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8UQE

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 26-residue linker (RING not modeled in density)

Functional Information from GO Data
ChainGOidnamespacecontents
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000151cellular_componentubiquitin ligase complex
B0000209biological_processprotein polyubiquitination
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0004842molecular_functionubiquitin-protein transferase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005768cellular_componentendosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006281biological_processDNA repair
B0006511biological_processubiquitin-dependent protein catabolic process
B0006513biological_processprotein monoubiquitination
B0006915biological_processapoptotic process
B0010008cellular_componentendosome membrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0019787molecular_functionubiquitin-like protein transferase activity
B0030514biological_processnegative regulation of BMP signaling pathway
B0030527molecular_functionstructural constituent of chromatin
B0031625molecular_functionubiquitin protein ligase binding
B0036211biological_processprotein modification process
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0046872molecular_functionmetal ion binding
B0046982molecular_functionprotein heterodimerization activity
B0051865biological_processprotein autoubiquitination
B0061630molecular_functionubiquitin protein ligase activity
B0061631molecular_functionubiquitin conjugating enzyme activity
B0070062cellular_componentextracellular exosome
B0070936biological_processprotein K48-linked ubiquitination
B0070979biological_processprotein K11-linked ubiquitination
B0085020biological_processprotein K6-linked ubiquitination
B1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
BALA3021-VAL3027

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
BARG2092-GLY2114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsZN_FING: RING-type => ECO:0000255|HAMAP-Rule:MF_03066
ChainResidueDetails
BCYS16-ARG55

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80XJ2
ChainResidueDetails
BSER70

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
BLYS1085

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS2034
BLYS2116
BLYS2120
BLYS3095

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
BGLU2035

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64524
ChainResidueDetails
BSER2036

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
BLYS2043
BLYS2085

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
BLYS2046
BLYS2108

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
BLYS2057

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
BARG2079

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
BARG2086
BARG2092

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
BTHR2115

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
BSER2112

site_idSWS_FT_FI14
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
BLYS2034

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22980979
ChainResidueDetails
BLYS3015

site_idSWS_FT_FI16
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
ChainResidueDetails
BLYS2120

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: N6-(beta-hydroxybutyryl)lysine; alternate => ECO:0000269|PubMed:27105115
ChainResidueDetails
BLYS3013

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
BLYS3036

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
BLYS3074
BLYS3075

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N5-methylglutamine => ECO:0000269|PubMed:24352239
ChainResidueDetails
BGLN3104

site_idSWS_FT_FI21
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22980979
ChainResidueDetails
BLYS3013

222036

PDB entries from 2024-07-03

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