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P40926

- MDHM_HUMAN

UniProt

P40926 - MDHM_HUMAN

Protein

Malate dehydrogenase, mitochondrial

Gene

MDH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate + NAD+ = oxaloacetate + NADH.PROSITE-ProRule annotation

    Enzyme regulationi

    Enzyme activity is enhanced by acetylation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571NAD1 Publication
    Binding sitei104 – 1041Substrate1 PublicationPROSITE-ProRule annotation
    Binding sitei110 – 1101Substrate1 PublicationPROSITE-ProRule annotation
    Binding sitei117 – 1171NAD1 Publication
    Binding sitei142 – 1421Substrate1 PublicationPROSITE-ProRule annotation
    Binding sitei176 – 1761Substrate1 PublicationPROSITE-ProRule annotation
    Active sitei200 – 2001Proton acceptorBy similarity
    Binding sitei251 – 2511NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 377NAD1 Publication
    Nucleotide bindingi140 – 1423NAD1 Publication

    GO - Molecular functioni

    1. L-malate dehydrogenase activity Source: UniProtKB
    2. malate dehydrogenase (NADP+) activity Source: Ensembl
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular carbohydrate metabolic process Source: InterPro
    3. cellular metabolic process Source: Reactome
    4. gluconeogenesis Source: Reactome
    5. glucose metabolic process Source: Reactome
    6. internal protein amino acid acetylation Source: UniProtKB
    7. malate metabolic process Source: UniProtKB
    8. NADH metabolic process Source: Ensembl
    9. oxaloacetate metabolic process Source: Ensembl
    10. small molecule metabolic process Source: Reactome
    11. tricarboxylic acid cycle Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07366-MONOMER.
    ReactomeiREACT_1520. Gluconeogenesis.
    REACT_1785. Citric acid cycle (TCA cycle).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
    Gene namesi
    Name:MDH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6971. MDH2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial inner membrane Source: Ensembl
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: UniProtKB
    5. nucleus Source: UniProt
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi185 – 1851K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-301; R-307 and R-314. 1 Publication
    Mutagenesisi301 – 3011K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-307 and R-314. 1 Publication
    Mutagenesisi307 – 3071K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-314. 1 Publication
    Mutagenesisi314 – 3141K → R: No activation of enzyme activity on treatment with TSA or NAM; when associated with R-185; R-301 and R-307. 1 Publication

    Organism-specific databases

    PharmGKBiPA30716.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424MitochondrionBy similarityAdd
    BLAST
    Chaini25 – 338314Malate dehydrogenase, mitochondrialPRO_0000018628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331O-linked (GlcNAc)By similarity
    Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
    Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
    Modified residuei91 – 911N6-acetyllysine; alternateBy similarity
    Modified residuei91 – 911N6-succinyllysine; alternateBy similarity
    Modified residuei165 – 1651N6-acetyllysine1 Publication
    Modified residuei185 – 1851N6-acetyllysine; alternate2 Publications
    Modified residuei185 – 1851N6-succinyllysine; alternateBy similarity
    Modified residuei203 – 2031N6-succinyllysineBy similarity
    Modified residuei215 – 2151N6-acetyllysine; alternateBy similarity
    Modified residuei215 – 2151N6-succinyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-acetyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-malonyllysine; alternateBy similarity
    Modified residuei239 – 2391N6-succinyllysine; alternateBy similarity
    Modified residuei269 – 2691N6-succinyllysineBy similarity
    Modified residuei296 – 2961N6-acetyllysine; alternateBy similarity
    Modified residuei296 – 2961N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-acetyllysine; alternate2 Publications
    Modified residuei301 – 3011N6-succinyllysine; alternateBy similarity
    Modified residuei307 – 3071N6-acetyllysine; alternate1 Publication
    Modified residuei307 – 3071N6-malonyllysine; alternate1 Publication
    Modified residuei307 – 3071N6-succinyllysine; alternateBy similarity
    Modified residuei314 – 3141N6-acetyllysine; alternate2 Publications
    Modified residuei314 – 3141N6-succinyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-acetyllysine; alternateBy similarity
    Modified residuei324 – 3241N6-succinyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
    Modified residuei329 – 3291N6-acetyllysine; alternate1 Publication
    Modified residuei329 – 3291N6-malonyllysine; alternateBy similarity
    Modified residuei335 – 3351N6-acetyllysine; alternate1 Publication
    Modified residuei335 – 3351N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    Acetylation is enhanced by up to 67% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with the appearance of tri-and tetraacetylations. Glucose also increases acetylation by about 60% By similarity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiP40926.
    PaxDbiP40926.
    PRIDEiP40926.

