Tag | Content |
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CPLM ID | CPLM-002517 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Propionyl-CoA carboxylase beta chain, mitochondrial |
Protein Synonyms/Alias | PCCase subunit beta; Propanoyl-CoA:carbon dioxide ligase subunit beta |
Gene Name | Pccb |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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62 | RRIDAQHKRGKLTAR | acetylation | [1] | 103 | GMAAEKNKFPGDSVV | acetylation | [1] | 435 | KITVITRKAYGGAYD | acetylation | [1] | 528 | LEVLASKKVHRPWRK | acetylation | [1] |
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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 | |
Sequence Annotation | DOMAIN 40 533 Carboxyltransferase. REGION 327 360 Acyl-CoA binding (Potential). MOD_RES 62 62 N6-acetyllysine (By similarity). |
Keyword | Acetylation; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 541 AA |
Protein Sequence | MAAVIRIRAM AAGTRLRVLN CGLGTTIRSL CSQPVSVNER IENKRHAALL GGGQRRIDAQ 60 HKRGKLTARE RISLLLDPGS FLESDMFVEH RCADFGMAAE KNKFPGDSVV TGRGRINGRL 120 VYVFSQDFTV FGGSLSGAHA QKICKIMDQA ITVGAPVIGL NDSGGARIQE GVESLAGYAD 180 IFLRNVTASG VIPQISLIMG PCAGGAVYSP ALTDFTFMVK DTSYLFITGP EFVKSVTNED 240 VTQEQLGGAK THTTVSGVAH RAFDNDVDAL CNLREFLNFL PLSNQDPASI RECHDPSDRL 300 VPELDTVVPL ESSKAYNMLD IIHAVIDERE FFEIMPNYAK NIVIGFARMN GRTVGIVGNQ 360 PNVASGCLDI NSSVKGARFV RFCDAFSIPL ITFVDVPGFL PGTAQEYGGI IRHGAKLLYA 420 FAEATVPKIT VITRKAYGGA YDVMSSKHLL GDTNYAWPTA EIAVMGAKGA VEIIFKGHED 480 VEAAQAEYVE KFANPFPAAV RGFVDDIIQP SSTRARICCD LEVLASKKVH RPWRKHANVP 540 L 541 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; TAS:RGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004658; F:propionyl-CoA carboxylase activity; TAS:RGD. GO:0009063; P:cellular amino acid catabolic process; TAS:RGD. GO:0009062; P:fatty acid catabolic process; TAS:RGD. |
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PRINTS | |