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P40925

- MDHC_HUMAN

UniProt

P40925 - MDHC_HUMAN

Protein

Malate dehydrogenase, cytoplasmic

Gene

MDH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.1 Publication
    3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH.1 Publication

    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 – 1621Substrate
    Active sitei187 – 1871Proton acceptorBy similarity

    Regions

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

    GO - Molecular functioni

    1. diiodophenylpyruvate reductase activity Source: UniProtKB-EC
    2. L-malate dehydrogenase activity Source: Reactome
    3. malic enzyme activity Source: ProtInc
    4. NAD binding Source: Ensembl

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular carbohydrate metabolic process Source: InterPro
    3. gluconeogenesis Source: Reactome
    4. glucose metabolic process Source: Reactome
    5. malate metabolic process Source: Ensembl
    6. NADH metabolic process Source: Ensembl
    7. oxaloacetate metabolic process Source: Ensembl
    8. small molecule metabolic process Source: Reactome
    9. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00361-MONOMER.
    ReactomeiREACT_1520. Gluconeogenesis.
    SABIO-RKP40925.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
    Alternative name(s):
    Cytosolic malate dehydrogenase
    Diiodophenylpyruvate reductase (EC:1.1.1.96)
    Gene namesi
    Name:MDH1
    Synonyms:MDHA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6970. MDH1.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30714.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 334333Malate dehydrogenase, cytoplasmicPRO_0000113409Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei110 – 1101N6-succinyllysineBy similarity
    Modified residuei118 – 1181N6-acetyllysine2 Publications
    Modified residuei121 – 1211N6-acetyllysine1 Publication
    Modified residuei214 – 2141N6-succinyllysineBy similarity
    Modified residuei298 – 2981N6-acetyllysine; alternate2 Publications
    Modified residuei298 – 2981N6-succinyllysine; alternateBy similarity
    Modified residuei318 – 3181N6-succinyllysineBy similarity
    Modified residuei333 – 3331Phosphoserine1 Publication

    Post-translational modificationi

    ISGylated.1 Publication
    Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP40925.
    PaxDbiP40925.
    PeptideAtlasiP40925.
    PRIDEiP40925.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00291005.
    UCD-2DPAGEP40925.

    PTM databases

    PhosphoSiteiP40925.

    Expressioni

    Gene expression databases

    ArrayExpressiP40925.
    BgeeiP40925.
    CleanExiHS_MDH1.
    GenevestigatoriP40925.

    Organism-specific databases

    HPAiCAB047333.
    HPA027296.
    HPA054276.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi110355. 21 interactions.
    IntActiP40925. 5 interactions.
    MINTiMINT-4999585.
    STRINGi9606.ENSP00000233114.

    Structurei

    3D structure databases

    ProteinModelPortaliP40925.
    SMRiP40925. Positions 2-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0039.
    HOVERGENiHBG006340.
    InParanoidiP40925.
    KOiK00025.
    OMAiNCLIASK.
    OrthoDBiEOG78H3TM.
    PhylomeDBiP40925.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P40925-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL    50
    DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD 100
    LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE 150
    NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV 200
    KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI 250
    CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV 300
    EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSA 334
    Length:334
    Mass (Da):36,426
    Last modified:January 23, 2007 - v4
    Checksum:i5F7ED9789CA1DB55
    GO
    Isoform 2 (identifier: P40925-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-89: Missing.

    Show »
    Length:245
    Mass (Da):27,025
    Checksum:iDEBC412374575BD9
    GO
    Isoform 3 (identifier: P40925-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRRCSYFPKDVTVFDKDDK

    Note: No experimental confirmation available.

    Show »
    Length:352
    Mass (Da):38,628
    Checksum:i058B25735B30BBC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Q → R in BAH12223. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8989Missing in isoform 2. 1 PublicationVSP_042661Add
    BLAST
    Alternative sequencei1 – 11M → MRRCSYFPKDVTVFDKDDK in isoform 3. 1 PublicationVSP_045847

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55654 mRNA. Translation: BAA09513.1.
    U20352 mRNA. Translation: AAC16436.1.
    CR457405 mRNA. Translation: CAG33686.1.
    AK295931 mRNA. Translation: BAH12223.1.
    AK300719 mRNA. Translation: BAG62394.1.
    AK312331 mRNA. Translation: BAG35252.1.
    AC016734 Genomic DNA. Translation: AAY14893.1.
    CH471053 Genomic DNA. Translation: EAW99959.1.
    BC001484 mRNA. Translation: AAH01484.1.
    CCDSiCCDS1874.1. [P40925-1]
    CCDS56121.1. [P40925-3]
    CCDS56122.1. [P40925-2]
    PIRiG01650.
    RefSeqiNP_001186040.1. NM_001199111.1. [P40925-3]
    NP_001186041.1. NM_001199112.1. [P40925-2]
    NP_005908.1. NM_005917.3. [P40925-1]
    XP_005264377.1. XM_005264320.1. [P40925-2]
    UniGeneiHs.526521.

    Genome annotation databases

    EnsembliENST00000233114; ENSP00000233114; ENSG00000014641. [P40925-1]
    ENST00000539945; ENSP00000438144; ENSG00000014641. [P40925-3]
    ENST00000544381; ENSP00000446395; ENSG00000014641. [P40925-2]
    GeneIDi4190.
    KEGGihsa:4190.
    UCSCiuc002scj.2. human. [P40925-1]

    Polymorphism databases

    DMDMi1708967.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Malate dehydrogenase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55654 mRNA. Translation: BAA09513.1 .
    U20352 mRNA. Translation: AAC16436.1 .
    CR457405 mRNA. Translation: CAG33686.1 .
    AK295931 mRNA. Translation: BAH12223.1 .
    AK300719 mRNA. Translation: BAG62394.1 .
    AK312331 mRNA. Translation: BAG35252.1 .
    AC016734 Genomic DNA. Translation: AAY14893.1 .
    CH471053 Genomic DNA. Translation: EAW99959.1 .
    BC001484 mRNA. Translation: AAH01484.1 .
    CCDSi CCDS1874.1. [P40925-1 ]
    CCDS56121.1. [P40925-3 ]
    CCDS56122.1. [P40925-2 ]
    PIRi G01650.
    RefSeqi NP_001186040.1. NM_001199111.1. [P40925-3 ]
    NP_001186041.1. NM_001199112.1. [P40925-2 ]
    NP_005908.1. NM_005917.3. [P40925-1 ]
    XP_005264377.1. XM_005264320.1. [P40925-2 ]
    UniGenei Hs.526521.

    3D structure databases

    ProteinModelPortali P40925.
    SMRi P40925. Positions 2-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110355. 21 interactions.
    IntActi P40925. 5 interactions.
    MINTi MINT-4999585.
    STRINGi 9606.ENSP00000233114.

    Chemistry

    BindingDBi P40925.
    ChEMBLi CHEMBL3560.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P40925.

    Polymorphism databases

    DMDMi 1708967.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00291005.
    UCD-2DPAGE P40925.

    Proteomic databases

    MaxQBi P40925.
    PaxDbi P40925.
    PeptideAtlasi P40925.
    PRIDEi P40925.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233114 ; ENSP00000233114 ; ENSG00000014641 . [P40925-1 ]
    ENST00000539945 ; ENSP00000438144 ; ENSG00000014641 . [P40925-3 ]
    ENST00000544381 ; ENSP00000446395 ; ENSG00000014641 . [P40925-2 ]
    GeneIDi 4190.
    KEGGi hsa:4190.
    UCSCi uc002scj.2. human. [P40925-1 ]

    Organism-specific databases

    CTDi 4190.
    GeneCardsi GC02P063727.
    HGNCi HGNC:6970. MDH1.
    HPAi CAB047333.
    HPA027296.
    HPA054276.
    MIMi 154200. gene.
    neXtProti NX_P40925.
    PharmGKBi PA30714.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0039.
    HOVERGENi HBG006340.
    InParanoidi P40925.
    KOi K00025.
    OMAi NCLIASK.
    OrthoDBi EOG78H3TM.
    PhylomeDBi P40925.
    TreeFami TF105826.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00361-MONOMER.
    Reactomei REACT_1520. Gluconeogenesis.
    SABIO-RK P40925.

    Miscellaneous databases

    ChiTaRSi MDH1. human.
    GenomeRNAii 4190.
    NextBioi 16510.
    PROi P40925.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40925.
    Bgeei P40925.
    CleanExi HS_MDH1.
    Genevestigatori P40925.

    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. "Molecular cloning and mapping of a human cDNA for cytosolic malate dehydrogenase (MDH1)."
      Tanaka T., Inazawa J., Nakamura Y.
      Genomics 32:128-130(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    2. Lo A.S.Y., Waye M.M.Y.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Cerebellum and Substantia nigra.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Placenta.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 205-213 AND 324-334, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. "The human myocardial two-dimensional gel protein database: update 1994."
      Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
      Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 168-181.
      Tissue: Heart.
    10. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 180-201 AND 299-310, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    11. "Biochemical and genetic identity of alpha-keto acid reductase and cytoplasmic malate dehydrogenase from human erythrocytes."
      Friedrich C.A., Ferrell R.E., Siciliano M.J., Kitto G.B.
      Ann. Hum. Genet. 52:25-37(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    12. Cited for: ISGYLATION.
    13. "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-118 AND LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity."
      Kim E.Y., Kim W.K., Kang H.J., Kim J.H., Chung S.J., Seo Y.S., Park S.G., Lee S.C., Bae K.H.
      J. Lipid Res. 53:1864-1876(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-118; LYS-121 AND LYS-298.

    Entry informationi

    Entry nameiMDHC_HUMAN
    AccessioniPrimary (citable) accession number: P40925
    Secondary accession number(s): B2R5V5
    , B4DUN2, B7Z3I7, F5H098, Q6I9V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3