    2D gel databases

    DOSAC-COBS-2DPAGEP40926.
    REPRODUCTION-2DPAGEIPI00291006.
    P40926.
    UCD-2DPAGEP40926.

    PTM databases

    PhosphoSiteiP40926.

    Expressioni

    Gene expression databases

    ArrayExpressiP40926.
    BgeeiP40926.
    CleanExiHS_MDH2.
    GenevestigatoriP40926.

    Organism-specific databases

    HPAiHPA019714.
    HPA019716.
    HPA019848.
    HPA026720.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi110356. 28 interactions.
    IntActiP40926. 12 interactions.
    MINTiMINT-1408946.
    STRINGi9606.ENSP00000327070.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 306
    Turni31 – 333
    Helixi37 – 459
    Beta strandi50 – 6011
    Helixi61 – 699
    Beta strandi71 – 744
    Beta strandi76 – 827
    Turni83 – 853
    Helixi86 – 905
    Beta strandi94 – 985
    Helixi110 – 1134
    Helixi114 – 13118
    Beta strandi135 – 1395
    Helixi144 – 15714
    Beta strandi165 – 1684
    Helixi171 – 18515
    Helixi189 – 1913
    Beta strandi196 – 1983
    Helixi202 – 2043
    Beta strandi205 – 2073
    Helixi209 – 2113
    Helixi220 – 24122
    Helixi249 – 26618
    Beta strandi273 – 2797
    Beta strandi282 – 29514
    Beta strandi298 – 3025
    Helixi310 – 33526

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DFDX-ray1.90A/B/C/D20-338[»]
    ProteinModelPortaliP40926.
    SMRiP40926. Positions 24-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40926.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213792.
    HOVERGENiHBG001662.
    InParanoidiP40926.
    KOiK00026.
    OMAiMVAEAMS.
    OrthoDBiEOG74R1R7.
    PhylomeDBiP40926.
    TreeFamiTF300834.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    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.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11540. PTHR11540. 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.
    TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEiPS00068. MDH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P40926-1) [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

    MLSALARPAS AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV    50
    SRLTLYDIAH TPGVAADLSH IETKAAVKGY LGPEQLPDCL KGCDVVVIPA 100
    GVPRKPGMTR DDLFNTNATI VATLTAACAQ HCPEAMICVI ANPVNSTIPI 150
    TAEVFKKHGV YNPNKIFGVT TLDIVRANTF VAELKGLDPA RVNVPVIGGH 200
    AGKTIIPLIS QCTPKVDFPQ DQLTALTGRI QEAGTEVVKA KAGAGSATLS 250
    MAYAGARFVF SLVDAMNGKE GVVECSFVKS QETECTYFST PLLLGKKGIE 300
    KNLGIGKVSS FEEKMISDAI PELKASIKKG EDFVKTLK 338
    Length:338
    Mass (Da):35,503
    Last modified:November 25, 2008 - v3
    Checksum:iAAB9F5E5B2FBC8CA
    GO
    Isoform 2 (identifier: P40926-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         144-185: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:296
    Mass (Da):30,875
    Checksum:i309B55235F0097F7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti301 – 3011K → R in BAG56955. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91A → V.2 Publications
    Corresponds to variant rs17849553 [ dbSNP | Ensembl ].
    VAR_047787

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei144 – 18542Missing in isoform 2. 1 PublicationVSP_055312Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047470 mRNA. Translation: AAC03787.1.
    AK290779 mRNA. Translation: BAF83468.1.
    AK293460 mRNA. Translation: BAG56955.1.
    AK316587 mRNA. Translation: BAG38175.1.
    AC005077 Genomic DNA. No translation available.
    AC006330 Genomic DNA. No translation available.
    CH471220 Genomic DNA. Translation: EAW71796.1.
    BC001917 mRNA. Translation: AAH01917.1.
    CCDSiCCDS5581.1. [P40926-1]
    CCDS64691.1. [P40926-2]
    RefSeqiNP_001269332.1. NM_001282403.1.
    NP_001269333.1. NM_001282404.1.
    NP_005909.2. NM_005918.3.
    UniGeneiHs.520967.

