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4DHZ

The structure of h/ceOTUB1-ubiquitin aldehyde-UBC13~Ub

Functional Information from GO Data
ChainGOidnamespacecontents
A0016579biological_processprotein deubiquitination
A0016787molecular_functionhydrolase activity
F0000151cellular_componentubiquitin ligase complex
F0000166molecular_functionnucleotide binding
F0000209biological_processprotein polyubiquitination
F0000724biological_processdouble-strand break repair via homologous recombination
F0000729biological_processDNA double-strand break processing
F0001650cellular_componentfibrillar center
F0003723molecular_functionRNA binding
F0004842molecular_functionubiquitin-protein transferase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006281biological_processDNA repair
F0006282biological_processregulation of DNA repair
F0006301biological_processDNA damage tolerance
F0006513biological_processprotein monoubiquitination
F0006974biological_processDNA damage response
F0016567biological_processprotein ubiquitination
F0016740molecular_functiontransferase activity
F0031371cellular_componentubiquitin conjugating enzyme complex
F0031372cellular_componentUBC13-MMS2 complex
F0031625molecular_functionubiquitin protein ligase binding
F0032991cellular_componentprotein-containing complex
F0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
F0043130molecular_functionubiquitin binding
F0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
F0045739biological_processpositive regulation of DNA repair
F0050852biological_processT cell receptor signaling pathway
F0061631molecular_functionubiquitin conjugating enzyme activity
F0070062cellular_componentextracellular exosome
F0070534biological_processprotein K63-linked ubiquitination
F0097027molecular_functionubiquitin-protein transferase activator activity
F0140374biological_processantiviral innate immune response
F1902523biological_processpositive regulation of protein K63-linked ubiquitination
F1902533biological_processpositive regulation of intracellular signal transduction
F1904262biological_processnegative regulation of TORC1 signaling
F2000781biological_processpositive regulation of double-strand break repair
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNVdkl.GrICLdiL
ChainResidueDetails
FTYR76-LEU91

site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS527-ASP552
ELYS527-ASP552

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsRegion: {"description":"Ubiquitin-conjugating enzyme E2 binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues13
DetailsRegion: {"description":"Free ubiquitin binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"Ubiquitin-conjugating enzyme E2 binding","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q96DC9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q96DC9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Interacts with free ubiquitin","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Interacts with free ubiquitin","evidences":[{"source":"PubMed","id":"22325355","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22367539","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DHZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"35927303","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues197
DetailsDomain: {"description":"OTU","evidences":[{"source":"PROSITE-ProRule","id":"PRU00139","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q96FW1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q5VVQ6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues146
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
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 Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)","evidences":[{"source":"PubMed","id":"16112642","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16122702","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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