CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022777
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SUMO-activating enzyme subunit 1 
Protein Synonyms/Alias
 Ubiquitin-like 1-activating enzyme E1A; SUMO-activating enzyme subunit 1, N-terminally processed 
Gene Name
 Sae1 
Gene Synonyms/Alias
 Aos1; Sua1; Ubl1a1; Uble1a 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
36LWGLEAQKRLRASRVacetylation[1]
36LWGLEAQKRLRASRVubiquitination[2]
145CSRDVIIKVDQICHRacetylation[1]
187EEKTKVAKVSQGVEDubiquitination[2]
199VEDGPEAKRAKLDSSubiquitination[2]
202GPEAKRAKLDSSETTacetylation[3]
212SSETTMVKKKVLFCPubiquitination[2]
232EVDWSGEKAKAALKRubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2 (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 2 2 N-acetylvaline; in SUMO-activating enzyme  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Ligase; Nucleus; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MVEKEEAGGG GGGGISEEEA AQYDRQIRLW GLEAQKRLRA SRVLIVGMKG LGAEIAKNLI 60
LAGVKGLTML DHEQVSPEDP GAQFLIQTGS VGRNRAEASL ERAQNLNPMV DVKVDTEDVE 120
KKPESFFTKF DAVCLTCCSR DVIIKVDQIC HRNSIKFFTG DVFGYHGYTF ANLGEHEFVE 180
EKTKVAKVSQ GVEDGPEAKR AKLDSSETTM VKKKVLFCPV KEALEVDWSG EKAKAALKRT 240
APDYFLLQVL LKFRTDKGRD PTSESYKEDA ELLLQIRNDV FDSLGISPDL LPDDFVRYCF 300
SEMAPVCAVV GGILAQEIVK ALSQRDPPHN NFFFFDGMKG SGIVECLGPQ 350 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
 GO:0019948; F:SUMO activating enzyme activity; IEA:Compara.
 GO:0016925; P:protein sumoylation; ISS:UniProtKB. 
Interpro
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd.
 IPR000011; UBQ/SUMO-activ_enz_E1-like. 
Pfam
 PF00899; ThiF 
SMART
  
PROSITE
  
PRINTS
 PR01849; UBIQUITINACT.