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7R2G

USP15 D1D2 in catalytically-competent state bound to mitoxantrone stack (isoform 2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLsnlGNtCFMNSaIQ
ChainResidueDetails
AGLY261-GLN276

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YnLiAVsnHyGgmgg..GHY
ChainResidueDetails
ATYR846-TYR863

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19553310","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21947082","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22344298","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24852371","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27368102","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"33093067","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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