SARDH_HUMAN - dbPTM
SARDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SARDH_HUMAN
UniProt AC Q9UL12
Protein Name Sarcosine dehydrogenase, mitochondrial
Gene Name SARDH
Organism Homo sapiens (Human).
Sequence Length 918
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MASLSRALRVAAAHPRQSPTRGMGPCNLSSAAGPTAEKSVPYQRTLKEGQGTSVVAQGPSRPLPSTANVVVIGGGSLGCQTLYHLAKLGMSGAVLLERERLTSGTTWHTAGLLWQLRPSDVEVELLAHTRRVVSRELEEETGLHTGWIQNGGLFIASNRQRLDEYKRLMSLGKAYGVESHVLSPAETKTLYPLMNVDDLYGTLYVPHDGTMDPAGTCTTLARAASARGAQVIENCPVTGIRVWTDDFGVRRVAGVETQHGSIQTPCVVNCAGVWASAVGRMAGVKVPLVAMHHAYVVTERIEGIQNMPNVRDHDASVYLRLQGDALSVGGYEANPIFWEEVSDKFAFGLFDLDWEVFTQHIEGAINRVPVLEKTGIKSTVCGPESFTPDHKPLMGEAPELRGFFLGCGFNSAGMMLGGGCGQELAHWIIHGRPEKDMHGYDIRRFHHSLTDHPRWIRERSHESYAKNYSVVFPHDEPLAGRNMRRDPLHEELLGQGCVFQERHGWERPGWFHPRGPAPVLEYDYYGAYGSRAHEDYAYRRLLADEYTFAFPPHHDTIKKECLACRGAAAVFDMSYFGKFYLVGLDARKAADWLFSADVSRPPGSTVYTCMLNHRGGTESDLTVSRLAPSHQASPLAPAFEGDGYYLAMGGAVAQHNWSHITTVLQDQKSQCQLIDSSEDLGMISIQGPASRAILQEVLDADLSNEAFPFSTHKLLRAAGHLVRAMRLSFVGELGWELHIPKASCVPVYRAVMAAGAKHGLINAGYRAIDSLSIEKGYRHWHADLRPDDSPLEAGLAFTCKLKSPVPFLGREALEQQRAAGLRRRLVCFTMEDKVPMFGLEAIWRNGQVVGHVRRADFGFAIDKTIAYGYIHDPSGGPVSLDFVKSGDYALERMGVTYGAQAHLKSPFDPNNKRVKGIY
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
3Phosphorylation-----MASLSRALRV
-----CCHHHHHHHH		26.1118691976
5Phosphorylation---MASLSRALRVAA
---CCHHHHHHHHHH		17.0127174698
38SuccinylationAAGPTAEKSVPYQRT
CCCCCCCCCCCCCEE		55.05-
38SuccinylationAAGPTAEKSVPYQRT
CCCCCCCCCCCCCEE		55.05-
108Tele-8alpha-FAD histidineLTSGTTWHTAGLLWQ
CCCCCCEEEEEEEEE		12.07-
108OtherLTSGTTWHTAGLLWQ
CCCCCCEEEEEEEEE		12.07-
166AcetylationRQRLDEYKRLMSLGK
HHHHHHHHHHHHHHH		36.692374979
173SuccinylationKRLMSLGKAYGVESH
HHHHHHHHHHCCCCC		43.67-
173AcetylationKRLMSLGKAYGVESH
HHHHHHHHHHCCCCC		43.67-
173SuccinylationKRLMSLGKAYGVESH
HHHHHHHHHHCCCCC		43.67-
175PhosphorylationLMSLGKAYGVESHVL
HHHHHHHHCCCCCCC		25.7830257219
187PhosphorylationHVLSPAETKTLYPLM
CCCCCCCCCCCEECC		31.2830257219
377SuccinylationVLEKTGIKSTVCGPE
EEEECCCCEEECCCC		41.23-
377SuccinylationVLEKTGIKSTVCGPE
EEEECCCCEEECCCC		41.23-
391SuccinylationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.42-
391SuccinylationESFTPDHKPLMGEAP
CCCCCCCCCCCCCCC		47.42-
410UbiquitinationFFLGCGFNSAGMMLG
