UniProt Accession

 ADT2_HUMAN; P05141; O43350 

Genbank Protein ID

 M57424; J02683; L78810; AC004000; BC056160; J03591 

Genbank Nucleotide ID

 AAA51737.1; AAA35579.1; AAB39266.1; AAB96347.1; AAH56160.1; AAA36749.1 

Protein Name

 ADP/ATP translocase 2 

Protein Synonyms/Alias

 ADP,ATP carrier protein 2; ADP,ATP carrier protein, fibroblast isoform; Adenine nucleotide translocator 2; ANT 2; Solute carrier family 25 member 5; ADP/ATP translocase 2, N-terminally processed 

Gene Name

 SLC25A5 

Gene Synonyms/Alias

 ANT2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	DAAVSFAKDFLAGGV	acetylation	[1]
10	DAAVSFAKDFLAGGV	ubiquitination	[2, 3]
23	GVAAAISKTAVAPIE	acetylation	[4, 5, 6, 7]
23	GVAAAISKTAVAPIE	malonylation	[8]
23	GVAAAISKTAVAPIE	ubiquitination	[2, 3, 7, 9, 10, 11]
33	VAPIERVKLLLQVQH	ubiquitination	[2, 3]
43	LQVQHASKQITADKQ	ubiquitination	[2, 3, 7, 9]
49	SKQITADKQYKGIID	ubiquitination	[7]
52	ITADKQYKGIIDCVV	methylation	[12, 13, 14]
52	ITADKQYKGIIDCVV	ubiquitination	[7]
63	DCVVRIPKEQGVLSF	ubiquitination	[2, 3]
92	QALNFAFKDKYKQIF	acetylation	[4, 15]
92	QALNFAFKDKYKQIF	malonylation	[8]
92	QALNFAFKDKYKQIF	ubiquitination	[2, 3, 9]
94	LNFAFKDKYKQIFLG	ubiquitination	[3, 9]
96	FAFKDKYKQIFLGGV	acetylation	[4, 5, 6]
96	FAFKDKYKQIFLGGV	malonylation	[8]
96	FAFKDKYKQIFLGGV	ubiquitination	[2, 3, 9]
105	IFLGGVDKRTQFWLY	acetylation	[4, 5, 7]
105	IFLGGVDKRTQFWLY	ubiquitination	[2, 3, 7, 9]
147	RLAADVGKAGAEREF	malonylation	[8]
147	RLAADVGKAGAEREF	ubiquitination	[2, 3, 7, 9, 10, 11, 16, 17]
163	GLGDCLVKIYKSDGI	acetylation	[4, 5, 6, 7]
163	GLGDCLVKIYKSDGI	ubiquitination	[2, 3, 7]
166	DCLVKIYKSDGIKGL	acetylation	[6]
166	DCLVKIYKSDGIKGL	ubiquitination	[2, 3, 7, 9]
199	FGIYDTAKGMLPDPK	acetylation	[4]
199	FGIYDTAKGMLPDPK	ubiquitination	[2, 9]
245	MMMQSGRKGTDIMYT	ubiquitination	[2, 3, 7]
268	IARDEGGKAFFKGAW	acetylation	[4, 6]
268	IARDEGGKAFFKGAW	ubiquitination	[2, 3, 7, 9]
272	EGGKAFFKGAWSNVL	acetylation	[4, 5, 6, 7, 15]
272	EGGKAFFKGAWSNVL	ubiquitination	[2, 3, 7, 9, 11, 16, 18]
295	LVLYDEIKKYT****	ubiquitination	[16]

Reference

 [1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] The first identification of lysine malonylation substrates and its regulatory enzyme.
 Peng C, Lu Z, Xie Z, Cheng Z, Chen Y, Tan M, Luo H, Zhang Y, He W, Yang K, Zwaans BM, Tishkoff D, Ho L, Lombard D, He TC, Dai J, Verdin E, Ye Y, Zhao Y.
 Mol Cell Proteomics. 2011 Dec;10(12):M111.012658. [PMID: 21908771]
 [9] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [11] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [12] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [13] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [14] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [15] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [16] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [17] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [18] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional 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. 

Sequence Annotation

 REPEAT 6 98 Solcar 1.
 REPEAT 111 201 Solcar 2.
 REPEAT 212 297 Solcar 3.
 MOTIF 235 240 Substrate recognition (By similarity).
 BINDING 80 80 Nucleotide (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 2 2 N-acetylthreonine; in ADP/ATP translocase
 MOD_RES 23 23 N6-malonyllysine.
 MOD_RES 42 42 Phosphoserine (By similarity).
 MOD_RES 52 52 N6,N6-dimethyllysine; alternate.
 MOD_RES 52 52 N6-methyllysine; alternate.
 MOD_RES 92 92 N6-malonyllysine.
 MOD_RES 96 96 N6-malonyllysine.
 MOD_RES 105 105 N6-acetyllysine.
 MOD_RES 147 147 N6-malonyllysine.
 MOD_RES 163 163 N6-acetyllysine.
 MOD_RES 166 166 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Chromosome partition; Complete proteome; Direct protein sequencing; Host-virus interaction; Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 298 AA 

Protein Sequence

Gene Ontology

 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
 GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
 GO:0071817; C:MMXD complex; IDA:UniProtKB.
 GO:0015207; F:adenine transmembrane transporter activity; TAS:ProtInc.
 GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
 GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
 GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization; IMP:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
 GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR002113; Aden_trnslctor.
 IPR002067; Mit_carrier.
 IPR018108; Mitochondrial_sb/sol_carrier.
 IPR023395; Mt_carrier_dom. 

Pfam

 PF00153; Mito_carr 

SMART

  

PROSITE

 PS50920; SOLCAR 

PRINTS

 PR00927; ADPTRNSLCASE.
 PR00926; MITOCARRIER.