dbPTM

ADT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADT2_HUMAN
UniProt AC	P05141
Protein Name	ADP/ATP translocase 2
Gene Name	SLC25A5
Organism	Homo sapiens (Human).
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..
Protein Sequence	MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWLYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFRGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MTDAAVSF -------CCHHHHHH	7.45	19413330
1	Sulfoxidation	-------MTDAAVSF -------CCHHHHHH	7.45	28465586
2	Acetylation	------MTDAAVSFA ------CCHHHHHHH	34.05	20068231
2	Phosphorylation	------MTDAAVSFA ------CCHHHHHHH	34.05	20068231
7	Phosphorylation	-MTDAAVSFAKDFLA -CCHHHHHHHHHHHH	18.11	19691289
10	Ubiquitination	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	21890473
10	Acetylation	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	21339330
10	Methylation	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	6271811
10	Ubiquitination	DAAVSFAKDFLAGGV HHHHHHHHHHHHHHH	47.18	21906983
22	Phosphorylation	GGVAAAISKTAVAPI HHHHHHHHCCCCCCH	21.16	30266825
23	Ubiquitination	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	21890473
23	N6-malonyllysine	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	-
23	2-Hydroxyisobutyrylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	-
23	Acetylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	23954790
23	Malonylation	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	26320211
23	Ubiquitination	GVAAAISKTAVAPIE HHHHHHHCCCCCCHH	34.10	21890473
24	Phosphorylation	VAAAISKTAVAPIER HHHHHHCCCCCCHHH	21.41	20860994
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	21890473
33	2-Hydroxyisobutyrylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	-
33	Acetylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	21466224
33	Malonylation	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	26320211
33	Ubiquitination	VAPIERVKLLLQVQH CCCHHHHHHHHHHHH	39.37	21890473
42	Phosphorylation	LLQVQHASKQITADK HHHHHHHHCCCCCCH	23.98	30266825
43	Ubiquitination	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	21890473
43	Acetylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	25953088
43	Methylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	30582699
43	Succinylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	-
43	Succinylation	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	23954790
43	Ubiquitination	LQVQHASKQITADKQ HHHHHHHCCCCCCHH	46.64	21890473
49	Ubiquitination	SKQITADKQYKGIID HCCCCCCHHHCCEEE	53.73	-
51	Phosphorylation	QITADKQYKGIIDCV CCCCCHHHCCEEEEE	19.54	29496907
52	"N6,N6,N6-trimethyllysine"	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	-
52	Acetylation	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	30582687
52	Methylation	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	31213526
52	Ubiquitination	ITADKQYKGIIDCVV CCCCHHHCCEEEEEE	40.93	-
63	2-Hydroxyisobutyrylation	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	-
63	Acetylation	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	25825284
63	Ubiquitination	DCVVRIPKEQGVLSF EEEEEECHHHCCEEE	61.37	21906983
69	Phosphorylation	PKEQGVLSFWRGNLA CHHHCCEEEECCCHH	21.98	30108239
81	Phosphorylation	NLANVIRYFPTQALN CHHHHHHHCHHHHHH	11.64	21712546
84	Phosphorylation	NVIRYFPTQALNFAF HHHHHCHHHHHHHHC	19.30	21712546
92	Ubiquitination	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	21890473
92	N6-malonyllysine	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
92	2-Hydroxyisobutyrylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	-
92	Acetylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	23954790
92	Malonylation	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	26320211
92	Ubiquitination	QALNFAFKDKYKQIF HHHHHHCHHHCCEEE	50.29	21890473
