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P06151

- LDHA_MOUSE

UniProt

P06151 - LDHA_MOUSE

Protein

L-lactate dehydrogenase A chain

Gene

Ldha

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-lactate + NAD+ = pyruvate + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991NADBy similarity
    Binding sitei106 – 1061SubstrateBy similarity
    Binding sitei138 – 1381NAD or substrateBy similarity
    Binding sitei169 – 1691SubstrateBy similarity
    Active sitei193 – 1931Proton acceptorBy similarity
    Binding sitei248 – 2481SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 5729NADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. L-lactate dehydrogenase activity Source: MGI
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. cellular response to extracellular stimulus Source: MGI
    3. glycolytic process Source: UniProtKB-KW
    4. lactate biosynthetic process from pyruvate Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00554; UER00611.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-lactate dehydrogenase A chain (EC:1.1.1.27)
    Short name:
    LDH-A
    Alternative name(s):
    LDH muscle subunit
    Short name:
    LDH-M
    Gene namesi
    Name:Ldha
    Synonyms:Ldh-1, Ldh1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:96759. Ldha.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. mitochondrion Source: MGI
    3. sperm fibrous sheath Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168414Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
    Modified residuei5 – 51N6-succinyllysine; alternate1 Publication
    Modified residuei14 – 141N6-acetyllysineBy similarity
    Modified residuei57 – 571N6-acetyllysineBy similarity
    Modified residuei81 – 811N6-acetyllysine1 Publication
    Modified residuei118 – 1181N6-acetyllysine; alternate1 Publication
    Modified residuei118 – 1181N6-succinyllysine; alternate1 Publication
    Modified residuei126 – 1261N6-acetyllysine1 Publication
    Modified residuei224 – 2241N6-acetyllysine1 Publication
    Modified residuei232 – 2321N6-acetyllysine1 Publication
    Modified residuei239 – 2391Phosphotyrosine1 Publication
    Modified residuei243 – 2431N6-acetyllysine1 Publication
    Modified residuei318 – 3181N6-acetyllysine; alternate1 Publication
    Modified residuei318 – 3181N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP06151.
    PaxDbiP06151.
    PRIDEiP06151.

    2D gel databases

    REPRODUCTION-2DPAGEP06151.
    SWISS-2DPAGEP06151.
    UCD-2DPAGEP06151.

    PTM databases

    PhosphoSiteiP06151.

    Expressioni

    Gene expression databases

    ArrayExpressiP06151.
    BgeeiP06151.
    CleanExiMM_LDHA.
    GenevestigatoriP06151.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HnrnpdQ606682EBI-444940,EBI-299932

    Protein-protein interaction databases

    BioGridi201127. 5 interactions.
    IntActiP06151. 14 interactions.
    MINTiMINT-1612559.

    Structurei

    3D structure databases

    ProteinModelPortaliP06151.
    SMRiP06151. Positions 4-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213793.
    HOVERGENiHBG000462.
    InParanoidiP06151.
    KOiK00016.
    PhylomeDBiP06151.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPiMF_00488. Lactate_dehydrog.
    InterProiIPR001557. L-lactate/malate_DH.
    IPR011304. L-lactate_DH.
    IPR018177. L-lactate_DH_AS.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    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.
    PRINTSiPR00086. LLDHDRGNASE.
    SUPFAMiSSF56327. SSF56327. 1 hit.
    TIGRFAMsiTIGR01771. L-LDH-NAD. 1 hit.
    PROSITEiPS00064. L_LDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATLKDQLIV NLLKEEQAPQ NKITVVGVGA VGMACAISIL MKDLADELAL    50
    VDVMEDKLKG EMMDLQHGSL FLKTPKIVSS KDYCVTANSK LVIITAGARQ 100
    QEGESRLNLV QRNVNIFKFI IPNIVKYSPH CKLLIVSNPV DILTYVAWKI 150
    SGFPKNRVIG SGCNLDSARF RYLMGERLGV HALSCHGWVL GEHGDSSVPV 200
    WSGVNVAGVS LKSLNPELGT DADKEQWKEV HKQVVDSAYE VIKLKGYTSW 250
    AIGLSVADLA ESIMKNLRRV HPISTMIKGL YGINEDVFLS VPCILGQNGI 300
    SDVVKVTLTP EEEARLKKSA DTLWGIQKEL QF 332
    Length:332
    Mass (Da):36,499
    Last modified:January 23, 2007 - v3
    Checksum:i5AEB41E1E0B95100
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111N → I(PubMed:3996406)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00309 Genomic DNA. Translation: CAA68410.1.
    X02520
    , X02521, X02522, X02523, X02524, X02525, X02526 Genomic DNA. Translation: CAA26360.1.
    U13687 mRNA. Translation: AAA21466.1.
    X03753 Genomic DNA. Translation: CAA27387.1.
    M17516 mRNA. Translation: AAA39424.1.
    CCDSiCCDS21289.1.
    PIRiA25205. DEMSLM.
    I48240.
    RefSeqiNP_034829.1. NM_010699.2.
    UniGeneiMm.29324.

