Mutagenesisi182 – 1854EIKD → AIAA in TRF4-182; lethal. 1 Publication
Mutagenesisi194 – 1941R → A in TRF4-194; lethal; when associated with A-195; A-196 and A-198.
Mutagenesisi195 – 1984EEIE → AIAA in TRF4-194; lethal.
Mutagenesisi217 – 2193DAD → AAA in TRF4-217; slow growth. 1 Publication
Mutagenesisi224 – 2252GS → AA in TRF4-224; lethal. 1 Publication
Mutagenesisi236 – 2383DID → AIA in TRF4-236; lethal. 3 Publications
Mutagenesisi275 – 2773KAR → AAA in TRF4-275; temperature sensitive. 1 Publication
Mutagenesisi282 – 2821K → A in TRF4-282; lethal; when associated with A-285.
Mutagenesisi285 – 2851E → A in TRF4-282; lethal; when associated with A-282.
Mutagenesisi309 – 3102RE → AA in TRF4-309; lethal. 1 Publication
Mutagenesisi332 – 3332RR → AA in TRF4-332; temperature sensitive. 1 Publication
Mutagenesisi378 – 3781E → A in TRF4-378; lethal; when associated with A-381.
Mutagenesisi381 – 3811E → A in TRF4-378; lethal; when associated with A-378.
Mutagenesisi425 – 4251D → A in TRF4-425; lethal; when associated with A-428 and A-429.
Mutagenesisi428 – 4292DE → AA in TRF4-425; lethal; when associated with A-425.
Mutagenesisi444 – 4452KK → AA in TRF4-444; lethal. 1 Publication
Mutagenesisi467 – 4693KDR → AAA in TRF4-467; temperature sensitive. 1 Publication
Mutagenesisi486 – 4872RD → AA in TRF4-486; lethal.
Mutagenesisi490 – 4923DER → AAA in TRF4-486; lethal.
Mutagenesisi502 – 5021E → A in TRF4-502; lethal; when associated with A-504.
Mutagenesisi504 – 5041E → A in TRF4-502; lethal; when associated with A-502.
Mutagenesisi508 – 5103KKR → AAA in TRF4-508; lethal. 1 Publication
Mutagenesisi559 – 5602KR → AA in TRF4-559; slow growth. 1 Publication
Mutagenesisi560 – 5601R → A in TRF4-559; slow growth; when associated with A-559.
Mutagenesisi572 – 5743EDD → AAA in TRF4-572; slow growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 584584Poly(A) RNA polymerase protein 2PRO_0000120314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei570 – 5701PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53632.

PTM databases

iPTMnetiP53632.

Interactioni

Subunit structurei

Component of the TRAMP complex (also called TRF4 complex) composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2. Interacts with NOP53 and POL2. Interacts directly with AIR2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIR1P405075EBI-19517,EBI-25083
AIR2Q1247612EBI-19517,EBI-31475
MTR4P4704710EBI-19517,EBI-11592

Protein-protein interaction databases

BioGridi34285. 401 interactions.
DIPiDIP-4214N.
IntActiP53632. 11 interactions.
MINTiMINT-500696.

Structurei

Secondary structure

1
584
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi122 – 1254Combined sources
Helixi162 – 1643Combined sources
Helixi175 – 18915Combined sources
Helixi194 – 21219Combined sources
Beta strandi220 – 2245Combined sources
Turni225 – 2295Combined sources
Beta strandi237 – 2415Combined sources
Helixi247 – 2493Combined sources
Helixi250 – 26314Combined sources
Beta strandi271 – 2777Combined sources
Beta strandi279 – 2857Combined sources
Turni286 – 2894Combined sources
Beta strandi290 – 2978Combined sources
Helixi303 – 31311Combined sources
Helixi318 – 33114Combined sources
Helixi337 – 3393Combined sources
Helixi344 – 35613Combined sources
Helixi359 – 3624Combined sources
Helixi368 – 3703Combined sources
Helixi372 – 38514Combined sources
Turni389 – 3913Combined sources
Beta strandi392 – 3998Combined sources
Beta strandi401 – 4055Combined sources
Helixi406 – 4083Combined sources
Helixi410 – 4123Combined sources
Beta strandi418 – 4203Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi428 – 4325Combined sources
Turni433 – 4364Combined sources
Helixi440 – 46223Combined sources
Helixi466 – 4694Combined sources
Turni476 – 4783Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MOWNMR-B573-584[»]
3NYBX-ray2.70A161-481[»]
4U4CX-ray2.40B111-160[»]
ProteinModelPortaliP53632.
SMRiP53632. Positions 161-481.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53632.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini371 – 43161PAP-associatedAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated
Contains 1 PAP-associated domain.Curated

Phylogenomic databases

GeneTreeiENSGT00400000022055.
HOGENOMiHOG000246586.
InParanoidiP53632.
KOiK03514.
OMAiTNNISRG.
OrthoDBiEOG7CNZS6.

Family and domain databases

InterProiIPR002058. PAP_assoc.
IPR002934. Polymerase_NTP_transf_dom.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAKSVTASS SKKIKNRHNG KVKKSKKIKK VRKPQKSISL NDENEVEILP
60 70 80 90 100
SRNEQETNKL PKDHVTADGI LVLEHKSDDD EGFDVYDGHF DNPTDIPSTT
110 120 130 140 150
EESKTPSLAV HGDEKDLANN DDFISLSASS EDEQAEQEEE REKQELEIKK
160 170 180 190 200
EKQKEILNTD YPWILNHDHS KQKEISDWLT FEIKDFVAYI SPSREEIEIR
210 220 230 240 250
NQTISTIREA VKQLWPDADL HVFGSYSTDL YLPGSDIDCV VTSELGGKES
260 270 280 290 300
RNNLYSLASH LKKKNLATEV EVVAKARVPI IKFVEPHSGI HIDVSFERTN
310 320 330 340 350
GIEAAKLIRE WLDDTPGLRE LVLIVKQFLH ARRLNNVHTG GLGGFSIICL
360 370 380 390 400
VFSFLHMHPR IITNEIDPKD NLGVLLIEFF ELYGKNFGYD DVALGSSDGY
410 420 430 440 450
PVYFPKSTWS AIQPIKNPFS LAIQDPGDES NNISRGSFNI RDIKKAFAGA
460 470 480 490 500
FDLLTNRCFE LHSATFKDRL GKSILGNVIK YRGKARDFKD ERGLVLNKAI
510 520 530 540 550
IENENYHKKR SRIIHDEDFA EDTVTSTATA TTTDDDYEIT NPPAKKAKIE
560 570 580
EKPESEPAKR NSGETYITVS SEDDDEDGYN PYTL
Length:584
Mass (Da):66,031
Last modified:October 1, 1996 - v1
Checksum:i8A58B29E4BFDC022
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31355 Genomic DNA. Translation: AAC49091.1.
Z48149 Genomic DNA. Translation: CAA88145.1.
Z74857 Genomic DNA. Translation: CAA99134.1.
AY723865 Genomic DNA. Translation: AAU09782.1.
BK006948 Genomic DNA. Translation: DAA10668.1.
PIRiS51882.
RefSeqiNP_014526.1. NM_001183369.1.

Genome annotation databases

EnsemblFungiiYOL115W; YOL115W; YOL115W.
GeneIDi854034.
KEGGisce:YOL115W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31355 Genomic DNA. Translation: AAC49091.1.
Z48149 Genomic DNA. Translation: CAA88145.1.
Z74857 Genomic DNA. Translation: CAA99134.1.
AY723865 Genomic DNA. Translation: AAU09782.1.
BK006948 Genomic DNA. Translation: DAA10668.1.
PIRiS51882.
RefSeqiNP_014526.1. NM_001183369.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MOWNMR-B573-584[»]
3NYBX-ray2.70A161-481[»]
4U4CX-ray2.40B111-160[»]
ProteinModelPortaliP53632.
SMRiP53632. Positions 161-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34285. 401 interactions.
DIPiDIP-4214N.
IntActiP53632. 11 interactions.
MINTiMINT-500696.

PTM databases

iPTMnetiP53632.

Proteomic databases

MaxQBiP53632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL115W; YOL115W; YOL115W.
GeneIDi854034.
KEGGisce:YOL115W.

Organism-specific databases

EuPathDBiFungiDB:YOL115W.
SGDiS000005475. PAP2.

Phylogenomic databases

GeneTreeiENSGT00400000022055.
HOGENOMiHOG000246586.
InParanoidiP53632.
KOiK03514.
OMAiTNNISRG.
OrthoDBiEOG7CNZS6.

Enzyme and pathway databases

BioCyciYEAST:G3O-33512-MONOMER.
BRENDAi4.2.99.B1. 984.

Miscellaneous databases

EvolutionaryTraceiP53632.
NextBioi975589.
PROiP53632.

Family and domain databases

InterProiIPR002058. PAP_assoc.
IPR002934. Polymerase_NTP_transf_dom.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of mutants of Saccharomyces cerevisiae requiring DNA topoisomerase I."
    Sadoff B.U., Heath-Pagliuso S., Castano I.B., Zhu Y., Kieff F.S., Christman M.F.
    Genetics 141:465-479(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element."
    Vandenbol M., Durand P., Portetelle D., Hilger F.
    Yeast 11:1069-1075(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Mitotic chromosome condensation in the rDNA requires TRF4 and DNA topoisomerase I in Saccharomyces cerevisiae."
    Castano I.B., Brzoska P.M., Sadoff B.U., Chen H., Christman M.F.
    Genes Dev. 10:2564-2576(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "A novel family of TRF (DNA topoisomerase I-related function) genes required for proper nuclear segregation."
    Castano I.B., Heath-Pagliuso S., Sadoff B.U., Fitzhugh D.J., Christman M.F.
    Nucleic Acids Res. 24:2404-2410(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin."
    Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A., Christman M.F.
    J. Biol. Chem. 274:7302-7308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Pol kappa: a DNA polymerase required for sister chromatid cohesion."
    Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F.
    Science 289:774-779(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 236-ASP--ASP-238.
  10. Cited for: NOMENCLATURE.
  11. "Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide reductase mRNA."
    Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III, Russell P.
    Cell 109:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Structure/function analysis of the Saccharomyces cerevisiae Trf4/Pol sigma DNA polymerase."
    Wang Z., Castano I.B., Adams C., Vu C., Fitzhugh D.J., Christman M.F.
    Genetics 160:381-391(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 131-GLU--GLU-133; 140-GLU--GLU-142; 182-GLU--ASP-185; 194-ARG--GLU-198; 217-ASP--ASP-219; 224-GLU-SER-225; 236-ASP--ASP-238; 275-LYS--ARG-277; 282-LYS--GLU-285; 309-ARG-GLU-310; 332-ARG-ARG-333; 378-GLU--GLU-381; 425-ASP--GLU-429; 444-LYS-LYS-445; 467-LYS--ARG-469; 486-ARG--ASP-490; 491-GLU-ARG-492; 502-GLU--GLU-504; 508-LYS--ARG-510; 559-LYS-ARG-560 AND 572-GLU--ASP-574.
  13. "Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma interact physically and functionally, suggesting a role for polymerase epsilon in sister chromatid cohesion."
    Edwards S., Li C.M., Levy D.L., Brown J., Snow P.M., Campbell J.L.
    Mol. Cell. Biol. 23:2733-2748(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POL2.
  14. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  15. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  16. "Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae."
    Kadaba S., Krueger A., Trice T., Krecic A.M., Hinnebusch A.G., Anderson J.T.
    Genes Dev. 18:1227-1240(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "RNA degradation by the exosome is promoted by a nuclear polyadenylation complex."
    LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E., Jacquier A., Tollervey D.
    Cell 121:713-724(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN TRAMP COMPLEX, FUNCTION OF THE TRAMP COMPLEX.
  18. "Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase."
    Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E., Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D., Jacquier A.
    Cell 121:725-737(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
  19. "Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity."
    Haracska L., Johnson R.E., Prakash L., Prakash S.
    Mol. Cell. Biol. 25:10183-10189(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "A new yeast poly(A) polymerase complex involved in RNA quality control."
    Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A., Langen H., Keith G., Keller W.
    PLoS Biol. 3:986-997(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE TRF4 COMPLEX.
  21. "Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome."
    Egecioglu D.E., Henras A.K., Chanfreau G.F.
    RNA 12:26-32(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S rRNA."
    Kadaba S., Wang X., Anderson J.T.
    RNA 12:508-521(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 236-ASP--ASP-238.
  23. "Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae."
    Reis C.C., Campbell J.L.
    Genetics 175:993-1010(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates processing of pre-rRNA by the exosome."
    Granato D.C., Machado-Santelli G.M., Oliveira C.C.
    FEBS J. 275:4164-4178(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOP53.
  25. "Structure and function of the polymerase core of TRAMP, a RNA surveillance complex."
    Hamill S., Wolin S.L., Reinisch K.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:15045-15050(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 161-481 IN COMPLEX WITH AIR2, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AIR2.

Entry informationi

Entry nameiPAP2_YEAST
AccessioniPrimary (citable) accession number: P53632
Secondary accession number(s): D6W1V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7550 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to have DNA polymerase activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.