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1U9A

HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0001650cellular_componentfibrillar center
A0004842molecular_functionubiquitin-protein transferase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0007059biological_processchromosome segregation
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0016925biological_processprotein sumoylation
A0019789molecular_functionSUMO transferase activity
A0030425cellular_componentdendrite
A0035255molecular_functionionotropic glutamate receptor binding
A0036211biological_processprotein modification process
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043398molecular_functionHLH domain binding
A0043425molecular_functionbHLH transcription factor binding
A0050804biological_processmodulation of chemical synaptic transmission
A0051168biological_processnuclear export
A0051301biological_processcell division
A0061656molecular_functionSUMO conjugating enzyme activity
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098978cellular_componentglutamatergic synapse
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A0106068cellular_componentSUMO ligase complex
Functional Information from PDB Data
site_idC93
Number of Residues2
DetailsCYS 93 IS THE CONSERVED UBIQUITIN-ACCEPTING CYSTEINE.
ChainResidue
ACYS93
AASN0

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
APHE82-LEU97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU00388
ChainResidueDetails
ACYS93

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Interaction with RANBP2 => ECO:0000250
ChainResidueDetails
AILE4
AVAL25
ALEU57

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate binding => ECO:0000250
ChainResidueDetails
AASP100

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ASER2

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ALYS65

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ASER71

site_idSWS_FT_FI7
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ALYS18

site_idSWS_FT_FI8
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ALYS48
ALYS101

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P63279
ChainResidueDetails
ALYS49

223166

PDB entries from 2024-07-31

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