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9HNW

USP1-UAF1 bound to Lys63-linked diubiquitin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006508biological_processproteolysis
A0006974biological_processDNA damage response
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009411biological_processresponse to UV
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
A0031647biological_processregulation of protein stability
A0035520biological_processmonoubiquitinated protein deubiquitination
A0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
A1904333biological_processpositive regulation of error-prone translesion synthesis
B0000724biological_processdouble-strand break repair via homologous recombination
B0003677molecular_functionDNA binding
B0003690molecular_functiondouble-stranded DNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005770cellular_componentlate endosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0035800molecular_functiondeubiquitinase activator activity
B0043130molecular_functionubiquitin binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0060255biological_processregulation of macromolecule metabolic process
B0080090biological_processregulation of primary metabolic process
B0090263biological_processpositive regulation of canonical Wnt signaling pathway
B1905168biological_processpositive regulation of double-strand break repair via homologous recombination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52
DLYS27-ASP52

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA
ChainResidueDetails
BLEU90-ALA104
BVAL132-VAL146

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLnnlGNtCYLNSiLQ
ChainResidueDetails
AGLY82-GLN97

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YgLfAVvmHsGitiss.GHY
ChainResidueDetails
ATYR576-TYR594

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15694335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16531995","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26388029","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BJQ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues39
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues39
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues42
DetailsRepeat: {"description":"WD 7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues39
DetailsRepeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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