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P25500

- PAPOA_BOVIN

UniProt

P25500 - PAPOA_BOVIN

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Protein
Poly(A) polymerase alpha
Gene
PAPOLA, PAP
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

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 RNA By similarity
Sitei158 – 1581Interaction with RNA By similarity
Metal bindingi167 – 1671Magnesium 2; catalytic
Binding sitei167 – 1671ATP
Binding sitei228 – 2281ATP
Binding sitei237 – 2371ATP
Sitei328 – 3281Interaction with RNA By similarity
Sitei399 – 3991Interaction with RNA By similarity
Sitei524 – 5241Interaction with RNA By 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. RNA binding Source: UniProtKB-KW
  3. magnesium ion binding Source: UniProtKB
  4. manganese ion binding Source: UniProtKB
  5. polynucleotide adenylyltransferase activity Source: UniProtKB

GO - Biological processi

  1. RNA polyadenylation Source: UniProtKB
  2. mRNA polyadenylation Source: RefGenome
  3. mRNA splicing, via spliceosome Source: RefGenome
  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. 1 Publication
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.
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. 1 Publication
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. 1 Publication
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.
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 alpha
PRO_0000051611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine By similarity
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Cross-linki445 – 445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Cross-linki506 – 506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Cross-linki507 – 507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei537 – 5371Phosphoserine; by MAPK By 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); alternate By similarity
Modified residuei734 – 7341N6-acetyllysine; alternate1 Publication
Cross-linki734 – 734Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By 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.
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.
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.

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.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005300.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP25500.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 643136Ser/Thr-rich
Add
BLAST
Regioni671 – 73969Required for interaction with NUDT21
Add
BLAST

Motif

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

Sequence similaritiesi

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

MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG    50
VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF 100
GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE 150
EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS 200
LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA 250
MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW 300
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE 350
ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI 400
LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE 450
NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPSH 500
VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS AMKTSPLNSS 550
GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT 600
QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH 650
KEESPKKTKT EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT 700
ATSLLASQKT SSTDLSDIPA LPANPIPVIK NSIKLRLNR 739
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei663 – 68321Missing in isoform Short.
VSP_004524Add
BLAST
Alternative sequencei709 – 7102KT → II in isoform Short.
VSP_004525
Alternative sequencei711 – 73929Missing in isoform Short.
VSP_004526Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801S → R in CAA45031. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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.

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: September 3, 2014
This is version 124 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

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