PAPOA_BOVIN
ID PAPOA_BOVIN Reviewed; 739 AA.
AC P25500;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Poly(A) polymerase alpha;
DE Short=PAP-alpha;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase alpha;
GN Name=PAPOLA; Synonyms=PAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN SEQUENCE
RP OF 1-21; 207-255 AND 386-397.
RC TISSUE=Thymus;
RX PubMed=1756732; DOI=10.1002/j.1460-2075.1991.tb05003.x;
RA Wahle E., Martin G., Schiltz E., Keller W.;
RT "Isolation and expression of cDNA clones encoding mammalian poly(A)
RT polymerase.";
RL EMBO J. 10:4251-4257(1991).
RN [2]
RP SEQUENCE REVISION.
RA Wahle E.;
RL Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 97-103 AND 445-468.
RC TISSUE=Heart muscle;
RX PubMed=1896071; DOI=10.1038/353229a0;
RA Raabe T., Bollum F.J., Manley J.L.;
RT "Primary structure and expression of bovine poly(A) polymerase.";
RL Nature 353:229-234(1991).
RN [4]
RP DOMAINS, AND MUTAGENESIS OF ASP-113; ASP-115; 162-ASP-GLY-163; ASP-167;
RP ASP-186; ASP-194; ASP-208; GLU-209; GLU-291; GLU-292; 431-GLU-GLU-432;
RP ASP-455; ASP-459 AND ASP-465.
RX PubMed=8665867; DOI=10.1002/j.1460-2075.1996.tb00617.x;
RA Martin G., Keller W.;
RT "Mutational analysis of mammalian poly(A) polymerase identifies a region
RT for primer binding and catalytic domain, homologous to the family X
RT polymerases, and to other nucleotidyltransferases.";
RL EMBO J. 15:2593-2603(1996).
RN [5]
RP PHOSPHORYLATION, AND FUNCTION.
RX PubMed=9463383; DOI=10.1093/emboj/17.4.1053;
RA Colgan D.F., Murthy K.G., Zhao W., Prives C., Manley J.L.;
RT "Inhibition of poly(A) polymerase requires p34cdc2/cyclin B phosphorylation
RT of multiple consensus and non-consensus sites.";
RL EMBO J. 17:1053-1062(1998).
RN [6]
RP ACETYLATION AT LYS-635; LYS-644; LYS-730 AND LYS-734, INTERACTION WITH
RP NUDT21 AND KPBN1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF LYS-635; LYS-644; LYS-730 AND LYS-734.
RX PubMed=17172643; DOI=10.1074/jbc.m609745200;
RA Shimazu T., Horinouchi S., Yoshida M.;
RT "Multiple histone deacetylases and the CREB-binding protein regulate pre-
RT mRNA 3'-end processing.";
RL J. Biol. Chem. 282:4470-4478(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-513 IN COMPLEX WITH ATP ANALOG
RP AND MANGANESE IONS.
RX PubMed=10944102; DOI=10.1093/emboj/19.16.4193;
RA Martin G., Keller W., Doublie S.;
RT "Crystal structure of mammalian poly(A) polymerase in complex with an
RT analog of ATP.";
RL EMBO J. 19:4193-4203(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-513 IN COMPLEX WITH MAGNESIUM
RP IONS; MANGANESE IONS AND ATP ANALOG, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF PHE-100; PHE-153; VAL-156;
RP ASP-167; ARG-199; ASN-202; GLY-203; LYS-228; LYS-232; TYR-237 AND VAL-247.
RX PubMed=15328606; DOI=10.1016/j.jmb.2004.06.047;
RA Martin G., Moglich A., Keller W., Doublie S.;
RT "Biochemical and structural insights into substrate binding and catalytic
RT mechanism of mammalian poly(A) polymerase.";
RL J. Mol. Biol. 341:911-925(2004).
CC -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also
CC required for the endoribonucleolytic cleavage reaction at some
CC polyadenylation sites. May acquire specificity through interaction with
CC a cleavage and polyadenylation specificity factor (CPSF) at its C-
CC terminus. {ECO:0000250|UniProtKB:P51003, ECO:0000269|PubMed:9463383}.
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:15328606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15328606};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15328606};
CC Note=Binds 2 magnesium ions. Also active with manganese.
