PLCL2_HUMAN - dbPTM
PLCL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCL2_HUMAN
UniProt AC Q9UPR0
Protein Name Inactive phospholipase C-like protein 2
Gene Name PLCL2
Organism Homo sapiens (Human).
Sequence Length 1127
Subcellular Localization Cytoplasm. Predominantly localized to perinuclear areas in both myoblast and myotube C2C12 cells..
Protein Description May play an role in the regulation of Ins(1,4,5)P3 around the endoplasmic reticulum..
Protein Sequence MAECGRGGAAGGALPTSPGPALGAKGALKAGVGEGGGGGGRLGHGRARYDSGGVSNGDCSLGVSGDEARASPTRGPRGVALAPTPSAVVCTLPRESKPGGLPRRSSIIKDGTKQKRERKKTVSFSSMPTEKKISSASDCINSMVEGSELKKVRSNSRIYHRYFLLDADMQSLRWEPSKKDSEKAKIDIKSIKEVRTGKNTDIFRSNGISDQISEDCAFSVIYGENYESLDLVANSADVANIWVTGLRYLISYGKHTLDMLESSQDNMRTSWVSQMFSEIDVDNLGHITLCNAVQCIRNLNPGLKTSKIELKFKELHKSKDKAGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNKEFLDTKDLMMFLEAEQGVAHINEEISLEIIHKYEPSKEGQEKGWLSIDGFTNYLMSPDCYIFDPEHKKVCQDMKQPLSHYFINSSHNTYLIEDQFRGPSDITGYIRALKMGCRSVELDVWDGPDNEPVIYTGHTMTSQIVFRSVIDIINKYAFFASEYPLILCLENHCSIKQQKVMVQHMKKLLGDKLYTTSPNVEESYLPSPDVLKGKILIKAKKLSSNCSGVEGDVTDEDEGAEMSQRMGKENMEQPNNVPVKRFQLCKELSELVSICKSVQFKEFQVSFQVQKYWEVCSFNEVLASKYANENPGDFVNYNKRFLARVFPSPMRIDSSNMNPQDFWKCGCQIVAMNFQTPGLMMDLNIGWFRQNGNCGYVLRPAIMREEVSFFSANTKDSVPGVSPQLLHIKIISGQNFPKPKGSGAKGDVVDPYVYVEIHGIPADCAEQRTKTVHQNGDAPIFDESFEFQINLPELAMVRFVVLDDDYIGDEFIGQYTIPFECLQTGYRHVPLQSLTGEVLAHASLFVHVAITNRRGGGKPHKRGLSVRKGKKSREYASLRTLWIKTVDEVFKNAQPPIRDATDLRENMQNAVVSFKELCGLSSVANLMQCMLAVSPRFLGPDNTPLVVLNLSEQYPTMELQGIVPEVLKKIVTTYDMMIQSLKALIENADAVYEKIVHCQKAAMEFHEHLHSIGTKEGLKERKLQKAVESFTWNITILKGQADLLKYAKNETLENLKQIHFAAVSCGLNKPGTENADVQKPRRSLEVIPEKANDETGE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAECGRGGA
------CCCCCCCCC		31.9019413330
6Methylation--MAECGRGGAAGGA
--CCCCCCCCCCCCC		52.62115389411
16PhosphorylationAAGGALPTSPGPALG
CCCCCCCCCCCCCCC		48.6923401153
17PhosphorylationAGGALPTSPGPALGA
CCCCCCCCCCCCCCC		26.3923401153
24AcetylationSPGPALGAKGALKAG
CCCCCCCCCCCCCCC		14.14-
49PhosphorylationLGHGRARYDSGGVSN
CCCCCCEECCCCCCC		17.3027251275
51PhosphorylationHGRARYDSGGVSNGD
CCCCEECCCCCCCCC		28.6328450419
55PhosphorylationRYDSGGVSNGDCSLG
EECCCCCCCCCCCCC		38.0728450419
60PhosphorylationGVSNGDCSLGVSGDE
CCCCCCCCCCCCCCC		32.6628450419
64PhosphorylationGDCSLGVSGDEARAS
CCCCCCCCCCCHHCC		38.4330576142
71PhosphorylationSGDEARASPTRGPRG
CCCCHHCCCCCCCCC		22.6623401153
73PhosphorylationDEARASPTRGPRGVA
CCHHCCCCCCCCCEE		45.8430576142
84PhosphorylationRGVALAPTPSAVVCT
CCEEECCCCCEEEEE		25.0327251275
86PhosphorylationVALAPTPSAVVCTLP
EEECCCCCEEEEECC		35.8527251275
91PhosphorylationTPSAVVCTLPRESKP
CCCEEEEECCCCCCC		28.3426552605
105PhosphorylationPGGLPRRSSIIKDGT
CCCCCCCCHHCCCCC		27.4524719451
106PhosphorylationGGLPRRSSIIKDGTK
CCCCCCCHHCCCCCH		26.9026437602
112PhosphorylationSSIIKDGTKQKRERK
CHHCCCCCHHHHHCC		40.2019664994
113UbiquitinationSIIKDGTKQKRERKK
HHCCCCCHHHHHCCC		60.3924816145
121PhosphorylationQKRERKKTVSFSSMP
HHHHCCCCCCCCCCC		25.1523401153
123PhosphorylationRERKKTVSFSSMPTE
HHCCCCCCCCCCCCH		25.3323401153
125PhosphorylationRKKTVSFSSMPTEKK
CCCCCCCCCCCCHHH		20.4423401153
126PhosphorylationKKTVSFSSMPTEKKI
CCCCCCCCCCCHHHC		27.1123401153
129PhosphorylationVSFSSMPTEKKISSA
CCCCCCCCHHHCCCH		52.3623401153
131AcetylationFSSMPTEKKISSASD
CCCCCCHHHCCCHHH		58.8620167786
132AcetylationSSMPTEKKISSASDC
CCCCCHHHCCCHHHH		41.4020167786
134PhosphorylationMPTEKKISSASDCIN
CCCHHHCCCHHHHHH		28.8224719451
135PhosphorylationPTEKKISSASDCINS
CCHHHCCCHHHHHHH		34.95-
137PhosphorylationEKKISSASDCINSMV
HHHCCCHHHHHHHHH		34.66-
147PhosphorylationINSMVEGSELKKVRS
HHHHHCCHHHHHHHC		26.6724719451
150AcetylationMVEGSELKKVRSNSR
HHCCHHHHHHHCCCC		45.2120167786
156PhosphorylationLKKVRSNSRIYHRYF
HHHHHCCCCEEEEEE		22.6923403867
159PhosphorylationVRSNSRIYHRYFLLD
HHCCCCEEEEEEECC		4.5218083107
162PhosphorylationNSRIYHRYFLLDADM
CCCEEEEEEECCCCH		5.8118083107
181PhosphorylationWEPSKKDSEKAKIDI
CCCCCCCCHHCCCCH		50.2918452278
190PhosphorylationKAKIDIKSIKEVRTG
HCCCCHHHHHHHHCC		38.9525022875
248PhosphorylationIWVTGLRYLISYGKH
HHHHHHHHHHHCCCH		17.27-
273PhosphorylationNMRTSWVSQMFSEID
HHCHHHHHHHHHHCC		15.07-
321AcetylationELHKSKDKAGTEVTK
HHHCCCCCCCCCCCH		53.0711794195
454PhosphorylationEDQFRGPSDITGYIR
EECCCCCCCHHHHHH		44.4629514088
457PhosphorylationFRGPSDITGYIRALK
CCCCCCHHHHHHHHH		28.9929514088
458PhosphorylationRGPSDITGYIRALKM
CCCCCHHHHHHHHHC		19.0632142685
459PhosphorylationGPSDITGYIRALKMG
CCCCHHHHHHHHHCC		4.4129514088
544PhosphorylationKLLGDKLYTTSPNVE
HHHCCCCCCCCCCCC		17.45-
554PhosphorylationSPNVEESYLPSPDVL
CCCCCHHHCCCHHHH		26.38-
573PhosphorylationLIKAKKLSSNCSGVE
EEEEEHHHCCCCCCC		28.5223403867
574PhosphorylationIKAKKLSSNCSGVEG
EEEEHHHCCCCCCCC		52.9023403867
577PhosphorylationKKLSSNCSGVEGDVT
EHHHCCCCCCCCCCC		50.5628102081
584PhosphorylationSGVEGDVTDEDEGAE
CCCCCCCCCHHHHHH		38.1130175587
593PhosphorylationEDEGAEMSQRMGKEN
HHHHHHHHHHHHHHC		13.2123403867
775AcetylationKPKGSGAKGDVVDPY
CCCCCCCCCCCCCCE		60.2026051181
784PhosphorylationDVVDPYVYVEIHGIP
CCCCCEEEEEEECCC		6.1123822953
789PhosphorylationYVYVEIHGIPADCAE
EEEEEEECCCHHHHH		32.98-
895PhosphorylationKPHKRGLSVRKGKKS
CCCCCCCCCCCCCCC		23.7724719451
898UbiquitinationKRGLSVRKGKKSREY
CCCCCCCCCCCCHHH		73.2929967540
910PhosphorylationREYASLRTLWIKTVD
HHHHHHHHEEHHHHH		31.5624719451
915PhosphorylationLRTLWIKTVDEVFKN
HHHEEHHHHHHHHHH		24.8524719451
951PhosphorylationFKELCGLSSVANLMQ
HHHHHCHHHHHHHHH		14.19-
952UbiquitinationKELCGLSSVANLMQC
HHHHCHHHHHHHHHH		30.2329967540
964PhosphorylationMQCMLAVSPRFLGPD
HHHHHHHCHHHHCCC		12.5424719451
987PhosphorylationLSEQYPTMELQGIVP
CCCCCCCCCCCCCCH		4.1232142685
994UbiquitinationMELQGIVPEVLKKIV
CCCCCCCHHHHHHHH		24.8624816145
1002PhosphorylationEVLKKIVTTYDMMIQ
HHHHHHHHHHHHHHH		24.10-
1003PhosphorylationVLKKIVTTYDMMIQS
HHHHHHHHHHHHHHH		13.46-
1004PhosphorylationLKKIVTTYDMMIQSL
HHHHHHHHHHHHHHH		7.77-
1015UbiquitinationIQSLKALIENADAVY
HHHHHHHHHCHHHHH		4.6024816145
1022PhosphorylationIENADAVYEKIVHCQ
HHCHHHHHHHHHHHH		17.1525147952
1024UbiquitinationNADAVYEKIVHCQKA
CHHHHHHHHHHHHHH		32.1329967540
1078UbiquitinationADLLKYAKNETLENL
HHHHHHHCCCHHHHH		52.8329967540
1113PhosphorylationDVQKPRRSLEVIPEK
CCCCCCCCCCCCCCC		30.1123401153
1120UbiquitinationSLEVIPEKANDETGE
CCCCCCCCCCCCCCC		47.3224816145
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PLCL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCL2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PLCL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHOC2_HUMANSHOC2physical
27173435
S35F5_HUMANSLC35F5physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLCL2_HUMAN

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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 THR-16; SER-17 AND THR-584, AND MASS 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-17; THR-584 ANDSER-1113, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-16; SER-17 AND THR-584, 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 THR-584 AND SER-1113, ANDMASS SPECTROMETRY.

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