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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8A9K

Cryo-EM structure of USP1-UAF1 bound to FANCI and mono-ubiquitinated FANCD2 with ML323 (consensus reconstruction)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0016020cellular_componentmembrane
A0031398biological_processpositive regulation of protein ubiquitination
A0036297biological_processinterstrand cross-link repair
A0070182molecular_functionDNA polymerase binding
A1990391cellular_componentDNA repair complex
B0000785cellular_componentchromatin
B0000793cellular_componentcondensed chromosome
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0007129biological_processhomologous chromosome pairing at meiosis
B0007276biological_processgamete generation
B0010332biological_processresponse to gamma radiation
B0016604cellular_componentnuclear body
B0031573biological_processmitotic intra-S DNA damage checkpoint signaling
B0034599biological_processcellular response to oxidative stress
B0036297biological_processinterstrand cross-link repair
B0045589biological_processregulation of regulatory T cell differentiation
B0048854biological_processbrain morphogenesis
B0050727biological_processregulation of inflammatory response
B0070182molecular_functionDNA polymerase binding
B0097150biological_processneuronal stem cell population maintenance
B1990391cellular_componentDNA repair complex
B1990918biological_processdouble-strand break repair involved in meiotic recombination
B2000348biological_processregulation of CD40 signaling pathway
D0001501biological_processskeletal system development
D0004197molecular_functioncysteine-type endopeptidase activity
D0004843molecular_functioncysteine-type deubiquitinase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005829cellular_componentcytosol
D0006281biological_processDNA repair
D0006282biological_processregulation of DNA repair
D0006508biological_processproteolysis
D0006974biological_processDNA damage response
D0008233molecular_functionpeptidase activity
D0008234molecular_functioncysteine-type peptidase activity
D0009411biological_processresponse to UV
D0016579biological_processprotein deubiquitination
D0016787molecular_functionhydrolase activity
D0031647biological_processregulation of protein stability
D0035520biological_processmonoubiquitinated protein deubiquitination
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D1904333biological_processpositive regulation of error-prone translesion synthesis
E0000724biological_processdouble-strand break repair via homologous recombination
E0003677molecular_functionDNA binding
E0003690molecular_functiondouble-stranded DNA binding
E0003697molecular_functionsingle-stranded DNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005764cellular_componentlysosome
E0005770cellular_componentlate endosome
E0005829cellular_componentcytosol
E0006281biological_processDNA repair
E0006974biological_processDNA damage response
E0007283biological_processspermatogenesis
E0007338biological_processsingle fertilization
E0008584biological_processmale gonad development
E0035264biological_processmulticellular organism growth
E0035800molecular_functiondeubiquitinase activator activity
E0043130molecular_functionubiquitin binding
E0043588biological_processskin development
E0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
E0048568biological_processembryonic organ development
E0048705biological_processskeletal system morphogenesis
E0048872biological_processhomeostasis of number of cells
E0050679biological_processpositive regulation of epithelial cell proliferation
E0060255biological_processregulation of macromolecule metabolic process
E0072520biological_processseminiferous tubule development
E0080090biological_processregulation of primary metabolic process
E1902525biological_processregulation of protein monoubiquitination
E1905168biological_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
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA
ChainResidueDetails
ELEU90-ALA104
EVAL132-VAL146
site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YgLfAVvmHsGitiss.GHY
ChainResidueDetails
DTYR576-TYR594
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17412408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17412408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"17412408","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17460694","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19589784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385258","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"11239454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19111657","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20603015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20603016","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20603073","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385258","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BJQ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues39
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues39
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues39
DetailsRepeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-10-22

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