dbPTM

ADT2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADT2_MOUSE
UniProt AC	P51881
Protein Name	ADP/ATP translocase 2
Gene Name	Slc25a5
Organism	Mus musculus (Mouse).
Sequence Length	298
Subcellular Localization	Mitochondrion inner membrane Multi-pass membrane protein.
Protein Description	Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane. As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (By similarity)..
Protein Sequence	MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFKGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIFISWMIAQSVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGSKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTDAAVSF -------CCHHHHHH	7.45	-
2	Acetylation	------MTDAAVSFA ------CCHHHHHHH	34.05	-
2	Phosphorylation	------MTDAAVSFA ------CCHHHHHHH	34.05	29472430
7	Phosphorylation	-MTDAAVSFAKDFLA -CCHHHHHHHHHHHH	18.11	30352176
10	Acetylation	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	23954790
10	Succinylation	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	26388266
10	Ubiquitination	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	-
22	Phosphorylation	GGVAAAISKTAVAPI HHHHHHHHCCCCCCH	21.16	22324799
23	N6-malonyllysine	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	-
23	Acetylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	23864654
23	Malonylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	26320211
23	Succinylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	-
23	Ubiquitination	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	-
24	Phosphorylation	VAAAISKTAVAPIER HHHHHHCCCCCCHHH	21.41	28542873
33	Acetylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	2393085
33	Malonylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	26320211
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	-
42	Phosphorylation	LLQVQHASKQITADK HHHHHHHHCCCCCCH	23.98	25521595
43	Acetylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	24062335
43	Glutarylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	24703693
43	Succinylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	-
43	Succinylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	23806337
43	Ubiquitination	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	-
46	Phosphorylation	QHASKQITADKQYKG HHHHCCCCCCHHHCC	26.72	23140645
49	Acetylation	SKQITADKQYKGIID HCCCCCCHHHCCEEE	53.73	23864654
49	Succinylation	SKQITADKQYKGIID HCCCCCCHHHCCEEE	53.73	24315375
52	"N6,N6,N6-trimethyllysine"	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	-
52	Acetylation	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	23576753
52	Methylation	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	-
57	S-nitrosocysteine	QYKGIIDCVVRIPKE HHCCEEEEEEEECHH	1.83	-
57	S-nitrosylation	QYKGIIDCVVRIPKE HHCCEEEEEEEECHH	1.83	21278135
63	Acetylation	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	22826441
63	Succinylation	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	24315375
63	Ubiquitination	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	-
69	Phosphorylation	PKEQGVLSFWRGNLA CHHHCCEEEECCCHH	21.98	24899341
81	Phosphorylation	NLANVIRYFPTQALN CHHHHHHHCHHHHHH	11.64	24925903
84	Phosphorylation	NVIRYFPTQALNFAF HHHHHCHHHHHHHHC	19.30	24925903
92	N6-malonyllysine	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
92	Acetylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	68463
92	Malonylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	26073543
92	Ubiquitination	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
94	Acetylation	LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC	55.74	7617775
95	Phosphorylation	NFAFKDKYKQIFLGG HHHCHHHCCEEEECC	20.47	29514104
96	N6-malonyllysine	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	Acetylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	24062335
96	Malonylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	26320211
96	Phosphoglycerylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	Ubiquitination	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
105	Acetylation	IFLGGVDKRTQFWRY EEECCCCCCHHHHHH	55.74	23806337
105	Malonylation	IFLGGVDKRTQFWRY EEECCCCCCHHHHHH	55.74	26320211
105	Phosphoglycerylation	IFLGGVDKRTQFWRY EEECCCCCCHHHHHH	55.74	-
105	Succinylation	IFLGGVDKRTQFWRY EEECCCCCCHHHHHH	55.74	-
105	Succinylation	IFLGGVDKRTQFWRY EEECCCCCCHHHHHH	55.74	23806337
112	Phosphorylation	KRTQFWRYFAGNLAS CCHHHHHHHHHCHHC	6.59	29899451
126	Phosphorylation	SGGAAGATSLCFVYP CCCCCCCCEEEEEEE	22.70	-
127	Phosphorylation	GGAAGATSLCFVYPL CCCCCCCEEEEEEEC	23.70	-
129	S-nitrosocysteine	AAGATSLCFVYPLDF CCCCCEEEEEEECCH	1.86	-
129	S-nitrosylation	AAGATSLCFVYPLDF CCCCCEEEEEEECCH	1.86	21278135
129	S-palmitoylation	AAGATSLCFVYPLDF CCCCCEEEEEEECCH	1.86	28526873
147	N6-malonyllysine	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	-
147	Acetylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	23576753
147	Glutarylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	24703693
147	Malonylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	26073543
147	Methylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	-
147	Succinylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	23806337
147	Ubiquitination	RLAADVGKAGAEREF HHHHHHHHHHHHHHC	43.42	-
155	Acetylation	AGAEREFKGLGDCLV HHHHHHCCCHHHHEE	48.77	23576753
155	Malonylation	AGAEREFKGLGDCLV HHHHHHCCCHHHHEE	48.77	26320211
155	Succinylation	AGAEREFKGLGDCLV HHHHHHCCCHHHHEE	48.77	-
155	Succinylation	AGAEREFKGLGDCLV HHHHHHCCCHHHHEE	48.77	23806337
155	Ubiquitination	AGAEREFKGLGDCLV HHHHHHCCCHHHHEE	48.77	-
160	S-nitrosocysteine	EFKGLGDCLVKIYKS HCCCHHHHEEEEECC	4.46	-
160	Glutathionylation	EFKGLGDCLVKIYKS HCCCHHHHEEEEECC	4.46	24333276
160	S-nitrosylation	EFKGLGDCLVKIYKS HCCCHHHHEEEEECC	4.46	22178444
160	S-palmitoylation	EFKGLGDCLVKIYKS HCCCHHHHEEEEECC	4.46	28526873
163	Acetylation	GLGDCLVKIYKSDGI CHHHHEEEEECCCCC	27.63	23576753
163	Malonylation	GLGDCLVKIYKSDGI CHHHHEEEEECCCCC	27.63	26073543
163	Succinylation	GLGDCLVKIYKSDGI CHHHHEEEEECCCCC	27.63	-
163	Ubiquitination	GLGDCLVKIYKSDGI CHHHHEEEEECCCCC	27.63	-
166	Acetylation	DCLVKIYKSDGIKGL HHEEEEECCCCCCHH	45.61	23576753
166	Malonylation	DCLVKIYKSDGIKGL HHEEEEECCCCCCHH	45.61	26320211
166	Succinylation	DCLVKIYKSDGIKGL HHEEEEECCCCCCHH	45.61	23806337
167	Phosphorylation	CLVKIYKSDGIKGLY HEEEEECCCCCCHHH	24.89	29514104
191	Phosphorylation	IIIYRAAYFGIYDTA EEEEEEHHHCCHHHC	11.01	25521595
195	Phosphorylation	RAAYFGIYDTAKGML EEHHHCCHHHCCCCC	13.97	25521595
197	Phosphorylation	AYFGIYDTAKGMLPD HHHCCHHHCCCCCCC	17.19	25367039
199	Acetylation	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	22826441
199	Malonylation	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	26320211
242	Phosphorylation	RRRMMMQSGRKGTDI HHHHHHHCCCCCCCE	23.75	24719451
245	Acetylation	MMMQSGRKGTDIMYT HHHHCCCCCCCEEEE	70.46	23806337
245	Succinylation	MMMQSGRKGTDIMYT HHHHCCCCCCCEEEE	70.46	23806337
247	Phosphorylation	MQSGRKGTDIMYTGT HHCCCCCCCEEEEEC	25.95	22817900
257	S-nitrosocysteine	MYTGTLDCWRKIARD EEEECHHHHHHHHHC	4.21	-
257	Glutathionylation	MYTGTLDCWRKIARD EEEECHHHHHHHHHC	4.21	24333276
257	S-nitrosylation	MYTGTLDCWRKIARD EEEECHHHHHHHHHC	4.21	24926564
257	S-palmitoylation	MYTGTLDCWRKIARD EEEECHHHHHHHHHC	4.21	28526873
268	Acetylation	IARDEGSKAFFKGAW HHHCCCCHHHHHHHH	61.13	23576753
268	Succinylation	IARDEGSKAFFKGAW HHHCCCCHHHHHHHH	61.13	-
268	Succinylation	IARDEGSKAFFKGAW HHHCCCCHHHHHHHH	61.13	23806337
268	Ubiquitination	IARDEGSKAFFKGAW HHHCCCCHHHHHHHH	61.13	-
272	Acetylation	EGSKAFFKGAWSNVL CCCHHHHHHHHHHHH	41.06	23201123
272	Succinylation	EGSKAFFKGAWSNVL CCCHHHHHHHHHHHH	41.06	24315375
276	Phosphorylation	AFFKGAWSNVLRGMG HHHHHHHHHHHHHCC	19.27	23737553
295	Malonylation	LVLYDEIKKYT---- EEEHHHHHHCC----	37.37	26073543

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 ADT2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	K	Methylation		-
Trimethylated by ANTKMT at Lys-52.

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 ADT2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ADT2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ADT2_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-23; LYS-92; LYS-155;LYS-163; LYS-166 AND LYS-199, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191 AND TYR-195, ANDMASS SPECTROMETRY.	18034455 [Abstract]

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