CC {ECO:0000269|PubMed:15328606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.229 mM for ATP {ECO:0000269|PubMed:15328606};
CC -!- SUBUNIT: Monomer (PubMed:10944102, PubMed:15328606). Found in a complex
CC with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the
CC interaction with AHCYL1 seems to increase interaction with FIP1L1 (By
CC similarity). Interacts with NUDT21; the interaction is diminished by
CC acetylation (PubMed:17172643). Interacts with KPNB1; the interaction
CC promotes PAP nuclear import and is inhibited by acetylation of PAP
CC (PubMed:17172643). {ECO:0000250|UniProtKB:P51003,
CC ECO:0000250|UniProtKB:Q61183, ECO:0000269|PubMed:10944102,
CC ECO:0000269|PubMed:15328606, ECO:0000269|PubMed:17172643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17172643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=P25500-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P25500-2; Sequence=VSP_004524, VSP_004525, VSP_004526;
CC -!- PTM: Polysumoylated. Varying sumolyation depending on tissue- and cell-
CC type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is
CC required for nuclear localization and enhances PAP stability.
CC Desumoylated by SENP1. Inhibits polymerase activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Hyperphosphorylation on multiple CDK2 consensus and non-consensus
CC sites in the C-terminal Ser/Thr-rich region represses PAP activity in
CC late M-phase. Phosphorylation/dephosphorylation may regulate the
CC interaction between PAP and CPSF (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated in the C-terminus. Acetylation decreases interaction
CC with NUDT21 and KPNB1, and inhibits nuclear localization through
CC inhibiting binding to the importin alpha/beta complex.
CC {ECO:0000269|PubMed:17172643}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; X61585; CAA43782.1; -; mRNA.
DR EMBL; X63436; CAA45031.1; -; mRNA.
DR PIR; S17875; S17875.
DR PIR; S17925; S17925.
DR PIR; S18642; S18642.
DR RefSeq; NP_788820.1; NM_176647.2. [P25500-1]
DR PDB; 1F5A; X-ray; 2.50 A; A=1-513.
DR PDB; 1Q78; X-ray; 2.80 A; A=1-514.
DR PDB; 1Q79; X-ray; 2.15 A; A=1-514.
DR PDBsum; 1F5A; -.
DR PDBsum; 1Q78; -.
DR PDBsum; 1Q79; -.
DR AlphaFoldDB; P25500; -.
DR SMR; P25500; -.
DR STRING; 9913.ENSBTAP00000005300; -.
DR iPTMnet; P25500; -.
DR PaxDb; P25500; -.
DR PRIDE; P25500; -.
DR Ensembl; ENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054. [P25500-1]
DR GeneID; 338051; -.
DR KEGG; bta:338051; -.
DR CTD; 10914; -.
DR VEuPathDB; HostDB:ENSBTAG00000004054; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000154598; -.
DR InParanoid; P25500; -.
DR OrthoDB; 326577at2759; -.
DR TreeFam; TF300842; -.
DR BRENDA; 2.7.7.19; 908.
DR SABIO-RK; P25500; -.
DR EvolutionaryTrace; P25500; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000004054; Expressed in thymus and 107 other tissues.
DR ExpressionAtlas; P25500; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese 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; ISS:UniProtKB.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; ISS:UniProtKB.
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; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Isopeptide bond; Magnesium; Manganese;
KW Metal-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transferase;
KW Ubl conjugation.
FT CHAIN 1..739
FT /note="Poly(A) polymerase alpha"
FT /id="PRO_0000051611"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..643
FT /note="Ser/Thr-rich"
FT REGION 580..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..739
FT /note="Required for interaction with NUDT21"
FT /evidence="ECO:0000269|PubMed:17172643"
FT MOTIF 490..507
FT /note="Nuclear localization signal 1"
FT MOTIF 644..659
FT /note="Nuclear localization signal 2"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 113..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 246..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT SITE 153
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 158
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 328
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 399
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 524
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51003"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51003"
FT MOD_RES 537
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:Q61183"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51003"
FT MOD_RES 635
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17172643"
FT MOD_RES 644
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17172643"
FT MOD_RES 730
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17172643"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51003"
FT MOD_RES 734
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17172643"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT CROSSLNK 506
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT CROSSLNK 507
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000305"
FT CROSSLNK 730
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 663..683
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1756732"
FT /id="VSP_004524"
FT VAR_SEQ 709..710
FT /note="KT -> II (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1756732"
FT /id="VSP_004525"
FT VAR_SEQ 711..739
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1756732"
FT /id="VSP_004526"
FT MUTAGEN 100
FT /note="F->D: Strongly decreased enzyme activity. Strongly
FT reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 113..115
FT /note="DID->AIA: Abolishes most of the specific and non-
FT specific polyadenylation activity."
