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7OIM

Mouse RNF213, with mixed nucleotides bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0002040biological_processsprouting angiogenesis
A0002376biological_processimmune system process
A0003689molecular_functionDNA clamp loader activity
A0004842molecular_functionubiquitin-protein transferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006511biological_processubiquitin-dependent protein catabolic process
A0006629biological_processlipid metabolic process
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0019216biological_processregulation of lipid metabolic process
A0042742biological_processdefense response to bacterium
A0046872molecular_functionmetal ion binding
A0051865biological_processprotein autoubiquitination
A0061630molecular_functionubiquitin protein ligase activity
A0061775molecular_functioncohesin loader activity
A0070534biological_processprotein K63-linked ubiquitination
A0098792biological_processxenophagy
A0120323biological_processlipid ubiquitination
A0140042biological_processlipid droplet formation
A0140584molecular_functionchromatin extrusion motor activity
A0140588biological_processchromatin looping
A0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
A0140849molecular_functionATP-dependent H2AZ histone chaperone activity
A2000051biological_processnegative regulation of non-canonical Wnt signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CdHvYClrCI
ChainResidueDetails
ACYS3962-ILE3971

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues39
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS3947-LEU3986

site_idSWS_FT_FI2
Number of Residues72
DetailsZN_FING: RZ-type => ECO:0000255|PROSITE-ProRule:PRU01325
ChainResidueDetails
AMET4429-THR4501

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile; for E3 ubiquitin-lipopolysaccharide ligase activity => ECO:0000255|PROSITE-ProRule:PRU01325
ChainResidueDetails
ACYS4462

site_idSWS_FT_FI4
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:32573437, ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY
ChainResidueDetails
AGLY1957
ACYS3982
ACYS3985
AGLU2060
AASP2116
ACYS3947
ACYS3950
ACYS3962
AHIS3964
ACYS3967
ACYS3970

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32573437, ECO:0007744|PDB:6TAY
ChainResidueDetails
AALA2114
ALYS2460

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32573437, ECO:0007744|PDB:6TAX
ChainResidueDetails
AARG2177
ASER2535

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01325
ChainResidueDetails
ACYS4451
AHIS4455
ACYS4471
ACYS4474

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q63HN8
ChainResidueDetails
ASER2234

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q63HN8
ChainResidueDetails
ALYS1128

227111

PDB entries from 2024-11-06

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