Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein phosphatase 1 regulatory subunit 7  

UniProtKB / Swiss-Prot ID :  PP1R7_HUMAN

Gene Name (Synonyms) : 
PPP1R7, SDS22  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  Regulatory subunit of protein phosphatase 1 (By similarity). 

Protein Sequence MAAERGAGQQQSQEMMEVDRRVESEESGDEEGKKHSSGIVADLSEQSLKDGEERGEEDPEEEHELPVDME...
Predicted Secondary Structure CCCCCCCCCCCHHHHHEEEEEEEECCCCCHHHHHCCCCCCCCCCEEECCCCCCCCCCCCHHHHHCCCCHH...
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
2N-acetylalanine.---MAAERG
---CCCCCC
20.31UniProtKB
Link-
12PhosphoserineGQQQSQEMM
CCCCHHHHH
24.62HPRD
Link-
12PhosphoserineGQQQSQEMM
CCCCHHHHH
24.62Phosphositeplus
Link-
24PhosphoserineRRVESEESG
EEEEECCCC
43.75HPRD
Link-
24PhosphoserineRRVESEESG
EEEEECCCC
43.75PhosphoELM
Link-
24PhosphoserineRRVESEESG
EEEEECCCC
43.75Phosphositeplus
Link-
24PhosphoserineRRVESEESG
EEEEECCCC
43.75SysPTM
Link-
24Phosphoserine.RRVESEESG
EEEEECCCC
43.75UniProtKB
Link-
27PhosphoserineESEESGDEE
EECCCCCHH
47.71HPRD
Link-
27PhosphoserineESEESGDEE
EECCCCCHH
47.71PhosphoELM
Link-
27PhosphoserineESEESGDEE
EECCCCCHH
47.71Phosphositeplus
Link-
27PhosphoserineESEESGDEE
EECCCCCHH
47.71SysPTM
Link-
27Phosphoserine.ESEESGDEE
EECCCCCHH
47.71UniProtKB
Link-
36PhosphoserineGKKHSSGIV
HHHCCCCCC
38.86Phosphositeplus
Link-
37PhosphoserineKKHSSGIVA
HHCCCCCCC
32.05HPRD
Link-
44PhosphoserineVADLSEQSL
CCCCCEEEC
33.85HPRD
Link-
44PhosphoserineVADLSEQSL
CCCCCEEEC
33.85Phosphositeplus
Link-
47PhosphoserineLSEQSLKDG
CCEEECCCC
33.08HPRD
Link-
47PhosphoserineLSEQSLKDG
CCEEECCCC
33.08Phosphositeplus
Link-
90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YRIGKIEGF
CCCCCCCHH
34.90Phosphositeplus
Link-
101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKKVKTLCL
CCCCCEEEE
44.66Phosphositeplus
Link-
133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DNQIKKIEN
CCCCCCCHH
37.62Phosphositeplus
Link-
162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EGVDKLTRL
CCCCCCCCC
49.72Phosphositeplus
Link-
168Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TRLKKLFLV
CCCCEEEEC
49.41Phosphositeplus
Link-
175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVNNKISKI
ECCCCCCCC
43.06Phosphositeplus
Link-
178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NKISKIENL
CCCCCCHHC
58.47Phosphositeplus
Link-
217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LFLGKNKIT
EECCCCCCC
58.16Phosphositeplus
Link-
222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NKITKLQNL
CCCCCCCHH
52.10Phosphositeplus
Link-
244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NRLTKIEGL
CCCCCCCCC
43.27Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PP1A_HUMANphysical interactionDIP:1069EDIP9037183
STAU1_HUMANphysical interactionEBI-443520
intact15303970
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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
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS SPECTROMETRY.
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures