Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Poly(A) polymerase gamma  

UniProtKB / Swiss-Prot ID :  PAPOG_HUMAN

Gene Name (Synonyms) : 
PAPOLG, PAP2, PAPG  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA. 

Protein Sequence MKEMSANTVLDSQRQQKHYGITSPISLASPKEIDHIYTQKLIDAMKPFGVFEDEEELNHRLVVLGKLNNL...
Predicted Secondary Structure CCCCCCCCEECCCCCCCEECCCCCEECCCCCHHHHHHHHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
22PhosphothreonineHYGITSPIS
EECCCCCEE
24.88HPRD
Link
22PhosphothreonineHYGITSPIS
EECCCCCEE
24.88Phosphositeplus
Link
23PhosphoserineYGITSPISL
ECCCCCEEC
20.51HPRD
Link
23PhosphoserineYGITSPISL
ECCCCCEEC
20.51PhosphoELM
Link
23PhosphoserineYGITSPISL
ECCCCCEEC
20.51Phosphositeplus
Link
23Phosphoserine.YGITSPISL
ECCCCCEEC
20.51UniProtKB
Link
26PhosphoserineTSPISLASP
CCCEECCCC
22.67Phosphositeplus
Link
29PhosphoserineISLASPKEI
EECCCCCHH
41.62PhosphoELM
Link
29PhosphoserineISLASPKEI
EECCCCCHH
41.62Phosphositeplus
Link
29Phosphoserine.ISLASPKEI
EECCCCCHH
41.62UniProtKB
Link
101PhosphoserineFTFGSYRLG
EEEECCEEC
11.68HPRD
Link
178PhosphoserineIQTISDNLD
CCCCCCCCC
24.67HPRD
Link
178PhosphoserineIQTISDNLD
CCCCCCCCC
24.67Phosphositeplus
Link
525PhosphoserineSKRLSLDSS
CCCCCCCCC
33.88HPRD
Link-
525PhosphoserineSKRLSLDSS
CCCCCCCCC
33.88Phosphositeplus
Link-
528PhosphoserineLSLDSSCLD
CCCCCCCCC
28.39Phosphositeplus
Link-
552PhosphoserineSKSDSPSVG
CCCCCCCCC
26.60HPRD
Link-
552PhosphoserineSKSDSPSVG
CCCCCCCCC
26.60PhosphoELM
Link-
597PhosphothreonineSTVKTVSPP
CCCCCCCCC
23.14HPRD
Link-
597PhosphothreonineSTVKTVSPP
CCCCCCCCC
23.14PhosphoELM
Link-
597PhosphothreonineSTVKTVSPP
CCCCCCCCC
23.14Phosphositeplus
Link-
597Phosphothreonine.STVKTVSPP
CCCCCCCCC
23.14UniProtKB
Link-
599PhosphoserineVKTVSPPTV
CCCCCCCCC
30.32PhosphoELM
Link-
599PhosphoserineVKTVSPPTV
CCCCCCCCC
30.32Phosphositeplus
Link-
599Phosphoserine.VKTVSPPTV
CCCCCCCCC
30.32UniProtKB
Link-
648PhosphoserineKRSHSPSID
CCCCCCCCC
22.91HPRD
Link-
648PhosphoserineKRSHSPSID
CCCCCCCCC
22.91PhosphoELM
Link-
648PhosphoserineKRSHSPSID
CCCCCCCCC
22.91Phosphositeplus
Link-
648PhosphoserineKRSHSPSID
CCCCCCCCC
22.91SysPTM
Link-
648Phosphoserine.KRSHSPSID
CCCCCCCCC
22.91UniProtKB
Link-
654PhosphothreonineSIDGTPKRL
CCCCCCCCC
23.14HPRD
Link-
654PhosphothreonineSIDGTPKRL
CCCCCCCCC
23.14PhosphoELM
Link-
654PhosphothreonineSIDGTPKRL
CCCCCCCCC
23.14Phosphositeplus
Link-
654PhosphothreonineSIDGTPKRL
CCCCCCCCC
23.14SysPTM
Link-
654Phosphothreonine.SIDGTPKRL
CCCCCCCCC
23.14UniProtKB
Link-
684PhosphoserineRKRKSVDAI
CCCCCCCCC
29.30HPRD
Link-
684PhosphoserineRKRKSVDAI
CCCCCCCCC
29.30PhosphoELM
Link-
684PhosphoserineRKRKSVDAI
CCCCCCCCC
29.30Phosphositeplus
Link-
684PhosphoserineRKRKSVDAI
CCCCCCCCC
29.30SysPTM
Link-
684Phosphoserine.RKRKSVDAI
CCCCCCCCC
29.30UniProtKB
Link-
697PhosphothreonineMPIPTIDTS
CCCCCCCCC
32.00HPRD
Link-
708PhosphoserineKRLPSKELP
CCCCCCCCC
43.27HPRD
Link-
708PhosphoserineKRLPSKELP
CCCCCCCCC
43.27Phosphositeplus
Link-
714PhosphoserineELPDSSSPV
CCCCCCCCC
30.67Phosphositeplus
Link-
715PhosphoserineLPDSSSPVP
CCCCCCCCC
46.14Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ZCHC7_HUMANENSP00000238714STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-597 AND SER-599, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-648; THR-654 ANDSER-684, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures