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P00338

- LDHA_HUMAN

UniProt

P00338 - LDHA_HUMAN

Protein

L-lactate dehydrogenase A chain

Gene

LDHA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 2 (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 – 991NAD1 Publication
    Binding sitei106 – 1061Substrate
    Binding sitei138 – 1381NAD or substrate1 Publication
    Binding sitei169 – 1691Substrate
    Active sitei193 – 1931Proton acceptor
    Binding sitei248 – 2481Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi29 – 5729NAD1 PublicationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. cellular metabolic process Source: Reactome
    3. cellular response to extracellular stimulus Source: Ensembl
    4. glycolytic process Source: UniProtKB
    5. pyruvate metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. substantia nigra development Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_2071. Pyruvate metabolism.
    SABIO-RKP00338.
    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):
    Cell proliferation-inducing gene 19 protein
    LDH muscle subunit
    Short name:
    LDH-M
    Renal carcinoma antigen NY-REN-59
    Gene namesi
    Name:LDHA
    ORF Names:PIG19
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6535. LDHA.

    Subcellular locationi

    GO - Cellular componenti

    1. cilium Source: Ensembl
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. mitochondrion Source: Ensembl
    6. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 11 (GSD11) [MIM:612933]: A metabolic disorder that results in exertional myoglobinuria, pain, cramps and easy fatigue.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease

    Organism-specific databases

    MIMi612933. phenotype.
    Orphaneti284426. Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
    PharmGKBiPA30319.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 332331L-lactate dehydrogenase A chainPRO_0000168411Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei5 – 51N6-acetyllysine; alternate1 Publication
    Modified residuei5 – 51N6-succinyllysine; alternateBy similarity
    Modified residuei10 – 101Phosphotyrosine1 Publication
    Modified residuei14 – 141N6-acetyllysine1 Publication
    Modified residuei57 – 571N6-acetyllysine1 Publication
    Modified residuei81 – 811N6-acetyllysine1 Publication
    Modified residuei118 – 1181N6-acetyllysine; alternate1 Publication
    Modified residuei118 – 1181N6-succinyllysine; alternateBy similarity
    Modified residuei126 – 1261N6-acetyllysine1 Publication
    Modified residuei224 – 2241N6-acetyllysineBy similarity
    Modified residuei232 – 2321N6-acetyllysineBy similarity
    Modified residuei239 – 2391PhosphotyrosineBy similarity
    Modified residuei243 – 2431N6-acetyllysineBy similarity
    Modified residuei318 – 3181N6-acetyllysine; alternate1 Publication
    Modified residuei318 – 3181N6-succinyllysine; alternateBy similarity

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP00338.
    PaxDbiP00338.
    PeptideAtlasiP00338.
    PRIDEiP00338.

    2D gel databases

    DOSAC-COBS-2DPAGEP00338.
    OGPiP00338.
    REPRODUCTION-2DPAGEIPI00217966.

    PTM databases

    PhosphoSiteiP00338.

    Expressioni

    Gene expression databases

    ArrayExpressiP00338.
    BgeeiP00338.
    CleanExiHS_LDHA.
    GenevestigatoriP00338.

    Organism-specific databases

    HPAiCAB015336.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSPA8P111424EBI-372327,EBI-351896

    Protein-protein interaction databases

    BioGridi110131. 65 interactions.
    IntActiP00338. 17 interactions.
    MINTiMINT-4998672.
    STRINGi9606.ENSP00000395337.

    Structurei

    Secondary structure

    1
    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 85
    Beta strandi9 – 124
    Beta strandi20 – 267
    Helixi30 – 4112
    Beta strandi46 – 516
    Helixi55 – 6713
    Helixi68 – 714
    Beta strandi77 – 793
    Helixi83 – 864
    Beta strandi90 – 945
    Helixi107 – 12721
    Beta strandi132 – 1354
    Beta strandi137 – 1393
    Helixi140 – 15112
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi164 – 17815
    Helixi182 – 1843
    Beta strandi189 – 1935
    Helixi194 – 1963
    Helixi201 – 2033
    Helixi211 – 2144
    Turni216 – 2194
    Beta strandi220 – 2223
    Helixi228 – 24518
    Helixi250 – 26415
    Beta strandi269 – 2768
    Beta strandi288 – 2969
    Beta strandi299 – 3046
    Helixi310 – 32718

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I10X-ray2.30A/B/C/D/E/F/G/H2-332[»]
    4AJPX-ray2.38A/B/C/D2-332[»]
    4JNKX-ray1.90A/B/C/D2-332[»]
    4L4RX-ray2.10A/H2-332[»]
    4L4SX-ray2.90A/H2-332[»]
    4M49X-ray2.05A/B/C/D2-332[»]
    ProteinModelPortaliP00338.
    SMRiP00338. Positions 2-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00338.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0039.
    HOGENOMiHOG000213793.
    HOVERGENiHBG000462.
    InParanoidiP00338.
    KOiK00016.
    OMAiYAPSAFV.
    OrthoDBiEOG7X0VH3.
    PhylomeDBiP00338.
    TreeFamiTF314963.

