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7V1M

Structural basis for the co-chaperone relationship of sNASP and ASF1b

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
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
D0005634cellular_componentnucleus
D0006325biological_processchromatin organization
E0000781cellular_componentchromosome, telomeric region
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0003723molecular_functionRNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0043505cellular_componentCENP-A containing nucleosome
E0045653biological_processnegative regulation of megakaryocyte differentiation
E0046982molecular_functionprotein heterodimerization activity
E0061644biological_processprotein localization to CENP-A containing chromatin
E0070062cellular_componentextracellular exosome
F0005634cellular_componentnucleus
F0006325biological_processchromatin organization
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: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
GSER164
HSER164

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
GSER323
HSER323

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CARG3
EARG3

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
CLYS5
ELYS5

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
CLYS8
CLYS16
CLYS44
ELYS8
ELYS16
ELYS44

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
CLYS12
CLYS31
CLYS77
CLYS91
ELYS12
ELYS31
ELYS77
ELYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
CLYS20
ELYS20

site_idSWS_FT_FI8
Number of Residues2
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
ESER47

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
CTYR51
ETYR51

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
CLYS59
ELYS59

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CLYS79
ELYS79
ALYS14
ALYS56

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
CTHR80
ETHR80

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTYR88
ETYR88
ALYS18
ALYS64

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
CLYS12
ELYS12

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
BARG26
CLYS91
ELYS91

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS20
CLYS59
CLYS79
ELYS20
ELYS59
ELYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
CLYS31
ELYS31

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15851689, ECO:0000269|PubMed:16185088
ChainResidueDetails
BSER31
ASER31

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
BLYS37
ALYS37

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
BTYR41
ATYR41

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BSER57
ASER57

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
BLYS79
ALYS79

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
BTHR80
ATHR80

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER86
ASER86

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
BTHR107
ATHR107

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
BLYS115
ALYS115

site_idSWS_FT_FI27
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
BLYS122
ALYS122

site_idSWS_FT_FI28
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
BLYS18
ALYS18

218853

PDB entries from 2024-04-24

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