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4H9N

Complex structure 1 of DAXX/H3.3(sub5)/H4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000775cellular_componentchromosome, centromeric region
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0000786cellular_componentnucleosome
A0000939cellular_componentinner kinetochore
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
A0001556biological_processoocyte maturation
A0001649biological_processosteoblast differentiation
A0001740cellular_componentBarr body
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006334biological_processnucleosome assembly
A0006997biological_processnucleus organization
A0007283biological_processspermatogenesis
A0007286biological_processspermatid development
A0007338biological_processsingle fertilization
A0007566biological_processembryo implantation
A0008283biological_processcell population proliferation
A0008584biological_processmale gonad development
A0030307biological_processpositive regulation of cell growth
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0031508biological_processpericentric heterochromatin formation
A0031509biological_processsubtelomeric heterochromatin formation
A0032200biological_processtelomere organization
A0032991cellular_componentprotein-containing complex
A0035264biological_processmulticellular organism growth
A0042692biological_processmuscle cell differentiation
A0043229cellular_componentintracellular organelle
A0046982molecular_functionprotein heterodimerization activity
A0048477biological_processoogenesis
A0070062cellular_componentextracellular exosome
A0090230biological_processregulation of centromere complex assembly
A1902340biological_processnegative regulation of chromosome condensation
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0042393molecular_functionhistone binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 201
ChainResidue
AARG52
APO4202
AHOH312
AHOH327
AHOH369

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 202
ChainResidue
AARG40
AARG42
APO4201
AHOH362

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 203
ChainResidue
AHIS39
AARG40

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 204
ChainResidue
AHIS113
AALA114
CGLN193

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 201
ChainResidue
BALA76
BARG78
BHOH318
BHOH333

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 C 401
ChainResidue
CARG273
CHIS300

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 C 402
ChainResidue
AHOH337
CSER184
CARG185
CARG186
CHOH626
CHOH700

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 C 403
ChainResidue
CLYS231
CARG234
CARG238
CHOH540

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 C 404
ChainResidue
CARG227
CARG230
CARG234

Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER178

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
CSER213

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BARG3

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
BLYS5

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
BLYS8
BLYS16
BLYS44

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
BLYS12
BLYS31
BLYS77
BLYS91

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
BLYS20

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
BSER47

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
BTYR51

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS59

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BLYS79
ALYS56

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
BTHR80

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTYR88
ALYS64

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
BLYS12

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
AARG26
BLYS91

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
BLYS20
BLYS59
BLYS79

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
BLYS31

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088
ChainResidueDetails
ASER31

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS37

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
ATYR41

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ASER57

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ALYS79

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ATHR80

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER86

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR107

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115

site_idSWS_FT_FI27
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122

site_idSWS_FT_FI28
Number of Residues1
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18

219140

PDB entries from 2024-05-01

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