| Tag | Content |
|---|
| CPLM ID | CPLM-002656 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial |
Protein Synonyms/Alias | 70 kDa mitochondrial autoantigen of primary biliary cirrhosis; PBC; Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2; PDC-E2; PDCE2 |
Gene Name | Dlat |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 305 | PTEVTSLKPQAPPPV | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. |
Sequence Annotation | DOMAIN 83 157 Lipoyl-binding 1.
DOMAIN 209 283 Lipoyl-binding 2.
REGION 344 375 E3- and/or E1-component binding domain
REGION 456 632 Catalytic (By similarity).
REGION 600 611 CoA-binding (By similarity).
ACT_SITE 605 605 Potential.
ACT_SITE 609 609 Potential.
MOD_RES 249 249 N6-lipoyllysine.
MOD_RES 451 451 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Acyltransferase; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glucose metabolism; Lipoyl; Mitochondrion; Reference proteome; Repeat; Transferase; Transit peptide; Tricarboxylic acid cycle. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 632 AA |
Protein Sequence | MWRVCARRVQ SAVPRAGFRA RWATLKGPRT GPAAVRCGSG IPSYGVRSLC GWSYGSATVP 60
RNRILQQLLG SPSRRSYSLP PHQKVPLPSL SPTMQAGTIA RWEKKEGEKI SEGDLIAEVE 120
TDKATVGFES LEECYMAKIL VPEGTRDVPV GSIICITVEK PQDIEAFKNY TLDSATAATQ 180
AAPAPAAAPA AAPAAPSASA PGSSYPVHMQ IVLPALSPTM TMGTVQRWEK KVGEKLSEGD 240
LLAEIETDKA TIGFEVQEEG YLAKILVPEG TRDVPLGTPL CIIVEKQEDI AAFADYRPTE 300
VTSLKPQAPP PVPPPVAAVP PIPQPLAPTP SAAPAGPKGR VFVSPLAKKL AAEKGIDLTQ 360
VKGTGPEGRI IKKDIDSFVP TKAAPAAAAA APPGPRVAPT PAGVFIDIPI SNIRRVIAQR 420
LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGKGKIS VNDFIIKASA LACLKVPEAN 480
SSWMDTVIRQ NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA SKAREGKLQP 540
HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG FDVASVMSVT 600
LSCDHRVVDG AVGAQWLAEF KKYLEKPVTM LL 632 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:RGD. GO:0045254; C:pyruvate dehydrogenase complex; IDA:RGD. GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IDA:RGD. GO:0000166; F:nucleotide binding; TAS:RGD. GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD. GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. GO:0030431; P:sleep; IEP:RGD. GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. |
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