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4BKX

The structure of HDAC1 in complex with the dimeric ELM2-SANT domain of MTA1 from the NuRD complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000118cellular_componenthistone deacetylase complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000785cellular_componentchromatin
B0000792cellular_componentheterochromatin
B0000976molecular_functiontranscription cis-regulatory region binding
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
B0001046molecular_functioncore promoter sequence-specific DNA binding
B0001222molecular_functiontranscription corepressor binding
B0002039molecular_functionp53 binding
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0003714molecular_functiontranscription corepressor activity
B0004407molecular_functionhistone deacetylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005667cellular_componenttranscription regulator complex
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006346biological_processDNA methylation-dependent heterochromatin formation
B0006357biological_processregulation of transcription by RNA polymerase II
B0006476biological_processprotein deacetylation
B0007492biological_processendoderm development
B0007623biological_processcircadian rhythm
B0008284biological_processpositive regulation of cell population proliferation
B0009913biological_processepidermal cell differentiation
B0010628biological_processpositive regulation of gene expression
B0010629biological_processnegative regulation of gene expression
B0010832biological_processnegative regulation of myotube differentiation
B0016581cellular_componentNuRD complex
B0016787molecular_functionhydrolase activity
B0017053cellular_componenttranscription repressor complex
B0019899molecular_functionenzyme binding
B0021766biological_processhippocampus development
B0030182biological_processneuron differentiation
B0030336biological_processnegative regulation of cell migration
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0031492molecular_functionnucleosomal DNA binding
B0032922biological_processcircadian regulation of gene expression
B0032991cellular_componentprotein-containing complex
B0033558molecular_functionprotein lysine deacetylase activity
B0035851molecular_functionKrueppel-associated box domain binding
B0036120biological_processcellular response to platelet-derived growth factor stimulus
B0042475biological_processodontogenesis of dentin-containing tooth
B0042659biological_processregulation of cell fate specification
B0042733biological_processembryonic digit morphogenesis
B0042826molecular_functionhistone deacetylase binding
B0043025cellular_componentneuronal cell body
B0043066biological_processnegative regulation of apoptotic process
B0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
B0043922biological_processnegative regulation by host of viral transcription
B0045814biological_processnegative regulation of gene expression, epigenetic
B0045892biological_processnegative regulation of DNA-templated transcription
B0045893biological_processpositive regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048511biological_processrhythmic process
B0048661biological_processpositive regulation of smooth muscle cell proliferation
B0048709biological_processoligodendrocyte differentiation
B0048714biological_processpositive regulation of oligodendrocyte differentiation
B0051059molecular_functionNF-kappaB binding
B0060766biological_processnegative regulation of androgen receptor signaling pathway
B0060789biological_processhair follicle placode formation
B0061029biological_processeyelid development in camera-type eye
B0061198biological_processfungiform papilla formation
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0070822cellular_componentSin3-type complex
B0070888molecular_functionE-box binding
B0090090biological_processnegative regulation of canonical Wnt signaling pathway
B0140297molecular_functionDNA-binding transcription factor binding
B0160008molecular_functionprotein decrotonylase activity
B0160009molecular_functionhistone decrotonylase activity
B1902455biological_processnegative regulation of stem cell population maintenance
B1902459biological_processpositive regulation of stem cell population maintenance
B1990841molecular_functionpromoter-specific chromatin binding
B2000273biological_processpositive regulation of signaling receptor activity
B2000736biological_processregulation of stem cell differentiation
B2001243biological_processnegative regulation of intrinsic apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 600
ChainResidue
BASP176
BHIS178
BASP264
BACT601

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ACT B 601
ChainResidue
BGLY301
BTYR303
BZN600
BHIS140
BHIS141
BASP176
BHIS178
BASP264

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 602
ChainResidue
BASP174
BASP176
BHIS178
BSER197
BPHE198

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 603
ChainResidue
BPHE187
BTHR190
BVAL193
BTYR222

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BARG270
BTYR303
BTHR304
BILE305
BARG306

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 502
ChainResidue
ALYS305
ATYR327
ATYR328
ALYS331
BLYS31
BSO4503

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 503
ChainResidue
ALYS305
BGLY27
BHIS28
BLYS31
BSO4502

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 504
ChainResidue
BARG55
BHIS57
BLYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:19182791, ECO:0000269|PubMed:28497810
ChainResidueDetails
BHIS141

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS74

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS220

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P70288
ChainResidueDetails
BCYS261
BCYS273

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17487921, 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
BSER393

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q92769
ChainResidueDetails
BSER406

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER409

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11602581, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER421

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11602581, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER423

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-methylated lysine; by EHMT2 => ECO:0000269|PubMed:18438403
ChainResidueDetails
BLYS432

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q92769
ChainResidueDetails
BLYS74

site_idSWS_FT_FI12
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS438
BLYS480

site_idSWS_FT_FI13
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297
ChainResidueDetails
BLYS444

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q92769
ChainResidueDetails
BLYS456
BLYS473

site_idSWS_FT_FI15
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
BLYS457

site_idSWS_FT_FI16
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS476

218500

数据于2024-04-17公开中

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