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P51003

- PAPOA_HUMAN

UniProt

P51003 - PAPOA_HUMAN

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Protein
Poly(A) polymerase alpha
Gene
PAPOLA, PAP
Organism
Homo sapiens (Human)
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.

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions. Also active with manganese By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091ATP By similarity
Metal bindingi113 – 1131Magnesium 1; catalytic By similarity
Metal bindingi113 – 1131Magnesium 2; catalytic By similarity
Metal bindingi115 – 1151Magnesium 1; catalytic By similarity
Metal bindingi115 – 1151Magnesium 2; catalytic By similarity
Sitei153 – 1531Interaction with RNA By similarity
Sitei158 – 1581Interaction with RNA By similarity
Metal bindingi167 – 1671Magnesium 2; catalytic By similarity
Binding sitei167 – 1671ATP By similarity
Binding sitei228 – 2281ATP By similarity
Binding sitei237 – 2371ATP By similarity
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 By similarity
Nucleotide bindingi113 – 1153ATP By similarity
Nucleotide bindingi246 – 2472ATP By similarity

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
Complete GO annotation...

GO - Biological processi

  1. RNA polyadenylation Source: UniProtKB
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA 3'-end processing Source: Reactome
  5. mRNA splicing, via spliceosome Source: Reactome
  6. termination of RNA polymerase II transcription Source: Reactome
  7. transcription from RNA polymerase II promoter Source: Reactome
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_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:14981. PAPOLA.

Subcellular locationi

Cytoplasm. Nucleus
Note: The 90 kDa form is nuclear while the 100 kDa and the 106 kDa forms are both nuclear and cytoplasmic.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Poly(A) polymerase alpha
PRO_0000051612Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine2 Publications
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 similarity
Modified residuei641 – 6411N6-acetyllysine By similarity
Modified residuei650 – 6501N6-acetyllysine By similarity
Modified residuei736 – 7361N6-acetyllysine; alternate By similarity
Cross-linki736 – 736Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Modified residuei740 – 7401N6-acetyllysine; alternate By similarity
Cross-linki740 – 740Glycyl 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 By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP51003.
PaxDbiP51003.
PeptideAtlasiP51003.
PRIDEiP51003.

PTM databases

PhosphoSiteiP51003.

Expressioni

Gene expression databases

ArrayExpressiP51003.
BgeeiP51003.
CleanExiHS_PAPOLA.
GenevestigatoriP51003.

Organism-specific databases

HPAiHPA001788.

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 similarity.2 Publications

Protein-protein interaction databases

BioGridi116119. 27 interactions.
DIPiDIP-27610N.
DIP-40865N.
IntActiP51003. 7 interactions.
MINTiMINT-125699.
STRINGi9606.ENSP00000216277.

Structurei

3D structure databases

ProteinModelPortaliP51003.
SMRiP51003. Positions 19-498.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 643136Ser/Thr-rich
Add
BLAST
Regioni677 – 74569Required for interaction with NUDT21
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi490 – 50718Nuclear localization signal 1 By similarity
Add
BLAST
Motifi650 – 66516Nuclear localization signal 2 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 575Poly-Glu
Compositional biasi504 – 5074Poly-Lys

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5186.
HOVERGENiHBG053502.
InParanoidiP51003.
KOiK14376.
OMAiSPVTTQG.
OrthoDBiEOG7XH6PT.
PhylomeDBiP51003.
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

Isoform 1 (identifier: P51003-1) [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 PKETDCVLTQ KLIETLKPFG    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 KQLHQLLPNH 500
VLQKKKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS ATKTSPLNSS 550
GSSQGRNSPA PAVTAASVTN IQATEVSVPQ VNSSESSGGT SSESIPQTAT 600
QPAISPPPKP TVSRVVSSTR LVNPPPRSSG NAATSGNAAT KIPTPIVGVK 650
RTSSPHKEES PKKTKTEEDE TSEDANCLAL SGHDKTEAKE QLDTETSTTQ 700
SETIQTAASL LASQKTSSTD LSDIPALPAN PIPVIKNSIK LRLNR 745
Length:745
Mass (Da):82,843
Last modified:January 23, 2007 - v4
Checksum:i14A00CCCDAD9B374
GO
Isoform 2 (identifier: P51003-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     280-285: EWPNPV → YVFRLY
     286-745: Missing.

Show »
Length:285
Mass (Da):32,626
Checksum:i5967D93F0375C54C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei280 – 2856EWPNPV → YVFRLY in isoform 2.
VSP_012895
Alternative sequencei286 – 745460Missing in isoform 2.
VSP_012896Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32PF → GTSNSPGHSSFSAPSTKKIK TTRKQNIAWC in CAD62628. 1 Publication
Sequence conflicti204 – 23835CRVTD…HNIYS → MRKPTSFCVLQFLSDISCFY TSFVLKLFIAILLTQ in CAD61935. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC000927 mRNA. Translation: AAH00927.1.
BC036014 mRNA. Translation: AAH36014.1.
BX248301 mRNA. Translation: CAD62628.1.
BX248753 mRNA. Translation: CAD66560.1.
BX161482 mRNA. Translation: CAD61935.1.
X76770 mRNA. No translation available.
CCDSiCCDS58334.1. [P51003-2]
CCDS9946.1. [P51003-1]
RefSeqiNP_001238935.1. NM_001252006.1. [P51003-2]
NP_001238936.1. NM_001252007.1.
NP_116021.2. NM_032632.4. [P51003-1]
UniGeneiHs.253726.

Genome annotation databases

EnsembliENST00000216277; ENSP00000216277; ENSG00000090060. [P51003-1]
ENST00000557320; ENSP00000450437; ENSG00000090060. [P51003-2]
ENST00000557471; ENSP00000450812; ENSG00000090060.
GeneIDi10914.
KEGGihsa:10914.
UCSCiuc001yfo.3. human. [P51003-2]
uc001yfq.3. human. [P51003-1]

Polymorphism databases

DMDMi59803092.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC000927 mRNA. Translation: AAH00927.1 .
BC036014 mRNA. Translation: AAH36014.1 .
BX248301 mRNA. Translation: CAD62628.1 .
BX248753 mRNA. Translation: CAD66560.1 .
BX161482 mRNA. Translation: CAD61935.1 .
X76770 mRNA. No translation available.
CCDSi CCDS58334.1. [P51003-2 ]
CCDS9946.1. [P51003-1 ]
RefSeqi NP_001238935.1. NM_001252006.1. [P51003-2 ]
NP_001238936.1. NM_001252007.1.
NP_116021.2. NM_032632.4. [P51003-1 ]
UniGenei Hs.253726.

3D structure databases

ProteinModelPortali P51003.
SMRi P51003. Positions 19-498.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116119. 27 interactions.
DIPi DIP-27610N.
DIP-40865N.
IntActi P51003. 7 interactions.
MINTi MINT-125699.
STRINGi 9606.ENSP00000216277.

PTM databases

PhosphoSitei P51003.

Polymorphism databases

DMDMi 59803092.

Proteomic databases

MaxQBi P51003.
PaxDbi P51003.
PeptideAtlasi P51003.
PRIDEi P51003.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216277 ; ENSP00000216277 ; ENSG00000090060 . [P51003-1 ]
ENST00000557320 ; ENSP00000450437 ; ENSG00000090060 . [P51003-2 ]
ENST00000557471 ; ENSP00000450812 ; ENSG00000090060 .
GeneIDi 10914.
KEGGi hsa:10914.
UCSCi uc001yfo.3. human. [P51003-2 ]
uc001yfq.3. human. [P51003-1 ]

Organism-specific databases

CTDi 10914.
GeneCardsi GC14P096969.
HGNCi HGNC:14981. PAPOLA.
HPAi HPA001788.
MIMi 605553. gene.
neXtProti NX_P51003.
PharmGKBi PA32932.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5186.
HOVERGENi HBG053502.
InParanoidi P51003.
KOi K14376.
OMAi SPVTTQG.
OrthoDBi EOG7XH6PT.
PhylomeDBi P51003.
TreeFami TF300842.

Enzyme and pathway databases

Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi PAPOLA. human.
GeneWikii PAPOLA.
GenomeRNAii 10914.
NextBioi 41453.
PROi P51003.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51003.
Bgeei P51003.
CleanExi HS_PAPOLA.
Genevestigatori P51003.

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

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Testis.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-725 (ISOFORMS 1 AND 2).
    Tissue: B-cell and Fetal brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-660 (ISOFORM 1).
  4. "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
    Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
    J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUDT21/CPSF5.
  5. "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
    Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
    EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CPSF1 AND FIP1L1, INTERACTION WITH FIP1L1.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPAPOA_HUMAN
AccessioniPrimary (citable) accession number: P51003
Secondary accession number(s): Q86SX4
, Q86TV0, Q8IYF5, Q9BVU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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