FT MUTAGEN 113
FT /note="D->H: Abolishes most of the specific and non-
FT specific polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 115
FT /note="D->H: Abolishes most of the specific and non-
FT specific polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 153
FT /note="F->A: Strongly reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 156
FT /note="V->A: Strongly decreased enzyme activity. Strongly
FT reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 162..163
FT /note="DG->HA: Small decrease in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 167
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:15328606,
FT ECO:0000269|PubMed:8665867"
FT MUTAGEN 167
FT /note="D->H: Abolishes most of the specific and non-
FT specific polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:15328606,
FT ECO:0000269|PubMed:8665867"
FT MUTAGEN 167
FT /note="D->N: Strongly decreased enzyme activity. Strongly
FT reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606,
FT ECO:0000269|PubMed:8665867"
FT MUTAGEN 186
FT /note="D->H: Small decrease in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 194
FT /note="D->H: No change in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 199
FT /note="R->A: Strongly reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 202
FT /note="N->A: Strongly decreased enzyme activity. Strongly
FT reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 203
FT /note="G->H: Loss of enzyme activity. Strongly reduced
FT affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 208..209
FT /note="DE->AA: Reduces by 60% non-specific and specific
FT polyadenylation activity."
FT MUTAGEN 208
FT /note="D->A: Reduces by 60% non-specific rf and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 208
FT /note="D->H: Reduces by 20% non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 209
FT /note="E->A: No change in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 228
FT /note="K->A: Strongly decreased affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 232
FT /note="K->A: Decreased affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 237
FT /note="Y->A: Strongly decreased affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 247
FT /note="V->A,R: Strongly reduced affinity for RNA."
FT /evidence="ECO:0000269|PubMed:15328606"
FT MUTAGEN 291..292
FT /note="EE->AA: Abolishes most of non-specific
FT polyadenylation activity."
FT MUTAGEN 291
FT /note="E->A: Reduces by 60% non-specific polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 292
FT /note="E->A: No change in non-specific polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 308
FT /note="D->A: No change in non-specific and specific
FT polyadenylation activity."
FT MUTAGEN 317
FT /note="T->G: Strongly decreased affinity for ATP."
FT MUTAGEN 431..432
FT /note="EE->AA: No change in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 455
FT /note="D->A: Reduces by 30% non-specific polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 459
FT /note="D->A: No change in non-specific polyadenylation
FT activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 465
FT /note="D->A: No change in non-specific and specific
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:8665867"
FT MUTAGEN 635
FT /note="K->Q: Weak binding to KPBN1. Cytoplasmic location;
FT when associated with Q-644; Q-730 and Q-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 635
FT /note="K->R: Some decrease in acetylation. Binds KPBN1 and
FT localizes to the nucleus; when associated with R-644; R-730
FT and R-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 644
FT /note="K->Q: Weak binding to KPBN1. Cytoplasmic location;
FT when associated with Q-635; Q-730 and Q-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 644
FT /note="K->R: Large decrease in acetylation. Binds KPBN1 and
FT localizes to the nucleus; when associated with R-635; R-730
FT and R-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 730
FT /note="K->Q: Weak binding to KPBN1. Cytoplasmic location;
FT when associated with Q-635; Q-644 and Q-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 730
FT /note="K->R: Some decrease in acetylation. Binds KPBN1 and
FT localizes to the nucleus; when associated with R-635; R-644
FT and R-734."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 734
FT /note="K->Q: Weak binding to KPBN1. Cytoplasmic location;
FT when associated with Q-635; Q-644 and Q-730."
FT /evidence="ECO:0000269|PubMed:17172643"
FT MUTAGEN 734
FT /note="K->R: Some decrease in acetylation. Binds KPBN1 and
FT localizes to the nucleus; when associated with R-635; R-644
FT and R-730."
FT /evidence="ECO:0000269|PubMed:17172643"
FT CONFLICT 80
FT /note="S -> R (in Ref. 3; CAA45031)"
FT /evidence="ECO:0000305"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 55..82
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 195..211
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 217..233
FT /evidence="ECO:0007829|PDB:1Q79"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 246..259
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1Q79"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 306..310
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:1Q79"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 331..352
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 372..383
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1Q78"
FT STRAND 433..443
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 457..473
FT /evidence="ECO:0007829|PDB:1Q79"
FT STRAND 482..489
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:1Q79"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:1Q79"
SQ SEQUENCE 739 AA; 82441 MW; 7C89C15E33232CFF CRC64;
MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG VFEEEEELQR
RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA
PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE
DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI
LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK
LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS
FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD
MKIAAMHVKR KQLHQLLPSH VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS
AMKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT
QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH KEESPKKTKT
EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT ATSLLASQKT SSTDLSDIPA
LPANPIPVIK NSIKLRLNR
