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6YBT

Structure of a human 48S translational initiation complex - eIF3bgi

Functional Information from GO Data
ChainGOidnamespacecontents
10001732biological_processformation of cytoplasmic translation initiation complex
10002183biological_processcytoplasmic translational initiation
10003676molecular_functionnucleic acid binding
10003723molecular_functionRNA binding
10003743molecular_functiontranslation initiation factor activity
10005515molecular_functionprotein binding
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10005852cellular_componenteukaryotic translation initiation factor 3 complex
10006412biological_processtranslation
10006413biological_processtranslational initiation
10006446biological_processregulation of translational initiation
10010494cellular_componentcytoplasmic stress granule
10016282cellular_componenteukaryotic 43S preinitiation complex
10031369molecular_functiontranslation initiation factor binding
10033290cellular_componenteukaryotic 48S preinitiation complex
10045202cellular_componentsynapse
10060090molecular_functionmolecular adaptor activity
10070062cellular_componentextracellular exosome
10071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
10075522biological_processIRES-dependent viral translational initiation
10075525biological_processviral translational termination-reinitiation
20001732biological_processformation of cytoplasmic translation initiation complex
20002183biological_processcytoplasmic translational initiation
20003723molecular_functionRNA binding
20003743molecular_functiontranslation initiation factor activity
20005515molecular_functionprotein binding
20005737cellular_componentcytoplasm
20005829cellular_componentcytosol
20005852cellular_componenteukaryotic translation initiation factor 3 complex
20006412biological_processtranslation
20006413biological_processtranslational initiation
20016282cellular_componenteukaryotic 43S preinitiation complex
20033290cellular_componenteukaryotic 48S preinitiation complex
20045202cellular_componentsynapse
20070062cellular_componentextracellular exosome
20071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
u0001732biological_processformation of cytoplasmic translation initiation complex
u0002183biological_processcytoplasmic translational initiation
u0002188biological_processtranslation reinitiation
u0003723molecular_functionRNA binding
u0003729molecular_functionmRNA binding
u0003743molecular_functiontranslation initiation factor activity
u0005198molecular_functionstructural molecule activity
u0005515molecular_functionprotein binding
u0005654cellular_componentnucleoplasm
u0005730cellular_componentnucleolus
u0005737cellular_componentcytoplasm
u0005829cellular_componentcytosol
u0005852cellular_componenteukaryotic translation initiation factor 3 complex
u0005874cellular_componentmicrotubule
u0006412biological_processtranslation
u0006413biological_processtranslational initiation
u0014069cellular_componentpostsynaptic density
u0016020cellular_componentmembrane
u0016282cellular_componenteukaryotic 43S preinitiation complex
u0030971molecular_functionreceptor tyrosine kinase binding
u0032991cellular_componentprotein-containing complex
u0033290cellular_componenteukaryotic 48S preinitiation complex
u0043614cellular_componentmulti-eIF complex
u0070373biological_processnegative regulation of ERK1 and ERK2 cascade
u0071540cellular_componenteukaryotic translation initiation factor 3 complex, eIF3e
u0071541cellular_componenteukaryotic translation initiation factor 3 complex, eIF3m
u0075522biological_processIRES-dependent viral translational initiation
u0075525biological_processviral translational termination-reinitiation
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. VLTGsaDnSCRLWDC
ChainResidueDetails
2VAL67-CYS81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
1MET1

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
1SER78
1SER81

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648
ChainResidueDetails
1SER83
1SER85
uSER949
uSER1028
uSER1188
uSER1262

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308
ChainResidueDetails
1SER119
uSER1198
uSER1336

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
1SER125

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
1SER152
1SER164

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
1SER154

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
1LYS209
1LYS288
1LYS364

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
1SER239

223166

PDB entries from 2024-07-31

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