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8UQA

Crystal structure of RNF168 (RING)-UbcH5c fused to H2A-H2B via a 12-residue linker

Functional Information from GO Data
ChainGOidnamespacecontents
K0000122biological_processnegative regulation of transcription by RNA polymerase II
K0000151cellular_componentubiquitin ligase complex
K0000209biological_processprotein polyubiquitination
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0004842molecular_functionubiquitin-protein transferase activity
K0005515molecular_functionprotein binding
K0005524molecular_functionATP binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005768cellular_componentendosome
K0005829cellular_componentcytosol
K0005886cellular_componentplasma membrane
K0006281biological_processDNA repair
K0006511biological_processubiquitin-dependent protein catabolic process
K0006513biological_processprotein monoubiquitination
K0006915biological_processapoptotic process
K0010008cellular_componentendosome membrane
K0016567biological_processprotein ubiquitination
K0016740molecular_functiontransferase activity
K0019787molecular_functionubiquitin-like protein transferase activity
K0030514biological_processnegative regulation of BMP signaling pathway
K0030527molecular_functionstructural constituent of chromatin
K0031625molecular_functionubiquitin protein ligase binding
K0036211biological_processprotein modification process
K0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
K0046982molecular_functionprotein heterodimerization activity
K0051865biological_processprotein autoubiquitination
K0061630molecular_functionubiquitin protein ligase activity
K0061631molecular_functionubiquitin conjugating enzyme activity
K0070062cellular_componentextracellular exosome
K0070936biological_processprotein K48-linked ubiquitination
K0070979biological_processprotein K11-linked ubiquitination
K0085020biological_processprotein K6-linked ubiquitination
K1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
KALA3021-VAL3027

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
KARG2092-GLY2114

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(beta-hydroxybutyryl)lysine; alternate => ECO:0000269|PubMed:27105115
ChainResidueDetails
KLYS3013

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
KLYS3036

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
KLYS3074
KLYS3075

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
KLYS3095
KLYS2034
KLYS2116
KLYS2120

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N5-methylglutamine => ECO:0000269|PubMed:24352239
ChainResidueDetails
KGLN3104

site_idSWS_FT_FI6
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
KLYS3013

site_idSWS_FT_FI7
Number of Residues2
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
KLYS2120

site_idSWS_FT_FI8
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22713238, ECO:0000269|PubMed:22980979
ChainResidueDetails
KLYS3015

site_idSWS_FT_FI9
Number of Residues39
DetailsZN_FING: RING-type => ECO:0000255|HAMAP-Rule:MF_03066
ChainResidueDetails
KCYS16-ARG55

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80XJ2
ChainResidueDetails
KSER70

site_idSWS_FT_FI11
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133
ChainResidueDetails
KLYS1085

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
KGLU2035

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64524
ChainResidueDetails
KSER2036

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
KLYS2043
KLYS2085

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869
ChainResidueDetails
KLYS2046
KLYS2108

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
KLYS2057

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
KARG2079

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
KARG2086
KARG2092

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
KTHR2115

site_idSWS_FT_FI20
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
KSER2112

site_idSWS_FT_FI21
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
KLYS2034

226707

PDB entries from 2024-10-30

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