94	Acetylation	LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC	55.74	25953088
94	Ubiquitination	LNFAFKDKYKQIFLG HHHHCHHHCCEEEEC	55.74	-
96	Ubiquitination	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	21890473
96	N6-malonyllysine	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	2-Hydroxyisobutyrylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	-
96	Acetylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	23954790
96	Malonylation	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	26320211
96	Ubiquitination	FAFKDKYKQIFLGGV HHCHHHCCEEEECCC	42.53	21890473
105	Ubiquitination	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	21890473
105	2-Hydroxyisobutyrylation	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	-
105	Acetylation	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	19608861
105	Malonylation	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	26320211
105	Succinylation	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	-
105	Succinylation	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	-
105	Ubiquitination	IFLGGVDKRTQFWLY EEECCCCCCCEEEEE	55.74	21890473
112	Phosphorylation	KRTQFWLYFAGNLAS CCCEEEEEECCCCCC	5.08	28857561
119	Phosphorylation	YFAGNLASGGAAGAT EECCCCCCCCCCCCC	40.71	20833797
126	Phosphorylation	SGGAAGATSLCFVYP CCCCCCCCEEEEEEE	22.70	20860994
127	Phosphorylation	GGAAGATSLCFVYPL CCCCCCCEEEEEEEC	23.70	28857561
129	S-nitrosylation	AAGATSLCFVYPLDF CCCCCEEEEEEECCH	1.86	25040305
139	Phosphorylation	YPLDFARTRLAADVG EECCHHHHHHHHHHH	26.97	20860994
140	Methylation	PLDFARTRLAADVGK ECCHHHHHHHHHHHH	19.44	-
147	Ubiquitination	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	21890473
147	N6-malonyllysine	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	-
147	2-Hydroxyisobutyrylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	-
147	Acetylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	25953088
147	Malonylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	26320211
147	Methylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	24129315
147	Succinylation	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	-
147	Ubiquitination	RLAADVGKAGAEREF HHHHHHHHHHHHHHH	43.42	21890473
155	Methylation	AGAEREFRGLGDCLV HHHHHHHCCHHHHEE	34.37	92469
160	S-nitrosocysteine	EFRGLGDCLVKIYKS HHCCHHHHEEEEEEC	4.46	-
160	S-nitrosylation	EFRGLGDCLVKIYKS HHCCHHHHEEEEEEC	4.46	19483679
160	S-palmitoylation	EFRGLGDCLVKIYKS HHCCHHHHEEEEEEC	4.46	29575903
163	Ubiquitination	GLGDCLVKIYKSDGI CHHHHEEEEEECCCC	27.63	21890473
163	2-Hydroxyisobutyrylation	GLGDCLVKIYKSDGI CHHHHEEEEEECCCC	27.63	-
163	Acetylation	GLGDCLVKIYKSDGI CHHHHEEEEEECCCC	27.63	19608861
163	Malonylation	GLGDCLVKIYKSDGI CHHHHEEEEEECCCC	27.63	26320211
163	Ubiquitination	GLGDCLVKIYKSDGI CHHHHEEEEEECCCC	27.63	21890473
165	Phosphorylation	GDCLVKIYKSDGIKG HHHEEEEEECCCCCH	9.95	29496907
166	Ubiquitination	DCLVKIYKSDGIKGL HHEEEEEECCCCCHH	45.61	21890473
166	Acetylation	DCLVKIYKSDGIKGL HHEEEEEECCCCCHH	45.61	23236377
166	Methylation	DCLVKIYKSDGIKGL HHEEEEEECCCCCHH	45.61	90061
166	Ubiquitination	DCLVKIYKSDGIKGL HHEEEEEECCCCCHH	45.61	21890473
167	Phosphorylation	CLVKIYKSDGIKGLY HEEEEEECCCCCHHH	24.89	23312004
191	Phosphorylation	IIIYRAAYFGIYDTA EEEEEEHHHCCHHHC	11.01	21082442
195	Nitration	RAAYFGIYDTAKGML EEHHHCCHHHCCCCC	13.97	-
195	Phosphorylation	RAAYFGIYDTAKGML EEHHHCCHHHCCCCC	13.97	21082442
197	Phosphorylation	AYFGIYDTAKGMLPD HHHCCHHHCCCCCCC	17.19	26356563
199	Ubiquitination	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	21890473
199	2-Hydroxyisobutyrylation	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	-
199	Acetylation	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	23954790
199	Sumoylation	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	19608861
