Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ONB

Structure of the U2 5' module of the A3'-SSA complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000124cellular_componentSAGA complex
A0000375biological_processRNA splicing, via transesterification reactions
A0000398biological_processmRNA splicing, via spliceosome
A0003676molecular_functionnucleic acid binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005681cellular_componentspliceosomal complex
A0005684cellular_componentU2-type spliceosomal complex
A0005686cellular_componentU2 snRNP
A0005689cellular_componentU12-type spliceosomal complex
A0005730cellular_componentnucleolus
A0006282biological_processregulation of DNA repair
A0006397biological_processmRNA processing
A0008380biological_processRNA splicing
A0030620molecular_functionU2 snRNA binding
A0042177biological_processnegative regulation of protein catabolic process
A0043484biological_processregulation of RNA splicing
A0044877molecular_functionprotein-containing complex binding
A0045893biological_processpositive regulation of DNA-templated transcription
A0071005cellular_componentU2-type precatalytic spliceosome
A0071013cellular_componentcatalytic step 2 spliceosome
A1903241biological_processU2-type prespliceosome assembly
B0000124cellular_componentSAGA complex
B0000398biological_processmRNA splicing, via spliceosome
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005681cellular_componentspliceosomal complex
B0005684cellular_componentU2-type spliceosomal complex
B0005686cellular_componentU2 snRNP
B0005689cellular_componentU12-type spliceosomal complex
B0006282biological_processregulation of DNA repair
B0006397biological_processmRNA processing
B0008380biological_processRNA splicing
B0043484biological_processregulation of RNA splicing
B0045893biological_processpositive regulation of DNA-templated transcription
B0071005cellular_componentU2-type precatalytic spliceosome
B0071011cellular_componentprecatalytic spliceosome
B1903241biological_processU2-type prespliceosome assembly
B1990935molecular_functionsplicing factor binding
C0000245biological_processspliceosomal complex assembly
C0000375biological_processRNA splicing, via transesterification reactions
C0000398biological_processmRNA splicing, via spliceosome
C0000785cellular_componentchromatin
C0003723molecular_functionRNA binding
C0003729molecular_functionmRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005681cellular_componentspliceosomal complex
C0005684cellular_componentU2-type spliceosomal complex
C0005686cellular_componentU2 snRNP
C0005689cellular_componentU12-type spliceosomal complex
C0005730cellular_componentnucleolus
C0006338biological_processchromatin remodeling
C0006397biological_processmRNA processing
C0008380biological_processRNA splicing
C0016607cellular_componentnuclear speck
C0031981cellular_componentnuclear lumen
C0034693cellular_componentU11/U12 snRNP
C0045943biological_processpositive regulation of transcription by RNA polymerase I
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0045945biological_processpositive regulation of transcription by RNA polymerase III
C0071004cellular_componentU2-type prespliceosome
C0071005cellular_componentU2-type precatalytic spliceosome
C0071013cellular_componentcatalytic step 2 spliceosome
C0110016cellular_componentB-WICH complex
C1903241biological_processU2-type prespliceosome assembly
C1990935molecular_functionsplicing factor binding
D0000398biological_processmRNA splicing, via spliceosome
D0003677molecular_functionDNA binding
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005681cellular_componentspliceosomal complex
D0005684cellular_componentU2-type spliceosomal complex
D0005686cellular_componentU2 snRNP
D0005689cellular_componentU12-type spliceosomal complex
D0006397biological_processmRNA processing
D0008270molecular_functionzinc ion binding
D0008380biological_processRNA splicing
D0016363cellular_componentnuclear matrix
D0016607cellular_componentnuclear speck
D0045893biological_processpositive regulation of DNA-templated transcription
D0046872molecular_functionmetal ion binding
D0048863biological_processstem cell differentiation
D0071005cellular_componentU2-type precatalytic spliceosome
D0071011cellular_componentprecatalytic spliceosome
D1903241biological_processU2-type prespliceosome assembly
I0000398biological_processmRNA splicing, via spliceosome
I0003723molecular_functionRNA binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005681cellular_componentspliceosomal complex
I0005684cellular_componentU2-type spliceosomal complex
I0005686cellular_componentU2 snRNP
I0005689cellular_componentU12-type spliceosomal complex
I0006397biological_processmRNA processing
I0008380biological_processRNA splicing
I0016607cellular_componentnuclear speck
I0071005cellular_componentU2-type precatalytic spliceosome
I0071011cellular_componentprecatalytic spliceosome
I0071013cellular_componentcatalytic step 2 spliceosome
I1903241biological_processU2-type prespliceosome assembly
K0000375biological_processRNA splicing, via transesterification reactions
K0000398biological_processmRNA splicing, via spliceosome
K0003676molecular_functionnucleic acid binding
K0003723molecular_functionRNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005681cellular_componentspliceosomal complex
K0005684cellular_componentU2-type spliceosomal complex
K0005686cellular_componentU2 snRNP
