CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022858
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; HRIHFB2115 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65NRQFLFQKKHVGRSKubiquitination[1, 2, 3]
66RQFLFQKKHVGRSKAubiquitination[2]
77RSKAQVAKESVLQFYubiquitination[1, 2, 3, 4]
153GQVTTIKKGVTECYEubiquitination[2]
164ECYECHPKPTQRTFPubiquitination[2]
236SNEDGDIKRISTKEWacetylation[5]
241DIKRISTKEWAKSTGacetylation[5]
241DIKRISTKEWAKSTGubiquitination[1, 2, 3]
245ISTKEWAKSTGYDPVubiquitination[1, 2, 3, 6]
253STGYDPVKLFTKLFKubiquitination[1, 3, 6]
257DPVKLFTKLFKDDIRubiquitination[1, 2, 3, 6]
260KLFTKLFKDDIRYLLubiquitination[2]
271RYLLTMDKLWRKRKPacetylation[7]
271RYLLTMDKLWRKRKPubiquitination[1, 2, 3]
316DQQVLDVKSYARLFSubiquitination[1, 2, 3, 8]
324SYARLFSKSIETLRVacetylation[7]
324SYARLFSKSIETLRVubiquitination[1, 2, 3]
336LRVHLAEKGDGAELIubiquitination[1, 3]
420CRTIFLNKQPNPRKKubiquitination[1, 2, 3]
467TVLTLQDKIVKEKFAubiquitination[1, 2, 3]
472QDKIVKEKFAMVAPDubiquitination[1, 3]
505TEANNHKKLSEFGIRubiquitination[2]
540LHSEDLGKDVEFEVVsumoylation[9]
617RKRKLDEKENLSAKRacetylation[7]
Reference
 [1] 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]
 [2] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634] 
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. 
Sequence Annotation
 NP_BIND 24 29 ATP.
 NP_BIND 56 59 ATP.
 NP_BIND 95 96 ATP.
 NP_BIND 117 122 ATP.
 ACT_SITE 173 173 Glycyl thioester intermediate.
 METAL 158 158 Zinc.
 METAL 161 161 Zinc.
 METAL 441 441 Zinc.
 METAL 444 444 Zinc.
 BINDING 48 48 ATP.
 BINDING 72 72 ATP.
 MOD_RES 271 271 N6-acetyllysine.
 MOD_RES 507 507 Phosphoserine.
 MOD_RES 592 592 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Ligase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 640 AA 
Protein Sequence
MALSRGLPRE LAEAVAGGRV LVVGAGGIGC ELLKNLVLTG FSHIDLIDLD TIDVSNLNRQ 60
FLFQKKHVGR SKAQVAKESV LQFYPKANIV AYHDSIMNPD YNVEFFRQFI LVMNALDNRA 120
ARNHVNRMCL AADVPLIESG TAGYLGQVTT IKKGVTECYE CHPKPTQRTF PGCTIRNTPS 180
EPIHCIVWAK YLFNQLFGEE DADQEVSPDR ADPEAAWEPT EAEARARASN EDGDIKRIST 240
KEWAKSTGYD PVKLFTKLFK DDIRYLLTMD KLWRKRKPPV PLDWAEVQSQ GEETNASDQQ 300
NEPQLGLKDQ QVLDVKSYAR LFSKSIETLR VHLAEKGDGA ELIWDKDDPS AMDFVTSAAN 360
LRMHIFSMNM KSRFDIKSMA GNIIPAIATT NAVIAGLIVL EGLKILSGKI DQCRTIFLNK 420
QPNPRKKLLV PCALDPPNPN CYVCASKPEV TVRLNVHKVT VLTLQDKIVK EKFAMVAPDV 480
QIEDGKGTIL ISSEEGETEA NNHKKLSEFG IRNGSRLQAD DFLQDYTLLI NILHSEDLGK 540
DVEFEVVGDA PEKVGPKQAE DAAKSITNGS DDGAQPSTST AQEQDDVLIV DSDEEDSSNN 600
ADVSEEERSR KRKLDEKENL SAKRSRIEQK EELDDVIALD 640 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008047; F:enzyme activator activity; TAS:ProtInc.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0019948; F:SUMO activating enzyme activity; IDA:UniProtKB.
 GO:0016925; P:protein sumoylation; IDA: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