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

9FGQ

Structure of human APC3loop 375-381 bound to the NCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0010467biological_processgene expression
A0016020cellular_componentmembrane
A0032200biological_processtelomere organization
A0032991cellular_componentprotein-containing complex
A0040029biological_processepigenetic regulation of gene expression
A0045296molecular_functioncadherin binding
A0070062cellular_componentextracellular exosome
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
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0000786cellular_componentnucleosome
C0003674molecular_functionmolecular_function
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0008150biological_processbiological_process
C0031492molecular_functionnucleosomal DNA binding
C0031507biological_processheterochromatin formation
C0070062cellular_componentextracellular exosome
D0000781cellular_componentchromosome, telomeric region
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0005829cellular_componentcytosol
D0006334biological_processnucleosome assembly
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0010467biological_processgene expression
E0016020cellular_componentmembrane
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0040029biological_processepigenetic regulation of gene expression
E0045296molecular_functioncadherin binding
E0070062cellular_componentextracellular exosome
F0000781cellular_componentchromosome, telomeric region
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0003723molecular_functionRNA binding
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0016020cellular_componentmembrane
F0030527molecular_functionstructural constituent of chromatin
F0032200biological_processtelomere organization
F0032991cellular_componentprotein-containing complex
F0043505cellular_componentCENP-A containing nucleosome
F0045653biological_processnegative regulation of megakaryocyte differentiation
F0061644biological_processprotein localization to CENP-A containing chromatin
F0070062cellular_componentextracellular exosome
G0000786cellular_componentnucleosome
G0003674molecular_functionmolecular_function
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0008150biological_processbiological_process
G0031492molecular_functionnucleosomal DNA binding
G0031507biological_processheterochromatin formation
G0070062cellular_componentextracellular exosome
H0000781cellular_componentchromosome, telomeric region
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0005829cellular_componentcytosol
H0006334biological_processnucleosome assembly
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

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_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

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 Residues2
DetailsMOD_RES: N-acetylproline => ECO:0000250|UniProtKB:P23527
ChainResidueDetails
DPRO-2
HPRO-2
LTHR205
LTHR446

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: ADP-ribosyl glutamic acid => ECO:0000269|PubMed:27530147
ChainResidueDetails
DGLU-1
HGLU-1
KTHR312
KTHR429
LTHR209
LTHR244
LTHR313
LTHR430

site_idSWS_FT_FI3
Number of Residues16
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
DLYS2
HLYS8
HLYS12
HLYS13
HLYS17
HLYS20
HLYS40
HLYS82
DLYS8
DLYS12
DLYS13
DLYS17
DLYS20
DLYS40
DLYS82
HLYS2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:34874266
ChainResidueDetails
DSER3
HSER3
GLYS9
GLYS95

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322
ChainResidueDetails
DLYS9
HLYS9
BLYS44
FLYS8
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711
ChainResidueDetails
DSER11
HSER11
BLYS77
BLYS91
FLYS12
FLYS31
FLYS77
FLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS21
HLYS21
GLYS74
GLYS75

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS31
DLYS113
DLYS117
HLYS31
HLYS113
HLYS117

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DGLU32
HGLU32

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475
ChainResidueDetails
DSER33
HSER33
CLYS125
GLYS118
GLYS119
GLYS125

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DLYS43
DLYS105
HLYS43
HLYS105

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
DLYS54
HLYS54
ELYS18
ELYS64

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG76
HARG76
GLYS119

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG83
DARG89
HARG83
HARG89

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR112
HTHR112
FLYS91

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER109
HSER109
BLYS79
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
DLYS2
HLYS2

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16713563
ChainResidueDetails
ALYS37
DLYS117
HLYS117

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
DLYS17
HLYS17

site_idSWS_FT_FI20
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DLYS31
HLYS31

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ALYS79
ELYS79

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ATHR80
ETHR80

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI27
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
ELYS18

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon