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L-lactate dehydrogenase A chain (LDH-A) (EC 1.1.1.27) (Cell proliferation-inducing gene 19 protein) (LDH muscle subunit) (LDH-M) (Renal carcinoma antigen NY-REN-59)

 LDHA_HUMAN              Reviewed;         332 AA.
P00338; B4DKQ2; B7Z5E3; D3DQY3; F8W819; Q53G53; Q6IBM7; Q6ZNV1;
Q9UDE8; Q9UDE9;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 215.
RecName: Full=L-lactate dehydrogenase A chain;
Short=LDH-A;
EC=1.1.1.27;
AltName: Full=Cell proliferation-inducing gene 19 protein;
AltName: Full=LDH muscle subunit;
Short=LDH-M;
AltName: Full=Renal carcinoma antigen NY-REN-59;
Name=LDHA; ORFNames=PIG19;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3838278; DOI=10.1111/j.1432-1033.1985.tb08711.x;
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] (ISOFORM 1).
PubMed=3000353; DOI=10.1042/bj2310537;
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] (ISOFORMS 2; 3 AND 4).
TISSUE=Umbilical cord;
PubMed=14702039; DOI=10.1038/ng1285;
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 GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[10]
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 IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-121 AND 160-175.
PubMed=1953713; DOI=10.1016/S0006-291X(05)81177-5;
Maekawa M., Sudo K., Li S.S., Kanno T.;
"Analysis of genetic mutations in human lactate dehydrogenase-A(M)
deficiency using DNA conformation polymorphism in combination with
polyacrylamide gradient gel and silver staining.";
Biochem. Biophys. Res. Commun. 180:1083-1090(1991).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 250-254.
PubMed=1959923; DOI=10.1007/BF00204925;
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).
[13]
INVOLVEMENT IN GSD11.
PubMed=2334430; DOI=10.1016/0006-291X(90)92374-9;
Maekawa M., Sudo K., Kanno T., Li S.S.;
"Molecular characterization of genetic mutation in human lactate
dehydrogenase-A (M) deficiency.";
Biochem. Biophys. Res. Commun. 168:677-682(1990).
[14]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
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).
[15]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
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.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-14; LYS-57; LYS-81;
LYS-118; LYS-126 AND LYS-318, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-310, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADH AND
SUBSTRATE ANALOG, AND HOMOTETRAMERIZATION.
PubMed=11276087;
DOI=10.1002/1097-0134(20010501)43:2<175::AID-PROT1029>3.0.CO;2-#;
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).
[28]
VARIANT CYS-315.
PubMed=1445373;
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).
[29]
VARIANT GLU-222.
PubMed=7908613;
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).
-!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
-!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
lactate from pyruvate: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11276087}.
-!- INTERACTION:
P11142:HSPA8; NbExp=4; IntAct=EBI-372327, EBI-351896;
P07195:LDHB; NbExp=8; IntAct=EBI-10195200, EBI-358748;
Q499Y8:MAPK10; NbExp=5; IntAct=EBI-10195200, EBI-10241715;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P00338-1; Sequence=Displayed;
Name=2;
IsoId=P00338-2; Sequence=VSP_014261, VSP_042787;
Note=No experimental confirmation available.;
Name=3;
IsoId=P00338-3; Sequence=VSP_042206;
Name=4;
IsoId=P00338-4; Sequence=VSP_042786;
Name=5;
IsoId=P00338-5; Sequence=VSP_042788, VSP_042789;
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- DISEASE: Glycogen storage disease 11 (GSD11) [MIM:612933]: A
metabolic disorder that results in exertional myoglobinuria, pain,
cramps and easy fatigue. {ECO:0000269|PubMed:2334430}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Lactate dehydrogenase entry;
URL="https://en.wikipedia.org/wiki/Lactate_dehydrogenase";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Another dark horse
- Issue 109 of September 2009;
URL="https://web.expasy.org/spotlight/back_issues/109";
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EMBL; X02152; CAA26088.1; -; mRNA.
EMBL; X03077; CAA26879.1; -; Genomic_DNA.
EMBL; X03078; CAA26879.1; JOINED; Genomic_DNA.
EMBL; X03079; CAA26879.1; JOINED; Genomic_DNA.
EMBL; X03080; CAA26879.1; JOINED; Genomic_DNA.
EMBL; X03081; CAA26879.1; JOINED; Genomic_DNA.
EMBL; X03082; CAA26879.1; JOINED; Genomic_DNA.
EMBL; X03083; CAA26879.1; JOINED; Genomic_DNA.
EMBL; AY423727; AAS00490.1; -; mRNA.
EMBL; AK130587; BAC85389.1; -; mRNA.
EMBL; AK296667; BAG59264.1; -; mRNA.
EMBL; AK298834; BAH12879.1; -; mRNA.
EMBL; CR456775; CAG33056.1; -; mRNA.
EMBL; CR541714; CAG46515.1; -; mRNA.
EMBL; AK223078; BAD96798.1; -; mRNA.
EMBL; AC084117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68395.1; -; Genomic_DNA.
EMBL; CH471064; EAW68396.1; -; Genomic_DNA.
EMBL; BC067223; AAH67223.1; -; mRNA.
EMBL; S66853; AAB20418.1; -; Genomic_DNA.
CCDS; CCDS44549.1; -. [P00338-4]
CCDS; CCDS53609.1; -. [P00338-3]
CCDS; CCDS53610.1; -. [P00338-2]
CCDS; CCDS53611.1; -. [P00338-5]
CCDS; CCDS7839.1; -. [P00338-1]
PIR; A00347; DEHULM.
RefSeq; NP_001128711.1; NM_001135239.1. [P00338-4]
RefSeq; NP_001158886.1; NM_001165414.1. [P00338-3]
RefSeq; NP_001158887.1; NM_001165415.1. [P00338-2]
RefSeq; NP_001158888.1; NM_001165416.1. [P00338-5]
RefSeq; NP_005557.1; NM_005566.3. [P00338-1]
UniGene; Hs.2795; -.
PDB; 1I10; X-ray; 2.30 A; A/B/C/D/E/F/G/H=2-332.
PDB; 4AJP; X-ray; 2.38 A; A/B/C/D=2-332.
PDB; 4JNK; X-ray; 1.90 A; A/B/C/D=2-332.
PDB; 4L4R; X-ray; 2.10 A; A/H=2-332.
PDB; 4L4S; X-ray; 2.90 A; A/H=2-332.
PDB; 4M49; X-ray; 2.05 A; A/B/C/D=2-332.
PDB; 4OJN; X-ray; 2.40 A; A/B/C/D/E/F/G/H=2-332.
PDB; 4OKN; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-332.
PDB; 4QO7; X-ray; 2.14 A; A/B/C/D=2-332.
PDB; 4QO8; X-ray; 2.00 A; A/B/C/D=2-332.
PDB; 4QSM; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-332.
PDB; 4QT0; X-ray; 3.20 A; A/B/C/D/E/F/G/H=2-332.
PDB; 4R68; X-ray; 2.11 A; A/B/C/D=2-332.
PDB; 4R69; X-ray; 3.19 A; A/B/C/D=2-332.
PDB; 4RLS; X-ray; 1.91 A; A/B/C/D=2-332.
PDB; 4ZVV; X-ray; 2.20 A; A/B/C/D=1-332.
PDB; 5IXS; X-ray; 2.05 A; A/B/C/D=2-332.
PDB; 5IXY; X-ray; 3.00 A; A/B/C/D=2-332.
PDBsum; 1I10; -.
PDBsum; 4AJP; -.
PDBsum; 4JNK; -.
PDBsum; 4L4R; -.
PDBsum; 4L4S; -.
PDBsum; 4M49; -.
PDBsum; 4OJN; -.
PDBsum; 4OKN; -.
PDBsum; 4QO7; -.
PDBsum; 4QO8; -.
PDBsum; 4QSM; -.
PDBsum; 4QT0; -.
PDBsum; 4R68; -.
PDBsum; 4R69; -.
PDBsum; 4RLS; -.
PDBsum; 4ZVV; -.
PDBsum; 5IXS; -.
PDBsum; 5IXY; -.
ProteinModelPortal; P00338; -.
SMR; P00338; -.
BioGrid; 110131; 146.
IntAct; P00338; 37.
MINT; MINT-4998672; -.
STRING; 9606.ENSP00000445175; -.
BindingDB; P00338; -.
ChEMBL; CHEMBL4835; -.
DrugBank; DB02483; Etheno-Nad.
DrugBank; DB00157; NADH.
DrugBank; DB02701; Nicotinamide.
DrugBank; DB03940; Oxamic Acid.
iPTMnet; P00338; -.
PhosphoSitePlus; P00338; -.
SwissPalm; P00338; -.
BioMuta; LDHA; -.
DMDM; 126047; -.
DOSAC-COBS-2DPAGE; P00338; -.
OGP; P00338; -.
REPRODUCTION-2DPAGE; IPI00217966; -.
EPD; P00338; -.
PaxDb; P00338; -.
PeptideAtlas; P00338; -.
PRIDE; P00338; -.
TopDownProteomics; P00338-1; -. [P00338-1]
TopDownProteomics; P00338-4; -. [P00338-4]
TopDownProteomics; P00338-5; -. [P00338-5]
DNASU; 3939; -.
Ensembl; ENST00000227157; ENSP00000227157; ENSG00000134333. [P00338-5]
Ensembl; ENST00000379412; ENSP00000368722; ENSG00000134333. [P00338-1]
Ensembl; ENST00000396222; ENSP00000379524; ENSG00000134333. [P00338-2]
Ensembl; ENST00000422447; ENSP00000395337; ENSG00000134333. [P00338-1]
Ensembl; ENST00000430553; ENSP00000406172; ENSG00000134333. [P00338-4]
Ensembl; ENST00000540430; ENSP00000445175; ENSG00000134333. [P00338-3]
Ensembl; ENST00000542179; ENSP00000445331; ENSG00000134333. [P00338-1]
GeneID; 3939; -.
KEGG; hsa:3939; -.
UCSC; uc001mol.4; human. [P00338-1]
CTD; 3939; -.
DisGeNET; 3939; -.
EuPathDB; HostDB:ENSG00000134333.13; -.
GeneCards; LDHA; -.
HGNC; HGNC:6535; LDHA.
HPA; CAB015336; -.
MalaCards; LDHA; -.
MIM; 150000; gene.
MIM; 612933; phenotype.
neXtProt; NX_P00338; -.
OpenTargets; ENSG00000134333; -.
Orphanet; 284426; Glycogen storage disease due to lactate dehydrogenase M-subunit deficiency.
PharmGKB; PA30319; -.
eggNOG; KOG1495; Eukaryota.
eggNOG; COG0039; LUCA.
GeneTree; ENSGT00550000074541; -.
HOGENOM; HOG000213793; -.
HOVERGEN; HBG000462; -.
InParanoid; P00338; -.
KO; K00016; -.
OMA; MDLMQTA; -.
OrthoDB; EOG091G0HME; -.
PhylomeDB; P00338; -.
TreeFam; TF314963; -.
Reactome; R-HSA-70268; Pyruvate metabolism.
SABIO-RK; P00338; -.
SIGNOR; P00338; -.
UniPathway; UPA00554; UER00611.
ChiTaRS; LDHA; human.
EvolutionaryTrace; P00338; -.
GeneWiki; LDHA; -.
GenomeRNAi; 3939; -.
PRO; PR:P00338; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000134333; -.
CleanEx; HS_LDHA; -.
ExpressionAtlas; P00338; baseline and differential.
Genevisible; P00338; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0004459; F:L-lactate dehydrogenase activity; EXP:Reactome.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0006096; P:glycolytic process; NAS:UniProtKB.
GO; GO:0006089; P:lactate metabolic process; IEA:Ensembl.
GO; GO:0019674; P:NAD metabolic process; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048569; P:post-embryonic animal organ development; IEA:Ensembl.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
Gene3D; 3.90.110.10; -; 1.
HAMAP; MF_00488; Lactate_dehydrog; 1.
InterPro; IPR001557; L-lactate/malate_DH.
InterPro; IPR011304; L-lactate_DH.
InterPro; IPR018177; L-lactate_DH_AS.
InterPro; IPR022383; Lactate/malate_DH_C.
InterPro; IPR001236; Lactate/malate_DH_N.
InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF02866; Ldh_1_C; 1.
Pfam; PF00056; Ldh_1_N; 1.
PIRSF; PIRSF000102; Lac_mal_DH; 1.
PRINTS; PR00086; LLDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF56327; SSF56327; 1.
TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
PROSITE; PS00064; L_LDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
Glycogen storage disease; Isopeptide bond; NAD; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.10}.
CHAIN 2 332 L-lactate dehydrogenase A chain.
/FTId=PRO_0000168411.
NP_BIND 29 57 NAD. {ECO:0000269|PubMed:11276087}.
ACT_SITE 193 193 Proton acceptor.
BINDING 99 99 NAD. {ECO:0000269|PubMed:11276087}.
BINDING 106 106 Substrate.
BINDING 138 138 NAD or substrate.
{ECO:0000269|PubMed:11276087}.
BINDING 169 169 Substrate.
BINDING 248 248 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.10}.
MOD_RES 5 5 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 5 5 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 10 10 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 14 14 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 18 18 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 118 118 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 118 118 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 239 239 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 243 243 N6-acetyllysine.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 318 318 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 318 318 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P06151}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000250|UniProtKB:P04642}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MGEPSGGYTYTQTSIFLFHAKIPFGSKSNM (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042206.
VAR_SEQ 82 139 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042786.
VAR_SEQ 230 274 VHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRV
HPVS -> CRYTLGDPKGAAILKSSDVISFHCLGYNRILGG
GCACCPFYLICD (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014261.
VAR_SEQ 237 241 SAYEV -> RVFTE (in isoform 5).
{ECO:0000305}.
/FTId=VSP_042788.
VAR_SEQ 242 332 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_042789.
VAR_SEQ 275 332 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042787.
VARIANT 161 161 S -> R (in dbSNP:rs5030621).
/FTId=VAR_059374.
VARIANT 222 222 K -> E (in dbSNP:rs748436361).
{ECO:0000269|PubMed:7908613,
ECO:0000269|Ref.6}.
/FTId=VAR_004180.
VARIANT 315 315 R -> C (in dbSNP:rs200093825).
{ECO:0000269|PubMed:1445373}.
/FTId=VAR_004181.
HELIX 4 8 {ECO:0000244|PDB:4JNK}.
STRAND 9 12 {ECO:0000244|PDB:4JNK}.
STRAND 20 26 {ECO:0000244|PDB:4JNK}.
HELIX 30 41 {ECO:0000244|PDB:4JNK}.
STRAND 46 51 {ECO:0000244|PDB:4JNK}.
HELIX 55 67 {ECO:0000244|PDB:4JNK}.
HELIX 68 71 {ECO:0000244|PDB:4JNK}.
STRAND 77 79 {ECO:0000244|PDB:4JNK}.
HELIX 83 86 {ECO:0000244|PDB:4JNK}.
STRAND 90 94 {ECO:0000244|PDB:4JNK}.
HELIX 107 127 {ECO:0000244|PDB:4JNK}.
STRAND 132 135 {ECO:0000244|PDB:4JNK}.
STRAND 137 139 {ECO:0000244|PDB:4JNK}.
HELIX 140 151 {ECO:0000244|PDB:4JNK}.
HELIX 155 157 {ECO:0000244|PDB:4JNK}.
STRAND 158 160 {ECO:0000244|PDB:4JNK}.
HELIX 164 178 {ECO:0000244|PDB:4JNK}.
HELIX 182 184 {ECO:0000244|PDB:4JNK}.
STRAND 189 193 {ECO:0000244|PDB:4JNK}.
HELIX 194 196 {ECO:0000244|PDB:4JNK}.
STRAND 197 199 {ECO:0000244|PDB:4R68}.
HELIX 201 203 {ECO:0000244|PDB:4JNK}.
HELIX 211 214 {ECO:0000244|PDB:4JNK}.
TURN 216 219 {ECO:0000244|PDB:4JNK}.
STRAND 220 222 {ECO:0000244|PDB:1I10}.
HELIX 228 245 {ECO:0000244|PDB:4JNK}.
HELIX 250 264 {ECO:0000244|PDB:4JNK}.
STRAND 269 276 {ECO:0000244|PDB:4JNK}.
STRAND 288 296 {ECO:0000244|PDB:4JNK}.
STRAND 299 304 {ECO:0000244|PDB:4JNK}.
HELIX 310 327 {ECO:0000244|PDB:4JNK}.
SEQUENCE 332 AA; 36689 MW; 401E8604CEB7F908 CRC64;
MATLKDQLIY NLLKEEQTPQ NKITVVGVGA VGMACAISIL MKDLADELAL VDVIEDKLKG
EMMDLQHGSL FLRTPKIVSG KDYNVTANSK LVIITAGARQ QEGESRLNLV QRNVNIFKFI
IPNVVKYSPN CKLLIVSNPV DILTYVAWKI SGFPKNRVIG SGCNLDSARF RYLMGERLGV
HPLSCHGWVL GEHGDSSVPV WSGMNVAGVS LKTLHPDLGT DKDKEQWKEV HKQVVESAYE
VIKLKGYTSW AIGLSVADLA ESIMKNLRRV HPVSTMIKGL YGIKDDVFLS VPCILGQNGI
SDLVKVTLTS EEEARLKKSA DTLWGIQKEL QF


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