Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7CIZ

Crystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 dimer and MCM2 HBD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0000781	cellular_component	chromosome, telomeric region
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0006325	biological_process	chromatin organization
B	0006334	biological_process	nucleosome assembly
B	0016020	cellular_component	membrane
B	0030527	molecular_function	structural constituent of chromatin
B	0032200	biological_process	telomere organization
B	0032991	cellular_component	protein-containing complex
B	0043505	cellular_component	CENP-A containing nucleosome
B	0045653	biological_process	negative regulation of megakaryocyte differentiation
B	0046982	molecular_function	protein heterodimerization activity
B	0061644	biological_process	protein localization to CENP-A containing chromatin
B	0070062	cellular_component	extracellular exosome
C	0003677	molecular_function	DNA binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0006270	biological_process	DNA replication initiation
C	0042555	cellular_component	MCM complex
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0000781	cellular_component	chromosome, telomeric region
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0003723	molecular_function	RNA binding
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005694	cellular_component	chromosome
F	0006325	biological_process	chromatin organization
F	0006334	biological_process	nucleosome assembly
F	0016020	cellular_component	membrane
F	0030527	molecular_function	structural constituent of chromatin
F	0032200	biological_process	telomere organization
F	0032991	cellular_component	protein-containing complex
F	0043505	cellular_component	CENP-A containing nucleosome
F	0045653	biological_process	negative regulation of megakaryocyte differentiation
F	0046982	molecular_function	protein heterodimerization activity
F	0061644	biological_process	protein localization to CENP-A containing chromatin
F	0070062	cellular_component	extracellular exosome
G	0003677	molecular_function	DNA binding
G	0005524	molecular_function	ATP binding
G	0005634	cellular_component	nucleus
G	0006270	biological_process	DNA replication initiation
G	0042555	cellular_component	MCM complex
I	0000786	cellular_component	nucleosome
I	0003677	molecular_function	DNA binding
I	0030527	molecular_function	structural constituent of chromatin
I	0046982	molecular_function	protein heterodimerization activity
J	0000781	cellular_component	chromosome, telomeric region
J	0000786	cellular_component	nucleosome
J	0003677	molecular_function	DNA binding
J	0003723	molecular_function	RNA binding
J	0005515	molecular_function	protein binding
J	0005576	cellular_component	extracellular region
J	0005634	cellular_component	nucleus
J	0005654	cellular_component	nucleoplasm
J	0005694	cellular_component	chromosome
J	0006325	biological_process	chromatin organization
J	0006334	biological_process	nucleosome assembly
J	0016020	cellular_component	membrane
J	0030527	molecular_function	structural constituent of chromatin
J	0032200	biological_process	telomere organization
J	0032991	cellular_component	protein-containing complex
J	0043505	cellular_component	CENP-A containing nucleosome
J	0045653	biological_process	negative regulation of megakaryocyte differentiation
J	0046982	molecular_function	protein heterodimerization activity
J	0061644	biological_process	protein localization to CENP-A containing chromatin
J	0070062	cellular_component	extracellular exosome
K	0003677	molecular_function	DNA binding
K	0005524	molecular_function	ATP binding
K	0005634	cellular_component	nucleus
K	0006270	biological_process	DNA replication initiation
K	0042555	cellular_component	MCM complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue SO4 B 201

Chain	Residue
A	ARG63
B	THR30
B	PRO32
B	ARG36
B	HOH307
B	HOH309
B	HOH314

site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 B 202

Chain	Residue
B	ARG35
B	LYS31
B	PRO32

Functional Information from PROSITE/UniProt

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	DNA_BIND:

Chain	Residue	Details
B	LYS16-LYS20
F	LYS16-LYS20
J	LYS16-LYS20

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:17967882

Chain	Residue	Details
B	SER1
F	SER1
J	SER1

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	ARG3
F	ARG3
J	ARG3

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-lactoyllysine; alternate => ECO:0000269\|PubMed:31645732

Chain	Residue	Details
B	LYS5
F	LYS5
J	LYS5

site_id	SWS_FT_FI5
Number of Residues	9
Details	MOD_RES: N6-propionyllysine; alternate => ECO:0000269\|PubMed:17267393

Chain	Residue	Details
B	LYS8
B	LYS16
B	LYS44
F	LYS8
F	LYS16
F	LYS44
J	LYS8
J	LYS16
J	LYS44

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
B	LYS12
J	LYS31
J	LYS77
J	LYS91
B	LYS31
B	LYS77
B	LYS91
F	LYS12
F	LYS31
F	LYS77
F	LYS91
J	LYS12

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269\|PubMed:12086618, ECO:0000269\|PubMed:15964846, ECO:0000269\|PubMed:17967882, ECO:0000269\|PubMed:27338793

Chain	Residue	Details
B	LYS20
F	LYS20
J	LYS20

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_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

Chain	Residue	Details
B	SER47
F	SER47
J	SER47

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
B	TYR51
F	TYR51
J	TYR51

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
B	LYS59
F	LYS59
J	LYS59

site_id	SWS_FT_FI11
Number of Residues	3
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	LYS79
F	LYS79
J	LYS79

site_id	SWS_FT_FI12
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P62806

Chain	Residue	Details
B	THR80
F	THR80
J	THR80

site_id	SWS_FT_FI13
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	TYR88
F	TYR88
J	TYR88

site_id	SWS_FT_FI14
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:25218447

Chain	Residue	Details
B	LYS12
F	LYS12
J	LYS12

site_id	SWS_FT_FI15
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:19818714

Chain	Residue	Details
B	LYS91
F	LYS91
J	LYS91

site_id	SWS_FT_FI16
Number of Residues	9
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
B	LYS20
B	LYS59
B	LYS79
F	LYS20
F	LYS59
F	LYS79
J	LYS20
J	LYS59
J	LYS79

site_id	SWS_FT_FI17
Number of Residues	3
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269\|PubMed:30886146

Chain	Residue	Details
B	LYS31
F	LYS31
J	LYS31

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)