CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032057
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NEDD8-activating enzyme E1 catalytic subunit 
Protein Synonyms/Alias
 cDNA FLJ58044, highly similar to NEDD8-activating enzyme E1 catalytic subunit (EC 6.3.2.-); cDNA, FLJ79439, highly similar to NEDD8-activating enzyme E1 catalytic subunit (EC 6.3.2.-) 
Gene Name
 UBA3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
83VRMLQWPKEQPFGEGubiquitination[1, 2]
107HIQWIFQKSLERASQubiquitination[1, 2, 3, 4, 5, 6]
130RLTQGVVKRIIPAVAubiquitination[1, 2, 3, 6, 7]
184YTFEAERKENCPACSubiquitination[1, 3, 4, 6, 7]
221NSASLQMKSPAITATubiquitination[1, 2, 4, 7]
232ITATLEGKNRTLYLQacetylation[8]
232ITATLEGKNRTLYLQubiquitination[1, 2, 6, 7]
254RTRPNLSKTLKELGLubiquitination[6]
257PNLSKTLKELGLVDGubiquitination[1, 6]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 286 AA 
Protein Sequence
MLISLLNYED GVLDPSSIVP LIDGGTEGFK GNARVILPGM TACIECTLEL YPPQVNFPMC 60
TIASMPRLPE HCIEYVRMLQ WPKEQPFGEG VPLDGDDPEH IQWIFQKSLE RASQYNIRGV 120
TYRLTQGVVK RIIPAVASTN AVIAAVCATE VFKIATSAYI PLNNYLVFND VDGLYTYTFE 180
AERKENCPAC SQLPQNIQFS PSAKLQEVLD YLTNSASLQM KSPAITATLE GKNRTLYLQS 240
VTSIEERTRP NLSKTLKELG LVDGQELAVA DVTTPQTVLF KLHFTS 286 
Gene Ontology
 GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0019781; F:NEDD8 activating enzyme activity; IEA:Compara.
 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:InterPro.
 GO:0051726; P:regulation of cell cycle; IEA:Compara. 
Interpro
 IPR014929; E2_binding.
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR023318; Ub_act_enz_dom_a.
 IPR000127; UBact_repeat.
 IPR019572; Ubiquitin-activating_enzyme.
 IPR018074; UBQ-activ_enz_E1_AS. 
Pfam
 PF08825; E2_bind
 PF10585; UBA_e1_thiolCys
 PF02134; UBACT 
SMART
  
PROSITE
 PS00865; UBIQUITIN_ACTIVAT_2 
PRINTS