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P05141

- ADT2_HUMAN

UniProt

P05141 - ADT2_HUMAN

Protein

ADP/ATP translocase 2

Gene

SLC25A5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 7 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei80 – 801NucleotideBy similarity

    GO - Molecular functioni

    1. adenine transmembrane transporter activity Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. adenine transport Source: GOC
    2. chromosome segregation Source: UniProtKB-KW
    3. energy reserve metabolic process Source: Reactome
    4. negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: UniProtKB
    5. positive regulation of cell proliferation Source: UniProtKB
    6. regulation of insulin secretion Source: Reactome
    7. small molecule metabolic process Source: Reactome
    8. transport Source: ProtInc
    9. viral process Source: Reactome

    Keywords - Biological processi

    Chromosome partition, Host-virus interaction, Transport

    Enzyme and pathway databases

    ReactomeiREACT_18325. Regulation of insulin secretion.
    REACT_8016. Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabilization.

    Protein family/group databases

    TCDBi2.A.29.1.1. the mitochondrial carrier (mc) family.

    Names & Taxonomyi

    Protein namesi
    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
    Cleaved into the following chain:
    Gene namesi
    Name:SLC25A5
    Synonyms:ANT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:10991. SLC25A5.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: UniProtKB
    4. mitochondrial inner membrane Source: Reactome
    5. mitochondrial nucleoid Source: BHF-UCL
    6. mitochondrion Source: UniProt
    7. MMXD complex Source: UniProtKB
    8. nucleus Source: UniProt

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35867.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 298298ADP/ATP translocase 2PRO_0000423220Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate3 Publications
    Chaini2 – 298297ADP/ATP translocase 2, N-terminally processedPRO_0000090579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in ADP/ATP translocase 2, N-terminally processed4 Publications
    Modified residuei23 – 231N6-malonyllysine1 Publication
    Modified residuei43 – 431N6-succinyllysineBy similarity
    Modified residuei52 – 521N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei52 – 521N6-methyllysine; alternate1 Publication
    Modified residuei92 – 921N6-malonyllysine1 Publication
    Modified residuei96 – 961N6-malonyllysine1 Publication
    Modified residuei105 – 1051N6-acetyllysine; alternate1 Publication
    Modified residuei105 – 1051N6-succinyllysine; alternateBy similarity
    Modified residuei147 – 1471N6-acetyllysine; alternateBy similarity
    Modified residuei147 – 1471N6-malonyllysine; alternate1 Publication
    Modified residuei147 – 1471N6-succinyllysine; alternateBy similarity
    Modified residuei163 – 1631N6-acetyllysine1 Publication
    Modified residuei166 – 1661N6-acetyllysineBy similarity
    Modified residuei268 – 2681N6-acetyllysine; alternateBy similarity
    Modified residuei268 – 2681N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    MaxQBiP05141.
    PaxDbiP05141.
    PRIDEiP05141.

    PTM databases

    PhosphoSiteiP05141.

    Expressioni

    Gene expression databases

    ArrayExpressiP05141.
    BgeeiP05141.
    CleanExiHS_SLC25A5.
    GenevestigatoriP05141.

    Interactioni

    Subunit structurei

    Homodimer. Component of the MMXD complex, which includes CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5. Interacts with HIV-1 Vpr.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-355133,EBI-5323863
    SIRT4Q9Y6E72EBI-355133,EBI-2606540
    SLC35F6Q8N3572EBI-355133,EBI-713484

    Protein-protein interaction databases

    BioGridi106789. 97 interactions.
    DIPiDIP-33873N.
    IntActiP05141. 63 interactions.
    MINTiMINT-1162449.
    STRINGi9606.ENSP00000360671.

    Structurei

    3D structure databases

    ProteinModelPortaliP05141.
    SMRiP05141. Positions 2-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 3935Helical; Name=1By similarityAdd
    BLAST
    Transmembranei75 – 10026Helical; Name=2By similarityAdd
    BLAST
    Transmembranei109 – 14335Helical; Name=3By similarityAdd
    BLAST
    Transmembranei176 – 20227Helical; Name=4By similarityAdd
    BLAST
    Transmembranei207 – 24135Helical; Name=5By similarityAdd
    BLAST
    Transmembranei273 – 29826Helical; Name=6By similarityAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati6 – 9893Solcar 1Add
    BLAST
    Repeati111 – 20191Solcar 2Add
    BLAST
    Repeati212 – 29786Solcar 3Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi235 – 2406Substrate recognitionBy similarity

    Sequence similaritiesi

    Contains 3 Solcar repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG238123.
    HOVERGENiHBG108348.
    InParanoidiP05141.
    KOiK05863.
    OMAiSSYSAMN.
    OrthoDBiEOG7T1RBR.
    PhylomeDBiP05141.
    TreeFamiTF300743.

    Family and domain databases

    Gene3Di1.50.40.10. 1 hit.
    InterProiIPR002113. Aden_trnslctor.
    IPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view]
    PfamiPF00153. Mito_carr. 3 hits.
    [Graphical view]
    PRINTSiPR00927. ADPTRNSLCASE.
    PR00926. MITOCARRIER.
    SUPFAMiSSF103506. SSF103506. 1 hit.
    PROSITEiPS50920. SOLCAR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05141-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ    50
    YKGIIDCVVR IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL 100
    GGVDKRTQFW LYFAGNLASG GAAGATSLCF VYPLDFARTR LAADVGKAGA 150
    EREFRGLGDC LVKIYKSDGI KGLYQGFNVS VQGIIIYRAA YFGIYDTAKG 200
    MLPDPKNTHI VISWMIAQTV TAVAGLTSYP FDTVRRRMMM QSGRKGTDIM 250
    YTGTLDCWRK IARDEGGKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT 298
    Length:298
    Mass (Da):32,852
    Last modified:January 11, 2011 - v7
    Checksum:iDC53D083E7217AFE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61V → L in AAA35579. (PubMed:3031073)Curated
    Sequence conflicti43 – 431K → M in BAG37698. (PubMed:14702039)Curated
    Sequence conflicti66 – 661G → E in AAA35579. (PubMed:3031073)Curated
    Sequence conflicti162 – 1621V → G in AAA36749. (PubMed:2829183)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111L → R.4 Publications
    Corresponds to variant rs371749 [ dbSNP | Ensembl ].
    VAR_030039

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57424 Genomic DNA. Translation: AAA51737.1.
    J02683 mRNA. Translation: AAA35579.1.
    L78810 Genomic DNA. Translation: AAB39266.1.
    AK315292 mRNA. Translation: BAG37698.1.
    AC004000 Genomic DNA. Translation: AAB96347.1.
    BC056160 mRNA. Translation: AAH56160.1.
    J03591 mRNA. Translation: AAA36749.1.
    CCDSiCCDS14578.1.
    PIRiA29132.
    RefSeqiNP_001143.2. NM_001152.4.
    UniGeneiHs.632282.

    Genome annotation databases

    EnsembliENST00000317881; ENSP00000360671; ENSG00000005022.
    GeneIDi292.
    KEGGihsa:292.
    UCSCiuc004erh.4. human.

    Polymorphism databases

    DMDMi317373597.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57424 Genomic DNA. Translation: AAA51737.1 .
    J02683 mRNA. Translation: AAA35579.1 .
    L78810 Genomic DNA. Translation: AAB39266.1 .
    AK315292 mRNA. Translation: BAG37698.1 .
    AC004000 Genomic DNA. Translation: AAB96347.1 .
    BC056160 mRNA. Translation: AAH56160.1 .
    J03591 mRNA. Translation: AAA36749.1 .
    CCDSi CCDS14578.1.
    PIRi A29132.
    RefSeqi NP_001143.2. NM_001152.4.
    UniGenei Hs.632282.

    3D structure databases

    ProteinModelPortali P05141.
    SMRi P05141. Positions 2-294.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106789. 97 interactions.
    DIPi DIP-33873N.
    IntActi P05141. 63 interactions.
    MINTi MINT-1162449.
    STRINGi 9606.ENSP00000360671.

    Chemistry

    DrugBanki DB00720. Clodronate.

    Protein family/group databases

    TCDBi 2.A.29.1.1. the mitochondrial carrier (mc) family.

    PTM databases

    PhosphoSitei P05141.

    Polymorphism databases

    DMDMi 317373597.

    Proteomic databases

    MaxQBi P05141.
    PaxDbi P05141.
    PRIDEi P05141.

    Protocols and materials databases

    DNASUi 292.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317881 ; ENSP00000360671 ; ENSG00000005022 .
    GeneIDi 292.
    KEGGi hsa:292.
    UCSCi uc004erh.4. human.

    Organism-specific databases

    CTDi 292.
    GeneCardsi GC0XP118602.
    H-InvDB HIX0028379.
    HGNCi HGNC:10991. SLC25A5.
    MIMi 300150. gene.
    neXtProti NX_P05141.
    PharmGKBi PA35867.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238123.
    HOVERGENi HBG108348.
    InParanoidi P05141.
    KOi K05863.
    OMAi SSYSAMN.
    OrthoDBi EOG7T1RBR.
    PhylomeDBi P05141.
    TreeFami TF300743.

    Enzyme and pathway databases

    Reactomei REACT_18325. Regulation of insulin secretion.
    REACT_8016. Vpr-mediated induction of apoptosis by mitochondrial outer membrane permeabilization.

    Miscellaneous databases

    ChiTaRSi SLC25A5. human.
    GenomeRNAii 292.
    NextBioi 1191.
    PROi P05141.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05141.
    Bgeei P05141.
    CleanExi HS_SLC25A5.
    Genevestigatori P05141.

    Family and domain databases

    Gene3Di 1.50.40.10. 1 hit.
    InterProi IPR002113. Aden_trnslctor.
    IPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view ]
    Pfami PF00153. Mito_carr. 3 hits.
    [Graphical view ]
    PRINTSi PR00927. ADPTRNSLCASE.
    PR00926. MITOCARRIER.
    SUPFAMi SSF103506. SSF103506. 1 hit.
    PROSITEi PS50920. SOLCAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "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].
    6. "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.
    7. 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, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. 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, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    9. "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.
    10. "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.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-105 AND LYS-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: MALONYLATION AT LYS-23; LYS-92; LYS-96 AND LYS-147.
    16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiADT2_HUMAN
    AccessioniPrimary (citable) accession number: P05141
    Secondary accession number(s): B2RCV1, O43350
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 168 of the entry and version 7 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    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.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3