2N1A

Docked structure between SUMO1 and ZZ-domain from CBP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001741	cellular_component	XY body
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005643	cellular_component	nuclear pore
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006281	biological_process	DNA repair
A	0006355	biological_process	regulation of DNA-templated transcription
A	0008076	cellular_component	voltage-gated potassium channel complex
A	0008134	molecular_function	transcription factor binding
A	0010621	biological_process	negative regulation of transcription by transcription factor localization
A	0015459	molecular_function	potassium channel regulator activity
A	0016604	cellular_component	nuclear body
A	0016605	cellular_component	PML body
A	0016607	cellular_component	nuclear speck
A	0016925	biological_process	protein sumoylation
A	0019899	molecular_function	enzyme binding
A	0030578	biological_process	PML body organization
A	0031334	biological_process	positive regulation of protein-containing complex assembly
A	0031386	molecular_function	protein tag activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031647	biological_process	regulation of protein stability
A	0031965	cellular_component	nuclear membrane
A	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
A	0032880	biological_process	regulation of protein localization
A	0034605	biological_process	cellular response to heat
A	0042308	biological_process	negative regulation of protein import into nucleus
A	0043392	biological_process	negative regulation of DNA binding
A	0043433	biological_process	negative regulation of DNA-binding transcription factor activity
A	0044388	molecular_function	small protein activating enzyme binding
A	0044389	molecular_function	ubiquitin-like protein ligase binding
A	0045759	biological_process	negative regulation of action potential
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0050821	biological_process	protein stabilization
A	0060021	biological_process	roof of mouth development
A	0071276	biological_process	cellular response to cadmium ion
A	0086004	biological_process	regulation of cardiac muscle cell contraction
A	0090204	biological_process	protein localization to nuclear pore
A	0097165	cellular_component	nuclear stress granule
A	0098978	cellular_component	glutamatergic synapse
A	0099523	cellular_component	presynaptic cytosol
A	0099524	cellular_component	postsynaptic cytosol
A	1901017	biological_process	negative regulation of potassium ion transmembrane transporter activity
A	1902260	biological_process	negative regulation of delayed rectifier potassium channel activity
A	1903169	biological_process	regulation of calcium ion transmembrane transport
A	1990381	molecular_function	ubiquitin-specific protease binding
B	0004402	molecular_function	histone acetyltransferase activity
B	0006355	biological_process	regulation of DNA-templated transcription
B	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 300

Chain	Residue
B	CYS209
B	CYS212
B	CYS231
B	CYS234

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	CYS222
B	CYS225
B	HIS240
B	HIS242

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Functional Information from PROSITE/UniProt

site_id	PS01357
Number of Residues	26
Details	ZF_ZZ_1 Zinc finger ZZ-type signature. CneCkhhvet..RWhCtv...CeDYdLCinC

Chain	Residue	Details
B	CYS209-CYS234

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	ZN_FING: ZZ-type => ECO:0000255|PROSITE-ProRule:PRU00228

Chain	Residue	Details
B	ARG204-ASP252

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00228

Chain	Residue	Details
B	CYS209
B	CYS212
B	CYS222
B	CYS225
B	CYS231
B	CYS234
B	HIS240
B	HIS242

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
B	LYS243
B	LYS246

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER32

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS7

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site_id	SWS_FT_FI6
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) => ECO:0000269|PubMed:27068747

Chain	Residue	Details
A	GLY97

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site_id	SWS_FT_FI7
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS16

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site_id	SWS_FT_FI8
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS17

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site_id	SWS_FT_FI9
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS23
A	LYS39
A	LYS45
A	LYS46

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site_id	SWS_FT_FI10
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)

Chain	Residue	Details
A	LYS25

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site_id	SWS_FT_FI11
Number of Residues	1
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS37

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