dbPTM

YRDC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	YRDC_HUMAN
UniProt AC	Q86U90
Protein Name	YrdC domain-containing protein, mitochondrial
Gene Name	YRDC
Organism	Homo sapiens (Human).
Sequence Length	279
Subcellular Localization	Mitochondrion . Membrane Peripheral membrane protein. Predominantly localized in the plasma membrane..
Protein Description	May regulate the activity of some transporters..
Protein Sequence	MSPARRCRGMRAAVAASVGLSEGPAGSRSGRLFRPPSPAPAAPGARLLRLPGSGAVQAASPERAGWTEALRAAVAELRAGAVVAVPTDTLYGLACAASCSAALRAVYRLKGRSEAKPLAVCLGRVADVYRYCRVRVPEGLLKDLLPGPVTLVMERSEELNKDLNPFTPLVGIRIPDHAFMQDLAQMFEGPLALTSANLSSQASSLNVEEFQDLWPQLSLVIDGGQIGDGQSPECRLGSTVVDLSVPGKFGIIRPGCALESTTAILQQKYGLLPSHASYL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSPARRCRG ------CCHHHHHHH	27.54	24719451
17	Phosphorylation	MRAAVAASVGLSEGP HHHHHHHHHCCCCCC	13.64	24641631
21	O-linked_Glycosylation	VAASVGLSEGPAGSR HHHHHCCCCCCCCCC	34.28	23301498
21	Phosphorylation	VAASVGLSEGPAGSR HHHHHCCCCCCCCCC	34.28	28555341
27	Phosphorylation	LSEGPAGSRSGRLFR CCCCCCCCCCCCCCC	25.94	28555341
29	Phosphorylation	EGPAGSRSGRLFRPP CCCCCCCCCCCCCCC	29.93	26270265
34	Methylation	SRSGRLFRPPSPAPA CCCCCCCCCCCCCCC	46.97	54560703
37	Phosphorylation	GRLFRPPSPAPAAPG CCCCCCCCCCCCCCC	36.05	29255136
49	Methylation	APGARLLRLPGSGAV CCCCEEEECCCCCCC	43.35	115920229
53	Phosphorylation	RLLRLPGSGAVQAAS EEEECCCCCCCCCCC	22.95	29396449
60	Phosphorylation	SGAVQAASPERAGWT CCCCCCCCHHHCCHH	30.24	29255136
67	Phosphorylation	SPERAGWTEALRAAV CHHHCCHHHHHHHHH	15.51	26074081
87	Phosphorylation	GAVVAVPTDTLYGLA CCEEEECCCHHHHHH	34.71	29978859
89	Phosphorylation	VVAVPTDTLYGLACA EEEECCCHHHHHHHH	25.10	29978859
91	Phosphorylation	AVPTDTLYGLACAAS EECCCHHHHHHHHHH	16.52	29978859
98	Phosphorylation	YGLACAASCSAALRA HHHHHHHHHHHHHHH	7.06	29978859
100	Phosphorylation	LACAASCSAALRAVY HHHHHHHHHHHHHHH	17.68	29978859
116	Ubiquitination	LKGRSEAKPLAVCLG HCCCCCCCCHHHHHH	36.19	-
116	Acetylation	LKGRSEAKPLAVCLG HCCCCCCCCHHHHHH	36.19	27452117
150	O-linked_Glycosylation	DLLPGPVTLVMERSE HHCCCCEEEEEECHH	19.44	23301498
161	Ubiquitination	ERSEELNKDLNPFTP ECHHHHCCCCCCCCC	75.99	27667366
167	Phosphorylation	NKDLNPFTPLVGIRI CCCCCCCCCCCCCCC	19.57	27050516
238	Phosphorylation	SPECRLGSTVVDLSV CCCCCCCCEEEEECC	23.71	21406692
239	Phosphorylation	PECRLGSTVVDLSVP CCCCCCCEEEEECCC	23.81	21406692
244	Phosphorylation	GSTVVDLSVPGKFGI CCEEEEECCCCCCCC	23.08	21406692
277	Phosphorylation	GLLPSHASYL----- CCCCCHHHCC-----	22.88	28796482
278	Phosphorylation	LLPSHASYL------ CCCCHHHCC------	19.74	28796482

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 YRDC_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of YRDC_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 YRDC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of YRDC_HUMAN !!

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 YRDC_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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-37 AND SER-60, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-60, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.	16964243 [Abstract]
"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-37, AND MASSSPECTROMETRY.	17081983 [Abstract]