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2LEN

Solution structure of UCHL1 S18Y variant

Functional Information from GO Data
ChainGOidnamespacecontents
A0002176biological_processmale germ cell proliferation
A0002931biological_processresponse to ischemia
A0004197molecular_functioncysteine-type endopeptidase activity
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006511biological_processubiquitin-dependent protein catabolic process
A0007409biological_processaxonogenesis
A0007412biological_processaxon target recognition
A0007628biological_processadult walking behavior
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0008242molecular_functionomega peptidase activity
A0016241biological_processregulation of macroautophagy
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
A0019896biological_processaxonal transport of mitochondrion
A0030163biological_processprotein catabolic process
A0030424cellular_componentaxon
A0030547molecular_functionsignaling receptor inhibitor activity
A0031625molecular_functionubiquitin protein ligase binding
A0031694molecular_functionalpha-2A adrenergic receptor binding
A0042755biological_processeating behavior
A0043022molecular_functionribosome binding
A0043025cellular_componentneuronal cell body
A0043130molecular_functionubiquitin binding
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043409biological_processnegative regulation of MAPK cascade
A0044306cellular_componentneuron projection terminus
A0045821biological_processpositive regulation of glycolytic process
A0050905biological_processneuromuscular process
A0055001biological_processmuscle cell development
A0071466biological_processcellular response to xenobiotic stimulus
A1904115cellular_componentaxon cytoplasm
Functional Information from PROSITE/UniProt
site_idPS00140
Number of Residues17
DetailsUCH_1 Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site. QtigNSCGtigLIHAVA
ChainResidueDetails
AGLN84-ALA100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsPropeptide: {"description":"Removed in mature form","featureId":"PRO_0000414311","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues219
DetailsDomain: {"description":"UCH catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsRegion: {"description":"Interaction with ubiquitin","evidences":[{"source":"PubMed","id":"20439756","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20439756","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20439756","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsSite: {"description":"Susceptible to oxidation","evidences":[{"source":"PubMed","id":"14722078","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8639624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsSite: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"37316325","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q00981","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsLipidation: {"description":"S-farnesyl cysteine","evidences":[{"source":"PubMed","id":"19261853","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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