CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002839
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase isozyme L1 
Protein Synonyms/Alias
 UCH-L1; Neuron cytoplasmic protein 9.5; PGP 9.5; PGP9.5; Ubiquitin thioesterase L1 
Gene Name
 UCHL1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MQLKPMEINPEubiquitination[1, 2, 3, 4]
15INPEMLNKVLSRLGVubiquitination[2]
65QHENFRKKQIEELKGubiquitination[1, 3, 4]
71KKQIEELKGQEVSPKubiquitination[1, 3, 4]
78KGQEVSPKVYFMKQTubiquitination[2, 4]
83SPKVYFMKQTIGNSCubiquitination[2]
115FEDGSVLKQFLSETEubiquitination[2, 3, 4, 5]
123QFLSETEKMSPEDRAubiquitination[4]
135DRAKCFEKNEAIQAAubiquitination[3, 4]
157GQCRVDDKVNFHFILubiquitination[1, 3, 4, 6]
195SSEDTLLKDAAKVCRacetylation[7]
195SSEDTLLKDAAKVCRubiquitination[4]
Reference
 [1] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861
Functional Description
 Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity. 
Sequence Annotation
 REGION 5 10 Interaction with ubiquitin.
 REGION 211 216 Interaction with ubiquitin.
 ACT_SITE 90 90 Nucleophile.
 ACT_SITE 161 161 Proton donor.
 LIPID 220 220 S-farnesyl cysteine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Hydrolase; Ligase; Lipoprotein; Membrane; Neurodegeneration; Oxidation; Parkinson disease; Parkinsonism; Polymorphism; Prenylation; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 223 AA 
Protein Sequence
MQLKPMEINP EMLNKVLSRL GVAGQWRFVD VLGLEEESLG SVPAPACALL LLFPLTAQHE 60
NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLGFED GSVLKQFLSE 120
TEKMSPEDRA KCFEKNEAIQ AAHDAVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP 180
FPVNHGASSE DTLLKDAAKV CREFTEREQG EVRFSAVALC KAA 223 
Gene Ontology
 GO:0030424; C:axon; IEA:Compara.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008242; F:omega peptidase activity; IDA:UniProtKB.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; TAS:UniProtKB.
 GO:0007628; P:adult walking behavior; IEA:Compara.
 GO:0007412; P:axon target recognition; IEA:Compara.
 GO:0019896; P:axon transport of mitochondrion; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0042755; P:eating behavior; IEA:Compara.
 GO:0048747; P:muscle fiber development; IEA:Compara.
 GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
 GO:0050905; P:neuromuscular process; IEA:Compara.
 GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
 GO:0006950; P:response to stress; IEA:Compara.
 GO:0019233; P:sensory perception of pain; IEA:Compara.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Compara. 
Interpro
 IPR001578; Peptidase_C12. 
Pfam
 PF01088; Peptidase_C12 
SMART
  
PROSITE
 PS00140; UCH_1 
PRINTS
 PR00707; UBCTHYDRLASE.