CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005092
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-activating enzyme E1 1 
Protein Synonyms/Alias
  
Gene Name
 UBA1 
Gene Synonyms/Alias
 YKL210W 
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
28RQLYVLGKEAMLKMQubiquitination[1]
53GLGVEIAKNVVLAGVubiquitination[1]
244AFRIGSVKEYGEYKKacetylation[2]
381VLKACSGKFTPLKQFubiquitination[1]
408KNFPRNEKTTQPVNSubiquitination[1]
494PKDVGKNKSEVAAEAubiquitination[1]
561RRCVFYRKPLLESGTubiquitination[1]
572ESGTLGTKGNTQVIIubiquitination[1, 3]
595SSRDPPEKSIPLCTLubiquitination[1, 3]
608TLRSFPNKIDHTIAWacetylation[2]
608TLRSFPNKIDHTIAWubiquitination[1, 3]
665ISDSLSSKPHNFEDCubiquitination[1]
674HNFEDCIKWARLEFEubiquitination[1]
712EPFWSGAKRAPTPLEubiquitination[1]
752KSDDSNSKPNVDEYKubiquitination[1]
888LYKLIDNKTDIEQYKubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] 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]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin- E1 thioester and free AMP. 
Sequence Annotation
 REPEAT 27 164 1-1.
 REPEAT 425 579 1-2.
 NP_BIND 444 473 ATP (By similarity).
 REGION 27 579 2 approximate repeats.
 ACT_SITE 600 600 Glycyl thioester intermediate (By
 MOD_RES 265 265 Phosphoserine.
 MOD_RES 914 914 Phosphoserine.  
Keyword
 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1024 AA 
Protein Sequence
MSSNNSGLSA AGEIDESLYS RQLYVLGKEA MLKMQTSNVL ILGLKGLGVE IAKNVVLAGV 60
KSMTVFDPEP VQLADLSTQF FLTEKDIGQK RGDVTRAKLA ELNAYVPVNV LDSLDDVTQL 120
SQFQVVVATD TVSLEDKVKI NEFCHSSGIR FISSETRGLF GNTFVDLGDE FTVLDPTGEE 180
PRTGMVSDIE PDGTVTMLDD NRHGLEDGNF VRFSEVEGLD KLNDGTLFKV EVLGPFAFRI 240
GSVKEYGEYK KGGIFTEVKV PRKISFKSLK QQLSNPEFVF SDFAKFDRAA QLHLGFQALH 300
QFAVRHNGEL PRTMNDEDAN ELIKLVTDLS VQQPEVLGEG VDVNEDLIKE LSYQARGDIP 360
GVVAFFGGLV AQEVLKACSG KFTPLKQFMY FDSLESLPDP KNFPRNEKTT QPVNSRYDNQ 420
IAVFGLDFQK KIANSKVFLV GSGAIGCEML KNWALLGLGS GSDGYIVVTD NDSIEKSNLN 480
RQFLFRPKDV GKNKSEVAAE AVCAMNPDLK GKINAKIDKV GPETEEIFND SFWESLDFVT 540
NALDNVDART YVDRRCVFYR KPLLESGTLG TKGNTQVIIP RLTESYSSSR DPPEKSIPLC 600
TLRSFPNKID HTIAWAKSLF QGYFTDSAEN VNMYLTQPNF VEQTLKQSGD VKGVLESISD 660
SLSSKPHNFE DCIKWARLEF EKKFNHDIKQ LLFNFPKDAK TSNGEPFWSG AKRAPTPLEF 720
DIYNNDHFHF VVAGASLRAY NYGIKSDDSN SKPNVDEYKS VIDHMIIPEF TPNANLKIQV 780
NDDDPDPNAN AANGSDEIDQ LVSSLPDPST LAGFKLEPVD FEKDDDTNHH IEFITACSNC 840
RAQNYFIETA DRQKTKFIAG RIIPAIATTT SLVTGLVNLE LYKLIDNKTD IEQYKNGFVN 900
LALPFFGFSE PIASPKGEYN NKKYDKIWDR FDIKGDIKLS DLIEHFEKDE GLEITMLSYG 960
VSLLYASFFP PKKLKERLNL PITQLVKLVT KKDIPAHVST MILEICADDK EGEDVEVPFI 1020
TIHL 1024 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0004839; F:ubiquitin activating enzyme activity; IDA:SGD.
 GO:0016567; P:protein ubiquitination; IDA:SGD. 
Interpro
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd.
 IPR018965; Ub-activating_enz_e1_C.
 IPR023280; Ub-like_act_enz_cat_cys_dom.
 IPR000127; UBact_repeat.
 IPR019572; Ubiquitin-activating_enzyme.
 IPR018075; UBQ-activ_enz_E1.
 IPR018074; UBQ-activ_enz_E1_AS.
 IPR000011; UBQ/SUMO-activ_enz_E1-like. 
Pfam
 PF00899; ThiF
 PF09358; UBA_e1_C
 PF10585; UBA_e1_thiolCys
 PF02134; UBACT 
SMART
 SM00985; UBA_e1_C 
PROSITE
 PS00536; UBIQUITIN_ACTIVAT_1
 PS00865; UBIQUITIN_ACTIVAT_2 
PRINTS
 PR01849; UBIQUITINACT.