    Genome annotation databases

    EnsembliENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229.
    GeneIDi16828.
    KEGGimmu:16828.
    UCSCiuc009gzm.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00309 Genomic DNA. Translation: CAA68410.1 .
    X02520
    , X02521 , X02522 , X02523 , X02524 , X02525 , X02526 Genomic DNA. Translation: CAA26360.1 .
    U13687 mRNA. Translation: AAA21466.1 .
    X03753 Genomic DNA. Translation: CAA27387.1 .
    M17516 mRNA. Translation: AAA39424.1 .
    CCDSi CCDS21289.1.
    PIRi A25205. DEMSLM.
    I48240.
    RefSeqi NP_034829.1. NM_010699.2.
    UniGenei Mm.29324.

    3D structure databases

    ProteinModelPortali P06151.
    SMRi P06151. Positions 4-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201127. 5 interactions.
    IntActi P06151. 14 interactions.
    MINTi MINT-1612559.

    PTM databases

    PhosphoSitei P06151.

    2D gel databases

    REPRODUCTION-2DPAGE P06151.
    SWISS-2DPAGE P06151.
    UCD-2DPAGE P06151.

    Proteomic databases

    MaxQBi P06151.
    PaxDbi P06151.
    PRIDEi P06151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048209 ; ENSMUSP00000036386 ; ENSMUSG00000063229 .
    GeneIDi 16828.
    KEGGi mmu:16828.
    UCSCi uc009gzm.2. mouse.

    Organism-specific databases

    CTDi 3939.
    MGIi MGI:96759. Ldha.

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213793.
    HOVERGENi HBG000462.
    InParanoidi P06151.
    KOi K00016.
    PhylomeDBi P06151.

    Enzyme and pathway databases

    UniPathwayi UPA00554 ; UER00611 .

    Miscellaneous databases

    ChiTaRSi LDHA. mouse.
    NextBioi 290734.
    PROi P06151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06151.
    Bgeei P06151.
    CleanExi MM_LDHA.
    Genevestigatori P06151.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.110.10. 1 hit.
    HAMAPi MF_00488. Lactate_dehydrog.
    InterProi IPR001557. L-lactate/malate_DH.
    IPR011304. L-lactate_DH.
    IPR018177. L-lactate_DH_AS.
    IPR022383. Lactate/malate_DH_C.
    IPR001236. Lactate/malate_DH_N.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    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.
    PRINTSi PR00086. LLDHDRGNASE.
    SUPFAMi SSF56327. SSF56327. 1 hit.
    TIGRFAMsi TIGR01771. L-LDH-NAD. 1 hit.
    PROSITEi PS00064. L_LDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the mouse lactate dehydrogenase-A functional gene: comparison of the exon-intron organization of dehydrogenase genes."
      Fukasawa K.M., Li S.S.-L.
      Genetics 116:99-105(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/10.
      Tissue: Liver.
    2. "Protein structure and gene organization of mouse lactate dehydrogenase-A isozyme."
      Li S.S.-L., Tiano H.F., Fukasawa K.M., Yagi K., Shimizu M., Sharief F.S., Nakashima Y., Pan Y.E.
      Eur. J. Biochem. 149:215-225(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Lactate dehydrogenase-A mRNAs in mouse testis and somatic tissues containing different 5' noncoding sequences."
      Hiraoka Y., Li S.S.-L.
      J. Genet. Mol. Biol. 1:1-6(1990)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: DBA/2J.
    4. "Nucleotide sequence of the putative regulatory region of mouse lactate dehydrogenase-A gene."
      Fukasawa K.M., Li S.S.-L.
      Biochem. J. 235:435-439(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
    5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-14; 23-73; 82-99; 107-126; 133-149; 158-169; 172-177; 213-228; 233-243; 246-265; 269-315 AND 319-328, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. "Isolation and characterization of a cDNA and a pseudogene for mouse lactate dehydrogenase-A isozyme."
      Akai K., Yagi K., Tiano H.F., Pan Y.-C.E., Shimizu M., Fong K., Jungmann R.A., Li S.S.-L.
      Int. J. Biochem. 17:645-648(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-332.
    7. Cited for: ISGYLATION.
    8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-81; LYS-118; LYS-126; LYS-224; LYS-232; LYS-243 AND LYS-318, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-118 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiLDHA_MOUSE
    AccessioniPrimary (citable) accession number: P06151
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3