    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]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00338-1) [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

    MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL    50
    VDVIEDKLKG EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ 100
    QEGESRLNLV QRNVNIFKFI IPNVVKYSPN CKLLIVSNPV DILTYVAWKI 150
    SGFPKNRVIG SGCNLDSARF RYLMGERLGV HPLSCHGWVL GEHGDSSVPV 200
    WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE VIKLKGYTSW 250
    AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI 300
    SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF 332
    Length:332
    Mass (Da):36,689
    Last modified:January 23, 2007 - v2
    Checksum:i401E8604CEB7F908
    GO
    Isoform 2 (identifier: P00338-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         230-274: VHKQVVESAY...KNLRRVHPVS → CRYTLGDPKG...ACCPFYLICD
         275-332: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:274
    Mass (Da):30,057
    Checksum:iD43CB4ACB426D6F0
    GO
    Isoform 3 (identifier: P00338-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:361
    Mass (Da):39,837
    Checksum:iD47D88F7C90BF11D
    GO
    Isoform 4 (identifier: P00338-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         82-139: Missing.

    Show »
    Length:274
    Mass (Da):30,205
    Checksum:i1EB83D11978134AD
    GO
    Isoform 5 (identifier: P00338-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         237-241: SAYEV → RVFTE
         242-332: Missing.

    Show »
    Length:241
    Mass (Da):26,712
    Checksum:i20B4A3E33A1ED002
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti161 – 1611S → R.
    Corresponds to variant rs5030621 [ dbSNP | Ensembl ].
    VAR_059374
    Natural varianti222 – 2221K → E.2 Publications
    VAR_004180
    Natural varianti315 – 3151R → C.1 Publication
    VAR_004181

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGEPSGGYTYTQTSIFLFHA KIPFGSKSNM in isoform 3. 1 PublicationVSP_042206
    Alternative sequencei82 – 13958Missing in isoform 4. 1 PublicationVSP_042786Add
    BLAST
    Alternative sequencei230 – 27445VHKQV…VHPVS → CRYTLGDPKGAAILKSSDVI SFHCLGYNRILGGGCACCPF YLICD in isoform 2. 1 PublicationVSP_014261Add
    BLAST
    Alternative sequencei237 – 2415SAYEV → RVFTE in isoform 5. CuratedVSP_042788
    Alternative sequencei242 – 33291Missing in isoform 5. CuratedVSP_042789Add
    BLAST
    Alternative sequencei275 – 33258Missing in isoform 2. 1 PublicationVSP_042787Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02152 mRNA. Translation: CAA26088.1.
    X03077
    , X03078, X03079, X03080, X03081, X03082, X03083 Genomic DNA. Translation: CAA26879.1.
    AY423727 mRNA. Translation: AAS00490.1.
    AK130587 mRNA. Translation: BAC85389.1.
    AK296667 mRNA. Translation: BAG59264.1.
    AK298834 mRNA. Translation: BAH12879.1.
    CR456775 mRNA. Translation: CAG33056.1.
    CR541714 mRNA. Translation: CAG46515.1.
    AK223078 mRNA. Translation: BAD96798.1.
    AC084117 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68395.1.
    CH471064 Genomic DNA. Translation: EAW68396.1.
    BC067223 mRNA. Translation: AAH67223.1.
    S66853 Genomic DNA. Translation: AAB20418.1.
    CCDSiCCDS44549.1. [P00338-4]
    CCDS53609.1. [P00338-3]
    CCDS53610.1. [P00338-2]
    CCDS53611.1. [P00338-5]
    CCDS7839.1. [P00338-1]
    PIRiA00347. DEHULM.
    RefSeqiNP_001128711.1. NM_001135239.1. [P00338-4]
    NP_001158886.1. NM_001165414.1. [P00338-3]
    NP_001158887.1. NM_001165415.1. [P00338-2]
    NP_001158888.1. NM_001165416.1. [P00338-5]
    NP_005557.1. NM_005566.3. [P00338-1]
    UniGeneiHs.2795.

    Genome annotation databases

    EnsembliENST00000227157; ENSP00000227157; ENSG00000134333. [P00338-5]
    ENST00000379412; ENSP00000368722; ENSG00000134333. [P00338-1]
    ENST00000396222; ENSP00000379524; ENSG00000134333. [P00338-2]
    ENST00000422447; ENSP00000395337; ENSG00000134333. [P00338-1]
    ENST00000430553; ENSP00000406172; ENSG00000134333. [P00338-4]
    ENST00000540430; ENSP00000445175; ENSG00000134333. [P00338-3]
    ENST00000542179; ENSP00000445331; ENSG00000134333. [P00338-1]
    GeneIDi3939.
    KEGGihsa:3939.
    UCSCiuc001mok.3. human. [P00338-1]
    uc001mol.3. human. [P00338-5]
    uc009yho.2. human. [P00338-4]
    uc010rdd.2. human. [P00338-3]
    uc021qep.1. human. [P00338-2]

    Polymorphism databases

    DMDMi126047.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Lactate dehydrogenase entry

    Protein Spotlight

    Another dark horse - Issue 109 of September 2009

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02152 mRNA. Translation: CAA26088.1 .
    X03077
    , X03078 , X03079 , X03080 , X03081 , X03082 , X03083 Genomic DNA. Translation: CAA26879.1 .
    AY423727 mRNA. Translation: AAS00490.1 .
    AK130587 mRNA. Translation: BAC85389.1 .
    AK296667 mRNA. Translation: BAG59264.1 .
    AK298834 mRNA. Translation: BAH12879.1 .
    CR456775 mRNA. Translation: CAG33056.1 .
    CR541714 mRNA. Translation: CAG46515.1 .
    AK223078 mRNA. Translation: BAD96798.1 .
    AC084117 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68395.1 .
    CH471064 Genomic DNA. Translation: EAW68396.1 .
    BC067223 mRNA. Translation: AAH67223.1 .
    S66853 Genomic DNA. Translation: AAB20418.1 .
    CCDSi CCDS44549.1. [P00338-4 ]
    CCDS53609.1. [P00338-3 ]
    CCDS53610.1. [P00338-2 ]
    CCDS53611.1. [P00338-5 ]
    CCDS7839.1. [P00338-1 ]
    PIRi A00347. DEHULM.
    RefSeqi NP_001128711.1. NM_001135239.1. [P00338-4 ]
    NP_001158886.1. NM_001165414.1. [P00338-3 ]
    NP_001158887.1. NM_001165415.1. [P00338-2 ]
    NP_001158888.1. NM_001165416.1. [P00338-5 ]
    NP_005557.1. NM_005566.3. [P00338-1 ]
    UniGenei Hs.2795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1I10 X-ray 2.30 A/B/C/D/E/F/G/H 2-332 [» ]
    4AJP X-ray 2.38 A/B/C/D 2-332 [» ]
    4JNK X-ray 1.90 A/B/C/D 2-332 [» ]
    4L4R X-ray 2.10 A/H 2-332 [» ]
    4L4S X-ray 2.90 A/H 2-332 [» ]
    4M49 X-ray 2.05 A/B/C/D 2-332 [» ]
    ProteinModelPortali P00338.
    SMRi P00338. Positions 2-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110131. 65 interactions.
    IntActi P00338. 17 interactions.
    MINTi MINT-4998672.
    STRINGi 9606.ENSP00000395337.

    Chemistry

    BindingDBi P00338.
    ChEMBLi CHEMBL4835.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P00338.

    Polymorphism databases

    DMDMi 126047.

    2D gel databases

    DOSAC-COBS-2DPAGE P00338.
    OGPi P00338.
    REPRODUCTION-2DPAGE IPI00217966.

    Proteomic databases

    MaxQBi P00338.
    PaxDbi P00338.
    PeptideAtlasi P00338.
    PRIDEi P00338.

    Protocols and materials databases

    DNASUi 3939.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227157 ; ENSP00000227157 ; ENSG00000134333 . [P00338-5 ]
    ENST00000379412 ; ENSP00000368722 ; ENSG00000134333 . [P00338-1 ]
    ENST00000396222 ; ENSP00000379524 ; ENSG00000134333 . [P00338-2 ]
    ENST00000422447 ; ENSP00000395337 ; ENSG00000134333 . [P00338-1 ]
    ENST00000430553 ; ENSP00000406172 ; ENSG00000134333 . [P00338-4 ]
    ENST00000540430 ; ENSP00000445175 ; ENSG00000134333 . [P00338-3 ]
    ENST00000542179 ; ENSP00000445331 ; ENSG00000134333 . [P00338-1 ]
    GeneIDi 3939.
    KEGGi hsa:3939.
    UCSCi uc001mok.3. human. [P00338-1 ]
    uc001mol.3. human. [P00338-5 ]
    uc009yho.2. human. [P00338-4 ]
    uc010rdd.2. human. [P00338-3 ]
    uc021qep.1. human. [P00338-2 ]

    Organism-specific databases

    CTDi 3939.
    GeneCardsi GC11P018415.
    HGNCi HGNC:6535. LDHA.
    HPAi CAB015336.
    MIMi 150000. gene.
    612933. phenotype.
    neXtProti NX_P00338.
    Orphaneti 284426. Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
    PharmGKBi PA30319.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0039.
    HOGENOMi HOG000213793.
    HOVERGENi HBG000462.
    InParanoidi P00338.
    KOi K00016.
    OMAi YAPSAFV.
    OrthoDBi EOG7X0VH3.
    PhylomeDBi P00338.
    TreeFami TF314963.

    Enzyme and pathway databases

    UniPathwayi UPA00554 ; UER00611 .
    Reactomei REACT_2071. Pyruvate metabolism.
    SABIO-RK P00338.

    Miscellaneous databases

    ChiTaRSi LDHA. human.
    EvolutionaryTracei P00338.
    GeneWikii LDHA.
    GenomeRNAii 3939.
    NextBioi 15469.
    PROi P00338.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00338.
    Bgeei P00338.
    CleanExi HS_LDHA.
    Genevestigatori P00338.

    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. "Nucleotide sequences of the cDNA and an intronless pseudogene for human lactate dehydrogenase-A isozyme."
      Tsujibo H., Tiano H.F., Li S.S.-L.
      Eur. J. Biochem. 147:9-15(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic organization of human lactate dehydrogenase-A gene."
      Chung F.Z., Tsujibo H., Bhattacharyya U., Sharief F.S., Li S.S.-L.
      Biochem. J. 231:537-541(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Identification of a human proliferation-inducing gene."
      Kim J.W.
      Submitted (SEP-2003) 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 2; 3 AND 4).
      Tissue: Umbilical cord.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-222.
      Tissue: Gastric carcinoma.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Bone marrow.
    10. Bienvenut W.V.
      Submitted (MAR-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 43-57; 60-73; 77-112; 133-149; 158-169; 233-243; 306-315 AND 319-328, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    11. "Analysis of genetic mutations in human lactate dehydrogenase-A(M) deficiency using DNA conformation polymorphism in combination with polyacrylamide gradient gel and silver staining."
      Maekawa M., Sudo K., Li S.S., Kanno T.
      Biochem. Biophys. Res. Commun. 180:1083-1090(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-121 AND 160-175.
    12. "Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification."
      Maekawa M., Sudo K., Li S.S., Kanno T.
      Hum. Genet. 88:34-38(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-254.
    13. "Molecular characterization of genetic mutation in human lactate dehydrogenase-A (M) deficiency."
      Maekawa M., Sudo K., Kanno T., Li S.S.
      Biochem. Biophys. Res. Commun. 168:677-682(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN GSD11.
    14. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    15. Cited for: ISGYLATION.
    16. "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].
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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 ALA-2; LYS-5; LYS-14; LYS-57; LYS-81; LYS-118; LYS-126 AND LYS-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase."
      Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.
      Proteins 43:175-185(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, HOMOTETRAMERIZATION.
    23. "Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit."
      Sudo K., Maekawa M., Shioya M., Ikeda K., Takahashi N., Isogai Y., Li S.S.-L., Kanno T., Machida K., Toriumi J.
      Biochem. Int. 27:1051-1057(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-315.
    24. "Fast-type electrophoretic variant of lactate dehydrogenase M(A) and comparison with other missense mutations in lactate dehydrogenase M(A) and H(B) genes."
      Maekawa M., Sudo K., Kobayashi A., Sugiyama E., Li S.S.-L., Kanno T.
      Clin. Chem. 40:665-668(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-222.

    Entry informationi

    Entry nameiLDHA_HUMAN
    AccessioniPrimary (citable) accession number: P00338
    Secondary accession number(s): B4DKQ2
    , B7Z5E3, D3DQY3, F8W819, Q53G53, Q6IBM7, Q6ZNV1, Q9UDE8, Q9UDE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 181 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3