| Tag | Content |
|---|
| CPLM ID | CPLM-019329 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial |
Protein Synonyms/Alias | Dehydrogenase E1 and transketolase domain-containing protein 1 |
Gene Name | DHTKD1 |
Gene Synonyms/Alias | KIAA1630 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 537 | LLRFVGMKSVEVPRE | ubiquitination | [1] |
|
Reference | [1] 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 | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). |
Sequence Annotation | |
Keyword | Charcot-Marie-Tooth disease; Complete proteome; Disease mutation; Glycolysis; Mitochondrion; Neurodegeneration; Neuropathy; Oxidoreductase; Polymorphism; Reference proteome; Thiamine pyrophosphate; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 919 AA |
Protein Sequence | MASATAAAAR RGLGRALPLF WRGYQTERGV YGYRPRKPES REPQGALERP PVDHGLARLV 60
TVYCEHGHKA AKINPLFTGQ ALLENVPEIQ ALVQTLQGPF HTAGLLNMGK EEASLEEVLV 120
YLNQIYCGQI SIETSQLQSQ DEKDWFAKRF EELQKETFTT EERKHLSKLM LESQEFDHFL 180
ATKFSTVKRY GGEGAESMMG FFHELLKMSA YSGITDVIIG MPHRGRLNLL TGLLQFPPEL 240
MFRKMRGLSE FPENFSATGD VLSHLTSSVD LYFGAHHPLH VTMLPNPSHL EAVNPVAVGK 300
TRGRQQSRQD GDYSPDNSAQ PGDRVICLQV HGDASFCGQG IVPETFTLSN LPHFRIGGSV 360
HLIVNNQLGY TTPAERGRSS LYCSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR 420
KDVIIDLLCY RQWGHNELDE PFYTNPIMYK IIRARKSIPD TYAEHLIAGG LMTQEEVSEI 480
KSSYYAKLND HLNNMAHYRP PALNLQAHWQ GLAQPEAQIT TWSTGVPLDL LRFVGMKSVE 540
VPRELQMHSH LLKTHVQSRM EKMMDGIKLD WATAEALALG SLLAQGFNVR LSGQDVGRGT 600
FSQRHAIVVC QETDDTYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL 660
WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGIVILLPHG YDGAGPDHSS CRIERFLQMC 720
DSAEEGVDGD TVNMFVVHPT TPAQYFHLLR RQMVRNFRKP LIVASPKMLL RLPAAVSTLQ 780
EMAPGTTFNP VIGDSSVDPK KVKTLVFCSG KHFYSLVKQR ESLGAKKHDF AIIRVEELCP 840
FPLDSLQQEM SKYKHVKDHI WSQEEPQNMG PWSFVSPRFE KQLACKLRLV GRPPLPVPAV 900
GIGTVHLHQH EDILAKTFA 919 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:EC. GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. GO:0006096; P:glycolysis; IEA:UniProtKB-KW. GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |