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9D1Z

Structure of G75Q Ubiquitin bound to KLHDC3-EloB/C

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007131biological_processreciprocal meiotic recombination
A0016567biological_processprotein ubiquitination
A0031462cellular_componentCul2-RING ubiquitin ligase complex
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0051321biological_processmeiotic cell cycle
A0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
A1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
B0006368biological_processtranscription elongation by RNA polymerase II
B0030891cellular_componentVCB complex
B0070449cellular_componentelongin complex
C0006511biological_processubiquitin-dependent protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
DLYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
BMET1
DARG72

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62869
ChainResidueDetails
BTHR84

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
DSER65

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
DTHR66

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
DGLY76

site_idSWS_FT_FI6
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
DLYS6

site_idSWS_FT_FI7
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
DGLY76

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
DLYS11
DLYS48

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
DLYS27

site_idSWS_FT_FI10
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
DLYS29

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
DLYS33

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
DLYS63

237735

PDB entries from 2025-06-18

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