Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  PEST proteolytic signal-containing nuclear protein  

UniProtKB / Swiss-Prot ID :  PCNP_HUMAN

Gene Name (Synonyms) : 
PCNP  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  May be involved in cell cycle regulation. 

Protein Sequence MADGKAGDEKPEKSQRAGAAGGPEEEAEKPVKTKTVSSSNGGESSSRSAEKRSAEEEAADLPTKPTKISK...
Predicted Secondary Structure CCCCCCCCCCCHHHHHCCCCCCCHHHHHCCCCCEEECCCCCCCCCHHHHHHHHHHHHHHCCCCCCCHHHH...
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
64N6-acetyllysineDLPTKPTKI
CCCCCCCHH
49.07HPRD
Link-
64N6-acetyllysineDLPTKPTKI
CCCCCCCHH
49.07Phosphositeplus
Link-
64N6-acetyllysine.DLPTKPTKI
CCCCCCCHH
49.07UniProtKB
Link-
66PhosphothreoninePTKPTKISK
CCCCCHHHH
42.43HPRD
Link-
66PhosphothreoninePTKPTKISK
CCCCCHHHH
42.43PhosphoELM
Link-
66PhosphothreoninePTKPTKISK
CCCCCHHHH
42.43Phosphositeplus
Link-
66Phosphothreonine.PTKPTKISK
CCCCCHHHH
42.43UniProtKB
Link-
69PhosphoserinePTKISKFGF
CCHHHHHHH
24.40HPRD
Link-
69PhosphoserinePTKISKFGF
CCHHHHHHH
24.40PhosphoELM
Link-
69PhosphoserinePTKISKFGF
CCHHHHHHH
24.40Phosphositeplus
Link-
69Phosphoserine.PTKISKFGF
CCHHHHHHH
24.40UniProtKB
Link-
77PhosphoserineFAIGSQTTK
HHHCCCCCC
20.45HPRD
Link-
77PhosphoserineFAIGSQTTK
HHHCCCCCC
20.45PhosphoELM
Link-
77PhosphoserineFAIGSQTTK
HHHCCCCCC
20.45Phosphositeplus
Link-
77Phosphoserine.FAIGSQTTK
HHHCCCCCC
20.45UniProtKB
Link-
87PhosphoserineASAISIKLG
CCEEEEEEC
17.25HPRD
Link-
87PhosphoserineASAISIKLG
CCEEEEEEC
17.25PhosphoELM
Link-
87PhosphoserineASAISIKLG
CCEEEEEEC
17.25Phosphositeplus
Link-
87PhosphoserineASAISIKLG
CCEEEEEEC
17.25SysPTM
Link-
87Phosphoserine.ASAISIKLG
CCEEEEEEC
17.25UniProtKB
Link-
101PhosphothreonineETVPTLAPK
CCCCCCCCC
31.08HPRD
Link-
101PhosphothreonineETVPTLAPK
CCCCCCCCC
31.08Phosphositeplus
Link-
106PhosphothreonineLAPKTLSVA
CCCCCEEEE
24.17Phosphositeplus
Link-
108PhosphoserinePKTLSVAAA
CCCEEEEEC
18.23Phosphositeplus
Link-
119PhosphoserineEDEDSEPEE
CCCCCCHHH
53.67HPRD
Link-
119PhosphoserineEDEDSEPEE
CCCCCCHHH
53.67PhosphoELM
Link-
119PhosphoserineEDEDSEPEE
CCCCCCHHH
53.67Phosphositeplus
Link-
119PhosphoserineEDEDSEPEE
CCCCCCHHH
53.67SysPTM
Link-
119Phosphoserine.EDEDSEPEE
CCCCCCHHH
53.67UniProtKB
Link-
139PhosphothreonineIGRDTPTSA
CCCCCCCCC
27.40HPRD
Link-
139PhosphothreonineIGRDTPTSA
CCCCCCCCC
27.40PhosphoELM
Link-
139PhosphothreonineIGRDTPTSA
CCCCCCCCC
27.40Phosphositeplus
Link-
139PhosphothreonineIGRDTPTSA
CCCCCCCCC
27.40SysPTM
Link-
139Phosphothreonine.IGRDTPTSA
CCCCCCCCC
27.40UniProtKB
Link-
141PhosphothreonineRDTPTSAGP
CCCCCCCCC
33.05Phosphositeplus
Link-
142PhosphoserineDTPTSAGPN
CCCCCCCCC
32.22HPRD
Link-
142PhosphoserineDTPTSAGPN
CCCCCCCCC
32.22PhosphoELM
Link-
142PhosphoserineDTPTSAGPN
CCCCCCCCC
32.22Phosphositeplus
Link-
142Phosphoserine.DTPTSAGPN
CCCCCCCCC
32.22UniProtKB
Link-
147PhosphoserineAGPNSFNKG
CCCCCCCCC
33.07HPRD
Link-
147PhosphoserineAGPNSFNKG
CCCCCCCCC
33.07PhosphoELM
Link-
147PhosphoserineAGPNSFNKG
CCCCCCCCC
33.07Phosphositeplus
Link-
147Phosphoserine.AGPNSFNKG
CCCCCCCCC
33.07UniProtKB
Link-
150N6-acetyllysineNSFNKGKHG
CCCCCCCCC
68.29HPRD
Link-
150N6-acetyllysineNSFNKGKHG
CCCCCCCCC
68.29Phosphositeplus
Link-
150N6-acetyllysine.NSFNKGKHG
CCCCCCCCC
68.29UniProtKB
Link-
152N6-acetyllysineFNKGKHGFS
CCCCCCCCC
42.01HPRD
Link-
152N6-acetyllysineFNKGKHGFS
CCCCCCCCC
42.01Phosphositeplus
Link-
152N6-acetyllysine.FNKGKHGFS
CCCCCCCCC
42.01UniProtKB
Link-
156PhosphoserineKHGFSDNQK
CCCCCCCHH
40.00Phosphositeplus
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
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-150 AND LYS-152, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-119 AND SER-147, ANDMASS SPECTROMETRY.
"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 THR-139, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66; SER-69; SER-77;THR-139; SER-142 AND SER-147, AND MASS 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-87; SER-119 AND THR-139,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-119, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures