Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7V6Q

Crystal structure of sNASP-ASF1A-H3.1-H4 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0010467biological_processgene expression
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0040029biological_processepigenetic regulation of gene expression
B0043229cellular_componentintracellular organelle
B0045296molecular_functioncadherin binding
B0046982molecular_functionprotein heterodimerization activity
B0070062cellular_componentextracellular exosome
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
E0005634cellular_componentnucleus
E0006325biological_processchromatin organization
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0010467biological_processgene expression
F0016020cellular_componentmembrane
F0030527molecular_functionstructural constituent of chromatin
F0032200biological_processtelomere organization
F0032991cellular_componentprotein-containing complex
F0040029biological_processepigenetic regulation of gene expression
F0043229cellular_componentintracellular organelle
F0045296molecular_functioncadherin binding
F0046982molecular_functionprotein heterodimerization activity
F0070062cellular_componentextracellular exosome
G0000781cellular_componentchromosome, telomeric region
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0003723molecular_functionRNA binding
G0005515molecular_functionprotein binding
G0005576cellular_componentextracellular region
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0006334biological_processnucleosome assembly
G0016020cellular_componentmembrane
G0030527molecular_functionstructural constituent of chromatin
G0032200biological_processtelomere organization
G0032991cellular_componentprotein-containing complex
G0043505cellular_componentCENP-A containing nucleosome
G0045653biological_processnegative regulation of megakaryocyte differentiation
G0046982molecular_functionprotein heterodimerization activity
G0061644biological_processprotein localization to CENP-A containing chromatin
G0070062cellular_componentextracellular exosome
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 Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
DTHR123
HTHR123

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
DSER127
HSER127

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DGLU170
HGLU170

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DLEU176
DLYS191
DGLU299
HLEU176
HLYS191
HGLU299

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DILE189
HILE189
CLYS77
CLYS91
GLYS12
GLYS31
GLYS77
GLYS91

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99MD9
ChainResidueDetails
DLEU243
DGLU288
HLEU243
HGLU288

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DLEU244
HLEU244

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DGLU121
HGLU121

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR138
HTHR138

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER141
HSER141
FLYS14
FLYS56

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR151
HTHR151

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER158
HSER158
FLYS18
FLYS64

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER164
HSER164

site_idSWS_FT_FI14
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
BARG26
CLYS91
GLYS91

site_idSWS_FT_FI15
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS20
CLYS59
CLYS79
GLYS20
GLYS59
GLYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
CLYS31
GLYS31

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:15983376, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708
ChainResidueDetails
BLYS36
FLYS36

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:15983376
ChainResidueDetails
BLYS37
FLYS37

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
BTYR41
FTYR41

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BSER57
FSER57

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
BLYS79
FLYS79

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BTHR80
FTHR80

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
BSER86
FSER86

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
BTHR107
FTHR107

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS115
FLYS115

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
BLYS122
FLYS122

site_idSWS_FT_FI27
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
BLYS18
FLYS18

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon