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9B83

Cryo-EM structure of human ADAR1 in complex with dsRNA derived from human GLI1 gene

Functional Information from GO Data
ChainGOidnamespacecontents
A0001649biological_processosteoblast differentiation
A0002244biological_processhematopoietic progenitor cell differentiation
A0002376biological_processimmune system process
A0002566biological_processsomatic diversification of immune receptors via somatic mutation
A0003677molecular_functionDNA binding
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0003726molecular_functiondouble-stranded RNA adenosine deaminase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006382biological_processadenosine to inosine editing
A0006396biological_processRNA processing
A0006397biological_processmRNA processing
A0006915biological_processapoptotic process
A0008251molecular_functiontRNA-specific adenosine deaminase activity
A0009615biological_processresponse to virus
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0016553biological_processbase conversion or substitution editing
A0016787molecular_functionhydrolase activity
A0030218biological_processerythrocyte differentiation
A0030288cellular_componentouter membrane-bounded periplasmic space
A0031047biological_processregulatory ncRNA-mediated gene silencing
A0031054biological_processpre-miRNA processing
A0031981cellular_componentnuclear lumen
A0034219biological_processcarbohydrate transmembrane transport
A0035196biological_processmiRNA processing
A0035455biological_processresponse to interferon-alpha
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0044387biological_processnegative regulation of protein kinase activity by regulation of protein phosphorylation
A0044530cellular_componentsupraspliceosomal complex
A0045070biological_processpositive regulation of viral genome replication
A0045087biological_processinnate immune response
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0060216biological_processdefinitive hemopoiesis
A0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
A0061484biological_processhematopoietic stem cell homeostasis
A0070922biological_processRISC complex assembly
A0097284biological_processhepatocyte apoptotic process
A0098586biological_processcellular response to virus
A1900369biological_processnegative regulation of post-transcriptional gene silencing by regulatory ncRNA
A1901982molecular_functionmaltose binding
A1903944biological_processnegative regulation of hepatocyte apoptotic process
B0001649biological_processosteoblast differentiation
B0002244biological_processhematopoietic progenitor cell differentiation
B0002376biological_processimmune system process
B0002566biological_processsomatic diversification of immune receptors via somatic mutation
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0003726molecular_functiondouble-stranded RNA adenosine deaminase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0006382biological_processadenosine to inosine editing
B0006396biological_processRNA processing
B0006397biological_processmRNA processing
B0006915biological_processapoptotic process
B0008251molecular_functiontRNA-specific adenosine deaminase activity
B0009615biological_processresponse to virus
B0015768biological_processmaltose transport
B0016020cellular_componentmembrane
B0016553biological_processbase conversion or substitution editing
B0016787molecular_functionhydrolase activity
B0030218biological_processerythrocyte differentiation
B0030288cellular_componentouter membrane-bounded periplasmic space
B0031047biological_processregulatory ncRNA-mediated gene silencing
B0031054biological_processpre-miRNA processing
B0031981cellular_componentnuclear lumen
B0034219biological_processcarbohydrate transmembrane transport
B0035196biological_processmiRNA processing
B0035455biological_processresponse to interferon-alpha
B0042597cellular_componentperiplasmic space
B0042956biological_processmaltodextrin transmembrane transport
B0044387biological_processnegative regulation of protein kinase activity by regulation of protein phosphorylation
B0044530cellular_componentsupraspliceosomal complex
B0045070biological_processpositive regulation of viral genome replication
B0045087biological_processinnate immune response
B0046872molecular_functionmetal ion binding
B0051607biological_processdefense response to virus
B0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B0060216biological_processdefinitive hemopoiesis
B0060339biological_processnegative regulation of type I interferon-mediated signaling pathway
B0061484biological_processhematopoietic stem cell homeostasis
B0070922biological_processRISC complex assembly
B0097284biological_processhepatocyte apoptotic process
B0098586biological_processcellular response to virus
B1900369biological_processnegative regulation of post-transcriptional gene silencing by regulatory ncRNA
B1901982molecular_functionmaltose binding
B1903944biological_processnegative regulation of hepatocyte apoptotic process
Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO-158-ASN-141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00240
ChainResidueDetails
AGLU912
BGLU912

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00240
ChainResidueDetails
AHIS910
ACYS966
ACYS1036
BHIS910
BCYS966
BCYS1036

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P55266
ChainResidueDetails
ASER285
BSER285

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER481
ASER629
ASER636
ASER814
BSER481
BSER629
BSER636
BSER814

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR601
BTHR601

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR603
BTHR603

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER614
ASER823
BSER614
BSER823

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR808
BTHR808

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER825
BSER825

site_idSWS_FT_FI10
Number of Residues10
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS384
BLYS875
ALYS408
ALYS580
ALYS875
BLYS384
BLYS408
BLYS580

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS418
BLYS418

236620

PDB entries from 2025-05-28

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