dbPTM

ACADV_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACADV_MOUSE
UniProt AC	P50544
Protein Name	Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene Name	Acadvl
Organism	Mus musculus (Mouse).
Sequence Length	656
Subcellular Localization	Mitochondrion inner membrane.
Protein Description	Active toward esters of long-chain and very long chain fatty acids such as palmitoyl-CoA, myristoyl-CoA and stearoyl-CoA. Can accommodate substrate acyl chain lengths as long as 24 carbons, but shows little activity for substrates of less than 12 carbons (By similarity)..
Protein Sequence	MQSARMTPSVGRQLLRLGARSSRSTTVLQGQPRPISAQRLYAREATQAVLDKPETLSSDASTREKPARAESKSFAVGMFKGQLTIDQVFPYPSVLSEEQAQFLKELVGPVARFFEEVNDPAKNDALEKVEDDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQREKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAIPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPSENVLGEVGDGFKVAVNILNNGRFGMAATLAGTMKSLIAKAVDHATNRTQFGDKIHNFGVIQEKLARMAILQYVTESMAYMLSANMDQGFKDFQIEAAISKIFCSEAAWKVADECIQIMGGMGFMKEPGVERVLRDIRIFRIFEGANDILRLFVALQGCMDKGKELTGLGNALKNPFGNVGLLMGEAGKQLRRRTGIGSGLSLSGIVHPELSRSGELAVQALDQFATVVEAKLVKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGYPTAQHEKMLCDSWCIEAATRIRENMASLQSSPQHQELFRNFRSISKAMVENGGLVTGNPLGI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Acetylation	ATQAVLDKPETLSSD HHHHHHCCCCCCCCC	40.36	23576753
55	Phosphorylation	AVLDKPETLSSDAST HHHCCCCCCCCCCCC	40.23	27742792
57	Phosphorylation	LDKPETLSSDASTRE HCCCCCCCCCCCCCC	33.32	26525534
58	Phosphorylation	DKPETLSSDASTREK CCCCCCCCCCCCCCC	40.07	27742792
61	Phosphorylation	ETLSSDASTREKPAR CCCCCCCCCCCCCCC	32.75	27742792
62	Phosphorylation	TLSSDASTREKPARA CCCCCCCCCCCCCCH	44.56	27742792
71	Phosphorylation	EKPARAESKSFAVGM CCCCCHHCCCCCCEE	32.39	22817900
72	Acetylation	KPARAESKSFAVGMF CCCCHHCCCCCCEEE	40.89	23576753
72	Succinylation	KPARAESKSFAVGMF CCCCHHCCCCCCEEE	40.89	-
72	Succinylation	KPARAESKSFAVGMF CCCCHHCCCCCCEEE	40.89	23806337
73	Phosphorylation	PARAESKSFAVGMFK CCCHHCCCCCCEEEC	27.93	21082442
80	Acetylation	SFAVGMFKGQLTIDQ CCCCEEECCCEEEEE	36.53	23864654
122	Glutarylation	EEVNDPAKNDALEKV HHHCCHHHCCHHHHH	61.83	24703693
122	Ubiquitination	EEVNDPAKNDALEKV HHHCCHHHCCHHHHH	61.83	-
122	Succinylation	EEVNDPAKNDALEKV HHHCCHHHCCHHHHH	61.83	26388266
122	Acetylation	EEVNDPAKNDALEKV HHHCCHHHCCHHHHH	61.83	23864654
128	Succinylation	AKNDALEKVEDDTLQ HHCCHHHHHCHHHHH	52.34	-
128	Ubiquitination	AKNDALEKVEDDTLQ HHCCHHHHHCHHHHH	52.34	-
128	Acetylation	AKNDALEKVEDDTLQ HHCCHHHHHCHHHHH	52.34	23576753
128	Succinylation	AKNDALEKVEDDTLQ HHCCHHHHHCHHHHH	52.34	23806337
196	Acetylation	GILLYGTKAQREKYL CEEEECCHHHHHHCC	37.85	23806337
196	Succinylation	GILLYGTKAQREKYL CEEEECCHHHHHHCC	37.85	23806337
196	Succinylation	GILLYGTKAQREKYL CEEEECCHHHHHHCC	37.85	-
201	Acetylation	GTKAQREKYLPRVAS CCHHHHHHCCCCHHC	55.03	23201123
208	Phosphorylation	KYLPRVASGQALAAF HCCCCHHCCCEEEHH	28.69	30352176
216	S-nitrosylation	GQALAAFCLTEPSSG CCEEEHHHHCCCCCC	3.84	21278135
