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P25500

- PAPOA_BOVIN

UniProt

P25500 - PAPOA_BOVIN

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Protein

Poly(A) polymerase alpha

Gene

PAPOLA

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions. Also active with manganese.1 Publication

Kineticsi

  1. KM=0.229 mM for ATP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091ATP
Metal bindingi113 – 1131Magnesium 1; catalytic
Metal bindingi113 – 1131Magnesium 2; catalytic
Metal bindingi115 – 1151Magnesium 1; catalytic
Metal bindingi115 – 1151Magnesium 2; catalytic
Sitei153 – 1531Interaction with RNABy similarity
Sitei158 – 1581Interaction with RNABy similarity
Metal bindingi167 – 1671Magnesium 2; catalytic
Binding sitei167 – 1671ATP
Binding sitei228 – 2281ATP
Binding sitei237 – 2371ATP
Sitei328 – 3281Interaction with RNABy similarity
Sitei399 – 3991Interaction with RNABy similarity
Sitei524 – 5241Interaction with RNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi100 – 1023ATP
Nucleotide bindingi113 – 1153ATP
Nucleotide bindingi246 – 2472ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. manganese ion binding Source: UniProtKB
  4. polynucleotide adenylyltransferase activity Source: UniProtKB
  5. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mRNA polyadenylation Source: RefGenome
  2. mRNA splicing, via spliceosome Source: RefGenome
  3. RNA polyadenylation Source: UniProtKB
  4. termination of RNA polymerase II transcription Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_203211. mRNA 3'-end processing.
REACT_205948. mRNA Splicing - Major Pathway.
REACT_225642. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A) polymerase alpha (EC:2.7.7.19)
Short name:
PAP-alpha
Alternative name(s):
Polynucleotide adenylyltransferase alpha
Gene namesi
Name:PAPOLA
Synonyms:PAP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 21

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. nucleus Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001F → D: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi113 – 1153DID → AIA: Abolishes most of the specific and non-specific polyadenylation activity.
Mutagenesisi113 – 1131D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication
Mutagenesisi115 – 1151D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication
Mutagenesisi153 – 1531F → A: Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi156 – 1561V → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi162 – 1632DG → HA: Small decrease in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi167 – 1671D → A: Loss of enzyme activity. 2 Publications
Mutagenesisi167 – 1671D → H: Abolishes most of the specific and non-specific polyadenylation activity. 2 Publications
Mutagenesisi167 – 1671D → N: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 2 Publications
Mutagenesisi186 – 1861D → H: Small decrease in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi194 – 1941D → H: No change in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi199 – 1991R → A: Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi202 – 2021N → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi203 – 2031G → H: Loss of enzyme activity. Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi208 – 2092DE → AA: Reduces by 60% non-specific and specific polyadenylation activity.
Mutagenesisi208 – 2081D → A: Reduces by 60% non-specific rf and specific polyadenylation activity. 1 Publication
Mutagenesisi208 – 2081D → H: Reduces by 20% non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi209 – 2091E → A: No change in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi228 – 2281K → A: Strongly decreased affinity for ATP. 1 Publication
Mutagenesisi232 – 2321K → A: Decreased affinity for ATP. 1 Publication
Mutagenesisi237 – 2371Y → A: Strongly decreased affinity for ATP. 1 Publication
Mutagenesisi247 – 2471V → A or R: Strongly reduced affinity for RNA. 1 Publication
Mutagenesisi291 – 2922EE → AA: Abolishes most of non-specific polyadenylation activity.
Mutagenesisi291 – 2911E → A: Reduces by 60% non-specific polyadenylation activity. 1 Publication
Mutagenesisi292 – 2921E → A: No change in non-specific polyadenylation activity. 1 Publication
Mutagenesisi308 – 3081D → A: No change in non-specific and specific polyadenylation activity.
Mutagenesisi317 – 3171T → G: Strongly decreased affinity for ATP.
Mutagenesisi431 – 4322EE → AA: No change in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi455 – 4551D → A: Reduces by 30% non-specific polyadenylation activity. 1 Publication
Mutagenesisi459 – 4591D → A: No change in non-specific polyadenylation activity. 1 Publication
Mutagenesisi465 – 4651D → A: No change in non-specific and specific polyadenylation activity. 1 Publication
Mutagenesisi635 – 6351K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-644; Q-730 and Q-734. 1 Publication
Mutagenesisi635 – 6351K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-644; R-730 and R-734. 1 Publication
Mutagenesisi644 – 6441K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-730 and Q-734. 1 Publication
Mutagenesisi644 – 6441K → R: Large decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-730 and R-734. 1 Publication
Mutagenesisi730 – 7301K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-734. 1 Publication
Mutagenesisi730 – 7301K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-734. 1 Publication
Mutagenesisi734 – 7341K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-730. 1 Publication
Mutagenesisi734 – 7341K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-730. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 739739Poly(A) polymerase alphaPRO_0000051611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki445 – 445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki506 – 506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Cross-linki507 – 507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Modified residuei537 – 5371Phosphoserine; by MAPKBy similarity
Modified residuei635 – 6351N6-acetyllysine1 Publication
Modified residuei644 – 6441N6-acetyllysine1 Publication
Modified residuei730 – 7301N6-acetyllysine; alternate1 Publication
Cross-linki730 – 730Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei734 – 7341N6-acetyllysine; alternate1 Publication
Cross-linki734 – 734Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity

Post-translational modificationi

Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity).By similarity
Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity).By similarity
Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP25500.

Expressioni

Gene expression databases

ExpressionAtlasiP25500. baseline.

Interactioni

Subunit structurei

Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1 (By similarity). Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP.By similarity3 Publications

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005300.

Structurei

Secondary structure

1
739
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 233Combined sources
Helixi33 – 4614Combined sources
Helixi47 – 493Combined sources
Helixi55 – 8228Combined sources
Helixi87 – 904Combined sources
Beta strandi96 – 1005Combined sources
Helixi101 – 1055Combined sources
Beta strandi114 – 1207Combined sources
Helixi126 – 1294Combined sources
Helixi132 – 1387Combined sources
Beta strandi143 – 1497Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi164 – 1729Combined sources
Beta strandi176 – 1783Combined sources
Helixi187 – 1904Combined sources
Helixi195 – 21117Combined sources
Beta strandi213 – 2153Combined sources
Helixi217 – 23317Combined sources
Turni239 – 2424Combined sources
Helixi246 – 25914Combined sources
Helixi265 – 27713Combined sources
Turni302 – 3043Combined sources
Helixi306 – 3105Combined sources
Beta strandi318 – 3214Combined sources
Turni325 – 3284Combined sources
Helixi331 – 35222Combined sources
Helixi358 – 3614Combined sources
Helixi367 – 3704Combined sources
Beta strandi372 – 38312Combined sources
Helixi384 – 39512Combined sources
Helixi398 – 4069Combined sources
Beta strandi411 – 4166Combined sources
Beta strandi428 – 4303Combined sources
Beta strandi433 – 44311Combined sources
Helixi457 – 47317Combined sources
Beta strandi482 – 4898Combined sources
Helixi490 – 4934Combined sources
Helixi494 – 4963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5AX-ray2.50A1-513[»]
1Q78X-ray2.80A1-514[»]
1Q79X-ray2.15A1-514[»]
ProteinModelPortaliP25500.
SMRiP25500. Positions 19-498.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25500.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 643136Ser/Thr-richAdd
BLAST
Regioni671 – 73969Required for interaction with NUDT21Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 50718Nuclear localization signal 1Add
BLAST
Motifi644 – 65916Nuclear localization signal 2Add
BLAST

Sequence similaritiesi

Belongs to the poly(A) polymerase family.Curated

Phylogenomic databases

eggNOGiCOG5186.
GeneTreeiENSGT00390000017928.
HOGENOMiHOG000204376.
HOVERGENiHBG053502.
InParanoidiP25500.
KOiK14376.
OMAiSPVTTQG.
TreeFamiTF300842.

Family and domain databases

Gene3Di3.30.70.590. 1 hit.
InterProiIPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR007012. PolA_pol_cen_dom.
IPR007010. PolA_pol_RNA-bd_dom.
IPR014492. PolyA_polymerase.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view]
PIRSFiPIRSF018425. PolyA_polymerase. 1 hit.
SUPFAMiSSF55003. SSF55003. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Long (identifier: P25500-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG
60 70 80 90 100
VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF
110 120 130 140 150
GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE
160 170 180 190 200
EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS
210 220 230 240 250
LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA
260 270 280 290 300
MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
310 320 330 340 350
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE
360 370 380 390 400
ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI
410 420 430 440 450
LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE
460 470 480 490 500
NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPSH
510 520 530 540 550
VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS AMKTSPLNSS
560 570 580 590 600
GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT
610 620 630 640 650
QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH
660 670 680 690 700
KEESPKKTKT EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT
710 720 730
ATSLLASQKT SSTDLSDIPA LPANPIPVIK NSIKLRLNR
Length:739
Mass (Da):82,441
Last modified:January 23, 2007 - v3
Checksum:i7C89C15E33232CFF
GO
Isoform Short (identifier: P25500-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     663-683: Missing.
     709-710: KT → II
     711-739: Missing.

Note: No experimental confirmation available.

