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 27-MAR-2024, entry version 185. 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 sumoylation 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}. 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; 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.ENSBTAP00000070125; -. DR iPTMnet; P25500; -. DR PaxDb; 9913-ENSBTAP00000005300; -. DR Ensembl; ENSBTAT00000005300.5; ENSBTAP00000005300.4; ENSBTAG00000004054.6. [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 TreeFam; TF300842; -. DR BRENDA; 2.7.7.19; 908. DR Reactome; R-BTA-72187; mRNA 3'-end processing. DR Reactome; R-BTA-72203; Processing of Capped Intron-Containing Pre-mRNA. DR Reactome; R-BTA-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-BTA-77595; Processing of Intronless Pre-mRNAs. DR SABIO-RK; P25500; -. DR EvolutionaryTrace; P25500; -. DR Proteomes; UP000009136; Chromosome 21. DR Bgee; ENSBTAG00000004054; Expressed in thymus and 107 other cell types or tissues. DR ExpressionAtlas; P25500; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. 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:1990817; F:poly(A) RNA polymerase activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0180010; P:co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway; ISS:UniProtKB. DR GO; GO:0180011; P:cytoplasmic polyadenylation; IEA:Ensembl. DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central. DR CDD; cd05402; NT_PAP_TUTase; 1. DR Gene3D; 1.10.1410.10; -; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR011068; NuclTrfase_I-like_C. DR InterPro; IPR007012; PolA_pol_cen_dom. DR InterPro; IPR048840; PolA_pol_NTPase. DR InterPro; IPR007010; PolA_pol_RNA-bd_dom. DR InterPro; IPR014492; PolyA_polymerase. DR PANTHER; PTHR10682; POLY A POLYMERASE; 1. DR PANTHER; PTHR10682:SF9; POLY(A) POLYMERASE ALPHA; 1. DR Pfam; PF04928; PAP_central; 1. DR Pfam; PF20750; PAP_NTPase; 1. DR Pfam; PF04926; PAP_RNA-bind; 2. DR PIRSF; PIRSF018425; PolyA_polymerase; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 1. DR SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1. DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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 FT non-specific polyadenylation activity." FT MUTAGEN 113 FT /note="D->H: Abolishes most of the specific and FT non-specific polyadenylation activity." FT /evidence="ECO:0000269|PubMed:8665867" FT MUTAGEN 115 FT /note="D->H: Abolishes most of the specific and FT non-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 FT non-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 //