PAPOB_HUMAN
ID PAPOB_HUMAN Reviewed; 637 AA.
AC Q9NRJ5; Q75LH1; Q8NE14;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Poly(A) polymerase beta {ECO:0000305};
DE Short=PAP-beta;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase beta;
DE AltName: Full=Testis-specific poly(A) polymerase;
GN Name=PAPOLB {ECO:0000312|HGNC:HGNC:15970}; Synonyms=PAPT;
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].
RA Lee Y., Kim H., Chung J., Lee Y.;
RT "Testis-specific poly(A) polymerase gene is conserved in human and mouse.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 -!- 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 -!- SUBUNIT: Interacts with GSG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81013.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS07561.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF218840; AAF81013.1; ALT_INIT; mRNA.
DR EMBL; AC092610; AAS07561.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC036653; AAH36653.2; -; mRNA.
DR CCDS; CCDS78202.1; -.
DR RefSeq; NP_064529.4; NM_020144.4.
DR AlphaFoldDB; Q9NRJ5; -.
DR SMR; Q9NRJ5; -.
DR BioGRID; 121233; 5.
DR STRING; 9606.ENSP00000384700; -.
DR iPTMnet; Q9NRJ5; -.
DR PhosphoSitePlus; Q9NRJ5; -.
DR BioMuta; PAPOLB; -.
DR DMDM; 18203318; -.
DR jPOST; Q9NRJ5; -.
DR MassIVE; Q9NRJ5; -.
DR MaxQB; Q9NRJ5; -.
DR PaxDb; Q9NRJ5; -.
DR PeptideAtlas; Q9NRJ5; -.
DR PRIDE; Q9NRJ5; -.
DR ProteomicsDB; 82380; -.
DR Antibodypedia; 24543; 81 antibodies from 20 providers.
DR DNASU; 56903; -.
DR Ensembl; ENST00000404991.2; ENSP00000384700.2; ENSG00000218823.2.
DR GeneID; 56903; -.
DR KEGG; hsa:56903; -.
DR MANE-Select; ENST00000404991.2; ENSP00000384700.2; NM_020144.5; NP_064529.4.
DR UCSC; uc003snk.4; human.
DR CTD; 56903; -.
DR GeneCards; PAPOLB; -.
DR HGNC; HGNC:15970; PAPOLB.
DR HPA; ENSG00000218823; Tissue enriched (testis).
DR MIM; 607436; gene.
DR neXtProt; NX_Q9NRJ5; -.
DR OpenTargets; ENSG00000218823; -.
DR PharmGKB; PA32933; -.
DR VEuPathDB; HostDB:ENSG00000218823; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000164307; -.
DR HOGENOM; CLU_011511_1_2_1; -.
DR InParanoid; Q9NRJ5; -.
DR OMA; ITAMHLR; -.
DR OrthoDB; 326577at2759; -.
DR PhylomeDB; Q9NRJ5; -.
DR TreeFam; TF300842; -.
DR PathwayCommons; Q9NRJ5; -.
DR SIGNOR; Q9NRJ5; -.
DR BioGRID-ORCS; 56903; 4 hits in 313 CRISPR screens.
DR GenomeRNAi; 56903; -.
DR Pharos; Q9NRJ5; Tbio.
DR PRO; PR:Q9NRJ5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NRJ5; protein.
DR Bgee; ENSG00000218823; Expressed in sperm and 19 other tissues.
DR ExpressionAtlas; Q9NRJ5; baseline and differential.
DR Genevisible; Q9NRJ5; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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; IPR014492; PolyA_polymerase.
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; 1.
DR PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..637
FT /note="Poly(A) polymerase beta"
FT /id="PRO_0000051622"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 /evidence="ECO:0000250"
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 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 247..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 154
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 400
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 525
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT CONFLICT 67
FT /note="E -> D (in Ref. 3; AAH36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="E -> Q (in Ref. 3; AAH36653)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="M -> V (in Ref. 3; AAH36653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 71813 MW; DEF83370A87D10B8 CRC64;
MMPFPVTTQG PPQPAPPPNR YGVSSPISLA VPKETDCLLT QRLIETLRPF GVFEEEEELQ
RRILVLEKLN NLVKEWIREI SESKSLPQSV IENVGGKIFT FGSYRLGVHT KGADIDALCV
APSHVDRSDF FTSFYAKLKL QEEVKDLRAV EEAFVPVIKL CFDGIEIDIL FARLALQTIP
EDLDLRDDSL LKNLDIRCIR SLNGCRVTDE ILHLVPNIDN FRLTLRAIKL WAKCHNIYSN
ILGFLGGVSW AMLVARTCQL YPNAVASTLV RKFFLVFSEW EWPNPVLLKE PEERNLNLPV
WDPRVNPSDR YHLMPIITPA YPQQNSTYNV SISTRMVMIE EFKQGLAITH EILLSKAEWS
KLFEAPSFFQ KYKHYIVLLA SASTEKQHLE WVGLVESKIR ILVGSLEKNE FITLAHVNPQ
SFPAPKENPD MEEFRTMWVI GLGLKKPDNS EILSIDLTYD IQSFTDTVYR QAVNSKMFEM
GMKITAMHLR RKELHQLLPH HVLQDKKAHS TEGRRLTDLN DSSFDLSAGC ENSMSVPSST
STMKTGPLIS SSQGRNSPAL AVMTASVANI QATEFSLQQV NTNESSGVAL NESIPHAVSQ
PAISPSPKAM VARVVSSTCL ISHPDLQETQ QQTYLIL
