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5IFE

Crystal structure of the human SF3b core 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
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN D 201
ChainResidue
DCYS23
DCYS26
DCYS58
DCYS61

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN D 202
ChainResidue
DCYS11
DCYS46
DCYS49
DCYS85

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN D 203
ChainResidue
DCYS33
DCYS72
DCYS75
DCYS30

site_idAC4
Number of Residues3
Detailsbinding site for residue K A 1301
ChainResidue
AVAL610
AASN612
AGLN636

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 Residues5
DetailsSITE: Interaction with SF3B5 => ECO:0000269|PubMed:27720643
ChainResidueDetails
DCYS46
DCYS49
DCYS58
DCYS61
DCYS72
DCYS75
DCYS85
AGLY284
AGLU306
AGLU352
AARG429
AASN916

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Interaction with SF3B1 => ECO:0000269|PubMed:27720643
ChainResidueDetails
AASN988
ALYS1171

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER156
CCYS677
CGLU1205

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR235
CTHR426
ATHR1200

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS3

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER94
CLYS554
CLYS562

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR142

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Citrulline => ECO:0000250
ChainResidueDetails
CARG157

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER194

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
CTHR203

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR207

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR211

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q99NB9
ChainResidueDetails
CLYS214

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR223

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR227

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99NB9
ChainResidueDetails
CSER229

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:12105215
ChainResidueDetails
CTHR244

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:12105215
ChainResidueDetails
CTHR248

site_idSWS_FT_FI19
Number of Residues5
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR257
CTHR261
CTHR278
CTHR303
CTHR313

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR267

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR273

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER287

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR296

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983
ChainResidueDetails
CTHR299

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER322

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR326

site_idSWS_FT_FI27
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
CTHR328

site_idSWS_FT_FI28
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER332

site_idSWS_FT_FI29
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692
ChainResidueDetails
CTHR341

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
CSER344

site_idSWS_FT_FI31
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692
ChainResidueDetails
CSER349

site_idSWS_FT_FI32
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR436
CTHR350

site_idSWS_FT_FI33
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR354

site_idSWS_FT_FI34
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER400

site_idSWS_FT_FI35
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by DYRK1A => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR434

site_idSWS_FT_FI36
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER488

site_idSWS_FT_FI37
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS214

site_idSWS_FT_FI38
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS430

site_idSWS_FT_FI39
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:28112733
ChainResidueDetails
CLYS413

221051

PDB entries from 2024-06-12

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