CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007359
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative zinc metalloproteinase YIL108W 
Protein Synonyms/Alias
  
Gene Name
 YIL108W 
Gene Synonyms/Alias
  
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
5***MVGSKDIDLFNLubiquitination[1]
189VRSEKTVKEIQDPDIubiquitination[2]
202DIAQQNSKGKNTGALubiquitination[2]
245LDTHWDGKLIRGHAAubiquitination[1, 2]
473DLRARLPKNELAKFGubiquitination[2]
478LPKNELAKFGNTFKLubiquitination[1, 2]
513VQPLDMSKYGFSKNVubiquitination[1]
518MSKYGFSKNVQGIKSubiquitination[1, 2, 3]
524SKNVQGIKSPLYGRSubiquitination[2]
568VRFYYKEKPTGTKDAubiquitination[2]
573KEKPTGTKDAPASKPubiquitination[1, 2]
579TKDAPASKPSVPPRNubiquitination[1, 2]
590PPRNYFSKITHSIKNubiquitination[1, 2]
596SKITHSIKNHASINEubiquitination[1, 2]
Reference
 [1] 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]
 [2] 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]
 [3] Systematic approach for validating the ubiquitinated proteome.
 Seyfried NT, Xu P, Duong DM, Cheng D, Hanfelt J, Peng J.
 Anal Chem. 2008 Jun 1;80(11):4161-9. [PMID: 18433149] 
Functional Description
  
Sequence Annotation
 ACT_SITE 319 319 By similarity.
 METAL 318 318 Zinc; catalytic (By similarity).
 METAL 322 322 Zinc; catalytic (By similarity).
 METAL 328 328 Zinc; catalytic (By similarity).
 MOD_RES 361 361 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 696 AA 
Protein Sequence
MVGSKDIDLF NLRENEQIVS PCLIVHGKCN KQNGAKTVQV QHPQLPPITY PIHNQFFKAT 60
VILTPGENKL TFVTDTNTAR TIVCYYTPLT QNPPVHLCLI LAKDSPLQFD SPREQKDREG 120
GNGLELAIKK LRLGARLMQA YTNEQMLRNS MGNRTFPFVE EFTWDTLFER PAMRNTIKIH 180
VVRSEKTVKE IQDPDIAQQN SKGKNTGALF GIAMDALKSY GGPFTNNEKP VQAACMFLDT 240
HWDGKLIRGH AALGGGDDSI KLAIFGSHGL YSWPTCLEQL VPYFTDETRS STSEVANDCN 300
ECGTYWECLT ITLGAFMHEI GHLLGCPHQE SGVMLRGYTT LNRSFLTKEA YSVRTNSTGA 360
SPPIFPKEEC TWNRLDTVRF LYHPSFTLPQ DYYDPSFMRP TKLGGYPNIK HSVYPLGNGS 420
CRILSPTGIY LIEIICDDLA RGHIEYLPVS LGGQGPQREV IVTLDDLRAR LPKNELAKFG 480
NTFKLKILSV NAPETEFDKF PSLLDVQPLD MSKYGFSKNV QGIKSPLYGR SDGGNAVGVV 540
AFDVRLVTAV RIYHGYALDG VRFYYKEKPT GTKDAPASKP SVPPRNYFSK ITHSIKNHAS 600
INEENLKSVL FGHETQNFTD ATLEPGEIII GFNLRCGAWV DAIQIITSHG RMTDMFGNKD 660
GGGFAELQPP NGQYILGVTG RVGQWVDAFG IIYGAL 696 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR001229; Mannose-bd_lectin.
 IPR024079; MetalloPept_cat_dom.
 IPR021917; Unchr_Zn-peptidase-like. 
Pfam
 PF01419; Jacalin
 PF12044; Metallopep 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS