P05141 (ADT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ADP/ATP translocase 2

Alternative name(s):
ADP,ATP carrier protein 2
ADP,ATP carrier protein, fibroblast isoform
Adenine nucleotide translocator 2
Short name=ANT 2
Solute carrier family 25 member 5

Gene names

Name:	SLC25A5
Synonyms:	ANT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11
Subunit structure	Homodimer. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with HIV-1 Vpr. Ref.9 Ref.11
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein.
Miscellaneous	The transmembrane helices are not perpendicular to the plane of the membrane, but cross the membrane at an angle. Odd-numbered transmembrane helices exhibit a sharp kink, due to the presence of a conserved proline residue By similarity.
Sequence similarities	Belongs to the mitochondrial carrier (TC 2.A.29) family. [View classification] Contains 3 Solcar repeats.

Ontologies

Keywords
Biological process	Chromosome partition Host-virus interaction Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW energy reserve metabolic process Traceable author statement. Source: Reactome negative regulation of mitochondrial outer membrane permeabilization Inferred from mutant phenotype PubMed 19154410. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype PubMed 19154410. Source: UniProtKB regulation of insulin secretion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MMXD complex Inferred from direct assay Ref.11. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc mitochondrial inner membrane Traceable author statement. Source: Reactome mitochondrial nucleoid Inferred from direct assay PubMed 18063578. Source: BHF-UCL
Molecular_function	adenine transmembrane transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
C2orf18	Q8N357	2	EBI-355133,EBI-713484
SIRT4	Q9Y6E7	2	EBI-355133,EBI-2606540

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.7
	Chain	2 – 298	297	ADP/ATP translocase 2		PRO_0000090579
Regions
	Transmembrane	5 – 39	35	Helical; Name=1; By similarity
	Transmembrane	75 – 100	26	Helical; Name=2; By similarity
	Transmembrane	109 – 143	35	Helical; Name=3; By similarity
	Transmembrane	176 – 202	27	Helical; Name=4; By similarity
	Transmembrane	207 – 241	35	Helical; Name=5; By similarity
	Transmembrane	273 – 298	26	Helical; Name=6; By similarity
	Repeat	6 – 98	93	Solcar 1
	Repeat	111 – 201	91	Solcar 2
	Repeat	212 – 297	86	Solcar 3
	Motif	235 – 240	6	Substrate recognition By similarity
Sites
	Binding site	80	1	Nucleotide By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine Ref.6 Ref.7
	Modified residue	23	1	N6-acetyllysine Ref.10
	Modified residue	23	1	N6-malonyllysine; alternate Ref.13
	Modified residue	42	1	Phosphoserine By similarity
	Modified residue	52	1	N6,N6-dimethyllysine; alternate Ref.7
	Modified residue	52	1	N6-methyllysine; alternate Ref.7
	Modified residue	92	1	N6-malonyllysine; alternate Ref.13
	Modified residue	96	1	N6-malonyllysine Ref.13
	Modified residue	105	1	N6-acetyllysine Ref.10
	Modified residue	147	1	N6-malonyllysine; alternate Ref.13
	Modified residue	163	1	N6-acetyllysine Ref.10
	Modified residue	166	1	N6-acetyllysine By similarity
	Modified residue	191	1	Phosphotyrosine By similarity
	Modified residue	195	1	Phosphotyrosine By similarity
	Modified residue	199	1	N6-acetyllysine By similarity
Natural variations
	Natural variant	111	1	L → R. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs371749 [ dbSNP | Ensembl ].		VAR_030039
Experimental info
	Sequence conflict	6	1	V → L in AAA35579. Ref.2
	Sequence conflict	66	1	G → E in AAA35579. Ref.2
	Sequence conflict	162	1	V → G in AAA36749. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P05141 [UniParc]. Last modified January 11, 2011. Version 7. Checksum: DC53D083E7217AFE	FASTA	298	32,852
	10 20 30 40 50 60 MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR 70 80 90 100 110 120 IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW LYFAGNLASG 130 140 150 160 170 180 GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFRGLGDC LVKIYKSDGI KGLYQGFNVS 190 200 210 220 230 240 VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI VISWMIAQTV TAVAGLTSYP FDTVRRRMMM 250 260 270 280 290 QSGRKGTDIM YTGTLDCWRK IARDEGGKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human fibroblast adenine nucleotide translocator gene. Molecular cloning and sequence." Ku D.-H., Kagan J., Chen S.-T., Chang C.-D., Baserga R., Wurzel J. J. Biol. Chem. 265:16060-16063(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-111. Tissue: Placenta.
[2]	"Molecular cloning of a cDNA for a human ADP/ATP carrier which is growth-regulated." Battini R., Ferrari S., Kaczmarek L., Calabretta B., Chen S.T., Baserga R. J. Biol. Chem. 262:4355-4358(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-111.
[3]	"Ordered shotgun sequencing of a 135 kb Xq25 YAC containing ANT2 and four possible genes, including three confirmed by EST matches." Chen C.N., Su Y., Baybayan P., Siruno A., Nagaraja R., Mazzarella R., Schlessinger D., Chen E. Nucleic Acids Res. 24:4034-4041(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-111.
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-111. Tissue: Eye.
[6]	Bienvenut W.V. Submitted (OCT-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-31; 34-43; 64-92; 141-147; 189-199 AND 273-296, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[7]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-23; 32-43; 50-60; 64-92; 81-92; 97-106; 112-138; 172-199; 207-235; 245-259 AND 281-295, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, METHYLATION AT LYS-52, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"Two distinct genes for ADP/ATP translocase are expressed at the mRNA level in adult human liver." Houldsworth J., Attardi G. Proc. Natl. Acad. Sci. U.S.A. 85:377-381(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-297. Tissue: Liver.
[9]	"Mitochondrial membrane permeabilization by HIV-1 Vpr." Deniaud A., Brenner C., Kroemer G. Mitochondrion 4:223-233(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 VPR.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-105 AND LYS-163, MASS SPECTROMETRY.
[11]	"MMXD, a TFIIH-independent XPD-MMS19 protein complex involved in chromosome segregation." Ito S., Tan L.J., Andoh D., Narita T., Seki M., Hirano Y., Narita K., Kuraoka I., Hiraoka Y., Tanaka K. Mol. Cell 39:632-640(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN MMXD COMPLEX.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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 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) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M57424 Genomic DNA. Translation: AAA51737.1. J02683 mRNA. Translation: AAA35579.1. L78810 Genomic DNA. Translation: AAB39266.1. AC004000 Genomic DNA. Translation: AAB96347.1. BC056160 mRNA. Translation: AAH56160.1. J03591 mRNA. Translation: AAA36749.1.
IPI	IPI00007188.
PIR	A29132.
RefSeq	NP_001143.2. NM_001152.4.
UniGene	Hs.632282.
3D structure databases
ProteinModelPortal	P05141.
SMR	P05141. Positions 2-294.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33873N.
IntAct	P05141. 27 interactions.
MINT	MINT-1162449.
STRING	9606.ENSP00000360671.
Protein family/group databases
TCDB	2.A.29.1.1. mitochondrial carrier (MC) family.
PTM databases
PhosphoSite	P05141.
Polymorphism databases
DMDM	113459.
Proteomic databases
PaxDb	P05141.
PRIDE	P05141.
Protocols and materials databases
DNASU	292.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000317881; ENSP00000360671; ENSG00000005022.
GeneID	292.
KEGG	hsa:292.
UCSC	uc004erh.4. human.
Organism-specific databases
CTD	292.
GeneCards	GC0XP118602.
H-InvDB	HIX0028379.
HGNC	HGNC:10991. SLC25A5.
MIM	300150. gene.
neXtProt	NX_P05141.
PharmGKB	PA35867.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG238123.
HOVERGEN	HBG108348.
InParanoid	P05141.
KO	K05863.
OMA	KNTHILV.
OrthoDB	EOG49CQ86.
PhylomeDB	P05141.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P05141.
Bgee	P05141.
CleanEx	HS_SLC25A5.
Genevestigator	P05141.
GermOnline	ENSG00000005022. Homo sapiens.
Family and domain databases
Gene3D	1.50.40.10. 1 hit.
InterPro	IPR002113. Aden_trnslctor. IPR002067. Mit_carrier. IPR018108. Mitochondrial_sb/sol_carrier. IPR023395. Mt_carrier_dom. [Graphical view]
Pfam	PF00153. Mito_carr. 3 hits. [Graphical view]
PRINTS	PR00927. ADPTRNSLCASE. PR00926. MITOCARRIER.
SUPFAM	SSF103506. Mitoch_carrier. 1 hit.
PROSITE	PS50920. SOLCAR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SLC25A5. human.
DrugBank	DB00720. Clodronate.
GenomeRNAi	292.
NextBio	1191.
SOURCE	Search...

Entry information

Entry name

ADT2_HUMAN

Accession

Primary (citable) accession number: P05141
Secondary accession number(s): O43350

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 152 of the entry and version 7 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.