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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5HPT

System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes: WWP1, Ubv P2.3 and UBCH7

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
C0000151cellular_componentubiquitin ligase complex
C0000166molecular_functionnucleotide binding
C0000209biological_processprotein polyubiquitination
C0003713molecular_functiontranscription coactivator activity
C0003723molecular_functionRNA binding
C0004842molecular_functionubiquitin-protein transferase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006355biological_processregulation of DNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0008283biological_processcell population proliferation
C0016567biological_processprotein ubiquitination
C0016740molecular_functiontransferase activity
C0019787molecular_functionubiquitin-like protein transferase activity
C0019899molecular_functionenzyme binding
C0031398biological_processpositive regulation of protein ubiquitination
C0031625molecular_functionubiquitin protein ligase binding
C0032446biological_processprotein modification by small protein conjugation
C0036211biological_processprotein modification process
C0044770biological_processcell cycle phase transition
C0045893biological_processpositive regulation of DNA-templated transcription
C0061631molecular_functionubiquitin conjugating enzyme activity
C0070979biological_processprotein K11-linked ubiquitination
C0071383biological_processcellular response to steroid hormone stimulus
C0071385biological_processcellular response to glucocorticoid stimulus
C0097027molecular_functionubiquitin-protein transferase activator activity
C1903955biological_processpositive regulation of protein targeting to mitochondrion
D0004842molecular_functionubiquitin-protein transferase activity
F0000151cellular_componentubiquitin ligase complex
F0000166molecular_functionnucleotide binding
F0000209biological_processprotein polyubiquitination
F0003713molecular_functiontranscription coactivator activity
F0003723molecular_functionRNA binding
F0004842molecular_functionubiquitin-protein transferase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006355biological_processregulation of DNA-templated transcription
F0006511biological_processubiquitin-dependent protein catabolic process
F0008283biological_processcell population proliferation
F0016567biological_processprotein ubiquitination
F0016740molecular_functiontransferase activity
F0019787molecular_functionubiquitin-like protein transferase activity
F0019899molecular_functionenzyme binding
F0031398biological_processpositive regulation of protein ubiquitination
F0031625molecular_functionubiquitin protein ligase binding
F0032446biological_processprotein modification by small protein conjugation
F0036211biological_processprotein modification process
F0044770biological_processcell cycle phase transition
F0045893biological_processpositive regulation of DNA-templated transcription
F0061631molecular_functionubiquitin conjugating enzyme activity
F0070979biological_processprotein K11-linked ubiquitination
F0071383biological_processcellular response to steroid hormone stimulus
F0071385biological_processcellular response to glucocorticoid stimulus
F0097027molecular_functionubiquitin-protein transferase activator activity
F1903955biological_processpositive regulation of protein targeting to mitochondrion
G0004842molecular_functionubiquitin-protein transferase activity
Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNIdek.GqVCLpvI
ChainResidueDetails
CTYR75-ILE90
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00104","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Required for ubiquitin-thioester formation","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25474007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues294
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 438
ChainResidueDetails
CCYS86nucleofuge
site_idMCSA2
Number of Residues1
DetailsM-CSA 438
ChainResidueDetails
FCYS86nucleofuge

238895

PDB entries from 2025-07-16

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