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2PX9

The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications

Functional Information from GO Data
ChainGOidnamespacecontents
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000166molecular_functionnucleotide binding
B0000795cellular_componentsynaptonemal complex
B0001221molecular_functiontranscription coregulator binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005643cellular_componentnuclear pore
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006511biological_processubiquitin-dependent protein catabolic process
B0007049biological_processcell cycle
B0007059biological_processchromosome segregation
B0007084biological_processmitotic nuclear membrane reassembly
B0008134molecular_functiontranscription factor binding
B0016605cellular_componentPML body
B0016740molecular_functiontransferase activity
B0016925biological_processprotein sumoylation
B0019787molecular_functionubiquitin-like protein transferase activity
B0019789molecular_functionSUMO transferase activity
B0019899molecular_functionenzyme binding
B0030335biological_processpositive regulation of cell migration
B0032446biological_processprotein modification by small protein conjugation
B0036211biological_processprotein modification process
B0044388molecular_functionsmall protein activating enzyme binding
B0045892biological_processnegative regulation of DNA-templated transcription
B0048471cellular_componentperinuclear region of cytoplasm
B0051168biological_processnuclear export
B0051301biological_processcell division
B0061656molecular_functionSUMO conjugating enzyme activity
B0071535molecular_functionRING-like zinc finger domain binding
B0106068cellular_componentSUMO ligase complex
B1903755biological_processpositive regulation of SUMO transferase activity
B1990234cellular_componenttransferase complex
Functional Information from PROSITE/UniProt
site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PGCTIRnTP
ChainResidueDetails
APRO171-PRO179

site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
BPHE82-LEU97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Glycyl thioester intermediate
ChainResidueDetails
BCYS93

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Interaction with RANBP2
ChainResidueDetails
BILE4
BVAL25
BLEU57

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate binding
ChainResidueDetails
BASP100

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
BSER2
ALYS275

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS65
ALYS371

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:22509284, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER71

site_idSWS_FT_FI7
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
BLYS18

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS271
BLYS101

site_idSWS_FT_FI9
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS48

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS49

218853

PDB entries from 2024-04-24

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