CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024094
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SUMO-activating enzyme subunit 2 
Protein Synonyms/Alias
 Anthracycline-associated resistance ARX; Ubiquitin-like 1-activating enzyme E1B 
Gene Name
 Uba2 
Gene Synonyms/Alias
 Sae2; Uble1b 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
65NRQFLFQKKHVGRSKubiquitination[1]
257DPVKLFTKLFKDDIRubiquitination[1]
260KLFTKLFKDDIRYLLacetylation[2]
271RYLLTMDKLWRKRKPacetylation[2, 3, 4]
322SYASLFSKSIETLRVacetylation[2]
322SYASLFSKSIETLRVubiquitination[1]
334LRVHLAEKGDGAELIubiquitination[1]
407GLKILSGKIDQCRTIacetylation[2]
418CRTIFLNKQPNPRKKacetylation[2]
425KQPNPRKKLLVPCALacetylation[2]
445NCYVCASKPEVTVRLacetylation[2]
465TVLTLQDKIVKEKFAubiquitination[1]
503TEANNPKKLSDFGIRubiquitination[1]
611DDKARKRKLEENEAAacetylation[4]
Reference
 [1] 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]
 [2] 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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] 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
 NP_BIND 24 29 ATP (By similarity).
 NP_BIND 56 59 ATP (By similarity).
 NP_BIND 95 96 ATP (By similarity).
 NP_BIND 117 122 ATP (By similarity).
 ACT_SITE 173 173 Glycyl thioester intermediate
 METAL 158 158 Zinc (By similarity).
 METAL 161 161 Zinc (By similarity).
 METAL 439 439 Zinc (By similarity).
 METAL 442 442 Zinc (By similarity).
 BINDING 48 48 ATP (By similarity).
 BINDING 72 72 ATP (By similarity).
 MOD_RES 271 271 N6-acetyllysine (By similarity).
 MOD_RES 505 505 Phosphoserine (By similarity).
 MOD_RES 590 590 Phosphoserine (By similarity).  
Keyword
 Acetylation; ATP-binding; Complete proteome; Ligase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 638 AA 
Protein Sequence
MALSRGLPRE LAEAVSGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ 60
FLFQKKHVGR SKAQVAKESV LQFHPQANIE AHHDSIMNPD YNVEFFRQFI LVMNALDNRA 120
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS 180
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST 240
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEANADQQNE 300
PQLGLKDQQV LDVKSYASLF SKSIETLRVH LAEKGDGAEL IWDKDDPPAM DFVTSAANLR 360
MHIFSMNMKS RFDIKSMAGN IIPAIATTNA VIAGLIVLEG LKILSGKIDQ CRTIFLNKQP 420
NPRKKLLVPC ALDPPNTNCY VCASKPEVTV RLNVHKVTVL TLQDKIVKEK FAMVAPDVQI 480
EDGKGTILIS SEEGETEANN PKKLSDFGIR NGSRLQADDF LQDYTLLINI LHSEDLGKDV 540
EFEVVGDSPE KVGPKQAEDA AKSIANGSDD GAQPSTSTAQ EQDDVLIVDS DEEGPSNSTD 600
CSGDDKARKR KLEENEAAST KKCRLEQMED PDDVIALD 638 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0019948; F:SUMO activating enzyme activity; ISS:UniProtKB.
 GO:0016925; P:protein sumoylation; ISS:UniProtKB. 
Interpro
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd.
 IPR023280; Ub-like_act_enz_cat_cys_dom.
 IPR000127; UBact_repeat.
 IPR019572; Ubiquitin-activating_enzyme.
 IPR018074; UBQ-activ_enz_E1_AS. 
Pfam
 PF00899; ThiF
 PF10585; UBA_e1_thiolCys
 PF02134; UBACT 
SMART
  
PROSITE
 PS00536; UBIQUITIN_ACTIVAT_1
 PS00865; UBIQUITIN_ACTIVAT_2 
PRINTS