CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-045066
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Thimet oligopeptidase 
Protein Synonyms/Alias
  
Gene Name
 THOP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
95KMEDGKLKVTLKYPHubiquitination[1]
99GKLKVTLKYPHYFPLubiquitination[1, 2, 3]
109HYFPLLKKCHVPETRubiquitination[1]
118HVPETRRKVEEAFNCubiquitination[1]
128EAFNCRCKEENCAILacetylation[4]
136EENCAILKELVTLRAacetylation[4, 5]
136EENCAILKELVTLRAubiquitination[1]
182DELAQKLKPLGEQERubiquitination[1]
196RAVILELKRAECERRubiquitination[1, 3]
Reference
 [1] 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]
 [2] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 568 AA 
Protein Sequence
MFLFQEKVQK DSLRPEAARY LERLIKLGRR NGLHLPRETQ ENIKRIKKKL SLLCIDFNKN 60
LNEDTTFLPF TLQELGGLPE DFLNSLEKME DGKLKVTLKY PHYFPLLKKC HVPETRRKVE 120
EAFNCRCKEE NCAILKELVT LRAQKSRLLG FHTHADYVLE MNMAKTSQTV ATFLDELAQK 180
LKPLGEQERA VILELKRAEC ERRGLPFDGR IRAWDMRYYM NQVEETRYCV DQNLLKEYFP 240
VQVVTHGLLG IYQELLGLAF HHEEGASAWH EDVRLYTARD AASGEVVGKF YLDLYPREGK 300
YGHAACFGLQ PGCLRQDGSR QIAIAAMVAN FTKPTADAPS LLQHDEVETY FHEFGHVMHQ 360
LCSQAEFAMF SGTHVERDFV EAPSQMLENW VWEQEPLLRM SRHYRTGSAV PRELLEKLIE 420
SRQANTGLFN LRQIVLAKVD QALHTQTDAD PAEEYARLCQ EILGVPATPG TNMPATFGHL 480
AGGYDAQYYG YLWSEVYSMD MFHTRFKQEG VLNSKVGMDY RSCILRPGGS EDASAMLRRF 540
LGRDPKQDAF LLSKGLQVGG CEPEPQVC 568 
Gene Ontology
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR024079; MetalloPept_cat_dom.
 IPR024077; Neurolysin/TOP_dom2.
 IPR001567; Pept_M3A_M3B. 
Pfam
 PF01432; Peptidase_M3 
SMART
  
PROSITE
  
PRINTS