P06151 (LDHA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 138.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: L-lactate dehydrogenase A chain Short name=LDH-A EC=1.1.1.27 Alternative name(s): LDH muscle subunit Short name=LDH-M | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 332 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | (S)-lactate + NAD+ = pyruvate + NADH. |
| Pathway | Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Post-translational modification | ISGylated. Ref.7 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. LDH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein Ubl conjugation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cellular response to extracellular stimulusInferred from direct assay PubMed 10322635. Source: MGI glycolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cilium Inferred from direct assay PubMed 16687649. Source: MGI cytosolInferred from direct assay PubMed 11980919. Source: MGI mitochondrionInferred from direct assay PubMed 18614015. Source: MGI |
| Molecular_function | L-lactate dehydrogenase activity Inferred from direct assay PubMed 7323947. Source: MGI |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Hnrnpd | Q60668 | 2 | EBI-444940,EBI-299932 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 332 | 331 | L-lactate dehydrogenase A chain | PRO_0000168414 | |||||
Regions | |||||||||
| Nucleotide binding | 29 – 57 | 29 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 193 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 99 | 1 | NAD By similarity | ||||||
| Binding site | 106 | 1 | Substrate By similarity | ||||||
| Binding site | 138 | 1 | NAD or substrate By similarity | ||||||
| Binding site | 169 | 1 | Substrate By similarity | ||||||
| Binding site | 248 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 5 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 14 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 57 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 81 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 118 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 126 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 239 | 1 | Phosphotyrosine Ref.8 Ref.9 | ||||||
| Modified residue | 318 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 11 | 1 | N → I Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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, 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] | "Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Mast cell. |
| [9] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, MASS SPECTROMETRY. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y00309 Genomic DNA. Translation: CAA68410.1. X02520 X02526 Genomic DNA. Translation: CAA26360.1.U13687 mRNA. Translation: AAA21466.1. X03753 Genomic DNA. Translation: CAA27387.1. M17516 mRNA. Translation: AAA39424.1. |
| IPI | IPI00319994. |
| PIR | DEMSLM. A25205. I48240. |
| RefSeq | NP_034829.1. NM_010699.2. |
| UniGene | Mm.29324. |
3D structure databases | |
| ProteinModelPortal | P06151. |
| SMR | P06151. Positions 4-332. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P06151. 9 interactions. |
| MINT | MINT-1612559. |
PTM databases | |
| PhosphoSite | P06151. |
2D gel databases | |
| REPRODUCTION-2DPAGE | P06151. |
| SWISS-2DPAGE | P06151. |
| UCD-2DPAGE | P06151. |
Proteomic databases | |
| PaxDb | P06151. |
| PRIDE | P06151. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000048209; ENSMUSP00000036386; ENSMUSG00000063229. |
| GeneID | 16828. |
| KEGG | mmu:16828. |
| UCSC | uc009gzm.2. mouse. |
Organism-specific databases | |
| CTD | 3939. |
| MGI | MGI:96759. Ldha. |
Phylogenomic databases | |
| eggNOG | COG0039. |
| HOGENOM | HOG000213793. |
| HOVERGEN | HBG000462. |
| InParanoid | P06151. |
| KO | K00016. |
| OrthoDB | EOG4RR6HR. |
Enzyme and pathway databases | |
| UniPathway | UPA00554; UER00611. |
Gene expression databases | |
| ArrayExpress | P06151. |
| Bgee | P06151. |
| CleanEx | MM_LDHA. |
| Genevestigator | P06151. |
| GermOnline | ENSMUSG00000063229. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| InterPro | 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] |
| PANTHER | PTHR11540. PTHR11540. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| PRINTS | PR00086. LLDHDRGNASE. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01771. L-LDH-NAD. 1 hit. |
| PROSITE | PS00064. L_LDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | LDHA. mouse. |
| NextBio | 290734. |
| SOURCE | Search... |
Entry information
| Entry name | LDHA_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P06151 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
