CDS2_HUMAN - dbPTM
CDS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDS2_HUMAN
UniProt AC O95674
Protein Name Phosphatidate cytidylyltransferase 2
Gene Name CDS2
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein
Matrix side .
Protein Description Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin..
Protein Sequence MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLRSHLIDKGMLTSTTEDE
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
2Phosphorylation------MTELRQRVA
------CCHHHHHHH		43.6726074081
19UbiquitinationPVAPPEDKESESEAK
CCCCCCCCCCCCCCC		62.5733845483
21PhosphorylationAPPEDKESESEAKVD
CCCCCCCCCCCCCCC		52.7629255136
23PhosphorylationPEDKESESEAKVDGE
CCCCCCCCCCCCCCC		52.7329255136
31PhosphorylationEAKVDGETASDSESR
CCCCCCCCCCCCCCH		36.6729255136
33PhosphorylationKVDGETASDSESRAE
CCCCCCCCCCCCHHH		49.4429255136
35PhosphorylationDGETASDSESRAESA
CCCCCCCCCCHHHHC		34.6725159151
37PhosphorylationETASDSESRAESAPL
CCCCCCCCHHHHCCC		40.5223927012
41PhosphorylationDSESRAESAPLPVSA
CCCCHHHHCCCCCCC		33.9130278072
47PhosphorylationESAPLPVSADDTPEV
HHCCCCCCCCCCHHH		24.8430266825
51PhosphorylationLPVSADDTPEVLNRA
CCCCCCCCHHHHHHH		23.1530266825
60PhosphorylationEVLNRALSNLSSRWK
HHHHHHHHCHHHHHH		34.4428270605
63PhosphorylationNRALSNLSSRWKNWW
HHHHHCHHHHHHHHH		23.3128270605
175UbiquitinationFISFTLYLIGFCMFV
HHHHHHHHHHHHHHH		3.2922817900
179UbiquitinationTLYLIGFCMFVLSLV
HHHHHHHHHHHHHHH		1.4222817900
180UbiquitinationLYLIGFCMFVLSLVK
HHHHHHHHHHHHHHH		2.1322817900
184PhosphorylationGFCMFVLSLVKKHYR
HHHHHHHHHHHHHHH		26.3024719451
198 (in isoform 2)Ubiquitination-16.3121906983
249PhosphorylationFGFFFGRTPLIKLSP
HHHHHCCCCCEECCC		23.8724719451
250UbiquitinationGFFFGRTPLIKLSPK
HHHHCCCCCEECCCC		30.6322817900
253 (in isoform 1)Ubiquitination-51.0721890473
253UbiquitinationFGRTPLIKLSPKKTW
HCCCCCEECCCCCCC		51.0721906983
257UbiquitinationPLIKLSPKKTWEGFI
CCEECCCCCCCCCCH		60.5022817900
258UbiquitinationLIKLSPKKTWEGFIG
CEECCCCCCCCCCHH		63.3522817900
259PhosphorylationIKLSPKKTWEGFIGG
EECCCCCCCCCCHHH		34.57-
287UbiquitinationVMSGYRCFVCPVEYN
HHHCCEEEEEEEEEE		4.7222817900
289UbiquitinationSGYRCFVCPVEYNND
HCCEEEEEEEEEECC		1.2421890473
328UbiquitinationIQSVIGWKTVRMYPF
HHHHHCCEEEECCCC		31.7422817900
328 (in isoform 1)Ubiquitination-31.7421890473
357UbiquitinationGPFGGFFASGFKRAF
CCCCHHHHHCHHHHE		13.3922817900
365UbiquitinationSGFKRAFKIKDFANT
HCHHHHEEHHHHHHC		48.1122817900
367 (in isoform 1)Ubiquitination-47.5921890473
367UbiquitinationFKRAFKIKDFANTIP
HHHHEEHHHHHHCCC		47.5921890473
391PhosphorylationDCQYLMATFVNVYIA
HHHHHHHHHHHHHHH		17.7222617229
4352-HydroxyisobutyrylationLRSHLIDKGMLTSTT
HHHHHHHCCCCCCCC		38.95-
435 (in isoform 1)Ubiquitination-38.9521890473
435UbiquitinationLRSHLIDKGMLTSTT
HHHHHHHCCCCCCCC		38.9522817900
439PhosphorylationLIDKGMLTSTTEDE-
HHHCCCCCCCCCCC-		18.3521406692
440PhosphorylationIDKGMLTSTTEDE--
HHCCCCCCCCCCC--		29.3921406692
441PhosphorylationDKGMLTSTTEDE---
HCCCCCCCCCCC---		29.0321406692
442PhosphorylationKGMLTSTTEDE----
CCCCCCCCCCC----		41.0021406692
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 CDS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDS2_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 CDS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_HUMANTSG101physical
21988832
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 CDS2_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-37, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, 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-23 AND SER-33, AND MASSSPECTROMETRY.
"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-21; SER-33 AND SER-37,AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASSSPECTROMETRY.
"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-21, AND MASSSPECTROMETRY.

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