199	Ubiquitination	FGIYDTAKGMLPDPK HCCHHHCCCCCCCCC	47.12	21890473
206	Sumoylation	KGMLPDPKNTHIVIS CCCCCCCCCCEEEEE	80.16	-
215	Sulfoxidation	THIVISWMIAQTVTA CEEEEEHHHHHHHHH	1.13	28183972
242	Phosphorylation	RRRMMMQSGRKGTDI HHHHHHHCCCCCCCE	23.75	24719451
245	Ubiquitination	MMMQSGRKGTDIMYT HHHHCCCCCCCEEEE	70.46	21890473
245	2-Hydroxyisobutyrylation	MMMQSGRKGTDIMYT HHHHCCCCCCCEEEE	70.46	-
245	Ubiquitination	MMMQSGRKGTDIMYT HHHHCCCCCCCEEEE	70.46	21890473
247	Phosphorylation	MQSGRKGTDIMYTGT HHCCCCCCCEEEEEC	25.95	28857561
251	Phosphorylation	RKGTDIMYTGTLDCW CCCCCEEEEECHHHH	11.44	29496907
252	Phosphorylation	KGTDIMYTGTLDCWR CCCCEEEEECHHHHH	13.30	-
254	Phosphorylation	TDIMYTGTLDCWRKI CCEEEEECHHHHHHH	16.18	23898821
257	Glutathionylation	MYTGTLDCWRKIARD EEEECHHHHHHHHHC	4.21	22555962
268	Acetylation	IARDEGGKAFFKGAW HHHCCCCCEEHHHHH	53.53	25825284
268	Succinylation	IARDEGGKAFFKGAW HHHCCCCCEEHHHHH	53.53	-
268	Succinylation	IARDEGGKAFFKGAW HHHCCCCCEEHHHHH	53.53	23954790
268	Ubiquitination	IARDEGGKAFFKGAW HHHCCCCCEEHHHHH	53.53	19608861
272	Ubiquitination	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	21890473
272	2-Hydroxyisobutyrylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	-
272	Acetylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	23954790
272	Malonylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	26320211
272	Methylation	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	19608861
272	Ubiquitination	EGGKAFFKGAWSNVL CCCCEEHHHHHHHHH	41.06	21890473
276	Phosphorylation	AFFKGAWSNVLRGMG EEHHHHHHHHHHHCC	19.27	28857561
282	Sulfoxidation	WSNVLRGMGGAFVLV HHHHHHHCCCEEEEE	3.46	28183972
295	Acetylation	LVLYDEIKKYT---- EEEHHHHHHCC----	37.37	30582693
295	Ubiquitination	LVLYDEIKKYT---- EEEHHHHHHCC----	37.37	21906983
297	Phosphorylation	LYDEIKKYT------ EHHHHHHCC------	16.81	-

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_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RL7_HUMAN	RPL7	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL15_HUMAN	RPL15	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
RS6_HUMAN	RPS6	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RL23_HUMAN	RPL23	physical	22939629
RL11_HUMAN	RPL11	physical	22939629
RL21_HUMAN	RPL21	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RL23A_HUMAN	RPL23A	physical	22939629
RL4_HUMAN	RPL4	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
RL5_HUMAN	RPL5	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
RL9_HUMAN	RPL9	physical	22939629
RS8_HUMAN	RPS8	physical	22939629
RS21_HUMAN	RPS21	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
RS19_HUMAN	RPS19	physical	22939629
RT16_HUMAN	MRPS16	physical	22939629
ELAV1_HUMAN	ELAVL1	physical	22939629
HS90A_HUMAN	HSP90AA1	physical	22939629
LEG3_HUMAN	LGALS3	physical	22939629
RPN1_HUMAN	RPN1	physical	22939629
GRHPR_HUMAN	GRHPR	physical	22939629
RHOA_HUMAN	RHOA	physical	22939629
K2C1_HUMAN	KRT1	physical	22939629
LMNA_HUMAN	LMNA	physical	22939629
RT34_HUMAN	MRPS34	physical	22939629
NPTN_HUMAN	NPTN	physical	22939629
ANX11_HUMAN	ANXA11	physical	22939629
VA0D1_HUMAN	ATP6V0D1	physical	26344197
HNRPU_HUMAN	HNRNPU	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
PMM2_HUMAN	PMM2	physical	26344197
MCAT_HUMAN	SLC25A20	physical	26344197
SCMC1_HUMAN	SLC25A24	physical	26344197
ADT1_HUMAN	SLC25A4	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00720	Clodronate

Regulatory Network of ADT2_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-23; LYS-105; LYS-163 ANDLYS-199, AND MASS SPECTROMETRY.	19608861 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.	21908771 [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 TYR-195, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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