Tag | Content |
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CPLM ID | CPLM-017953 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NEDD8-activating enzyme E1 catalytic subunit |
Protein Synonyms/Alias | NEDD8-activating enzyme E1C; Ubiquitin-activating enzyme E1C; Ubiquitin-like modifier-activating enzyme 3; Ubiquitin-activating enzyme 3 |
Gene Name | UBA3 |
Gene Synonyms/Alias | UBE1C |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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246 | VRMLQWPKEQPFGEG | ubiquitination | [1] | 270 | HIQWIFQKSLERASQ | ubiquitination | [1] | 293 | RLTQGVVKRIIPAVA | ubiquitination | [1] | 384 | NSASLQMKSPAITAT | ubiquitination | [1] | 395 | ITATLEGKNRTLYLQ | ubiquitination | [1] |
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Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression. |
Sequence Annotation | NP_BIND 100 124 ATP. NP_BIND 148 171 ATP. REGION 53 70 Interaction with UBE2M N-terminus. REGION 157 161 Interaction with UBE2M N-terminus. REGION 192 217 Interaction with UBE2M N-terminus. REGION 227 229 Interaction with NEDD8. REGION 242 248 Interaction with NAE1. REGION 292 295 Interaction with NAE1. REGION 331 338 Interaction with UBE2M N-terminus. REGION 352 357 Interaction with NEDD8. REGION 368 463 Interaction with UBE2M core domain. ACT_SITE 237 237 Glycyl thioester intermediate. |
Keyword | 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Complete proteome; Ligase; Nucleotide-binding; Polymorphism; Reference proteome; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 463 AA |
Protein Sequence | MADGEEPMAV DGGCGDTGDW EGRWNHVKKF LERSGPFTHP DFEPSTESLQ FLLDTCKVLV 60 IGAGGLGCEL LKNLALSGFR QIHVIDMDTI DVSNLNRQFL FRPKDIGRPK AEVAAEFLND 120 RVPNCNVVPH FNKIQDFNDT FYRQFHIIVC GLDSIIARRW INGMLISLLN YEDGVLDPSS 180 IVPLIDGGTE GFKGNARVIL PGMTACIECT LELYPPQVNF PMCTIASMPR LPEHCIEYVR 240 MLQWPKEQPF GEGVPLDGDD PEHIQWIFQK SLERASQYNI RGVTYRLTQG VVKRIIPAVA 300 STNAVIAAVC ATEVFKIATS AYIPLNNYLV FNDVDGLYTY TFEAERKENC PACSQLPQNI 360 QFSPSAKLQE VLDYLTNSAS LQMKSPAITA TLEGKNRTLY LQSVTSIEER TRPNLSKTLK 420 ELGLVDGQEL AVADVTTPQT VLFKLHFTS 449 |
Gene Ontology | GO:0005634; C:nucleus; IDA:LIFEdb. GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0019781; F:NEDD8 activating enzyme activity; IEA:Compara. GO:0006464; P:cellular protein modification process; TAS:ProtInc. GO:0007113; P:endomitotic cell cycle; IEA:Compara. GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara. GO:0045116; P:protein neddylation; IEA:UniProtKB-UniPathway. GO:0006508; P:proteolysis; TAS:ProtInc. GO:0051726; P:regulation of cell cycle; IEA:Compara. |
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