dbPTM

ADT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADT1_HUMAN
UniProt AC	P12235
Protein Name	ADP/ATP translocase 1
Gene Name	SLC25A4
Organism	Homo sapiens (Human).
Sequence Length	298
Subcellular Localization	Mitochondrion inner membrane Multi-pass membrane protein.
Protein Description	Involved in mitochondrial ADP/ATP transport. Catalyzes the exchange of cytoplasmic ADP with mitochondrial ATP across the mitochondrial inner membrane..
Protein Sequence	MGDHAWSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIFVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGDHAWSFL ------CCHHHHHHH	35.10	-
7	Phosphorylation	-MGDHAWSFLKDFLA -CCHHHHHHHHHHHH	22.83	20833797
10	Acetylation	DHAWSFLKDFLAGGV HHHHHHHHHHHHHHH	44.41	19821825
22	Phosphorylation	GGVAAAVSKTAVAPI HHHHHHHCCCCCCCH	21.40	20068231
23	Acetylation	GVAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	23954790
23	Succinylation	GVAAAVSKTAVAPIE HHHHHHCCCCCCCHH	33.63	27452117
24	Phosphorylation	VAAAVSKTAVAPIER HHHHHCCCCCCCHHH	20.89	20860994
33	Acetylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	2402015
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	21890473
42	Phosphorylation	LLQVQHASKQISAEK HHHHHHHHHHCCHHH	23.98	30266825
43	Acetylation	LQVQHASKQISAEKQ HHHHHHHHHCCHHHH	53.05	25953088
43	Ubiquitination	LQVQHASKQISAEKQ HHHHHHHHHCCHHHH	53.05	21890473
46	Phosphorylation	QHASKQISAEKQYKG HHHHHHCCHHHHHCC	28.07	26437602
52	Acetylation	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	30582723
52	Ubiquitination	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	-
52	"N6,N6-dimethyllysine"	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	-
52	Methylation	ISAEKQYKGIIDCVV CCHHHHHCCEEEEEE	40.93	-
63	Ubiquitination	DCVVRIPKEQGFLSF EEEEECCHHHCCHHH	61.37	21906983
81	Phosphorylation	NLANVIRYFPTQALN CHHHHHHHCHHHHHH	11.64	21712546
84	Phosphorylation	NVIRYFPTQALNFAF HHHHHCHHHHHHHHC	19.30	21712546
92	Acetylation	QALNFAFKDKYKQLF HHHHHHCHHHCHHHH	50.29	68569
92	Ubiquitination	QALNFAFKDKYKQLF HHHHHHCHHHCHHHH	50.29	21890473
94	Acetylation	LNFAFKDKYKQLFLG HHHHCHHHCHHHHCC	55.74	7617769
96	Malonylation	FAFKDKYKQLFLGGV HHCHHHCHHHHCCCC	46.39	26320211
96	Ubiquitination	FAFKDKYKQLFLGGV HHCHHHCHHHHCCCC	46.39	21890473
96	Acetylation	FAFKDKYKQLFLGGV HHCHHHCHHHHCCCC	46.39	23954790
107	Ubiquitination	LGGVDRHKQFWRYFA CCCCHHHHHHHHHHH	48.35	-
112	Phosphorylation	RHKQFWRYFAGNLAS HHHHHHHHHHHCCCC	6.59	28857561
119	Phosphorylation	YFAGNLASGGAAGAT HHHHCCCCCCCCCCC	40.71	20833797
126	Phosphorylation	SGGAAGATSLCFVYP CCCCCCCCEEEEEEE	22.70	20860994
127	Phosphorylation	GGAAGATSLCFVYPL CCCCCCCEEEEEEEC	23.70	28857561
139	Phosphorylation	YPLDFARTRLAADVG EECCHHHHHHHHHHC	26.97	20860994
140	Methylation	PLDFARTRLAADVGK ECCHHHHHHHHHHCC	19.44	-
147	Acetylation	RLAADVGKGAAQREF HHHHHHCCCHHHHHH	45.27	27452117
147	Succinylation	RLAADVGKGAAQREF HHHHHHCCCHHHHHH	45.27	27452117
147	Ubiquitination	RLAADVGKGAAQREF HHHHHHCCCHHHHHH	45.27	-
147	Succinylation	RLAADVGKGAAQREF HHHHHHCCCHHHHHH	45.27	-
147	Methylation	RLAADVGKGAAQREF HHHHHHCCCHHHHHH	45.27	2403213
160	S-nitrosylation	EFHGLGDCIIKIFKS HHCCCCCEEEEEHHC	3.08	-
160	S-nitrosocysteine	EFHGLGDCIIKIFKS HHCCCCCEEEEEHHC	3.08	-
163	Acetylation	GLGDCIIKIFKSDGL CCCCEEEEEHHCCCC	23.37	25953088
166	Acetylation	DCIIKIFKSDGLRGL CEEEEEHHCCCCCHH	51.62	26051181
167	Phosphorylation	CIIKIFKSDGLRGLY EEEEEHHCCCCCHHH	26.60	20833797
174	Phosphorylation	SDGLRGLYQGFNVSV CCCCCHHHCCCCEEE	14.93	-
187	Phosphorylation	SVQGIIIYRAAYFGV EEEEEEEEEEHHHCC	5.47	-
191	Phosphorylation	IIIYRAAYFGVYDTA EEEEEEHHHCCHHCC	10.40	21082442
195	Phosphorylation	RAAYFGVYDTAKGML EEHHHCCHHCCCCCC	14.14	27259358
197	Phosphorylation	AYFGVYDTAKGMLPD HHHCCHHCCCCCCCC	16.75	26356563
199	Acetylation	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	26051181
199	Ubiquitination	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	21890473
199	Malonylation	FGVYDTAKGMLPDPK HCCHHCCCCCCCCCC	47.12	26320211
201	Sulfoxidation	VYDTAKGMLPDPKNV CHHCCCCCCCCCCCE	4.90	28183972
242	Phosphorylation	RRRMMMQSGRKGADI HHHHHHHCCCCCCCE	23.75	24719451
245	Succinylation	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	21890473
245	Ubiquitination	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	21890473
245	Succinylation	MMMQSGRKGADIMYT HHHHCCCCCCCEEEE	63.07	-
268	Acetylation	IAKDEGAKAFFKGAW HHHCHHHHHHHHHHH	57.49	27452117
272	Methylation	EGAKAFFKGAWSNVL HHHHHHHHHHHHHHH	41.06	19608861
272	Acetylation	EGAKAFFKGAWSNVL HHHHHHHHHHHHHHH	41.06	19608861
272	Succinylation	EGAKAFFKGAWSNVL HHHHHHHHHHHHHHH	41.06	21890473
272	Succinylation	EGAKAFFKGAWSNVL HHHHHHHHHHHHHHH	41.06	-
272	Ubiquitination	EGAKAFFKGAWSNVL HHHHHHHHHHHHHHH	41.06	19608861
276	Phosphorylation	AFFKGAWSNVLRGMG HHHHHHHHHHHHHCC	19.27	28857561
282	Sulfoxidation	WSNVLRGMGGAFVLV HHHHHHHCCCEEEEE	3.46	28183972
295	Ubiquitination	LVLYDEIKKYV---- EEEHHHHHHHC----	35.68	-
295	Acetylation	LVLYDEIKKYV---- EEEHHHHHHHC----	35.68	30582729

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
195	Y	Phosphorylation	Kinase	LCK	P06239	PSP
195	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ADT1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAX_HUMAN	BAX	physical	9748162
IKBA_HUMAN	NFKBIA	physical	11287411
RSSA_HUMAN	RPSA	physical	22939629
QCR1_HUMAN	UQCRC1	physical	22939629
RL10L_HUMAN	RPL10L	physical	22939629
GALT2_HUMAN	GALNT2	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
VA0D1_HUMAN	ATP6V0D1	physical	26344197
SCMC1_HUMAN	SLC25A24	physical	26344197
TBB4B_HUMAN	TUBB4B	physical	26344197
FAF2_HUMAN	FAF2	physical	26389662
NEK4_HUMAN	NEK4	physical	27173435

Drug and Disease Associations

Kegg Disease
H01118	Progressive external ophthalmoplegia (PEO)
OMIM Disease
609283	Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal dominant, 2 (PEOA2)
615418	Mitochondrial DNA depletion syndrome 12, cardiomyopathic type (MTDPS12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171	Adenosine triphosphate
DB00720	Clodronate

Regulatory Network of ADT1_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-96, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, AND MASSSPECTROMETRY.	18083107 [Abstract]