DGLB_HUMAN - dbPTM
DGLB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGLB_HUMAN
UniProt AC Q8NCG7
Protein Name Sn1-specific diacylglycerol lipase beta
Gene Name DAGLB
Organism Homo sapiens (Human).
Sequence Length 672
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in tissues. Required for axonal growth during development and for retrograde synaptic signaling at mature synapses..
Protein Sequence MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA
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
166PhosphorylationGGKMAPYSSAGPSHL
CCCCCCCCCCCCCCC		16.8023312004
167 (in isoform 4)Ubiquitination-31.25-
167PhosphorylationGKMAPYSSAGPSHLD
CCCCCCCCCCCCCCC		31.2523312004
167UbiquitinationGKMAPYSSAGPSHLD
CCCCCCCCCCCCCCC		31.2527667366
171PhosphorylationPYSSAGPSHLDSHDS
CCCCCCCCCCCCCCH		35.4528857561
175PhosphorylationAGPSHLDSHDSSQLL
CCCCCCCCCCHHHHH		35.2423663014
178PhosphorylationSHLDSHDSSQLLNGL
CCCCCCCHHHHHHHH		17.9823663014
179PhosphorylationHLDSHDSSQLLNGLK
CCCCCCHHHHHHHHH		30.7923663014
201S-palmitoylationETRIKLLCCCIGKDD
HHHHHHHHHHCCCCC		2.2929575903
202S-palmitoylationTRIKLLCCCIGKDDH
HHHHHHHHHCCCCCC		1.5929575903
203S-palmitoylationRIKLLCCCIGKDDHT
HHHHHHHHCCCCCCC		4.4829575903
206UbiquitinationLLCCCIGKDDHTRVA
HHHHHCCCCCCCCEE		39.82-
223UbiquitinationSTAELFSTYFSDTDL
CHHHHHHHHCCCCCC		22.6633845483
277 (in isoform 4)Ubiquitination-42.94-
289PhosphorylationMQFAAAAYGWPLYIY
HHHHHHHHCCCEEEE		18.2624043423
294PhosphorylationAAYGWPLYIYRNPLT
HHHCCCEEEECCCCC		7.5724043423
296PhosphorylationYGWPLYIYRNPLTGL
HCCCEEEECCCCCCC		7.2624043423
301PhosphorylationYIYRNPLTGLCRIGG
EEECCCCCCCCCCCC		29.3924043423
304S-palmitoylationRNPLTGLCRIGGDCC
CCCCCCCCCCCCCCC		2.9329575903
310S-palmitoylationLCRIGGDCCRSRTTD
CCCCCCCCCCCCCCC		2.0529575903
311S-palmitoylationCRIGGDCCRSRTTDY
CCCCCCCCCCCCCCC		5.4229575903
318PhosphorylationCRSRTTDYDLVGGDQ
CCCCCCCCCCCCCCE		14.75-
352UbiquitinationIHVSFHDKVYELPFL
EEEEECCCEEECCEE		37.8433845483
378PhosphorylationVAVRGTMSLQDVLTD
EEEECCCCHHHHHHH		23.7919664994
380 (in isoform 4)Ubiquitination-31.31-
380UbiquitinationVRGTMSLQDVLTDLS
EECCCCHHHHHHHCC		31.3123000965
384PhosphorylationMSLQDVLTDLSAESE
CCHHHHHHHCCCCCC		34.4419664994
406UbiquitinationVQDRLAHKGISQAAR
EHHHHHHCCHHHHHH		52.94-
442 (in isoform 2)Ubiquitination-14.6821890473
469PhosphorylationQVRCYAFSPPRGLWS
CCEEEECCCCCCHHH		26.3124719451
499 (in isoform 4)Ubiquitination-28.59-
499UbiquitinationLGKDVIPRLSVTNLE
HCCCCCCCCCCCCHH		28.5921890473
499UbiquitinationLGKDVIPRLSVTNLE
HCCCCCCCCCCCCHH		28.5921890473
509UbiquitinationVTNLEDLKRRILRVV
CCCHHHHHHHHHHHH		52.5323000965
564PhosphorylationQPLLGEQSLLTRWSP
CCCCCCHHHHHCCCC		22.5024719451
570PhosphorylationQSLLTRWSPAYSFSS
HHHHHCCCCCCCCCC		9.0721945579
573PhosphorylationLTRWSPAYSFSSDSP
HHCCCCCCCCCCCCC		17.4021945579
574PhosphorylationTRWSPAYSFSSDSPL
HCCCCCCCCCCCCCC		22.2823401153
576PhosphorylationWSPAYSFSSDSPLDS
CCCCCCCCCCCCCCC		27.5621945579
577PhosphorylationSPAYSFSSDSPLDSS
CCCCCCCCCCCCCCC		39.8521945579
579PhosphorylationAYSFSSDSPLDSSPK
CCCCCCCCCCCCCCC		29.3421945579
583PhosphorylationSSDSPLDSSPKYPPL
CCCCCCCCCCCCCCC		57.1121945579
584PhosphorylationSDSPLDSSPKYPPLY
CCCCCCCCCCCCCCC		25.6921945579
587PhosphorylationPLDSSPKYPPLYPPG
CCCCCCCCCCCCCCC		17.2923090842
591PhosphorylationSPKYPPLYPPGRIIH
CCCCCCCCCCCCEEE		17.1028450419
610S-palmitoylationGASGRFGCCSAAHYS
CCCCCCCCCHHHHHH		1.2029575903
611S-palmitoylationASGRFGCCSAAHYSA
CCCCCCCCHHHHHHC		2.9529575903
628UbiquitinationSHEAEFSKILIGPKM
CCHHCHHHHEECHHH		47.0221890473
628 (in isoform 1)Ubiquitination-47.0221890473
628UbiquitinationSHEAEFSKILIGPKM
CCHHCHHHHEECHHH		47.0222817900
650PhosphorylationILMRALDSVVSDRAA
HHHHHHHHHHCCCHH		25.8520068231
653PhosphorylationRALDSVVSDRAACVS
HHHHHHHCCCHHHHC		21.1520068231
667PhosphorylationSCPAQGVSSVDVA--
CCCCCCCCCCCCC--		31.3121130716
668PhosphorylationCPAQGVSSVDVA---
CCCCCCCCCCCC---		21.6727134283
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 DGLB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGLB_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 DGLB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DGLB_HUMAN !!
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 DGLB_HUMAN

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Related Literatures of Post-Translational Modification
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-570 AND SER-574, 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-579 AND SER-584, ANDMASS SPECTROMETRY.
"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-570, AND MASSSPECTROMETRY.
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-573, AND MASSSPECTROMETRY.

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