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UniProtKB/Swiss-Prot entry P00338


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LDHA_HUMAN
Primary accession number P00338
Secondary accession numbers Q53G53 Q6IBM7 Q6ZNV1
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 111)
Name and origin of the protein
Protein name L-lactate dehydrogenase A chain
Synonyms LDH-A
EC 1.1.1.27
LDH muscle subunit
LDH-M
Renal carcinoma antigen NY-REN-59
Cell proliferation-inducing gene 19 protein
Gene name
Name: LDHA
ORFNames: PIG19
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3838278 [NCBI, ExPASy, EBI, Israel, Japan]
Tsujibo H., Tiano H.F., Li S.S.-L.;
"Nucleotide sequences of the cDNA and an intronless pseudogene for human lactate dehydrogenase-A isozyme.";
Eur. J. Biochem. 147:9-15(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3000353 [NCBI, ExPASy, EBI, Israel, Japan]
Chung F.Z., Tsujibo H., Bhattacharyya U., Sharief F.S., Li S.S.-L.;
"Genomic organization of human lactate dehydrogenase-A gene.";
Biochem. J. 231:537-541(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kim J.W.;
"Identification of a human proliferation-inducing gene.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-222.
TISSUE=Gastric carcinoma;
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
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, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-254.
DOI=10.1007/BF00204925; PubMed=1959923 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa M., Sudo K., Li S.S., Kanno T.;
"Genotypic analysis of families with lactate dehydrogenase A (M) deficiency by selective DNA amplification.";
Hum. Genet. 88:34-38(1991).
[10]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; PubMed=10508479 [NCBI, ExPASy, EBI, Israel, Japan]
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADH AND SUBSTRATE ANALOG, AND HOMOTETRAMERIZATION.
DOI=10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#; PubMed=11276087 [NCBI, ExPASy, EBI, Israel, Japan]
Read J.A., Winter V.J., Eszes C.M., Sessions R.B., Brady R.L.;
"Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.";
Proteins 43:175-185(2001).
[14]
VARIANT CYS-315.
PubMed=1445373 [NCBI, ExPASy, EBI, Israel, Japan]
Sudo K., Maekawa M., Shioya M., Ikeda K., Takahashi N., Isogai Y., Li S.S.-L., Kanno T., Machida K., Toriumi J.;
"Molecular analysis of genetic mutation in electrophoretic variant of human lactate dehydrogenase-A(M) subunit.";
Biochem. Int. 27:1051-1057(1992).
[15]
VARIANT GLU-222.
PubMed=7908613 [NCBI, ExPASy, EBI, Israel, Japan]
Maekawa M., Sudo K., Kobayashi A., Sugiyama E., Li S.S.-L., Kanno T.;
"Fast-type electrophoretic variant of lactate dehydrogenase M(A) and comparison with other missense mutations in lactate dehydrogenase M(A) and H(B) genes.";
Clin. Chem. 40:665-668(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X02152; CAA26088.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03077; CAA26879.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03078; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03079; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03080; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03081; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03082; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03083; CAA26879.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY423727; AAS00490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK130587; BAC85389.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456775; CAG33056.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541714; CAG46515.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223078; BAD96798.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC067223; AAH67223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S66853; AAB20418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00347; DEHULM.
RefSeq NP_005557.1; -.
UniGene Hs.2795
3D structure databases
PDB
1I10; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-332.[ExPASy / RCSB / EBI]
PDBsum 1I10; -.
ModBase P00338.
Protein-protein interaction databases
IntAct P00338; -.
PTM databases
PhosphoSite P00338; -.
2D gel databases
Aarhus/Ghent-2DPAGE 2207; NEPHGE.
Cornea-2DPAGE P00338; -.
DOSAC-COBS-2DPAGE P00338; -.
OGP P00338; -.
REPRODUCTION-2DPAGE IPI00217966; -.
Organism-specific databases
H-InvDB HIX0009487; -.
HGNC HGNC:6535; LDHA.
GenAtlas LDHA.
HPA CAB015336; -.
MIM 150000; gene+phenotype. [NCBI / EBI]
Orphanet 2364; Lactate dehydrogenase deficiency.
PharmGKB PA30319; -.
GeneCards P00338.
Gene expression databases
ArrayExpress P00338; -.
CleanEx HS_LDHA; -.
GermOnline ENSG00000134333; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from ProtInc).
GO:0004459; Molecular function: L-lactate dehydrogenase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001557; L-lactate/malate_DHase.
IPR011304; L-lactate_DHase.
IPR001236; Lactate/malate_DHase.
IPR015955; Lactate_DHase/Glyco_Ohase_4_C.
Graphical view of domain structure.
Gene3D G3DSA:3.90.110.10; lact_mal_DH; 1.
Pfam PF02866; Ldh_1_C; 1.
PF00056; Ldh_1_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000102; Lac_mal_DH; 1.
PRINTS PR00086; LLDHDRGNASE.
TIGRFAMs TIGR01771; L-LDH-NAD; 1.
PROSITE PS00064; L_LDH; 1.
BLOCKS P00338.
ProtoNet P00338.
Proteomic databases
PeptideAtlas P00338; -.
Genome annotation databases
Ensembl ENSG00000134333; Homo sapiens. [Contig view]
GeneID 3939; -.
KEGG hsa:3939; -.
NMPDR fig|9606.3.peg.5346; -.
Phylogenomic databases
HOGENOM P00338; -.
HOVERGEN P00338; -.
Other
DrugBank DB00157; NADH.
LinkHub P00338; -.
NextBio 15469; -.
SOURCE LDHA; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing; Disease mutation; Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   332  331     L-lactate dehydrogenase A chain. PRO_0000168411
NP_BIND   29    57  29     NAD. 
ACT_SITE   193   193        Proton acceptor. 
BINDING   99    99        NAD. 
BINDING   106   106        Substrate. 
BINDING   138   138        NAD or substrate. 
BINDING   169   169        Substrate. 
BINDING   248   248        Substrate. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   239   239        Phosphotyrosine. 
VAR_SEQ   230   274        VHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRR VHPVS -> CRYTLGDPKGAAILKSSDVISFHCLGYNRILGGGCACCPF YLICD (in isoform 2). VSP_014261
VARIANT   222   222  1     K -> E. VAR_004180 [3D]
VARIANT   315   315  1     R -> C (in LDHA deficiency). VAR_004181 [3D]
HELIX   4     8  5      
STRAND   9    13  5      
STRAND   20    26  7      
HELIX   30    41  12      
STRAND   46    51  6      
HELIX   55    66  12      
HELIX   67    71  5      
STRAND   76    79  4      
HELIX   83    86  4      
STRAND   90    94  5      
HELIX   106   109  4      
HELIX   110   127  18      
STRAND   132   135  4      
STRAND   137   139  3      
HELIX   140   151  12      
HELIX   155   157  3      
STRAND   158   160  3      
HELIX   164   178  15      
HELIX   182   184  3      
STRAND   189   191  3      
HELIX   201   203  3      
HELIX   211   214  4      
TURN   216   219  4      
STRAND   220   222  3      
HELIX   228   245  18      
HELIX   250   264  15      
STRAND   269   276  8      
STRAND   288   296  9      
STRAND   299   304  6      
HELIX   310   327  18      
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 36689 Da [This is the MW of the unprocessed precursor] CRC64: 401E8604CEB7F908 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG 

        70         80         90        100        110        120 
EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI 

       130        140        150        160        170        180 
IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV 

       190        200        210        220        230        240 
HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE 

       250        260        270        280        290        300 
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI 

       310        320        330 
SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF 

P00338 in FASTA format

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