dbPTM

IVD_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IVD_MOUSE
UniProt AC	Q9JHI5
Protein Name	Isovaleryl-CoA dehydrogenase, mitochondrial
Gene Name	Ivd
Organism	Mus musculus (Mouse).
Sequence Length	424
Subcellular Localization	Mitochondrion matrix.
Protein Description
Protein Sequence	MATAIRLLGRRVSSWRLRPSPSPLAVPRRAHSILPVDDDINGLNEEQKQLRHTISKFLQENLAPKAQEIDQTNDFKNLREFWKQLGSLGVLGITAPVQYGGSGLGYLEHVLVMEEISRASGAVGLSYGAHSNLCVNQIVRNGNEAQKEKYLPKLISGEFIGALAMSEPNAGSDVVSMKLKAEKKGDHYVLNGNKFWITNGPDADILVVYAKTDLTAVPASRGITAFIVEKGMPGFSTSKKLDKLGMRGSNTCELVFEDCKVPAANVLSQESKGVYVLMSGLDLERLVLAGGPLGIMQAVLDHTIPYLHVREAFGQKIGQFQLMQGKMADMYTRLMASRQYVYNVAKACDEGHIIPKDCAGVILYAAECATQVALDGIQCLGGNGYINDFPMGRFLRDAKLYEIGAGTSEVRRLVIGRAFNADFR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	AVPRRAHSILPVDDD CCCCCCCCCCCCCCC	25.49	21082442
55	Phosphorylation	KQLRHTISKFLQENL HHHHHHHHHHHHHCC	20.64	24719451
56	Ubiquitination	QLRHTISKFLQENLA HHHHHHHHHHHHCCC	46.36	-
56	Succinylation	QLRHTISKFLQENLA HHHHHHHHHHHHCCC	46.36	-
56	Succinylation	QLRHTISKFLQENLA HHHHHHHHHHHHCCC	46.36	23806337
56	Acetylation	QLRHTISKFLQENLA HHHHHHHHHHHHCCC	46.36	23576753
65	Succinylation	LQENLAPKAQEIDQT HHHCCCHHHHHHCCC	58.03	23806337
65	Succinylation	LQENLAPKAQEIDQT HHHCCCHHHHHHCCC	58.03	-
65	Acetylation	LQENLAPKAQEIDQT HHHCCCHHHHHHCCC	58.03	23576753
65	Ubiquitination	LQENLAPKAQEIDQT HHHCCCHHHHHHCCC	58.03	-
76	Acetylation	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	23576753
76	Succinylation	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	23806337
76	Succinylation	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	-
76	Ubiquitination	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	-
76	Glutarylation	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	24703693
76	Malonylation	IDQTNDFKNLREFWK HCCCCCHHHHHHHHH	58.92	26320211
134	S-palmitoylation	YGAHSNLCVNQIVRN CCCCCCCCHHHHHHC	2.94	26165157
134	S-nitrosylation	YGAHSNLCVNQIVRN CCCCCCCCHHHHHHC	2.94	21278135
134	S-nitrosocysteine	YGAHSNLCVNQIVRN CCCCCCCCHHHHHHC	2.94	-
147	Acetylation	RNGNEAQKEKYLPKL HCCCHHHHHHHHHHH	64.32	23864654
149	Acetylation	GNEAQKEKYLPKLIS CCHHHHHHHHHHHHC	60.15	23864654
153	Acetylation	QKEKYLPKLISGEFI HHHHHHHHHHCCCHH	56.72	23954790
183	Acetylation	SMKLKAEKKGDHYVL EEEEEEECCCCEEEE	67.90	23201123
209	Phosphorylation	DADILVVYAKTDLTA CCCEEEEEEECCCCC	8.56	26643407
211	Succinylation	DILVVYAKTDLTAVP CEEEEEEECCCCCCC	25.53	23954790
212	Phosphorylation	ILVVYAKTDLTAVPA EEEEEEECCCCCCCC	28.24	26643407
215	Phosphorylation	VYAKTDLTAVPASRG EEEECCCCCCCCCCC	28.55	26643407
220	Phosphorylation	DLTAVPASRGITAFI CCCCCCCCCCCEEEE	25.60	26643407
224	Phosphorylation	VPASRGITAFIVEKG CCCCCCCEEEEEECC	20.52	23140645
230	Acetylation	ITAFIVEKGMPGFST CEEEEEECCCCCCCC	50.01	23864654
236	Phosphorylation	EKGMPGFSTSKKLDK ECCCCCCCCCHHHHH	37.37	23140645
237	Phosphorylation	KGMPGFSTSKKLDKL CCCCCCCCCHHHHHH	42.16	23140645
238	Phosphorylation	GMPGFSTSKKLDKLG CCCCCCCCHHHHHHC	26.96	23140645
239	Succinylation	MPGFSTSKKLDKLGM CCCCCCCHHHHHHCC	58.40	23806337
239	Acetylation	MPGFSTSKKLDKLGM CCCCCCCHHHHHHCC	58.40	23576753
260	Acetylation	ELVFEDCKVPAANVL EEEECCCCCCHHHHC	64.67	23576753
260	Succinylation	ELVFEDCKVPAANVL EEEECCCCCCHHHHC	64.67	23806337
260	Succinylation	ELVFEDCKVPAANVL EEEECCCCCCHHHHC	64.67	-
268	Phosphorylation	VPAANVLSQESKGVY CCHHHHCCCCCCCEE	27.85	29472430
271	Phosphorylation	ANVLSQESKGVYVLM HHHCCCCCCCEEEEE	27.37	29472430
272	Acetylation	NVLSQESKGVYVLMS HHCCCCCCCEEEEEC	52.20	23576753
316	Succinylation	VREAFGQKIGQFQLM HHHHHHCCHHHHHHH	49.54	-
316	Succinylation	VREAFGQKIGQFQLM HHHHHHCCHHHHHHH	49.54	23806337
316	Acetylation	VREAFGQKIGQFQLM HHHHHHCCHHHHHHH	49.54	23806337
346	Acetylation	QYVYNVAKACDEGHI HHHHHHHHHCCCCCC	45.31	23864654
348	S-nitrosocysteine	VYNVAKACDEGHIIP HHHHHHHCCCCCCCC	4.89	-
348	S-nitrosylation	VYNVAKACDEGHIIP HHHHHHHCCCCCCCC	4.89	21278135
399	Acetylation	GRFLRDAKLYEIGAG CCHHCCCEEEEECCC	56.76	19857771
399	Ubiquitination	GRFLRDAKLYEIGAG CCHHCCCEEEEECCC	56.76	-

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 IVD_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
76	K	Acetylation		23806337
Acetylation of Lys-76 is observed in liver mitochondria from fasted mice but not from fed mice.

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 IVD_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IVD_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-76, AND MASS SPECTROMETRY.	16916647 [Abstract]

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