Search Results

Overview

Uniprot ID	P29803
Protein Name	Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
Gene Name	PDHA2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
242	AASPDYYKRGNFIPG
61	LTRAEGLKYYRMMLT

Function

Together with PDHB forms the heterotetrameric E1 subunit of the pyruvate dehydrogenase (PDH) complex in testis (PubMed:14638692). The PDH complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) (Probable). The E1 subunit catalyzes both the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate and the reductive acetylation of a lipoyl group covalently linked to the lipoyl-bearing domains of E2 (PubMed:16436377)

Protein Sequence

10 MLAAFISRVL 20 RRVAQKSARR 30 VLVASRNSSN 40 DATFEIKKCD 50 LYLLEEGPPV 60 TTVLTRAEGL 70 KYYRMMLTVR 80 RMELKADQLY 90 KQKFIRGFCH 100 LCDGQEACCV 110 GLEAGINPSD 120 HVITSYRAHG 130 VCYTRGLSVR 140 SILAELTGRR 150 GGCAKGKGGS 160 MHMYTKNFYG 170 GNGIVGAQGP 180 LGAGIALACK 190 YKGNDEICLT 200 LYGDGAANQG 210 QIAEAFNMAA 220 LWKLPCVFIC 230 ENNLYGMGTS 240 TERAAASPDY 250 YKRGNFIPGL 260 KVDGMDVLCV 270 REATKFAANY 280 CRSGKGPILM 290 ELQTYRYHGH 300 SMSDPGVSYR 310 TREEIQEVRS 320 KRDPIIILQD 330 RMVNSKLATV 340 EELKEIGAEV 350 RKEIDDAAQF 360 ATTDPEPHLE 370 ELGHHIYSSD 380 SSFEVRGANP WIKFKSVS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005759	mitochondrial matrix
Cellular Component	GO:0005739	mitochondrion
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0045254	pyruvate dehydrogenase complex
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0004739	pyruvate dehydrogenase (acetyl-transferring) activity
Biological Process	GO:0006006	glucose metabolic process
Biological Process	GO:0006086	pyruvate decarboxylation to acetyl-CoA
Biological Process	GO:0006099	tricarboxylic acid cycle

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.