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Protein Page:
DLAT (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
DLAT the E2 component of the pyruvate dehydrogenase complex (PDHC) that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. Contains two lipoyl-binding domains. The PDHC plays a major role in controlling the balance between lipid and glucose oxidation depending on substrate availability. The activity of the PDHC is tightly regulated by phosphorylation of the E1 components by the PDHKs. The pyruvate dehydrogenase (PDH) holoenzyme is a multi-enzyme complex (PDHC) that contains 20-30 copies of pyruvate decarboxylase tetramers (2 alpha:2 beta)(E1), 60 copies of dihydrolipoamide acetyltransferase (E2), six homo-dimers of dihydrolipoamide dehydrogenase (E3), plus E3 binding proteins. PDHKs are recruited to the PDHC by binding to a lipoyl group covalently attached to K174 of the inner lipoyl domain of the E2 component. Note: This description may include information from UniProtKB.
Protein type: Transferase; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 2.3.1.12; Carbohydrate Metabolism - pyruvate; Mitochondrial; Carbohydrate Metabolism - citrate (TCA) cycle
Cellular Component: mitochondrion; mitochondrial matrix; mitochondrial pyruvate dehydrogenase complex
Molecular Function: dihydrolipoyllysine-residue acetyltransferase activity; protein binding
Biological Process: cellular metabolic process; tricarboxylic acid cycle; glucose metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process
Reference #:  P10515 (UniProtKB)
Alt. Names/Synonyms: 70 kDa mitochondrial autoantigen of primary biliary cirrhosis; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; dihydrolipoamide S-acetyltransferase; Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial; DLAT; DLTA; E2 component of pyruvate dehydrogenase complex; M2 antigen complex 70 kDa subunit; ODP2; PBC; PDC-E2; PDCE2; Pyruvate dehydrogenase complex component E2
Gene Symbols: DLAT
Molecular weight: 68,997 Da
Basal Isoelectric point: 7.96  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DLAT

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  RCSB PDB  |  DISEASE  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 T35-p VPGTPRVtSRSGPAP
0 1 Y52 RNSVTTGYGGVRALC
0 1 A57 TGYGGVRALCGWTPS
0 1 A67 GWTPSSGATPRNRLL
0 2 S80-p LLLQLLGsPGRRYYS
0 2 S100-p KVPLPSLsPTMQAGT
0 1 T154-p KILVAEGtRDVPIGA
0 1 T312-p DYRPTEVtDLKPQVP
0 2 S358-p PKGRVFVsPLAkKLA
0 4 K362-a VFVsPLAkKLAVEKG
0 2 K376 GIDLTQVKGTGPDGR
0 1 S391-p ITKKDIDsFVPSKVA
0 17 K462-a GEVLLVRkELNkILE
0 19 K466-a LVRkELNkILEGRSK
0 1 K473 kILEGRSKIsVNDFI
0 4 S475-p LEGRSKIsVNDFIIK
0 2 K547 DVVSLATKAREGKLQ
0 10 R636 AQWLAEFRKYLEKPI
0 2 K637 QWLAEFRKYLEKPIT
0 1 K641 EFRKYLEKPITMLL_
  mouse

 
S35-p GPGAPCGsPRIGPAA
Y52-p CGSGIPRyGVRsLCG
S56-p IPRyGVRsLCGWSSG
T66-p GWSSGSGtVPRNRLL
S79 LLRQLLGSPSRRSYS
S99-p KVPLPSLsPTMQAGT
T153 KILVPEGTRDVPVGS
T311 DYRPTEVTSLKPQAA
S353 PKGRVFVSPLAKKLA
K357 VFVSPLAKKLAAEKG
K371-a GIDLTQVkGTGPEGR
S386 IIKKDIDSFVPSKAA
K457 GEVLLVRKELNkMLE
K461-a LVRKELNkMLEGKGk
K468-u kMLEGKGkIsVNDFI
S470-p LEGKGkIsVNDFIIK
K542 DVVSLASKAREGKLQ
K631-a AQWLAEFkkYLEkPI
K632-a QWLAEFkkYLEkPIT
K636-u EFkkYLEkPITMLL_
  rat

 
G27 ARWATLKGPRTGPAA
Y44 CGSGIPSYGVRSLCG
S48 IPSYGVRSLCGWSYG
T58 GWSYGSATVPRNRIL
S71 ILQQLLGSPSRRSYS
S91 KVPLPSLSPTMQAGT
T145 KILVPEGTRDVPVGS
T302 DYRPTEVTSLKPQAP
S344 PKGRVFVSPLAKKLA
K348 VFVSPLAKKLAAEKG
K362 GIDLTQVKGTGPEGR
S377 IIKKDIDSFVPTKAA
K447 GEVLLVRKELNKMLE
K451 LVRKELNKMLEGKGK
K458 KMLEGKGKISVNDFI
S460 LEGKGKISVNDFIIK
K532-a DVVSLASkAREGKLQ
K621-a AQWLAEFkKYLEKPV
K622 QWLAEFkKYLEKPVT
K626 EFkKYLEKPVTMLL_
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