UniProt Accession

 LDHA_HUMAN; P00338; B4DKQ2; B7Z5E3; D3DQY3; F8W819; Q53G53; Q6IBM7; Q6ZNV1; Q9UDE8; Q9UDE9 

Genbank Protein ID

 X02152; X03077; X03078; X03079; X03080; X03081; X03082; X03083; AY423727; AK130587; AK296667; AK298834; CR456775; CR541714; AK223078; AC084117; CH471064; CH471064; BC067223; S66853 

Genbank Nucleotide ID

 CAA26088.1; CAA26879.1; CAA26879.1; CAA26879.1; CAA26879.1; CAA26879.1; CAA26879.1; CAA26879.1; AAS00490.1; BAC85389.1; BAG59264.1; BAH12879.1; CAG33056.1; CAG46515.1; BAD96798.1; EAW68395.1; EAW68396.1; AAH67223.1; AAB20418.1 

Protein Name

 L-lactate dehydrogenase A chain 

Protein Synonyms/Alias

 LDH-A; Cell proliferation-inducing gene 19 protein; LDH muscle subunit; LDH-M; Renal carcinoma antigen NY-REN-59 

Gene Name

 LDHA 

Gene Synonyms/Alias

 PIG19 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	AKIPFGSKSNMATLK	ubiquitination	[1]
34	KSNMATLKDQLIYNL	ubiquitination	[2, 3]
43	QLIYNLLKEEQTPQN	ubiquitination	[2, 3]
88	DVIEDKLKGEMMDLQ	ubiquitination	[2, 3]
105	SLFLRTPKIVSGKDY	ubiquitination	[3]
110	TPKIVSGKDYNVTAN	ubiquitination	[2, 3]
147	QRNVNIFKFIIPNVV	ubiquitination	[2, 3]
155	FIIPNVVKYSPNCKL	ubiquitination	[2, 3]
251	HPDLGTDKDKEQWKE	ubiquitination	[3]
253	DLGTDKDKEQWKEVH	ubiquitination	[3]
261	EQWKEVHKQVVESAY	ubiquitination	[3]
272	ESAYEVIKLKGYTSW	ubiquitination	[2, 3]
274	AYEVIKLKGYTSWAI	ubiquitination	[3]
307	HPVSTMIKGLYGIKD	ubiquitination	[2]
346	SEEEARLKKSADTLW	ubiquitination	[3]
347	EEEARLKKSADTLWG	ubiquitination	[2, 3]
357	DTLWGIQKELQF***	ubiquitination	[3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

Functional Description

  

Sequence Annotation

 NP_BIND 29 57 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 5 5 N6-acetyllysine.
 MOD_RES 10 10 Phosphotyrosine.
 MOD_RES 14 14 N6-acetyllysine.
 MOD_RES 57 57 N6-acetyllysine.
 MOD_RES 81 81 N6-acetyllysine.
 MOD_RES 118 118 N6-acetyllysine.
 MOD_RES 126 126 N6-acetyllysine.
 MOD_RES 239 239 Phosphotyrosine (By similarity).
 MOD_RES 318 318 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Glycogen storage disease; Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 332 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0004459; F:L-lactate dehydrogenase activity; NAS:UniProtKB.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
 GO:0031668; P:cellular response to extracellular stimulus; IEA:Compara.
 GO:0006096; P:glycolysis; NAS:UniProtKB.
 GO:0006090; P:pyruvate metabolic process; TAS:Reactome. 

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. 

Pfam

 PF02866; Ldh_1_C
 PF00056; Ldh_1_N 

SMART

  

PROSITE

 PS00064; L_LDH 

PRINTS

 PR00086; LLDHDRGNASE.