Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GPN-loop GTPase 1  

UniProtKB / Swiss-Prot ID :  GPN1_HUMAN

Gene Name (Synonyms) : 
GPN1, MBDIN, XAB1 HUSSY-23  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. May be involved in nuclear localization of XPA. 

Protein Sequence MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQRLTGHLHAQGTPPYVINLDPAVHEVPFPANIDI...
Predicted Secondary Structure  -
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
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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
2N-acetylalanine.---MAASAA
---
15.32UniProtKB
Link-
4Phosphoserine-MAASAAAA
-
14.65Phosphositeplus
Link-
4Phosphoserine-MAASAAAA
-
14.65SysPTM
Link-
13PhosphoserineELQASGGPR
31.18Phosphositeplus
Link-
278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERLKKSLAN
56.12Phosphositeplus
Link-
297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERLRKDMGS
57.57Phosphositeplus
Link-
308PhosphothreonineLDAGTAKDS
32.05PhosphoELM
Link-
308PhosphothreonineLDAGTAKDS
32.05Phosphositeplus
Link-
312PhosphoserineTAKDSLSPV
30.00PhosphoELM
Link-
312PhosphoserineTAKDSLSPV
30.00Phosphositeplus
Link-
312PhosphoserineTAKDSLSPV
30.00SysPTM
Link-
312Phosphoserine.TAKDSLSPV
30.00UniProtKB
Link-
314PhosphoserineKDSLSPVLH
19.53PhosphoELM
Link-
314PhosphoserineKDSLSPVLH
19.53Phosphositeplus
Link-
314PhosphoserineKDSLSPVLH
19.53SysPTM
Link-
314PhosphoserineKDSLSPVLH
19.53SysPTM
Link-
314Phosphoserine.KDSLSPVLH
19.53UniProtKB
Link-
328PhosphothreonineLTRGTLDEE
27.96Phosphositeplus
Link-
338PhosphoserineEEADSDTDD
49.83PhosphoELM
Link-
338PhosphoserineEEADSDTDD
49.83Phosphositeplus
Link-
338PhosphoserineEEADSDTDD
49.83SysPTM
Link-
338Phosphoserine.EEADSDTDD
49.83UniProtKB
Link-
340PhosphothreonineADSDTDDID
39.25Phosphositeplus
Link-
340PhosphothreonineADSDTDDID
39.25SysPTM
Link-
340Phosphothreonine.ADSDTDDID
39.25UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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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
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND THR-340, ANDMASS SPECTROMETRY.
"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-312; SER-314 ANDSER-338, AND MASS SPECTROMETRY.
"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 SER-338, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASSSPECTROMETRY.
"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-338, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, 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-312 AND SER-314, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures