dbPTM

ADT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADT1_MOUSE
UniProt AC	P48962
Protein Name	ADP/ATP translocase 1
Gene Name	Slc25a4
Organism	Mus musculus (Mouse).
Sequence Length	298
Subcellular Localization	Mitochondrion inner membrane Multi-pass membrane protein. The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria.
Protein Description	Involved in mitochondrial ADP/ATP transport. Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane..
Protein Sequence	MGDQALSFLKDFLAGGIAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGSSQREFNGLGDCLTKIFKSDGLKGLYQGFSVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTLDCWRKIAKDEGANAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGDQALSFL ------CCHHHHHHH	35.42	-
7	Phosphorylation	-MGDQALSFLKDFLA -CCHHHHHHHHHHHH	31.39	20495213
10	Acetylation	DQALSFLKDFLAGGI HHHHHHHHHHHHHHH	44.41	24062335
10	Ubiquitination	DQALSFLKDFLAGGI HHHHHHHHHHHHHHH	44.41	-
10	Succinylation	DQALSFLKDFLAGGI HHHHHHHHHHHHHHH	44.41	26388266
22	Phosphorylation	GGIAAAVSKTAVAPI HHHHHHHCCCCCCCH	21.40	27742792
23	Acetylation	GIAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	23864654
23	Ubiquitination	GIAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	-
23	Succinylation	GIAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	-
23	Malonylation	GIAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	25418362
24	Phosphorylation	IAAAVSKTAVAPIER HHHHHCCCCCCCHHH	20.89	28542873
33	Acetylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	24062335
33	Malonylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	26320211
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	-
42	Phosphorylation	LLQVQHASKQISAEK HHHHHHHHHHCCHHH	23.98	25521595
43	Acetylation	LQVQHASKQISAEKQ HHHHHHHHHCCHHHH	53.05	23806337
43	Succinylation	LQVQHASKQISAEKQ HHHHHHHHHCCHHHH	53.05	23806337
43	Ubiquitination	LQVQHASKQISAEKQ HHHHHHHHHCCHHHH	53.05	-
46	Phosphorylation	QHASKQISAEKQYKG HHHHHHCCHHHHHCC	28.07	23737553
52	Methylation	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	-
52	Acetylation	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	23576753
57	S-nitrosylation	QYKGIIDCVVRIPKE HHCCEEEEEEECCHH	1.83	21278135
57	S-nitrosocysteine	QYKGIIDCVVRIPKE HHCCEEEEEEECCHH	1.83	-
63	Ubiquitination	DCVVRIPKEQGFLSF EEEEECCHHHCCHHH	61.37	-
63	Succinylation	DCVVRIPKEQGFLSF EEEEECCHHHCCHHH	61.37	23806337
63	Acetylation	DCVVRIPKEQGFLSF EEEEECCHHHCCHHH	61.37	24062335
69	Phosphorylation	PKEQGFLSFWRGNLA CHHHCCHHHHCCCHH	22.09	22817900
81	Phosphorylation	NLANVIRYFPTQALN CHHHHHHHCHHHHHH	11.64	24925903
84	Phosphorylation	NVIRYFPTQALNFAF HHHHHCHHHHHHHHC	19.30	24925903
92	Ubiquitination	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
92	Acetylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	23864654
92	Malonylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	26320211
92	Phosphoglycerylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
92	Succinylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
94	Acetylation	LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC	55.74	24062335
96	Malonylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	26320211
96	Phosphoglycerylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	Ubiquitination	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	Acetylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	23864654
112	Phosphorylation	RHKQFWRYFAGNLAS HHHHHHHHHHHCCCC	6.59	29899451
126	Phosphorylation	SGGAAGATSLCFVYP CCCCCCCCEEEEEEE	22.70	-
127	Phosphorylation	GGAAGATSLCFVYPL CCCCCCCEEEEEEEC	23.70	-
129	S-nitrosocysteine	AAGATSLCFVYPLDF CCCCCEEEEEEECCC	1.86	-
129	S-nitrosylation	AAGATSLCFVYPLDF CCCCCEEEEEEECCC	1.86	24895380
129	Glutathionylation	AAGATSLCFVYPLDF CCCCCEEEEEEECCC	1.86	24333276
147	Succinylation	RLAADVGKGSSQREF HHHHCCCCCCCCHHC	56.31	23806337
147	Ubiquitination	RLAADVGKGSSQREF HHHHCCCCCCCCHHC	56.31	27667366
147	Succinylation	RLAADVGKGSSQREF HHHHCCCCCCCCHHC	56.31	-
147	Acetylation	RLAADVGKGSSQREF HHHHCCCCCCCCHHC	56.31	23806337
147	Methylation	RLAADVGKGSSQREF HHHHCCCCCCCCHHC	56.31	-
149	Phosphorylation	AADVGKGSSQREFNG HHCCCCCCCCHHCCC	27.12	26824392
150	Phosphorylation	ADVGKGSSQREFNGL HCCCCCCCCHHCCCH	41.76	25521595
160	S-nitrosylation	EFNGLGDCLTKIFKS HCCCHHHHHHHHHHH	5.02	24895380
160	S-nitrosocysteine	EFNGLGDCLTKIFKS HCCCHHHHHHHHHHH	5.02	-
163	Acetylation	GLGDCLTKIFKSDGL CHHHHHHHHHHHCCC	32.95	22733758
166	Ubiquitination	DCLTKIFKSDGLKGL HHHHHHHHHCCCCHH	51.62	-
166	Acetylation	DCLTKIFKSDGLKGL HHHHHHHHHCCCCHH	51.62	22826441
166	Succinylation	DCLTKIFKSDGLKGL HHHHHHHHHCCCCHH	51.62	23806337
167	Phosphorylation	CLTKIFKSDGLKGLY HHHHHHHHCCCCHHH	26.60	25338131
191	Phosphorylation	IIIYRAAYFGVYDTA EEEEEEHHHCCHHCC	10.40	25521595
195	Phosphorylation	RAAYFGVYDTAKGML EEHHHCCHHCCCCCC	14.14	25521595
197	Phosphorylation	AYFGVYDTAKGMLPD HHHCCHHCCCCCCCC	16.75	27742792
199	Acetylation	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	23236377
242	Phosphorylation	RRRMMMQSGRKGADI HHHHHHHCCCCCCCE	23.75	25338131
245	Acetylation	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	23806337
245	Succinylation	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	23806337
245	Succinylation	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	-
257	S-nitrosylation	MYTGTLDCWRKIAKD EEEECHHHHHHHHHC	4.21	24895380
257	S-nitrosocysteine	MYTGTLDCWRKIAKD EEEECHHHHHHHHHC	4.21	-
260	Acetylation	GTLDCWRKIAKDEGA ECHHHHHHHHHCCCC	23.63	24062335
263	Succinylation	DCWRKIAKDEGANAF HHHHHHHHCCCCCHH	60.84	23806337
263	Ubiquitination	DCWRKIAKDEGANAF HHHHHHHHCCCCCHH	60.84	-
263	Acetylation	DCWRKIAKDEGANAF HHHHHHHHCCCCCHH	60.84	24062335
272	Glutarylation	EGANAFFKGAWSNVL CCCCHHHHHHHHHHH	41.06	24703693
272	Succinylation	EGANAFFKGAWSNVL CCCCHHHHHHHHHHH	41.06	23806337
272	Acetylation	EGANAFFKGAWSNVL CCCCHHHHHHHHHHH	41.06	23864654
272	Succinylation	EGANAFFKGAWSNVL CCCCHHHHHHHHHHH	41.06	-
272	Ubiquitination	EGANAFFKGAWSNVL CCCCHHHHHHHHHHH	41.06	-
276	Phosphorylation	AFFKGAWSNVLRGMG HHHHHHHHHHHHHCC	19.27	23737553

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 ADT1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ADT1_MOUSE !!

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 ADT1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BCLF1_HUMAN	BCLAF1	physical	20360068

Drug and Disease Associations

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

Regulatory Network of ADT1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, AND MASSSPECTROMETRY.	17114649 [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-195, AND MASSSPECTROMETRY.	18034455 [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-10, AND MASSSPECTROMETRY.	17451654 [Abstract]