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4HGA

Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX

Functional Information from GO Data
ChainGOidnamespacecontents
A0042393molecular_functionhistone binding
B0000775cellular_componentchromosome, centromeric region
B0000781cellular_componentchromosome, telomeric region
B0000785cellular_componentchromatin
B0000786cellular_componentnucleosome
B0000939cellular_componentinner kinetochore
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
B0001556biological_processoocyte maturation
B0001649biological_processosteoblast differentiation
B0001740cellular_componentBarr body
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0006997biological_processnucleus organization
B0007283biological_processspermatogenesis
B0007286biological_processspermatid development
B0007338biological_processsingle fertilization
B0007566biological_processembryo implantation
B0008283biological_processcell population proliferation
B0008584biological_processmale gonad development
B0030307biological_processpositive regulation of cell growth
B0030527molecular_functionstructural constituent of chromatin
B0031492molecular_functionnucleosomal DNA binding
B0031508biological_processpericentric heterochromatin formation
B0031509biological_processsubtelomeric heterochromatin formation
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0035264biological_processmulticellular organism growth
B0042692biological_processmuscle cell differentiation
B0043229cellular_componentintracellular organelle
B0046982molecular_functionprotein heterodimerization activity
B0048477biological_processoogenesis
B0070062cellular_componentextracellular exosome
B0090230biological_processregulation of centromere complex assembly
B1902340biological_processnegative regulation of chromosome condensation
C0000781cellular_componentchromosome, telomeric region
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0006334biological_processnucleosome assembly
C0016020cellular_componentmembrane
C0030527molecular_functionstructural constituent of chromatin
C0032200biological_processtelomere organization
C0032991cellular_componentprotein-containing complex
C0043505cellular_componentCENP-A containing nucleosome
C0045653biological_processnegative regulation of megakaryocyte differentiation
C0046982molecular_functionprotein heterodimerization activity
C0061644biological_processprotein localization to CENP-A containing chromatin
C0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PC4 A 401
ChainResidue
ATYR259
AARG260
AGLY261
AARG323

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PC4 A 402
ChainResidue
AMET312
AGLN187
AARG190
ATHR262
ATYR264
AGLN308

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PC4 A 403
ChainResidue
AMET369
AMET369

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PC4 B 201
ChainResidue
AGLN383
BMET120
CLEU49

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
CGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
BLYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
BPRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsDNA_BIND:
ChainResidueDetails
CLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
CSER1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CARG3

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
CLYS5

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
CLYS8
CLYS16
CLYS44

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
CLYS12
CLYS31
CLYS77
CLYS91

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
CLYS20

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, 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
CSER47

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
CTYR51

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
CLYS59

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CLYS79
BLYS56

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CTHR80

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTYR88
BLYS64

site_idSWS_FT_FI14
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
CLYS12

site_idSWS_FT_FI15
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
BARG26
CLYS91

site_idSWS_FT_FI16
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS20
CLYS59
CLYS79

site_idSWS_FT_FI17
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
CLYS31

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088
ChainResidueDetails
BSER31

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
BLYS37

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
BTYR41

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BSER57

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
BLYS79

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BTHR80

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER86

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
BTHR107

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS115

site_idSWS_FT_FI27
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
BLYS122

site_idSWS_FT_FI28
Number of Residues1
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
BLYS18

222036

PDB entries from 2024-07-03

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