    Genome annotation databases

    EnsembliENST00000315758; ENSP00000327070; ENSG00000146701. [P40926-1]
    ENST00000432020; ENSP00000408649; ENSG00000146701. [P40926-2]
    GeneIDi4191.
    KEGGihsa:4191.
    UCSCiuc003ueo.3. human. [P40926-1]

    Polymorphism databases

    DMDMi215274114.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Malate dehydrogenase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047470 mRNA. Translation: AAC03787.1 .
    AK290779 mRNA. Translation: BAF83468.1 .
    AK293460 mRNA. Translation: BAG56955.1 .
    AK316587 mRNA. Translation: BAG38175.1 .
    AC005077 Genomic DNA. No translation available.
    AC006330 Genomic DNA. No translation available.
    CH471220 Genomic DNA. Translation: EAW71796.1 .
    BC001917 mRNA. Translation: AAH01917.1 .
    CCDSi CCDS5581.1. [P40926-1 ]
    CCDS64691.1. [P40926-2 ]
    RefSeqi NP_001269332.1. NM_001282403.1.
    NP_001269333.1. NM_001282404.1.
    NP_005909.2. NM_005918.3.
    UniGenei Hs.520967.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DFD X-ray 1.90 A/B/C/D 20-338 [» ]
    ProteinModelPortali P40926.
    SMRi P40926. Positions 24-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110356. 28 interactions.
    IntActi P40926. 12 interactions.
    MINTi MINT-1408946.
    STRINGi 9606.ENSP00000327070.

    Chemistry

    BindingDBi P40926.
    ChEMBLi CHEMBL5917.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P40926.

    Polymorphism databases

    DMDMi 215274114.

    2D gel databases

    DOSAC-COBS-2DPAGE P40926.
    REPRODUCTION-2DPAGE IPI00291006.
    P40926.
    UCD-2DPAGE P40926.

    Proteomic databases

    MaxQBi P40926.
    PaxDbi P40926.
    PRIDEi P40926.

    Protocols and materials databases

    DNASUi 4191.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315758 ; ENSP00000327070 ; ENSG00000146701 . [P40926-1 ]
    ENST00000432020 ; ENSP00000408649 ; ENSG00000146701 . [P40926-2 ]
    GeneIDi 4191.
    KEGGi hsa:4191.
    UCSCi uc003ueo.3. human. [P40926-1 ]

    Organism-specific databases

    CTDi 4191.
    GeneCardsi GC07P075677.
    HGNCi HGNC:6971. MDH2.
    HPAi HPA019714.
    HPA019716.
    HPA019848.
    HPA026720.
    MIMi 154100. gene.
    neXtProti NX_P40926.
    PharmGKBi PA30716.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213792.
    HOVERGENi HBG001662.
    InParanoidi P40926.
    KOi K00026.
    OMAi MVAEAMS.
    OrthoDBi EOG74R1R7.
    PhylomeDBi P40926.
    TreeFami TF300834.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07366-MONOMER.
    Reactomei REACT_1520. Gluconeogenesis.
    REACT_1785. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    ChiTaRSi Mdh2. human.
    EvolutionaryTracei P40926.
    GeneWikii Malate_dehydrogenase_2.
    GenomeRNAii 4191.
    NextBioi 16514.
    PROi P40926.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40926.
    Bgeei P40926.
    CleanExi HS_MDH2.
    Genevestigatori P40926.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    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.
    IPR010097. Malate_DH_type1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11540. PTHR11540. 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 TIGR01772. MDH_euk_gproteo. 1 hit.
    PROSITEi PS00068. MDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human homolog of mouse and pig MDH mRNA."
      Hu G.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-9.
    2. "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 AND 2).
      Tissue: Kidney and Tongue.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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] (ISOFORM 1), VARIANT VAL-9.
      Tissue: Lung.
    6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "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-165; LYS-185; LYS-301; LYS-314; LYS-329 AND LYS-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION AT LYS-185; LYS-301; LYS-307 AND LYS-314, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-185; LYS-301; LYS-307 AND LYS-314.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: MALONYLATION AT LYS-307.
    12. "Crystal structure of human malate dehydrogenase type 2."
      Structural genomics consortium (SGC)
      Submitted (MAR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 20-338 IN COMPLEX WITH NAD AND SUBSTRATE, SUBUNIT.

    Entry informationi

    Entry nameiMDHM_HUMAN
    AccessioniPrimary (citable) accession number: P40926
    Secondary accession number(s): A8K414
    , B2RE78, B4DE44, E9PDB2, O43682
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3