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8BPB

Cryo-EM structure of the human SIN3B histone deacetylase core complex at 2.8 Angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000785cellular_componentchromatin
A0000805cellular_componentX chromosome
A0000806cellular_componentY chromosome
A0001741cellular_componentXY body
A0003682molecular_functionchromatin binding
A0003714molecular_functiontranscription corepressor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006355biological_processregulation of DNA-templated transcription
A0030336biological_processnegative regulation of cell migration
A0030849cellular_componentautosome
A0045892biological_processnegative regulation of DNA-templated transcription
A0070822cellular_componentSin3-type complex
B0000118cellular_componenthistone deacetylase complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000781cellular_componentchromosome, telomeric region
B0000785cellular_componentchromatin
B0001975biological_processresponse to amphetamine
B0003300biological_processcardiac muscle hypertrophy
B0003682molecular_functionchromatin binding
B0003723molecular_functionRNA binding
B0004407molecular_functionhistone deacetylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0008284biological_processpositive regulation of cell population proliferation
B0009410biological_processresponse to xenobiotic stimulus
B0009913biological_processepidermal cell differentiation
B0010718biological_processpositive regulation of epithelial to mesenchymal transition
B0010944biological_processnegative regulation of transcription by competitive promoter binding
B0010977biological_processnegative regulation of neuron projection development
B0016358biological_processdendrite development
B0016581cellular_componentNuRD complex
B0016787molecular_functionhydrolase activity
B0019213molecular_functiondeacetylase activity
B0019899molecular_functionenzyme binding
B0030336biological_processnegative regulation of cell migration
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0031000biological_processresponse to caffeine
B0031072molecular_functionheat shock protein binding
B0031492molecular_functionnucleosomal DNA binding
B0031507biological_processheterochromatin formation
B0032496biological_processresponse to lipopolysaccharide
B0032732biological_processpositive regulation of interleukin-1 production
B0032760biological_processpositive regulation of tumor necrosis factor production
B0032922biological_processcircadian regulation of gene expression
B0032967biological_processpositive regulation of collagen biosynthetic process
B0032991cellular_componentprotein-containing complex
B0033558molecular_functionprotein lysine deacetylase activity
B0034605biological_processcellular response to heat
B0035094biological_processresponse to nicotine
B0035098cellular_componentESC/E(Z) complex
B0036211biological_processprotein modification process
B0042220biological_processresponse to cocaine
B0042393molecular_functionhistone binding
B0042475biological_processodontogenesis of dentin-containing tooth
B0042531biological_processpositive regulation of tyrosine phosphorylation of STAT protein
B0042659biological_processregulation of cell fate specification
B0042733biological_processembryonic digit morphogenesis
B0042826molecular_functionhistone deacetylase binding
B0043066biological_processnegative regulation of apoptotic process
B0043433biological_processnegative regulation of DNA-binding transcription factor activity
B0045347biological_processnegative regulation of MHC class II biosynthetic process
B0045862biological_processpositive regulation of proteolysis
B0045892biological_processnegative regulation of DNA-templated transcription
B0045893biological_processpositive regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048149biological_processbehavioral response to ethanol
B0048511biological_processrhythmic process
B0048714biological_processpositive regulation of oligodendrocyte differentiation
B0051059molecular_functionNF-kappaB binding
B0055093biological_processresponse to hyperoxia
B0060789biological_processhair follicle placode formation
B0061000biological_processnegative regulation of dendritic spine development
B0061029biological_processeyelid development in camera-type eye
B0061198biological_processfungiform papilla formation
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0070301biological_processcellular response to hydrogen peroxide
B0070822cellular_componentSin3-type complex
B0071300biological_processcellular response to retinoic acid
B0071560biological_processcellular response to transforming growth factor beta stimulus
B0140297molecular_functionDNA-binding transcription factor binding
B0160008molecular_functionprotein decrotonylase activity
B0160009molecular_functionhistone decrotonylase activity
B0160010molecular_functionprotein de-2-hydroxyisobutyrylase activity
B1902437biological_processpositive regulation of male mating behavior
B1902455biological_processnegative regulation of stem cell population maintenance
B1902459biological_processpositive regulation of stem cell population maintenance
B1903351biological_processcellular response to dopamine
B1904645biological_processresponse to amyloid-beta
B1990841molecular_functionpromoter-specific chromatin binding
B2000273biological_processpositive regulation of signaling receptor activity
B2000736biological_processregulation of stem cell differentiation
B2000757biological_processnegative regulation of peptidyl-lysine acetylation
Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues44
DetailsZF_PHD_1 Zinc finger PHD-type signature. CdsCkeggdl.......................................LcCdh..Cpaa.FHlqCcnpplseemlppge...............................WmChrC
ChainResidueDetails
CCYS59-CYS102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsZN_FING: PHD-type 1 => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
CHIS56-ARG105
AGLU712

site_idSWS_FT_FI2
Number of Residues50
DetailsZN_FING: PHD-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
CVAL271-HIS321
BASP177
BHIS179
BPHE188
BTHR191
BVAL194
BSER198
BPHE199
BASP265

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPA
ChainResidueDetails
CSER61
CCYS62
CHIS79
CCYS82
CCYS59

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPA, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC
ChainResidueDetails
CCYS289
CCYS292
CHIS297
CCYS300
CCYS315
CHIS318
CCYS274
CCYS277

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER131

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692
ChainResidueDetails
BCYS274
CSER134

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER394

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER407

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER422

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER424

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS75

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS481

site_idSWS_FT_FI13
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
BLYS439

site_idSWS_FT_FI14
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS452
BLYS458
BLYS478

site_idSWS_FT_FI15
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS462

219869

PDB entries from 2024-05-15

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