CCCCCCCCCCCCCCC		19.08-
420UbiquitinationGMMLGGGCGQELAHW
CCCCCCCCHHHHHHH		6.02-
468PhosphorylationHESYAKNYSVVFPHD
CHHHCCCCEEECCCC		11.3527642862
559AcetylationPHHDTIKKECLACRG
CCCHHHHHHHHHCCC		50.22-
578UbiquitinationFDMSYFGKFYLVGLD
EEHHHCCEEEEEECC		22.42-
588UbiquitinationLVGLDARKAADWLFS
EEECCHHHHHHHHHH		50.04-
589UbiquitinationVGLDARKAADWLFSA
EECCHHHHHHHHHHC		12.71-
607UbiquitinationRPPGSTVYTCMLNHR
CCCCCEEEEEEECCC		8.36-
632UbiquitinationRLAPSHQASPLAPAF
ECCCCCCCCCCCCCC		14.00-
634UbiquitinationAPSHQASPLAPAFEG
CCCCCCCCCCCCCCC		35.24-
716UbiquitinationFSTHKLLRAAGHLVR
CCHHHHHHHHHHHHH		32.59-
744UbiquitinationLHIPKASCVPVYRAV
EECCHHHHHHHHHHH		4.85-
757UbiquitinationAVMAAGAKHGLINAG
HHHHHHHHHCHHHHC		36.97-
775AcetylationIDSLSIEKGYRHWHA
HHCCEECCCCCEEEC		60.62-
775UbiquitinationIDSLSIEKGYRHWHA
HHCCEECCCCCEEEC		60.62-
777PhosphorylationSLSIEKGYRHWHADL
CCEECCCCCEEECCC		15.4617693683
800UbiquitinationAGLAFTCKLKSPVPF
HCEEEEEECCCCCCC		56.76-
802SuccinylationLAFTCKLKSPVPFLG
EEEEEECCCCCCCCC		37.90-
802SuccinylationLAFTCKLKSPVPFLG
EEEEEECCCCCCCCC		37.90-
802AcetylationLAFTCKLKSPVPFLG
EEEEEECCCCCCCCC		37.90-
802UbiquitinationLAFTCKLKSPVPFLG
EEEEEECCCCCCCCC		37.90-
864PhosphorylationFGFAIDKTIAYGYIH
CCEEEECEEEEEEEE		13.69-
867PhosphorylationAIDKTIAYGYIHDPS
EEECEEEEEEEECCC		13.4522817900
869PhosphorylationDKTIAYGYIHDPSGG
ECEEEEEEEECCCCC		5.17-
884SuccinylationPVSLDFVKSGDYALE
CEEEEEECCCCHHHH		49.03-
884UbiquitinationPVSLDFVKSGDYALE
CEEEEEECCCCHHHH		49.03-
884SuccinylationPVSLDFVKSGDYALE
CEEEEEECCCCHHHH		49.03-
884AcetylationPVSLDFVKSGDYALE
CEEEEEECCCCHHHH		49.03-
904SuccinylationYGAQAHLKSPFDPNN
CCHHHCCCCCCCCCC		46.33-
904SuccinylationYGAQAHLKSPFDPNN
CCHHHCCCCCCCCCC		46.33-
904AcetylationYGAQAHLKSPFDPNN
CCHHHCCCCCCCCCC		46.33-
912UbiquitinationSPFDPNNKRVKGIY-
CCCCCCCCCCCCCC-		66.27-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SARDH_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 SARDH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE2N_HUMANUBE2Nphysical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
268900Sarcosinemia (SARCOS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SARDH_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-777, AND MASSSPECTROMETRY.

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