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5L8W

Structure of USP12-UB-PRG/UAF1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0046872molecular_functionmetal ion binding
A0101005molecular_functiondeubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue AYE A 401
ChainResidue
AASN43
AASN46
ACYS48
AGLN122
AGLY316
AHIS317
CGLY75

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS233
ACYS236
ACYS186
ACYS189

site_idAC3
Number of Residues2
Detailsbinding site for residue GOL A 403
ChainResidue
BSER155
BVAL159

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-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. GLvnfGNtCYCNSvLQ
ChainResidueDetails
AGLY40-GLN55

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YdLvAVvvHcGsgpnr.GHY
ChainResidueDetails
ATYR300-TYR318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
CARG54
CARG72

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Essential for function
ChainResidueDetails
CHIS68

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
CSER65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
CTHR66
ACYS233
ACYS236

site_idSWS_FT_FI5
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
CLYS6

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
CLYS63

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
CLYS11
CLYS48

site_idSWS_FT_FI8
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
CLYS27

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
CLYS29

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
CLYS33

225946

PDB entries from 2024-10-09

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