5KHO

Rasip1 RA domain in complex with Rap1B

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0007165	biological_process	signal transduction
B	0007165	biological_process	signal transduction
C	0000166	molecular_function	nucleotide binding
C	0003924	molecular_function	GTPase activity
C	0003925	molecular_function	G protein activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005811	cellular_component	lipid droplet
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005911	cellular_component	cell-cell junction
C	0007165	biological_process	signal transduction
C	0007264	biological_process	small GTPase-mediated signal transduction
C	0008283	biological_process	cell population proliferation
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0017156	biological_process	calcium-ion regulated exocytosis
C	0019003	molecular_function	GDP binding
C	0032486	biological_process	Rap protein signal transduction
C	0033625	biological_process	positive regulation of integrin activation
C	0035577	cellular_component	azurophil granule membrane
C	0044877	molecular_function	protein-containing complex binding
C	0045121	cellular_component	membrane raft
C	0045955	biological_process	negative regulation of calcium ion-dependent exocytosis
C	0051649	biological_process	establishment of localization in cell
C	0061028	biological_process	establishment of endothelial barrier
C	0070062	cellular_component	extracellular exosome
C	0070161	cellular_component	anchoring junction
C	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
C	0071320	biological_process	cellular response to cAMP
C	0098978	cellular_component	glutamatergic synapse
C	0099010	biological_process	modification of postsynaptic structure
C	1901888	biological_process	regulation of cell junction assembly
C	2000114	biological_process	regulation of establishment of cell polarity
C	2000301	biological_process	negative regulation of synaptic vesicle exocytosis
D	0000166	molecular_function	nucleotide binding
D	0003924	molecular_function	GTPase activity
D	0003925	molecular_function	G protein activity
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005811	cellular_component	lipid droplet
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005911	cellular_component	cell-cell junction
D	0007165	biological_process	signal transduction
D	0007264	biological_process	small GTPase-mediated signal transduction
D	0008283	biological_process	cell population proliferation
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity
D	0017156	biological_process	calcium-ion regulated exocytosis
D	0019003	molecular_function	GDP binding
D	0032486	biological_process	Rap protein signal transduction
D	0033625	biological_process	positive regulation of integrin activation
D	0035577	cellular_component	azurophil granule membrane
D	0044877	molecular_function	protein-containing complex binding
D	0045121	cellular_component	membrane raft
D	0045955	biological_process	negative regulation of calcium ion-dependent exocytosis
D	0051649	biological_process	establishment of localization in cell
D	0061028	biological_process	establishment of endothelial barrier
D	0070062	cellular_component	extracellular exosome
D	0070161	cellular_component	anchoring junction
D	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
D	0071320	biological_process	cellular response to cAMP
D	0098978	cellular_component	glutamatergic synapse
D	0099010	biological_process	modification of postsynaptic structure
D	1901888	biological_process	regulation of cell junction assembly
D	2000114	biological_process	regulation of establishment of cell polarity
D	2000301	biological_process	negative regulation of synaptic vesicle exocytosis

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 301

Chain	Residue
A	ASP206
A	ARG227
A	VAL238
A	TRP242
A	ARG250
B	ASP206
B	ARG227
B	TRP242

---

site_id	AC2
Number of Residues	5
Details	binding site for residue MG C 200

Chain	Residue
C	THR35
C	GNP201
C	HOH302
C	HOH303
C	SER17

---

site_id	AC3
Number of Residues	24
Details	binding site for residue GNP C 201

Chain	Residue
B	GLU258
C	GLY13
C	VAL14
C	GLY15
C	LYS16
C	SER17
C	ALA18
C	PHE28
C	VAL29
C	GLU30
C	TYR32
C	PRO34
C	THR35
C	GLY60
C	ASN116
C	LYS117
C	ASP119
C	LEU120
C	SER147
C	ALA148
C	LYS149
C	MG200
C	HOH302
C	HOH303

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MG D 200

Chain	Residue
D	SER17
D	THR35
D	GNP201
D	HOH301
D	HOH302

---

site_id	AC5
Number of Residues	21
Details	binding site for residue GNP D 201

Chain	Residue
D	GLY13
D	VAL14
D	GLY15
D	LYS16
D	SER17
D	ALA18
D	PHE28
D	VAL29
D	GLU30
D	TYR32
D	THR35
D	GLY60
D	ASN116
D	LYS117
D	ASP119
D	LEU120
D	SER147
D	ALA148
D	MG200
D	HOH301
D	HOH302

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Motif: {"description":"Effector region","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	34
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18309292","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"ADP-ribosylserine; by botulinum toxin","evidences":[{"source":"PubMed","id":"3141412","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	42
Details	Region: {"description":"Interaction with KRIT1","evidences":[{"source":"PubMed","id":"22577140","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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