CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012147
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NEDD8-activating enzyme E1 regulatory subunit 
Protein Synonyms/Alias
 Amyloid beta precursor protein-binding protein 1, 59 kDa; APP-BP1; Amyloid protein-binding protein 1; Proto-oncogene protein 1 
Gene Name
 NAE1 
Gene Synonyms/Alias
 APPBP1; HPP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MAQLGKLLKEQKYacetylation[1]
12GKLLKEQKYDRQLRLubiquitination[2]
167GYMRIIIKEHPVIESubiquitination[2, 3]
187LEDLRLDKPFPELREubiquitination[3]
253LIRQGILKNENGAPEubiquitination[2, 4]
299DRCINITKQTPSFWIubiquitination[3]
312WILARALKEFVAKEGubiquitination[2, 3]
317ALKEFVAKEGQGNLPubiquitination[2, 3, 4]
338DMIADSGKYIKLQNVubiquitination[2]
341ADSGKYIKLQNVYREubiquitination[3]
363AVGNHVAKLLQSIGQubiquitination[2, 3]
378APESISEKELKLLCSubiquitination[2, 4]
381SISEKELKLLCSNSAubiquitination[3]
456QVEEDIGKLKSCLTGubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [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] 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
 Regulatory 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. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation. 
Sequence Annotation
 REGION 331 344 Interaction with UBA3.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 6 6 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle; Cell membrane; Complete proteome; Membrane; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 534 AA 
Protein Sequence
MAQLGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV LPGIGSFTII 60
DGNQVSGEDA GNNFFLQRSS IGKNRAEAAM EFLQELNSDV SGSFVEESPE NLLDNDPSFF 120
CRFTVVVATQ LPESTSLRLA DVLWNSQIPL LICRTYGLVG YMRIIIKEHP VIESHPDNAL 180
EDLRLDKPFP ELREHFQSYD LDHMEKKDHS HTPWIVIIAK YLAQWYSETN GRIPKTYKEK 240
EDFRDLIRQG ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ 300
TPSFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSGKYI KLQNVYREKA KKDAAAVGNH 360
VAKLLQSIGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE EYGLDTINKD EIISSMDNPD 420
NEIVLYLMLR AVDRFHKQQG RYPGVSNYQV EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH 480
EFCRYGAAEP HTIAAFLGGA AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL 534 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0003824; F:catalytic activity; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0033314; P:mitotic DNA replication checkpoint; IDA:UniProtKB.
 GO:0045116; P:protein neddylation; IDA:UniProtKB.
 GO:0043523; P:regulation of neuron apoptotic process; IDA:UniProtKB.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd. 
Pfam
 PF00899; ThiF 
SMART
  
PROSITE
  
PRINTS