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Q9CR62

- M2OM_MOUSE

UniProt

Q9CR62 - M2OM_MOUSE

Protein

Mitochondrial 2-oxoglutarate/malate carrier protein

Gene

Slc25a11

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane in an electroneutral exchange for malate or other dicarboxylic acids, and plays an important role in several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism.By similarity

    GO - Biological processi

    1. transport Source: UniProtKB-KW

    Keywords - Biological processi

    Transport

    Protein family/group databases

    TCDBi2.A.29.2.11. the mitochondrial carrier (mc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial 2-oxoglutarate/malate carrier protein
    Short name:
    OGCP
    Alternative name(s):
    Solute carrier family 25 member 11
    Gene namesi
    Name:Slc25a11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1915113. Slc25a11.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: MGI
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 314313Mitochondrial 2-oxoglutarate/malate carrier proteinPRO_0000090626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei57 – 571N6-succinyllysine1 Publication
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei102 – 1021Phosphotyrosine1 Publication
    Modified residuei256 – 2561N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CR62.
    PaxDbiQ9CR62.
    PRIDEiQ9CR62.

    PTM databases

    PhosphoSiteiQ9CR62.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CR62.
    BgeeiQ9CR62.
    GenevestigatoriQ9CR62.

    Interactioni

    Protein-protein interaction databases

    BioGridi212490. 3 interactions.
    IntActiQ9CR62. 5 interactions.
    MINTiMINT-1851446.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CR62.
    SMRiQ9CR62. Positions 22-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4219Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei83 – 10119Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei119 – 14022Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei183 – 20220Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei222 – 24019Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei281 – 30020Helical; Name=6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati23 – 10886Solcar 1Add
    BLAST
    Repeati117 – 20892Solcar 2Add
    BLAST
    Repeati217 – 30690Solcar 3Add
    BLAST

    Sequence similaritiesi

    Contains 3 Solcar repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300113.
    GeneTreeiENSGT00750000117384.
    HOGENOMiHOG000165139.
    HOVERGENiHBG009528.
    InParanoidiQ9CR62.
    KOiK15104.
    OMAiFRISKHE.
    OrthoDBiEOG793B7Z.
    PhylomeDBiQ9CR62.
    TreeFamiTF354262.

    Family and domain databases

    Gene3Di1.50.40.10. 1 hit.
    InterProiIPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view]
    PfamiPF00153. Mito_carr. 3 hits.
    [Graphical view]
    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.

    Q9CR62-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATASPGAG RMDGKPRTSP KSVKFLFGGL AGMGATVFVQ PLDLVKNRMQ    50
    LSGEGAKTRE YKTSFHALTS ILKTEGLKGI YTGLSAGLLR QATYTTTRLG 100
    IYTVLFERLT GADGTPPGFL LKALIGMTAG ATGAFVGTPA EVALIRMTAD 150
    GRLPADQRRG YKNVFNALVR IAREEGVPTL WRGCIPTMAR AVVVNAAQLA 200
    SYSQSKQFLL DSGYFSDNIL CHFCASMISG LVTTAASMPV DIVKTRIQNM 250
    RMIDGKPEYK NGLDVLLKVV RYEGFFSLWK GFTPYYARLG PHTVLTFIFL 300
    EQMNKAYKRL FLSG 314
    Length:314
    Mass (Da):34,155
    Last modified:January 23, 2007 - v3
    Checksum:i1B19A5DB093941A3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK009824 mRNA. Translation: BAB26524.1.
    AK009487 mRNA. Translation: BAB26319.1.
    BC003455 mRNA. Translation: AAH03455.1.
    BC019631 mRNA. Translation: AAH19631.1.
    CCDSiCCDS24958.1.
    RefSeqiNP_077173.1. NM_024211.3.
    UniGeneiMm.296082.
    Mm.466994.

    Genome annotation databases

    EnsembliENSMUST00000014750; ENSMUSP00000014750; ENSMUSG00000014606.
    GeneIDi67863.
    KEGGimmu:67863.
    UCSCiuc007jvr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK009824 mRNA. Translation: BAB26524.1 .
    AK009487 mRNA. Translation: BAB26319.1 .
    BC003455 mRNA. Translation: AAH03455.1 .
    BC019631 mRNA. Translation: AAH19631.1 .
    CCDSi CCDS24958.1.
    RefSeqi NP_077173.1. NM_024211.3.
    UniGenei Mm.296082.
    Mm.466994.

    3D structure databases

    ProteinModelPortali Q9CR62.
    SMRi Q9CR62. Positions 22-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212490. 3 interactions.
    IntActi Q9CR62. 5 interactions.
    MINTi MINT-1851446.

    Protein family/group databases

    TCDBi 2.A.29.2.11. the mitochondrial carrier (mc) family.

    PTM databases

    PhosphoSitei Q9CR62.

    Proteomic databases

    MaxQBi Q9CR62.
    PaxDbi Q9CR62.
    PRIDEi Q9CR62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000014750 ; ENSMUSP00000014750 ; ENSMUSG00000014606 .
    GeneIDi 67863.
    KEGGi mmu:67863.
    UCSCi uc007jvr.2. mouse.

    Organism-specific databases

    CTDi 8402.
    MGIi MGI:1915113. Slc25a11.

    Phylogenomic databases

    eggNOGi NOG300113.
    GeneTreei ENSGT00750000117384.
    HOGENOMi HOG000165139.
    HOVERGENi HBG009528.
    InParanoidi Q9CR62.
    KOi K15104.
    OMAi FRISKHE.
    OrthoDBi EOG793B7Z.
    PhylomeDBi Q9CR62.
    TreeFami TF354262.

    Miscellaneous databases

    ChiTaRSi SLC25A11. mouse.
    NextBioi 325753.
    PROi Q9CR62.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CR62.
    Bgeei Q9CR62.
    Genevestigatori Q9CR62.

    Family and domain databases

    Gene3Di 1.50.40.10. 1 hit.
    InterProi IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view ]
    Pfami PF00153. Mito_carr. 3 hits.
    [Graphical view ]
    SUPFAMi SSF103506. SSF103506. 1 hit.
    PROSITEi PS50920. SOLCAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Tongue.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    3. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 79-90; 99-146; 163-170; 174-182; 191-206 AND 289-205, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiM2OM_MOUSE
    AccessioniPrimary (citable) accession number: Q9CR62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3