Show »
Length:689
Mass (Da):77,066
Checksum:i20BECA9A51B9ED1A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801S → R in CAA45031. (PubMed:1896071)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei663 – 68321Missing in isoform Short. 1 PublicationVSP_004524Add
BLAST
Alternative sequencei709 – 7102KT → II in isoform Short. 1 PublicationVSP_004525
Alternative sequencei711 – 73929Missing in isoform Short. 1 PublicationVSP_004526Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61585 mRNA. Translation: CAA43782.1.
X63436 mRNA. Translation: CAA45031.1.
PIRiS17875.
S17925.
S18642.
RefSeqiNP_788820.1. NM_176647.2. [P25500-1]
UniGeneiBt.109586.

Genome annotation databases

EnsembliENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054. [P25500-1]
GeneIDi338051.
KEGGibta:338051.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61585 mRNA. Translation: CAA43782.1 .
X63436 mRNA. Translation: CAA45031.1 .
PIRi S17875.
S17925.
S18642.
RefSeqi NP_788820.1. NM_176647.2. [P25500-1 ]
UniGenei Bt.109586.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F5A X-ray 2.50 A 1-513 [» ]
1Q78 X-ray 2.80 A 1-514 [» ]
1Q79 X-ray 2.15 A 1-514 [» ]
ProteinModelPortali P25500.
SMRi P25500. Positions 19-498.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000005300.

Proteomic databases

PRIDEi P25500.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000005300 ; ENSBTAP00000005300 ; ENSBTAG00000004054 . [P25500-1 ]
GeneIDi 338051.
KEGGi bta:338051.

Organism-specific databases

CTDi 10914.

Phylogenomic databases

eggNOGi COG5186.
GeneTreei ENSGT00390000017928.
HOGENOMi HOG000204376.
HOVERGENi HBG053502.
InParanoidi P25500.
KOi K14376.
OMAi SPVTTQG.
TreeFami TF300842.

Enzyme and pathway databases

Reactomei REACT_203211. mRNA 3'-end processing.
REACT_205948. mRNA Splicing - Major Pathway.
REACT_225642. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

EvolutionaryTracei P25500.
NextBioi 20812502.

Gene expression databases

ExpressionAtlasi P25500. baseline.

Family and domain databases

Gene3Di 3.30.70.590. 1 hit.
InterProi IPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR007012. PolA_pol_cen_dom.
IPR007010. PolA_pol_RNA-bd_dom.
IPR014492. PolyA_polymerase.
[Graphical view ]
Pfami PF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view ]
PIRSFi PIRSF018425. PolyA_polymerase. 1 hit.
SUPFAMi SSF55003. SSF55003. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase."
    Wahle E., Martin G., Schiltz E., Keller W.
    EMBO J. 10:4251-4257(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 1-21; 207-255 AND 386-397.
    Tissue: Thymus.
  2. Wahle E.
    Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Primary structure and expression of bovine poly(A) polymerase."
    Raabe T., Bollum F.J., Manley J.L.
    Nature 353:229-234(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 97-103 AND 445-468.
    Tissue: Heart muscle.
  4. "Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases."
    Martin G., Keller W.
    EMBO J. 15:2593-2603(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAINS, MUTAGENESIS OF ASP-113; ASP-115; 162-ASP-GLY-163; ASP-167; ASP-186; ASP-194; ASP-208; GLU-209; GLU-291; GLU-292; 431-GLU-GLU-432; ASP-455; ASP-459 AND ASP-465.
  5. "Inhibition of poly(A) polymerase requires p34cdc2/cyclin B phosphorylation of multiple consensus and non-consensus sites."
    Colgan D.F., Murthy K.G., Zhao W., Prives C., Manley J.L.
    EMBO J. 17:1053-1062(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, FUNCTION.
  6. "Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing."
    Shimazu T., Horinouchi S., Yoshida M.
    J. Biol. Chem. 282:4470-4478(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-635; LYS-644; LYS-730 AND LYS-734, INTERACTION WITH NUDT21 AND KPBN1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-635; LYS-644; LYS-730 AND LYS-734.
  7. "Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP."
    Martin G., Keller W., Doublie S.
    EMBO J. 19:4193-4203(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-513 IN COMPLEX WITH ATP ANALOG AND MANGANESE IONS.
  8. "Biochemical and structural insights into substrate binding and catalytic mechanism of mammalian poly(A) polymerase."
    Martin G., Moglich A., Keller W., Doublie S.
    J. Mol. Biol. 341:911-925(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-513 IN COMPLEX WITH MAGNESIUM IONS; MANGANESE IONS AND ATP ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF PHE-100; PHE-153; VAL-156; ASP-167; ARG-199; ASN-202; GLY-203; LYS-228; LYS-232; TYR-237 AND VAL-247.

Entry informationi

Entry nameiPAPOA_BOVIN
AccessioniPrimary (citable) accession number: P25500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3