dbPTM

ACADV_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACADV_HUMAN
UniProt AC	P49748
Protein Name	Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene Name	ACADVL
Organism	Homo sapiens (Human).
Sequence Length	655
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..
Protein Sequence	MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	QAARMAASLGRQLLR HHHHHHHHHHHHHHH	23.09	24961811
51	Acetylation	AAQLALDKSDSHPSD HHHHHHCCCCCCCCH	57.94	-
52	Phosphorylation	AQLALDKSDSHPSDA HHHHHCCCCCCCCHH	43.97	26437602
54	Phosphorylation	LALDKSDSHPSDALT HHHCCCCCCCCHHHH	44.37	25159151
57	Phosphorylation	DKSDSHPSDALTRKK CCCCCCCCHHHHCCC	30.05	26437602
61	Phosphorylation	SHPSDALTRKKPAKA CCCCHHHHCCCCCCC	42.01	20068231
71	Malonylation	KPAKAESKSFAVGMF CCCCCCCCCEEEEEE	40.89	26320211
71	Succinylation	KPAKAESKSFAVGMF CCCCCCCCCEEEEEE	40.89	-
71	Succinylation	KPAKAESKSFAVGMF CCCCCCCCCEEEEEE	40.89	-
71	Acetylation	KPAKAESKSFAVGMF CCCCCCCCCEEEEEE	40.89	88267
103	Acetylation	EEQTQFLKELVEPVS HHHHHHHHHHHHHHH	50.74	25038526
148	Phosphorylation	AFGLQVPSELGGVGL CCCCCCCHHHCCCCC	46.74	25332170
158	Phosphorylation	GGVGLCNTQYARLVE CCCCCCCCHHHHHHH	23.20	25332170
195	Succinylation	GILLFGTKAQKEKYL CEEEECCHHHHHHCC	49.56	-
195	Acetylation	GILLFGTKAQKEKYL CEEEECCHHHHHHCC	49.56	25953088
195	Succinylation	GILLFGTKAQKEKYL CEEEECCHHHHHHCC	49.56	23954790
195	Malonylation	GILLFGTKAQKEKYL CEEEECCHHHHHHCC	49.56	26320211
217	Phosphorylation	TVAAFCLTEPSSGSD EEEEEEECCCCCCCC	47.21	30576142
217	Acetylation	TVAAFCLTEPSSGSD EEEEEEECCCCCCCC	47.21	19608861
217 (in isoform 2)	Acetylation	-	47.21	-
223	Phosphorylation	LTEPSSGSDAASIRT ECCCCCCCCCCHHCC	26.48	30576142
231	Phosphorylation	DAASIRTSAVPSPCG CCCHHCCCCCCCCCC	19.88	30576142
237	S-nitrosocysteine	TSAVPSPCGKYYTLN CCCCCCCCCCEEEEC	9.60	-
237	S-nitrosylation	TSAVPSPCGKYYTLN CCCCCCCCCCEEEEC	9.60	-
239	Succinylation	AVPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	-
239	Acetylation	AVPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	19608861
239	Succinylation	AVPSPCGKYYTLNGS CCCCCCCCEEEECCC	41.63	27452117
247	Methylation	YYTLNGSKLWISNGG EEEECCCEEEEECCC	49.60	-
262	Acetylation	LADIFTVFAKTPVTD CCCEEEEEECCCCCC	5.39	19608861
265	Phosphorylation	IFTVFAKTPVTDPAT EEEEEECCCCCCCCC	21.40	21406692
268	Phosphorylation	VFAKTPVTDPATGAV EEECCCCCCCCCHHH	37.15	21406692
272	Phosphorylation	TPVTDPATGAVKEKI CCCCCCCCHHHHHHE	30.94	21406692
276	Succinylation	DPATGAVKEKITAFV CCCCHHHHHHEEEEE	53.40	-
276	Acetylation	DPATGAVKEKITAFV CCCCHHHHHHEEEEE	53.40	23954790
276	Succinylation	DPATGAVKEKITAFV CCCCHHHHHHEEEEE	53.40	27452117
276	Malonylation	DPATGAVKEKITAFV CCCCHHHHHHEEEEE	53.40	26320211
278	Acetylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	23954790
278	Succinylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	27452117
278	Malonylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	26320211
278	Succinylation	ATGAVKEKITAFVVE CCHHHHHHEEEEEEE	39.37	-
286	Methylation	ITAFVVERGFGGITH EEEEEEECCCCCCCC	33.84	-
298	Acetylation	ITHGPPEKKMGIKAS CCCCCCHHHCCCCCC	54.56	2402911
299	Ubiquitination	THGPPEKKMGIKASN CCCCCHHHCCCCCCC	40.47	-
299	Malonylation	THGPPEKKMGIKASN CCCCCHHHCCCCCCC	40.47	26320211
299	Acetylation	THGPPEKKMGIKASN CCCCCHHHCCCCCCC	40.47	7623897
309	Acetylation	IKASNTAEVFFDGVR CCCCCCEEEEECCEE	37.51	19608861
309 (in isoform 2)	Acetylation	-	37.51	-
328	Phosphorylation	NVLGEVGSGFKVAMH CCCCCCCCHHHHEEH	46.35	73680285
331	Succinylation	GEVGSGFKVAMHILN CCCCCHHHHEEHHHH	32.39	-
331	Acetylation	GEVGSGFKVAMHILN CCCCCHHHHEEHHHH	32.39	19608861
331	Succinylation	GEVGSGFKVAMHILN CCCCCHHHHEEHHHH	32.39	-
354	Acetylation	ALAGTMRGIIAKAVD HHHHHHHHHHHHHHH	12.58	19608861
372	Succinylation	NRTQFGEKIHNFGLI CCHHHHHHHHCCHHH	50.04	-
372	Succinylation	NRTQFGEKIHNFGLI CCHHHHHHHHCCHHH	50.04	27452117
372	Acetylation	NRTQFGEKIHNFGLI CCHHHHHHHHCCHHH	50.04	23954790
372	Ubiquitination	NRTQFGEKIHNFGLI CCHHHHHHHHCCHHH	50.04	-
382	Acetylation	NFGLIQEKLARMVML CCHHHHHHHHHHHHH	30.94	27452117
467 (in isoform 2)	Phosphorylation	-	2.33	-
480	Malonylation	ALQGCMDKGKELSGL HHHHHHHCCHHHCCH	45.02	26320211
480	Acetylation	ALQGCMDKGKELSGL HHHHHHHCCHHHCCH	45.02	26051181
482	Succinylation	QGCMDKGKELSGLGS HHHHHCCHHHCCHHH	62.31	-
482	Acetylation	QGCMDKGKELSGLGS HHHHHCCHHHCCHHH	62.31	23954790
482	Malonylation	QGCMDKGKELSGLGS HHHHHCCHHHCCHHH	62.31	26320211
482	Succinylation	QGCMDKGKELSGLGS HHHHHCCHHHCCHHH	62.31	27452117
485	Phosphorylation	MDKGKELSGLGSALK HHCCHHHCCHHHHHC	32.82	25159151
489	Phosphorylation	KELSGLGSALKNPFG HHHCCHHHHHCCCCC	35.16	25159151
492	Ubiquitination	SGLGSALKNPFGNAG CCHHHHHCCCCCCHH	63.39	21906983
507	Ubiquitination	LLLGEAGKQLRRRAG HHHHHHHHHHHHHCC	53.89	2189047
507	Acetylation	LLLGEAGKQLRRRAG HHHHHHHHHHHHHCC	53.89	80954809
512 (in isoform 3)	Phosphorylation	-	26.94	27251275
516 (in isoform 2)	Ubiquitination	-	20.81	21890473
517	Phosphorylation	RRRAGLGSGLSLSGL HHHCCCCCCCCHHCC	41.42	23312004
520	Phosphorylation	AGLGSGLSLSGLVHP CCCCCCCCHHCCCCH	24.82	23312004
522	Phosphorylation	LGSGLSLSGLVHPEL CCCCCCHHCCCCHHH	27.06	25849741
530	Phosphorylation	GLVHPELSRSGELAV CCCCHHHCCCHHHHH	23.80	23186163
530	Ubiquitination	GLVHPELSRSGELAV CCCCHHHCCCHHHHH	23.80	21890473
531 (in isoform 2)	Ubiquitination	-	62.40	21890473
545 (in isoform 3)	Phosphorylation	-	26.77	27251275
550	Acetylation	FATVVEAKLIKHKKG HHHHHHHHHHHCCCC	36.92	-
550	Succinylation	FATVVEAKLIKHKKG HHHHHHHHHHHCCCC	36.92	27452117
553	Ubiquitination	VVEAKLIKHKKGIVN HHHHHHHHCCCCCCC	60.86	-
556	Succinylation	AKLIKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	27452117
556	Acetylation	AKLIKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	-
556	Succinylation	AKLIKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	-
556	Malonylation	AKLIKHKKGIVNEQF HHHHHCCCCCCCHHH	54.30	26320211
586	Phosphorylation	VVVLSRASRSLSEGH HHHHHHHHCCCCCCC	22.69	19889959
588	Phosphorylation	VLSRASRSLSEGHPT HHHHHHCCCCCCCCC	33.48	23312004
590	Phosphorylation	SRASRSLSEGHPTAQ HHHHCCCCCCCCCHH	42.66	25849741
631	Phosphorylation	DPWQQELYRNFKSIS CHHHHHHHHHHHHHH	11.62	110745747
635	Sumoylation	QELYRNFKSISKALV HHHHHHHHHHHHHHH	50.89	-
635	Succinylation	QELYRNFKSISKALV HHHHHHHHHHHHHHH	50.89	27452117
635	Sumoylation	QELYRNFKSISKALV HHHHHHHHHHHHHHH	50.89	-
635	Malonylation	QELYRNFKSISKALV HHHHHHHHHHHHHHH	50.89	26320211
635	Acetylation	QELYRNFKSISKALV HHHHHHHHHHHHHHH	50.89	25953088
639	Ubiquitination	RNFKSISKALVERGG HHHHHHHHHHHHCCC	44.03	-
639	Succinylation	RNFKSISKALVERGG HHHHHHHHHHHHCCC	44.03	27452117
639	Succinylation	RNFKSISKALVERGG HHHHHHHHHHHHCCC	44.03	-
639	Acetylation	RNFKSISKALVERGG HHHHHHHHHHHHCCC	44.03	25825284
639	Malonylation	RNFKSISKALVERGG HHHHHHHHHHHHCCC	44.03	26320211
644	Methylation	ISKALVERGGVVTSN HHHHHHHCCCEECCC	39.42	-

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
586	S	Phosphorylation	Kinase	PKACA	P17612	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
237	C	S-nitrosylation		-
S-nitrosylation at Cys-237 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACADV_HUMAN	ACADVL	physical	9599005
ATP5L_HUMAN	ATP5L	physical	22939629
INT9_HUMAN	INTS9	physical	22939629
RSSA_HUMAN	RPSA	physical	21988832
GEPH_HUMAN	GPHN	physical	21988832
DHRS4_HUMAN	DHRS4	physical	28514442
APC_HUMAN	APC	physical	28514442

Drug and Disease Associations

Kegg Disease
H00525	Disorders of fatty-acid oxidation, including: Medium-chain (MC) acyl-CoA dehydrogenase (AD) deficien
OMIM Disease
201475	Acyl-CoA dehydrogenase very long-chain deficiency (ACADVLD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACADV_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-331, AND MASSSPECTROMETRY.	19608861 [Abstract]

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