CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008503
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-activating enzyme E1-like 
Protein Synonyms/Alias
 Polymerase-interacting protein 2; SMT3-activating enzyme subunit 2 
Gene Name
 UBA2 
Gene Synonyms/Alias
 PIP2; UAL1; YDR390C; D9509.10 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
396LRVLNLLKYAPTTKYacetylation[1]
402LKYAPTTKYTDLNMAacetylation[1]
622APSNKRTKLVNEPTNacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1. 
Sequence Annotation
 NP_BIND 28 33 ATP (By similarity).
 NP_BIND 60 63 ATP (By similarity).
 NP_BIND 121 126 ATP (By similarity).
 MOTIF 619 622 Nuclear localization signal (Potential).
 ACT_SITE 177 177 Glycyl thioester intermediate (By
 METAL 162 162 Zinc (By similarity).
 METAL 165 165 Zinc (By similarity).
 METAL 435 435 Zinc (By similarity).
 METAL 438 438 Zinc (By similarity).
 BINDING 52 52 ATP (By similarity).
 BINDING 76 76 ATP (By similarity).  
Keyword
 3D-structure; ATP-binding; Complete proteome; Ligase; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 636 AA 
Protein Sequence
MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI VDLDTIDLSN 60
LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM DISTFPLHWF EQFDIIFNAL 120
DNLAARRYVN KISQFLSLPL IESGTAGFDG YMQPIIPGKT ECFECTKKET PKTFPVCTIR 180
STPSQPIHCI VWAKNFLFNQ LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK 240
IIISRDASRI PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV 300
GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH IFNIPMKSVF 360
DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT TKYTDLNMAF TAKASNLSQN 420
RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS DCLNKMKLSD FVVLIREKYS YPQDISLLDA 480
SNQRLLFDYD FEDLNDRTLS EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC 540
SLPDVEVPLI KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI 600
NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD 636 
Gene Ontology
 GO:0031510; C:SUMO activating enzyme complex; IPI:SGD.
 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; IDA:SGD.
 GO:0016925; P:protein sumoylation; IMP:SGD. 
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
 PS00865; UBIQUITIN_ACTIVAT_2 
PRINTS