216	S-nitrosocysteine	GQALAAFCLTEPSSG CCEEEHHHHCCCCCC	3.84	-
238	S-nitrosylation	SSAIPSPCGKYYTLN HCCCCCCCCCEEEEC	9.60	23281369
238	Glutathionylation	SSAIPSPCGKYYTLN HCCCCCCCCCEEEEC	9.60	24333276
238	S-nitrosocysteine	SSAIPSPCGKYYTLN HCCCCCCCCCEEEEC	9.60	-
240	Ubiquitination	AIPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	-
240	Acetylation	AIPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	23576753
240	Succinylation	AIPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	-
240	Succinylation	AIPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	23806337
241	Phosphorylation	IPSPCGKYYTLNGSK CCCCCCCEEEECCCE	6.23	25195567
269	Ubiquitination	VFAKTPIKDAATGAV HEECCCCCHHCCHHH	42.38	-
269	Succinylation	VFAKTPIKDAATGAV HEECCCCCHHCCHHH	42.38	23806337
269	Malonylation	VFAKTPIKDAATGAV HEECCCCCHHCCHHH	42.38	26320211
269	Succinylation	VFAKTPIKDAATGAV HEECCCCCHHCCHHH	42.38	-
269	Acetylation	VFAKTPIKDAATGAV HEECCCCCHHCCHHH	42.38	23806337
277	Succinylation	DAATGAVKEKITAFV HHCCHHHHHHEEEEE	53.40	23806337
277	Succinylation	DAATGAVKEKITAFV HHCCHHHHHHEEEEE	53.40	-
277	Acetylation	DAATGAVKEKITAFV HHCCHHHHHHEEEEE	53.40	23576753
277	Glutarylation	DAATGAVKEKITAFV HHCCHHHHHHEEEEE	53.40	24703693
279	Succinylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	-
279	Acetylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	23576753
279	Succinylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	23806337
279	Malonylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	26320211
299	Ubiquitination	VTHGLPEKKMGIKAS CCCCCCHHHCCCCCC	46.23	-
299	Glutarylation	VTHGLPEKKMGIKAS CCCCCCHHHCCCCCC	46.23	24703693
299	Acetylation	VTHGLPEKKMGIKAS CCCCCCHHHCCCCCC	46.23	23576753
300	Succinylation	THGLPEKKMGIKASN CCCCCHHHCCCCCCC	40.47	26388266
300	Acetylation	THGLPEKKMGIKASN CCCCCHHHCCCCCCC	40.47	7623893
317	Ubiquitination	EVYFDGVKVPSENVL EEEECCEECCCCCCC	54.69	-
317	Acetylation	EVYFDGVKVPSENVL EEEECCEECCCCCCC	54.69	23576753
332	Succinylation	GEVGDGFKVAVNILN EECCCCCEEEEEEHH	34.51	-
332	Succinylation	GEVGDGFKVAVNILN EECCCCCEEEEEEHH	34.51	23806337
332	Acetylation	GEVGDGFKVAVNILN EECCCCCEEEEEEHH	34.51	23576753
332	Ubiquitination	GEVGDGFKVAVNILN EECCCCCEEEEEEHH	34.51	-
359	Acetylation	TMKSLIAKAVDHATN HHHHHHHHHHHHHCC	41.78	21728379
359	Ubiquitination	TMKSLIAKAVDHATN HHHHHHHHHHHHHCC	41.78	-
373	Succinylation	NRTQFGDKIHNFGVI CCCCHHHHHCCCHHH	46.36	-
373	Acetylation	NRTQFGDKIHNFGVI CCCCHHHHHCCCHHH	46.36	23864654
373	Ubiquitination	NRTQFGDKIHNFGVI CCCCHHHHHCCCHHH	46.36	-
373	Succinylation	NRTQFGDKIHNFGVI CCCCHHHHHCCCHHH	46.36	23806337
383	Acetylation	NFGVIQEKLARMAIL CCHHHHHHHHHHHHH	30.94	22826441
423	S-palmitoylation	AAISKIFCSEAAWKV HHHHHHHCCHHHHHH	4.01	28526873
423	S-nitrosocysteine	AAISKIFCSEAAWKV HHHHHHHCCHHHHHH	4.01	-
423	S-nitrosylation	AAISKIFCSEAAWKV HHHHHHHCCHHHHHH	4.01	21278135
434	S-nitrosylation	AWKVADECIQIMGGM HHHHHHHHHHHHCCC	2.60	21278135
434	S-nitrosocysteine	AWKVADECIQIMGGM HHHHHHHHHHHHCCC	2.60	-
478	S-nitrosocysteine	LFVALQGCMDKGKEL HHHHHHHHHHCCHHH	1.74	-
478	S-nitrosylation	LFVALQGCMDKGKEL HHHHHHHHHHCCHHH	1.74	21278135
481	Acetylation	ALQGCMDKGKELTGL HHHHHHHCCHHHCCH	45.02	24062335
483	Succinylation	QGCMDKGKELTGLGN HHHHHCCHHHCCHHH	56.12	-
483	Glutarylation	QGCMDKGKELTGLGN HHHHHCCHHHCCHHH	56.12	24703693
483	Acetylation	QGCMDKGKELTGLGN HHHHHCCHHHCCHHH	56.12	23576753
483	Succinylation	QGCMDKGKELTGLGN HHHHHCCHHHCCHHH	56.12	23806337
483	Malonylation	QGCMDKGKELTGLGN HHHHHCCHHHCCHHH	56.12	26320211
493	Acetylation	TGLGNALKNPFGNVG CCHHHHHCCCCCHHH	61.23	2393059
508	Ubiquitination	LLMGEAGKQLRRRTG HHHHHHHHHHHHHHC	53.89	-
514	Phosphorylation	GKQLRRRTGIGSGLS HHHHHHHHCCCCCCC	31.19	26060331
518	Phosphorylation	RRRTGIGSGLSLSGI HHHHCCCCCCCCCCC	34.34	22817900
521	Phosphorylation	TGIGSGLSLSGIVHP HCCCCCCCCCCCCCH	24.82	23737553
523	Phosphorylation	IGSGLSLSGIVHPEL CCCCCCCCCCCCHHH	24.09	9416463
551	Succinylation	FATVVEAKLVKHKKG HHHHHHHHHHHCCCC	40.06	26388266
551	Acetylation	FATVVEAKLVKHKKG HHHHHHHHHHHCCCC	40.06	23576753
557	Glutarylation	AKLVKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	24703693
557	Succinylation	AKLVKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	23806337
557	Malonylation	AKLVKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	26320211
557	Succinylation	AKLVKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	-
557	Acetylation	AKLVKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	23576753
591	Phosphorylation	SRASRSLSEGYPTAQ HHHHCHHHCCCCCHH	30.16	22817900
601	Acetylation	YPTAQHEKMLCDSWC CCCHHHHHHHHHHHH	34.74	23864654
621	Phosphorylation	RIRENMASLQSSPQH HHHHHHHHHCCCHHH	19.03	23737553
624	Phosphorylation	ENMASLQSSPQHQEL HHHHHHCCCHHHHHH	49.64	23737553
625	Phosphorylation	NMASLQSSPQHQELF HHHHHCCCHHHHHHH	18.67	23737553
640	Succinylation	RNFRSISKAMVENGG HHHHHHHHHHHHCCC	38.54	23806337
640	Acetylation	RNFRSISKAMVENGG HHHHHHHHHHHHCCC	38.54	23806337
640	Succinylation	RNFRSISKAMVENGG HHHHHHHHHHHHCCC	38.54	-

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 ACADV_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
238	C	S-nitrosylation		23281369
S-nitrosylation at Cys-238 in liver improves catalytic efficiency.

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 ACADV_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SOCS3_MOUSE	Socs3	physical	22093833

Drug and Disease Associations

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

Regulatory Network of ACADV_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-240 AND LYS-277, AND MASSSPECTROMETRY.	16916647 [Abstract]
Ubiquitylation
Reference	PubMed
"A proteomics approach to identify the ubiquitinated proteins in mouseheart."; Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,Choi H.W., Park Z.-Y., Yoo Y.J.; Biochem. Biophys. Res. Commun. 357:731-736(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-332, AND MASSSPECTROMETRY.	17451654 [Abstract]

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