K0005689cellular_componentU12-type spliceosomal complex
K0006397biological_processmRNA processing
K0008380biological_processRNA splicing
K0071005cellular_componentU2-type precatalytic spliceosome
K0071011cellular_componentprecatalytic spliceosome
K1903241biological_processU2-type prespliceosome assembly
K1990935molecular_functionsplicing factor binding
M0000245biological_processspliceosomal complex assembly
M0000389biological_processmRNA 3'-splice site recognition
M0000398biological_processmRNA splicing, via spliceosome
M0003676molecular_functionnucleic acid binding
M0003723molecular_functionRNA binding
M0005515molecular_functionprotein binding
M0005634cellular_componentnucleus
M0005654cellular_componentnucleoplasm
M0005681cellular_componentspliceosomal complex
M0005684cellular_componentU2-type spliceosomal complex
M0005686cellular_componentU2 snRNP
M0006397biological_processmRNA processing
M0008270molecular_functionzinc ion binding
M0008380biological_processRNA splicing
M0010976biological_processpositive regulation of neuron projection development
M0016607cellular_componentnuclear speck
M0046872molecular_functionmetal ion binding
M0071004cellular_componentU2-type prespliceosome
M0071005cellular_componentU2-type precatalytic spliceosome
M0071013cellular_componentcatalytic step 2 spliceosome
M1903241biological_processU2-type prespliceosome assembly
N0000375biological_processRNA splicing, via transesterification reactions
N0000389biological_processmRNA 3'-splice site recognition
N0000398biological_processmRNA splicing, via spliceosome
N0003676molecular_functionnucleic acid binding
N0003723molecular_functionRNA binding
N0005515molecular_functionprotein binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005681cellular_componentspliceosomal complex
N0005684cellular_componentU2-type spliceosomal complex
N0005686cellular_componentU2 snRNP
N0006397biological_processmRNA processing
N0008270molecular_functionzinc ion binding
N0008380biological_processRNA splicing
N0016607cellular_componentnuclear speck
N0046872molecular_functionmetal ion binding
N0071005cellular_componentU2-type precatalytic spliceosome
N0071013cellular_componentcatalytic step 2 spliceosome
N1903241biological_processU2-type prespliceosome assembly
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. FVCSATH
ChainResidueDetails
APHE287-HIS293
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues37
DetailsRegion: {"description":"Interaction with PHF5A, SF3B1 and SF3B5","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues56
DetailsRegion: {"description":"Interaction with SF3B1 and SF3B5","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues21
DetailsRegion: {"description":"Interaction with SF3B1","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues23
DetailsRegion: {"description":"Interaction with SF3B5","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues5
DetailsSite: {"description":"Interaction with SF3B5","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Interaction with SF3B1","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues5
DetailsSite: {"description":"Interaction with RNA","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues39
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues34
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues37
DetailsRepeat: {"description":"HEAT 3"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues34
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues38
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues38
DetailsRepeat: {"description":"HEAT 6"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues38
DetailsRepeat: {"description":"HEAT 7"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues38
DetailsRepeat: {"description":"HEAT 8"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues38
DetailsRepeat: {"description":"HEAT 9"}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues38
DetailsRepeat: {"description":"HEAT 10"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues38
DetailsRepeat: {"description":"HEAT 11"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues39
DetailsRegion: {"description":"Interaction with SF3B14"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues4
DetailsRegion: {"description":"Interaction with PHF5A","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues56
DetailsRegion: {"description":"Interaction with SF3B3 and SF3B5","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsSite: {"description":"Interaction with PHF5A","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues4
DetailsSite: {"description":"Interaction with SF3B3","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues16
DetailsRegion: {"description":"Interaction with SF3B1 and SF3B3","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues3
DetailsRegion: {"description":"Interaction with SF3B3","evidences":[{"source":"PubMed","id":"27720643","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28541300","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SYB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine; by PRMT9; alternate","evidences":[{"source":"PubMed","id":"25737013","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues61
DetailsZinc finger: {"description":"Matrin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00130","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon