Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P14152

- MDHC_MOUSE

UniProt

P14152 - MDHC_MOUSE

Protein

Malate dehydrogenase, cytoplasmic

Gene

Mdh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei92 – 921SubstrateBy similarity
    Binding sitei98 – 981SubstrateBy similarity
    Binding sitei105 – 1051NADBy similarity
    Binding sitei112 – 1121NADBy similarity
    Binding sitei131 – 1311SubstrateBy similarity
    Binding sitei162 – 1621SubstrateBy similarity
    Active sitei187 – 1871Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 177NADBy similarity
    Nucleotide bindingi129 – 1313NADBy similarity

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: UniProtKB-EC
    2. NAD binding Source: Ensembl

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. malate metabolic process Source: Ensembl
    3. NADH metabolic process Source: Ensembl
    4. oxaloacetate metabolic process Source: Ensembl
    5. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
    Alternative name(s):
    Cytosolic malate dehydrogenase
    Gene namesi
    Name:Mdh1
    Synonyms:Mor2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97051. Mdh1.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113410Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei110 – 1101N6-succinyllysine1 Publication
    Modified residuei118 – 1181N6-acetyllysine1 Publication
    Modified residuei121 – 1211N6-acetyllysineBy similarity
    Modified residuei214 – 2141N6-succinyllysine1 Publication
    Modified residuei298 – 2981N6-acetyllysine; alternateBy similarity
    Modified residuei298 – 2981N6-succinyllysine; alternate1 Publication
    Modified residuei318 – 3181N6-succinyllysine1 Publication
    Modified residuei333 – 3331PhosphoserineBy similarity

    Post-translational modificationi

    ISGylated.1 Publication
    Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP14152.
    PaxDbiP14152.
    PRIDEiP14152.

    2D gel databases

    COMPLUYEAST-2DPAGEP14152.
    REPRODUCTION-2DPAGEP14152.
    SWISS-2DPAGEP14152.
    UCD-2DPAGEP14152.

    PTM databases

    PhosphoSiteiP14152.

    Expressioni

    Gene expression databases

    ArrayExpressiP14152.
    BgeeiP14152.
    CleanExiMM_MDH1.
    GenevestigatoriP14152.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    IntActiP14152. 8 interactions.
    MINTiMINT-1869753.

    Structurei

    3D structure databases

    ProteinModelPortaliP14152.
    SMRiP14152. Positions 2-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0039.
    GeneTreeiENSGT00530000063410.
    HOGENOMiHOG000220953.
    HOVERGENiHBG006340.
    InParanoidiP14152.
    KOiK00025.
    OMAiNCLIASK.
    OrthoDBiEOG78H3TM.
    PhylomeDBiP14152.
    TreeFamiTF105826.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_01517. Malate_dehydrog_2.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR011274. Malate_DH_NAD-dep_euk.
    IPR010945. Malate_DH_type2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR23382. PTHR23382. 1 hit.
    PfamiPF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
    TIGR01758. MDH_euk_cyt. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14152-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL    50
    DGVLMELQDC ALPLLQDVIA TDKEEIAFKD LDVAVLVGSM PRREGMERKD 100
    LLKANVKIFK SQGTALEKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE 150
    NFSCLTRLDH NRAKSQIALK LGVTADDVKN VIIWGNHSST QYPDVNHAKV 200
    KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL SSAMSAAKAI 250
    ADHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 300
    EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA 334
    Length:334
    Mass (Da):36,511
    Last modified:January 23, 2007 - v3
    Checksum:i3B9F00372AA939DF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti92 – 921R → I in BAB23897. (PubMed:16141072)Curated
    Sequence conflicti177 – 1771D → N in BAE37915. (PubMed:16141072)Curated
    Sequence conflicti288 – 2881F → L(PubMed:3312200)Curated
    Sequence conflicti288 – 2881F → L(PubMed:3172222)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29462 mRNA. Translation: AAA39510.1.
    M36084 Genomic DNA. Translation: AAA37423.1.
    AK005237 mRNA. Translation: BAB23897.1.
    AK164785 mRNA. Translation: BAE37915.1.
    AK168545 mRNA. Translation: BAE40421.1.
    AL663049 Genomic DNA. Translation: CAI24411.1.
    BC050940 mRNA. Translation: AAH50940.2.
    CCDSiCCDS24466.1.
    PIRiS02654. DEMSMC.
    RefSeqiNP_032644.3. NM_008618.3.
    UniGeneiMm.212703.

    Genome annotation databases

    EnsembliENSMUST00000102874; ENSMUSP00000099938; ENSMUSG00000020321.
    GeneIDi17449.
    KEGGimmu:17449.
    UCSCiuc007idv.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29462 mRNA. Translation: AAA39510.1 .
    M36084 Genomic DNA. Translation: AAA37423.1 .
    AK005237 mRNA. Translation: BAB23897.1 .
    AK164785 mRNA. Translation: BAE37915.1 .
    AK168545 mRNA. Translation: BAE40421.1 .
    AL663049 Genomic DNA. Translation: CAI24411.1 .
    BC050940 mRNA. Translation: AAH50940.2 .
    CCDSi CCDS24466.1.
    PIRi S02654. DEMSMC.
    RefSeqi NP_032644.3. NM_008618.3.
    UniGenei Mm.212703.

    3D structure databases

    ProteinModelPortali P14152.
    SMRi P14152. Positions 2-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14152. 8 interactions.
    MINTi MINT-1869753.

    Chemistry

    ChEMBLi CHEMBL2176827.

    PTM databases

    PhosphoSitei P14152.

    2D gel databases

    COMPLUYEAST-2DPAGE P14152.
    REPRODUCTION-2DPAGE P14152.
    SWISS-2DPAGE P14152.
    UCD-2DPAGE P14152.

    Proteomic databases

    MaxQBi P14152.
    PaxDbi P14152.
    PRIDEi P14152.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102874 ; ENSMUSP00000099938 ; ENSMUSG00000020321 .
    GeneIDi 17449.
    KEGGi mmu:17449.
    UCSCi uc007idv.2. mouse.

    Organism-specific databases

    CTDi 4190.
    MGIi MGI:97051. Mdh1.

    Phylogenomic databases

    eggNOGi COG0039.
    GeneTreei ENSGT00530000063410.
    HOGENOMi HOG000220953.
    HOVERGENi HBG006340.
    InParanoidi P14152.
    KOi K00025.
    OMAi NCLIASK.
    OrthoDBi EOG78H3TM.
    PhylomeDBi P14152.
    TreeFami TF105826.

    Miscellaneous databases

    ChiTaRSi MDH1. mouse.
    NextBioi 292088.
    PROi P14152.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14152.
    Bgeei P14152.
    CleanExi MM_MDH1.
    Genevestigatori P14152.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_01517. Malate_dehydrog_2.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    IPR001252. Malate_DH_AS.
    IPR011274. Malate_DH_NAD-dep_euk.
    IPR010945. Malate_DH_type2.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR23382. PTHR23382. 1 hit.
    Pfami PF02866. Ldh_1_C. 1 hit.
    PF00056. Ldh_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01759. MalateDH-SF1. 1 hit.
    TIGR01758. MDH_euk_cyt. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase."
      Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S., Kuramitsu S., Kagamiyama H., Morino Y.
      J. Biol. Chem. 262:15127-15131(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural organization of the mouse cytosolic malate dehydrogenase gene: comparison with that of the mouse mitochondrial malate dehydrogenase gene."
      Setoyama C., Joh T., Tsuzuki T., Shimada K.
      J. Mol. Biol. 202:355-364(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C3H/He.
      Tissue: Liver.
    3. "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: Cerebellum, Mammary gland and Stomach.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    6. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 80-92; 126-142; 171-199; 206-230; 299-310 AND 325-334, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    7. Cited for: ISGYLATION.
    8. "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-110; LYS-214; LYS-298 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiMDHC_MOUSE
    AccessioniPrimary (citable) accession number: P14152
    Secondary accession number(s): Q3TP22, Q80Y13, Q9DB45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 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