SARDH_MOUSE - dbPTM
SARDH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SARDH_MOUSE
UniProt AC Q99LB7
Protein Name Sarcosine dehydrogenase, mitochondrial
Gene Name Sardh
Organism Mus musculus (Mouse).
Sequence Length 919
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MASLSRVLRVAATCPRGRAAWNLGLQPLATEARPTTEKSVPYQRTLKEEAQGASVVPQGPSQPLPSTANVVVIGGGSLGCQTLYHLAKLGVGGAVLLERERLTSGTTWHTAGLLWQLRPSDVEVELLAHTRQVVSRDLEEETGLHTGWIQNGGLFIASNQQRLNEYKRLMSLGKAYGIESHVLSPAETKSLYPLMNVDDLYGTLYVPQDGTMDPAGTCTTLTRAAVARGAQVIENCAVTGIRVRTDDFGVRRVAAVETEHGSIQTPCVVNCAGVWASKVGRMAGVKVPLVAMHHAYVVTERIEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWDVFTQHIEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGCGQELAHWIVHGRPEKDMYSYDIRRFHHSLTDHTRWIRERSHESYAKNYSVVFPHDEPLAGRNMRRDPLHEELLGQGCVFQERQGWERPGWFNPQETAQVLDYDYYGAYGNQAHKDYTYSRLLGDEYTFDFPPHHHMIQKECLACRGAAAVFNMSYFGKFYLLGVDARKAADWLFSADVNRPPGSTVYTCMLNQRGGTESDLTVSRLAPGTQASPLVPAFEGDCYYLAVGGAVAQHNWSHINTVLQDQEFRCQLMDSSEDLGMLSIQGPASRDILQDVLDADLSNEAFPFSTHQLVRAAGHLVRAIRLSFVGELGWELHVPRASCLPVYRAVMAAGARHGLVNAGYRAIDSLSIEKGYRHWHADLRPDDSPLEAGLAFTCKLKTSVPFLGREALEKQRATGLRRRLICLTVEEEVPMFGLEAIWRNGQVVGHVRRADFGFTVNKTIAYGYIRDPSGGPVSLDFVKNGEYALERMGVTYAAQVHLKSPFDPDNKRVKGIY
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
38AcetylationEARPTTEKSVPYQRT
CCCCCCCCCCCCHHH		55.4523806337
38SuccinylationEARPTTEKSVPYQRT
CCCCCCCCCCCCHHH		55.45-
38MalonylationEARPTTEKSVPYQRT
CCCCCCCCCCCCHHH		55.4526320211
38GlutarylationEARPTTEKSVPYQRT
CCCCCCCCCCCCHHH		55.4524703693
38SuccinylationEARPTTEKSVPYQRT
CCCCCCCCCCCCHHH		55.4523806337
109Tele-8alpha-FAD histidineLTSGTTWHTAGLLWQ
CCCCCCEEEEEEEEE		12.07-
109OtherLTSGTTWHTAGLLWQ
CCCCCCEEEEEEEEE		12.07-
167AcetylationQQRLNEYKRLMSLGK
HHHHHHHHHHHHHHH		32.6423864654
174SuccinylationKRLMSLGKAYGIESH
HHHHHHHHHHCCCCC		43.67-
174SuccinylationKRLMSLGKAYGIESH
HHHHHHHHHHCCCCC		43.6723806337
174AcetylationKRLMSLGKAYGIESH
HHHHHHHHHHCCCCC		43.6723576753
184PhosphorylationGIESHVLSPAETKSL
CCCCCCCCHHHCCCC		22.4529472430
188PhosphorylationHVLSPAETKSLYPLM
CCCCHHHCCCCCCCC		28.2129472430
189SuccinylationVLSPAETKSLYPLMN
CCCHHHCCCCCCCCC		29.9323806337
189AcetylationVLSPAETKSLYPLMN
CCCHHHCCCCCCCCC		29.9323806337
218S-palmitoylationTMDPAGTCTTLTRAA
CCCCCCCCHHHHHHH		2.4028526873
236S-palmitoylationGAQVIENCAVTGIRV
HCHHCCCCEEECEEE		1.7728526873
262PhosphorylationAVETEHGSIQTPCVV
EEEECCCCCCCCEEE		17.2728285833
278AcetylationCAGVWASKVGRMAGV
CCHHHHHHHHHHCCC		40.7523806337
278SuccinylationCAGVWASKVGRMAGV
CCHHHHHHHHHHCCC		40.7523806337
278SuccinylationCAGVWASKVGRMAGV
CCHHHHHHHHHHCCC		40.75-
286AcetylationVGRMAGVKVPLVAMH
HHHHCCCCCCEEEEE		36.9023864654
374AcetylationNRVPVLEKTGIKSTV
HCCCEEEECCCCEEE		48.1423864654
374SuccinylationNRVPVLEKTGIKSTV
HCCCEEEECCCCEEE		48.1423806337
374UbiquitinationNRVPVLEKTGIKSTV
HCCCEEEECCCCEEE		48.14-
378AcetylationVLEKTGIKSTVCGPE
EEEECCCCEEECCCC		41.2323806337
378SuccinylationVLEKTGIKSTVCGPE
EEEECCCCEEECCCC		41.23-
378SuccinylationVLEKTGIKSTVCGPE
EEEECCCCEEECCCC		41.2323806337
382S-palmitoylationTGIKSTVCGPESFTP
CCCCEEECCCCCCCC		8.3528526873
382S-nitrosylationTGIKSTVCGPESFTP
CCCCEEECCCCCCCC		8.3522178444
392UbiquitinationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.42-
392SuccinylationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.4223806337
392SuccinylationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.42-
392AcetylationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.4223806337
449PhosphorylationDIRRFHHSLTDHTRW
CHHHHHHHCCCCHHH		25.1329472430
451PhosphorylationRRFHHSLTDHTRWIR
HHHHHHCCCCHHHHH		28.8423140645
454PhosphorylationHHSLTDHTRWIRERS
HHHCCCCHHHHHHHC		30.4329472430
467AcetylationRSHESYAKNYSVVFP
HCCHHHHCCCEEECC		48.4623954790
467UbiquitinationRSHESYAKNYSVVFP
HCCHHHHCCCEEECC		48.46-
498S-nitrosylationEELLGQGCVFQERQG
HHHHCCCCCEECCCC		1.8122178444
498S-palmitoylationEELLGQGCVFQERQG
HHHHCCCCCEECCCC		1.8128526873
535SuccinylationAYGNQAHKDYTYSRL
CCCCCCCCCCCHHHH		56.28-
535SuccinylationAYGNQAHKDYTYSRL
CCCCCCCCCCCHHHH		56.2823806337
535AcetylationAYGNQAHKDYTYSRL
CCCCCCCCCCCHHHH		56.2823806337
560AcetylationPHHHMIQKECLACRG
CCHHHHHHHHHHHHH		39.2023576753
610S-palmitoylationPGSTVYTCMLNQRGG
CCCEEEEEEECCCCC		1.2728526873
672S-nitrosylationLQDQEFRCQLMDSSE
HHCCCHHHEECCCCC		4.4122178444
745S-palmitoylationLHVPRASCLPVYRAV
EECCHHHHHHHHHHH		4.9328526873
749PhosphorylationRASCLPVYRAVMAAG
HHHHHHHHHHHHHHH		7.3030165576
776UbiquitinationIDSLSIEKGYRHWHA
HHCCEECCCCCEEEC		60.62-
776AcetylationIDSLSIEKGYRHWHA
HHCCEECCCCCEEEC		60.6223576753
778PhosphorylationSLSIEKGYRHWHADL
CCEECCCCCEEECCC		15.46-
803UbiquitinationLAFTCKLKTSVPFLG
EEEEEEECCCCCCCC		25.01-
803SuccinylationLAFTCKLKTSVPFLG
EEEEEEECCCCCCCC		25.01-
803AcetylationLAFTCKLKTSVPFLG
EEEEEEECCCCCCCC		25.0123576753
803MalonylationLAFTCKLKTSVPFLG
EEEEEEECCCCCCCC		25.0126320211
803SuccinylationLAFTCKLKTSVPFLG
EEEEEEECCCCCCCC		25.0123806337
804PhosphorylationAFTCKLKTSVPFLGR
EEEEEECCCCCCCCH		45.4523140645
805PhosphorylationFTCKLKTSVPFLGRE
EEEEECCCCCCCCHH		26.6329472430
816SuccinylationLGREALEKQRATGLR
CCHHHHHHHHHHCCC		46.0323954790
816AcetylationLGREALEKQRATGLR
CCHHHHHHHHHHCCC		46.0323864654
875PhosphorylationYGYIRDPSGGPVSLD
EEEEECCCCCCEEEE		61.7523984901
880PhosphorylationDPSGGPVSLDFVKNG
CCCCCCEEEEEEECC		25.9229472430
885UbiquitinationPVSLDFVKNGEYALE
CEEEEEEECCCHHHH		60.26-
885SuccinylationPVSLDFVKNGEYALE
CEEEEEEECCCHHHH		60.26-
885AcetylationPVSLDFVKNGEYALE
CEEEEEEECCCHHHH		60.2623576753
885GlutarylationPVSLDFVKNGEYALE
CEEEEEEECCCHHHH		60.2624703693
885SuccinylationPVSLDFVKNGEYALE
CEEEEEEECCCHHHH		60.2623806337
905AcetylationYAAQVHLKSPFDPDN
EEEEEEECCCCCCCC		41.0023576753
905SuccinylationYAAQVHLKSPFDPDN
EEEEEEECCCCCCCC		41.00-
905SuccinylationYAAQVHLKSPFDPDN
EEEEEEECCCCCCCC		41.0023806337
913AcetylationSPFDPDNKRVKGIY-
CCCCCCCCCCCCCC-		66.9823806337
913GlutarylationSPFDPDNKRVKGIY-
CCCCCCCCCCCCCC-		66.9824703693
913MalonylationSPFDPDNKRVKGIY-
CCCCCCCCCCCCCC-		66.9826320211
913SuccinylationSPFDPDNKRVKGIY-
CCCCCCCCCCCCCC-		66.9823806337
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 SARDH_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of SARDH_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SARDH_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-885, AND MASS SPECTROMETRY.

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