Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Inactive phospholipase C-like protein 2  

UniProtKB / Swiss-Prot ID :  PLCL2_HUMAN

Gene Name (Synonyms) : 
PLCL2, KIAA1092, PLCE2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Note=Predominantly localized to perinuclear areas in both myoblast and myotube C2C12 cells (By similarity). 

Protein Function :  May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum (By similarity). 

Protein Sequence MAECGRGGAAGGALPTSPGPALGAKGALKAGVGEGGGGGGRLGHGRARYDSGGVSNGDCSLGVSGDEARA...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEECCCCCCCCC...
Protein Variant
LocationDescription
211Q -> R (in dbSNP:rs17853614). VAR_032507
635V -> M (in dbSNP:rs17857109). VAR_032508
742A -> V (in dbSNP:rs17857110). VAR_032509
809P -> H (in dbSNP:rs17853612). VAR_032510
890H -> R (in dbSNP:rs17853613). VAR_032511
- top -

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
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAECGR
---CCCCCC
31.90UniProtKB
Link-
16Phosphothreonine.GALPTSPGP
CCCCCCCCC
48.69UniProtKB
Link-
17PhosphoserineALPTSPGPA
CCCCCCCCC
26.39Phosphositeplus
Link-
17Phosphoserine.ALPTSPGPA
CCCCCCCCC
26.39UniProtKB
Link-
55PhosphoserineSGGVSNGDC
CCCCCCCCE
38.07HPRD
Link-
112PhosphothreonineIKDGTKQKR
HHCHHHHHH
40.20Phosphositeplus
Link-
121PhosphothreonineERKKTVSFS
HHHHHEEEC
25.15Phosphositeplus
Link-
123PhosphoserineKKTVSFSSM
HHHEEECCC
25.33Phosphositeplus
Link-
131N6-acetyllysineMPTEKKISS
CCCCCCCCC
58.86Phosphositeplus
Link-
132N6-acetyllysinePTEKKISSA
CCCCCCCCH
41.40Phosphositeplus
Link-
150N6-acetyllysineGSELKKVRS
CCEEEEEEC
45.21Phosphositeplus
Link-
159PhosphotyrosineNSRIYHRYF
CCEEEEEEE
4.52Phosphositeplus
Link-
162PhosphotyrosineIYHRYFLLD
EEEEEEEEE
5.81Phosphositeplus
Link-
584PhosphothreonineEGDVTDEDE
CCCCCCCCC
38.11PhosphoELM
Link-
584PhosphothreonineEGDVTDEDE
CCCCCCCCC
38.11Phosphositeplus
Link-
584PhosphothreonineEGDVTDEDE
CCCCCCCCC
38.11SysPTM
Link-
584Phosphothreonine.EGDVTDEDE
CCCCCCCCC
38.11UniProtKB
Link-
1113PhosphoserineKPRRSLEVI
HHHHHHHHC
30.11PhosphoELM
Link-
1113PhosphoserineKPRRSLEVI
HHHHHHHHC
30.11Phosphositeplus
Link-
1113PhosphoserineKPRRSLEVI
HHHHHHHHC
30.11SysPTM
Link-
1113Phosphoserine.KPRRSLEVI
HHHHHHHHC
30.11UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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 THR-16; SER-17 AND THR-584, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-584 AND SER-1113, ANDMASS 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-16; SER-17 AND THR-584, AND MASS 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-17; THR-584 ANDSER-1113, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures