PAPOG_HUMAN
ID PAPOG_HUMAN Reviewed; 736 AA.
AC Q9BWT3; B2RBH4; Q59G05; Q969N1; Q9H8L2; Q9HAD0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Poly(A) polymerase gamma;
DE Short=PAP-gamma;
DE EC=2.7.7.19 {ECO:0000269|PubMed:11287430, ECO:0000269|PubMed:11431479, ECO:0000269|PubMed:11463842};
DE AltName: Full=Neo-poly(A) polymerase;
DE Short=Neo-PAP {ECO:0000303|PubMed:11463842};
DE AltName: Full=Polynucleotide adenylyltransferase gamma;
DE AltName: Full=SRP RNA 3'-adenylating enzyme;
DE AltName: Full=Signal recognition particle RNA-adenylating enzyme;
DE Short=SRP RNA-adenylating enzyme;
GN Name=PAPOLG {ECO:0000312|HGNC:HGNC:14982}; Synonyms=PAP2, PAPG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=11287430; DOI=10.1074/jbc.m101905200;
RA Perumal K., Sinha K., Henning D., Reddy R.;
RT "Purification, characterization, and cloning of the cDNA of human signal
RT recognition particle RNA 3'-adenylating enzyme.";
RL J. Biol. Chem. 276:21791-21796(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Melanoma;
RX PubMed=11463842; DOI=10.1128/mcb.21.16.5614-5623.2001;
RA Topalian S.L., Kaneko S., Gonzales M.I., Bond G.L., Ward Y., Manley J.L.;
RT "Identification and functional characterization of neo-poly(A) polymerase,
RT an RNA processing enzyme overexpressed in human tumors.";
RL Mol. Cell. Biol. 21:5614-5623(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=11431479; DOI=10.1074/jbc.m104599200;
RA Kyriakopoulou C.B., Nordvarg H., Virtanen A.;
RT "A novel nuclear human poly(A) polymerase (PAP), PAP gamma.";
RL J. Biol. Chem. 276:33504-33511(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-736 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-648; THR-654 AND
RP SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-29; SER-525; SER-599;
RP SER-684 AND SER-708, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 1-508 IN COMPLEX WITH ATP AND
RP CALCIUM IONS.
RX PubMed=24076191; DOI=10.1016/j.jmb.2013.09.025;
RA Yang Q., Nausch L., Martin G., Keller W., Doublie S.;
RT "Crystal structure of human poly(A) polymerase gamma reveals a conserved
RT catalytic core for canonical poly(A) polymerases.";
RL J. Mol. Biol. 426:43-50(2014).
CC -!- FUNCTION: Responsible for the post-transcriptional adenylation of the
CC 3'-terminal of mRNA precursors and several small RNAs including signal
CC recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA,
CC and ribosomal 5S RNA. {ECO:0000269|PubMed:11287430,
CC ECO:0000269|PubMed:11463842}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:11287430, ECO:0000269|PubMed:11431479,
CC ECO:0000269|PubMed:11463842};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.051 uM for poly(A)(15) {ECO:0000269|PubMed:11431479};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11287430,
CC ECO:0000269|PubMed:11431479, ECO:0000269|PubMed:11463842}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BWT3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWT3-2; Sequence=VSP_054379;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in testis, and weakly in
CC other tissues. Overexpressed in several tumors.
CC {ECO:0000269|PubMed:11463842}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14604.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY029162; AAK31791.1; -; mRNA.
DR EMBL; AF312211; AAK83701.1; -; mRNA.
DR EMBL; AJ308101; CAC59751.1; -; mRNA.
DR EMBL; AK021867; BAB13919.1; -; mRNA.
DR EMBL; AK023544; BAB14604.1; ALT_INIT; mRNA.
DR EMBL; AK314663; BAG37221.1; -; mRNA.
DR EMBL; AC011245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00034.1; -; Genomic_DNA.
DR EMBL; BC111701; AAI11702.1; -; mRNA.
DR EMBL; BC113747; AAI13748.1; -; mRNA.
DR EMBL; AB209304; BAD92541.1; -; mRNA.
DR CCDS; CCDS1863.1; -. [Q9BWT3-1]
DR RefSeq; NP_075045.2; NM_022894.3. [Q9BWT3-1]
DR RefSeq; XP_005264557.1; XM_005264500.3. [Q9BWT3-2]
DR PDB; 4LT6; X-ray; 2.79 A; A/B=1-508.
DR PDBsum; 4LT6; -.
DR AlphaFoldDB; Q9BWT3; -.
DR SMR; Q9BWT3; -.
DR BioGRID; 122338; 27.
DR IntAct; Q9BWT3; 6.
DR STRING; 9606.ENSP00000238714; -.
DR GlyGen; Q9BWT3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BWT3; -.
DR PhosphoSitePlus; Q9BWT3; -.
DR BioMuta; PAPOLG; -.
DR DMDM; 116242699; -.
DR EPD; Q9BWT3; -.
DR jPOST; Q9BWT3; -.
DR MassIVE; Q9BWT3; -.
DR MaxQB; Q9BWT3; -.
DR PaxDb; Q9BWT3; -.
DR PeptideAtlas; Q9BWT3; -.
DR PRIDE; Q9BWT3; -.
DR ProteomicsDB; 62654; -.
DR ProteomicsDB; 79313; -. [Q9BWT3-1]
DR Antibodypedia; 30527; 135 antibodies from 21 providers.
DR DNASU; 64895; -.
DR Ensembl; ENST00000238714.8; ENSP00000238714.3; ENSG00000115421.13. [Q9BWT3-1]
DR GeneID; 64895; -.
DR KEGG; hsa:64895; -.
DR MANE-Select; ENST00000238714.8; ENSP00000238714.3; NM_022894.4; NP_075045.2.
DR UCSC; uc002sai.4; human. [Q9BWT3-1]
DR CTD; 64895; -.
DR DisGeNET; 64895; -.
DR GeneCards; PAPOLG; -.
DR HGNC; HGNC:14982; PAPOLG.
DR HPA; ENSG00000115421; Low tissue specificity.
DR MIM; 616865; gene.
DR neXtProt; NX_Q9BWT3; -.
DR OpenTargets; ENSG00000115421; -.
DR PharmGKB; PA32934; -.
DR VEuPathDB; HostDB:ENSG00000115421; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000156467; -.
DR HOGENOM; CLU_011511_1_2_1; -.
DR InParanoid; Q9BWT3; -.
DR OMA; FTEHVIM; -.
DR OrthoDB; 326577at2759; -.
DR PhylomeDB; Q9BWT3; -.
DR TreeFam; TF300842; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q9BWT3; -.
DR SABIO-RK; Q9BWT3; -.
DR SignaLink; Q9BWT3; -.
DR BioGRID-ORCS; 64895; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; PAPOLG; human.
DR GeneWiki; PAPOLG; -.
DR GenomeRNAi; 64895; -.
DR Pharos; Q9BWT3; Tbio.
DR PRO; PR:Q9BWT3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BWT3; protein.
DR Bgee; ENSG00000115421; Expressed in endothelial cell and 189 other tissues.
DR ExpressionAtlas; Q9BWT3; baseline and differential.
DR Genevisible; Q9BWT3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; IDA:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 2.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..736
FT /note="Poly(A) polymerase gamma"
FT /id="PRO_0000051624"
FT REGION 506..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24076191"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24076191"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24076191"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24076191"
FT BINDING 245..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24076191"
FT SITE 152
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 327
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 398
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 532
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 654
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 664..685
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_054379"
FT CONFLICT 31
FT /note="K -> E (in Ref. 1; AAK31791)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="P -> S (in Ref. 1; AAK31791)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="T -> I (in Ref. 1; AAK31791)"
FT /evidence="ECO:0000305"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 54..78
FT /evidence="ECO:0007829|PDB:4LT6"
FT TURN 79..83
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 163..171
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:4LT6"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:4LT6"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 330..350
FT /evidence="ECO:0007829|PDB:4LT6"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:4LT6"
FT TURN 366..368
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 371..382
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 383..394
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 432..442
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 456..472
FT /evidence="ECO:0007829|PDB:4LT6"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:4LT6"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:4LT6"
SQ SEQUENCE 736 AA; 82803 MW; B0F6F217AA36E552 CRC64;
MKEMSANTVL DSQRQQKHYG ITSPISLASP KEIDHIYTQK LIDAMKPFGV FEDEEELNHR
LVVLGKLNNL VKEWISDVSE SKNLPPSVVA TVGGKIFTFG SYRLGVHTKG ADIDALCVAP
RHVERSDFFQ SFFEKLKHQD GIRNLRAVED AFVPVIKFEF DGIEIDLVFA RLAIQTISDN
LDLRDDSRLR SLDIRCIRSL NGCRVTDEIL HLVPNKETFR LTLRAVKLWA KRRGIYSNML
GFLGGVSWAM LVARTCQLYP NAAASTLVHK FFLVFSKWEW PNPVLLKQPE ESNLNLPVWD
PRVNPSDRYH LMPIITPAYP QQNSTYNVST STRTVMVEEF KQGLAVTDEI LQGKSDWSKL
LEPPNFFQKY RHYIVLTASA STEENHLEWV GLVESKIRVL VGNLERNEFI TLAHVNPQSF
PGNKEHHKDN NYVSMWFLGI IFRRVENAES VNIDLTYDIQ SFTDTVYRQA NNINMLKEGM
KIEATHVKKK QLHHYLPAEI LQKKKKQSLS DVNRSSGGLQ SKRLSLDSSC LDSSRDTDNG
TPFNSPASKS DSPSVGETER NSAEPAAVIV EKPLSVPPAQ GLSIPVIGAK VDSTVKTVSP
PTVCTIPTVV GRNVIPRITT PHNPAQGQPH LNGMSNITKT VTPKRSHSPS IDGTPKRLKD
VEKFIRLEST FKDPRTAEER KRKSVDAIGG ESMPIPTIDT SRKKRLPSKE LPDSSSPVPA
NNIRVIKNSI RLTLNR
