CERS2_HUMAN - dbPTM
CERS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CERS2_HUMAN
UniProt AC Q96G23
Protein Name Ceramide synthase 2
Gene Name CERS2
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization Nucleus membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Suppresses the growth of cancer cells. May be involved in sphingolipid synthesis..
Protein Sequence MLQTLYDYFWWERLWLPVNLTWADLEDRDGRVYAKASDLYITLPLALLFLIVRYFFELYVATPLAALLNIKEKTRLRAPPNATLEHFYLTSGKQPKQVEVELLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTFYLIAFIAGMAVIVDKPWFYDMKKVWEGYPIQSTIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILISFSWFANYIRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNIFIVFAIVFIITRLVILPFWILHCTLVYPLELYPAFFGYYFFNSMMGVLQLLHIFWAYLILRMAHKFITGKLVEDERSDREETESSEGEEAAAGGGAKSRPLANGHPILNNNHRKND
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
19N-linked_GlycosylationERLWLPVNLTWADLE
HHHCCEEEEEECCCC		29.7916263699
21O-linked_GlycosylationLWLPVNLTWADLEDR
HCCEEEEEECCCCCC		17.2530059200
88PhosphorylationNATLEHFYLTSGKQP
CCEEEEEEECCCCCC		15.81-
93MalonylationHFYLTSGKQPKQVEV
EEEECCCCCCCEEEE		64.2926320211
93UbiquitinationHFYLTSGKQPKQVEV
EEEECCCCCCCEEEE		64.2923000965
96UbiquitinationLTSGKQPKQVEVELL
ECCCCCCCEEEEEEH		65.5623000965
104PhosphorylationQVEVELLSRQSGLSG
EEEEEEHHCCCCCCH		40.6824719451
113UbiquitinationQSGLSGRQVERWFRR
CCCCCHHHHHHHHHH		44.9721890473
116UbiquitinationLSGRQVERWFRRRRN
CCHHHHHHHHHHHCC		38.6923000965
128PhosphorylationRRNQDRPSLLKKFRE
HCCCCCCHHHHHHHH		47.4224719451
131UbiquitinationQDRPSLLKKFREASW
CCCCHHHHHHHHHHH		55.9827667366
1312-HydroxyisobutyrylationQDRPSLLKKFREASW
CCCCHHHHHHHHHHH		55.98-
132UbiquitinationDRPSLLKKFREASWR
CCCHHHHHHHHHHHH		50.01-
151UbiquitinationLIAFIAGMAVIVDKP
HHHHHHCCCEECCCC		1.6727667366
199PhosphorylationSLLFSIASDVKRKDF
HHHHHHHHHCCCCCH		41.0720166139
242O-linked_GlycosylationIMALHDSSDYLLESA
HHHHHCCCHHHHHHH		36.0130059200
334AcetylationAHKFITGKLVEDERS
HHHHHHCCHHCCCCC		40.4819823741
334UbiquitinationAHKFITGKLVEDERS
HHHHHHCCHHCCCCC		40.4829967540
341PhosphorylationKLVEDERSDREETES
CHHCCCCCCHHHHCC		38.6829255136
346PhosphorylationERSDREETESSEGEE
CCCCHHHHCCHHHHH		36.0929255136
348PhosphorylationSDREETESSEGEEAA
CCHHHHCCHHHHHHH		40.9029255136
349PhosphorylationDREETESSEGEEAAA
CHHHHCCHHHHHHHC		43.3129255136
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 CERS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CERS2_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 CERS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TECR_HUMANTECRphysical
20937905
DHB12_HUMANHSD17B12physical
20937905
ELOV1_HUMANELOVL1physical
20937905
ELOV2_HUMANELOVL2physical
20937905
ELOV3_HUMANELOVL3physical
20937905
ELOV4_HUMANELOVL4physical
20937905
ELOV5_HUMANELOVL5physical
20937905
ELOV6_HUMANELOVL6physical
20937905
ELOV7_HUMANELOVL7physical
20937905
S19A2_HUMANSLC19A2physical
21988832
PEX6_HUMANPEX6physical
21988832
S39A1_HUMANSLC39A1physical
21988832
S22A1_HUMANSLC22A1physical
21988832
BI1_HUMANTMBIM6physical
21988832
HS90A_HUMANHSP90AA1physical
20195357
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 CERS2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19, AND MASS SPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-341; THR-346; SER-348AND SER-349, 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 SER-341; THR-346; SER-348AND SER-349, AND MASS 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-341; THR-346; SER-348AND SER-349, 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-341; THR-346; SER-348AND SER-349, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, 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-341; THR-346; SER-348AND SER-349, AND MASS SPECTROMETRY.

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