DGKA_HUMAN - dbPTM
DGKA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DGKA_HUMAN
UniProt AC P23743
Protein Name Diacylglycerol kinase alpha
Gene Name DGKA
Organism Homo sapiens (Human).
Sequence Length 735
Subcellular Localization
Protein Description Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity..
Protein Sequence MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIYLEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEWVRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYTVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHCVWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNLSTSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRLFKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQNLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVLNIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLEGAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPMLMGPPPRSTNFFGFLS
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
9PhosphorylationAKERGLISPSDFAQL
CCCCCCCCHHHHHHH		24.3228122231
11PhosphorylationERGLISPSDFAQLQK
CCCCCCHHHHHHHHH		38.2724719451
18UbiquitinationSDFAQLQKYMEYSTK
HHHHHHHHHHHHCCC		55.97-
19PhosphorylationDFAQLQKYMEYSTKK
HHHHHHHHHHHCCCC		5.1326356563
22PhosphorylationQLQKYMEYSTKKVSD
HHHHHHHHCCCCHHH		12.7127273156
23PhosphorylationLQKYMEYSTKKVSDV
HHHHHHHCCCCHHHH		22.0526356563
24PhosphorylationQKYMEYSTKKVSDVL
HHHHHHCCCCHHHHH		33.7026356563
25UbiquitinationKYMEYSTKKVSDVLK
HHHHHCCCCHHHHHH		45.28-
26UbiquitinationYMEYSTKKVSDVLKL
HHHHCCCCHHHHHHH		47.24-
32UbiquitinationKKVSDVLKLFEDGEM
CCHHHHHHHHCCCHH		51.48-
39SulfoxidationKLFEDGEMAKYVQGD
HHHCCCHHHHHHCCC		4.8230846556
41 (in isoform 1)Ubiquitination-44.6421906983
41UbiquitinationFEDGEMAKYVQGDAI
HCCCHHHHHHCCCCC		44.6421906983
41 (in isoform 2)Ubiquitination-44.6421906983
50PhosphorylationVQGDAIGYEGFQQFL
HCCCCCCHHHHHHHH		13.5322817900
133PhosphorylationRNGILDSSEVDKIIL
CCCCCCHHHHHHHHH		41.1129759185
211UbiquitinationGQHMWRPKRFPRPVY
CCCCCCCCCCCCCCC		59.08-
218PhosphorylationKRFPRPVYCNLCESS
CCCCCCCCCCCCCCC		4.36-
239UbiquitinationGLSCNLCKYTVHDQC
CCCCCCCCCCCCCHH		47.31-
249UbiquitinationVHDQCAMKALPCEVS
CCCHHHHHCCCCEEH		28.39-
256PhosphorylationKALPCEVSTYAKSRK
HCCCCEEHHHCCCCC		8.0726552605
257PhosphorylationALPCEVSTYAKSRKD
CCCCEEHHHCCCCCC		32.4526552605
258PhosphorylationLPCEVSTYAKSRKDI
CCCEEHHHCCCCCCC		12.4326552605
260UbiquitinationCEVSTYAKSRKDIGV
CEEHHHCCCCCCCCC		40.14-
263UbiquitinationSTYAKSRKDIGVQSH
HHHCCCCCCCCCCCE		61.87-
335PhosphorylationILPPSSIYPSVLASG
CCCHHHHCHHHHHCC		7.4515773894
348PhosphorylationSGPDRKNSKTSQKTM
CCCCCCCCCCCCHHH		40.1029978859
350PhosphorylationPDRKNSKTSQKTMDD
CCCCCCCCCCHHHHH		35.8929978859
351PhosphorylationDRKNSKTSQKTMDDL
CCCCCCCCCHHHHHC		33.1629978859
353UbiquitinationKNSKTSQKTMDDLNL
CCCCCCCHHHHHCCC		45.6521906983
353 (in isoform 1)Ubiquitination-45.6521906983
353AcetylationKNSKTSQKTMDDLNL
CCCCCCCHHHHHCCC		45.6523749302
354PhosphorylationNSKTSQKTMDDLNLS
CCCCCCHHHHHCCCC		20.4229978859
355SulfoxidationSKTSQKTMDDLNLST
CCCCCHHHHHCCCCH		4.9321406390
361PhosphorylationTMDDLNLSTSEALRI
HHHHCCCCHHHCCCC		28.9029978859
362PhosphorylationMDDLNLSTSEALRID
HHHCCCCHHHCCCCC		33.4829978859
363PhosphorylationDDLNLSTSEALRIDP
HHCCCCHHHCCCCCC		19.9329978859
384UbiquitinationLLVFVNPKSGGKQGQ
EEEEECCCCCCCHHH		57.43-
388UbiquitinationVNPKSGGKQGQRVLW
ECCCCCCCHHHEEEE		55.57-
411UbiquitinationRQVFNLLKDGPEIGL
HHHHHHHHCCCCHHE		64.9021906983
411 (in isoform 1)Ubiquitination-64.9021906983
422UbiquitinationEIGLRLFKDVPDSRI
CHHEEEECCCCCCEE		63.51-
484UbiquitinationYEGQNLAKILKDLEM
CCCHHHHHHHHHHHH		52.3019608861
484AcetylationYEGQNLAKILKDLEM
CCCHHHHHHHHHHHH		52.3019608861
487UbiquitinationQNLAKILKDLEMSKV
HHHHHHHHHHHHHCC		64.8321906983
487 (in isoform 1)Ubiquitination-64.8321906983
492PhosphorylationILKDLEMSKVVHMDR
HHHHHHHHCCEEECC		16.96-
493 (in isoform 1)Ubiquitination-47.1421906983
493UbiquitinationLKDLEMSKVVHMDRW
HHHHHHHCCEEECCC		47.1421906983
501PhosphorylationVVHMDRWSVEVIPQQ
CEEECCCEEEECCCC		14.8629978859
509PhosphorylationVEVIPQQTEEKSDPV
EEECCCCCCCCCCCC		40.6429978859
513PhosphorylationPQQTEEKSDPVPFQI
CCCCCCCCCCCCEEE		50.8829978859
524PhosphorylationPFQIINNYFSIGVDA
CEEEECCCCEECCCH		8.3329978859
526PhosphorylationQIINNYFSIGVDASI
EEECCCCEECCCHHH		14.2029978859
532PhosphorylationFSIGVDASIAHRFHI
CEECCCHHHHHHHHH		18.8229978859
543UbiquitinationRFHIMREKYPEKFNS
HHHHHHHHCHHHHHH		56.60-
544PhosphorylationFHIMREKYPEKFNSR
HHHHHHHCHHHHHHH		16.3325839225
547UbiquitinationMREKYPEKFNSRMKN
HHHHCHHHHHHHHCC		45.39-
623PhosphorylationRRPHGDIYGINQALG
CCCCCCCCCHHHHHC		19.3825394399
632PhosphorylationINQALGATAKVITDP
HHHHHCCCEEEECCH		25.8026356563
634 (in isoform 1)Ubiquitination-29.8021906983
634UbiquitinationQALGATAKVITDPDI
HHHCCCEEEECCHHH		29.802190698
637PhosphorylationGATAKVITDPDILKT
CCCEEEECCHHHHHH		44.46-
643UbiquitinationITDPDILKTCVPDLS
ECCHHHHHHHCCCCC		39.97-
652AcetylationCVPDLSDKRLEVVGL
HCCCCCCCCEEEEEE		56.3525953088
652UbiquitinationCVPDLSDKRLEVVGL
HCCCCCCCCEEEEEE		56.35-
669PhosphorylationAIEMGQIYTKLKNAG
HHHHHHHHHHHHHHH		7.0229978859
670PhosphorylationIEMGQIYTKLKNAGR
HHHHHHHHHHHHHHH		31.3729978859
673UbiquitinationGQIYTKLKNAGRRLA
HHHHHHHHHHHHHHH		46.43-
681AcetylationNAGRRLAKCSEITFH
HHHHHHHCCCEEEEE		42.7725953088
681UbiquitinationNAGRRLAKCSEITFH
HHHHHHHCCCEEEEE		42.77-
691UbiquitinationEITFHTTKTLPMQID
EEEEEECCCCCCEEC		49.58-
714UbiquitinationCTIKITHKNQMPMLM
CEEEEEECCCCCEEC		39.98-
727PhosphorylationLMGPPPRSTNFFGFL
ECCCCCCCCCCCCCC		33.2124719451
735PhosphorylationTNFFGFLS-------
CCCCCCCC-------		35.5922617229
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
335YPhosphorylationKinaseLCKP06239
PSP
335YPhosphorylationKinaseSRCP00523
PSP
335YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DGKA_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 DGKA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ORC5_HUMANORC5physical
22939629
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
DB00163Vitamin E
Regulatory Network of DGKA_HUMAN

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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-484, 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 TYR-623, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-22, AND MASSSPECTROMETRY.

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