CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006879
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Obg-like ATPase 1 
Protein Synonyms/Alias
  
Gene Name
 OLA1 
Gene Synonyms/Alias
 YBR025C; YBR0309 
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
22GRPGNNLKAGIVGLAubiquitination[1]
33VGLANVGKSTFFQAIubiquitination[1]
79KLCEIYKKTASEVPAubiquitination[1]
98YDIAGLTKGASAGEGubiquitination[2]
155INQELRLKDIEFAQKacetylation[3]
155INQELRLKDIEFAQKubiquitination[1]
162KDIEFAQKALEGAEKacetylation[3]
169KALEGAEKIAKRGGQubiquitination[1]
192EEMDLITKIIKLLESacetylation[3]
195DLITKIIKLLESGQRacetylation[3]
195DLITKIIKLLESGQRubiquitination[1]
286EDAEEELKKLQTISAacetylation[3]
296QTISALPKIITTMRQacetylation[3]
296QTISALPKIITTMRQubiquitination[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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] 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]
 [3] 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
 Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP. 
Sequence Annotation
 DOMAIN 23 129 G.
 NP_BIND 30 35 ATP (By similarity).
 BINDING 233 233 ATP; via carbonyl oxygen (By similarity).
 MOD_RES 89 89 Phosphothreonine.
 MOD_RES 116 116 Phosphoserine.
 MOD_RES 119 119 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 394 AA 
Protein Sequence
MPPKKQVEEK KVLLGRPGNN LKAGIVGLAN VGKSTFFQAI TRCPLGNPAN YPFATIDPEE 60
ARVIVPSPRF DKLCEIYKKT ASEVPAHLTV YDIAGLTKGA SAGEGLGNAF LSHIRSVDSI 120
YQVVRCFDDA EIIHVEGDVD PVRDLEIINQ ELRLKDIEFA QKALEGAEKI AKRGGQSLEV 180
KQKKEEMDLI TKIIKLLESG QRVANHSWTS KEVEIINSMF LLTAKPCIYL INLSERDYIR 240
KKNKHLLRIK EWVDKYSPGD LIIPFSVSLE ERLSHMSPED AEEELKKLQT ISALPKIITT 300
MRQKLDLISF FTCGPDEVRE WTIRRGTKAP QAAGVIHNDL MNTFILAQVM KCEDVFEYKD 360
DSAIKAAGKL MQKGKDYVVE DGDIIYFRAG AGKN 394 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IDA:SGD.
 GO:0005525; F:GTP binding; IEA:InterPro. 
Interpro
 IPR012675; Beta-grasp_dom.
 IPR004396; CHP00092.
 IPR013029; DUF933.
 IPR006073; GTP_binding_domain.
 IPR027417; P-loop_NTPase.
 IPR012676; TGS-like.
 IPR023192; TGS-like_dom. 
Pfam
 PF01926; MMR_HSR1
 PF06071; YchF-GTPase_C 
SMART
  
PROSITE
  
PRINTS
 PR00326; GTP1OBG.