7VVB

Crystal Structure of KRas4A(GMPPNP-bound) in complex with the Ras-binding domain(RBD) of SIN1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0000165	biological_process	MAPK cascade
A	0000166	molecular_function	nucleotide binding
A	0001889	biological_process	liver development
A	0003924	molecular_function	GTPase activity
A	0003925	molecular_function	G protein activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005741	cellular_component	mitochondrial outer membrane
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0007165	biological_process	signal transduction
A	0007265	biological_process	Ras protein signal transduction
A	0007565	biological_process	female pregnancy
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009629	biological_process	response to gravity
A	0009898	cellular_component	cytoplasmic side of plasma membrane
A	0010628	biological_process	positive regulation of gene expression
A	0012505	cellular_component	endomembrane system
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0019002	molecular_function	GMP binding
A	0019003	molecular_function	GDP binding
A	0019221	biological_process	cytokine-mediated signaling pathway
A	0030275	molecular_function	LRR domain binding
A	0035900	biological_process	response to isolation stress
A	0043495	molecular_function	protein-membrane adaptor activity
A	0044877	molecular_function	protein-containing complex binding
A	0046579	biological_process	positive regulation of Ras protein signal transduction
A	0051384	biological_process	response to glucocorticoid
A	0051385	biological_process	response to mineralocorticoid
A	0051450	biological_process	myoblast proliferation
A	0060038	biological_process	cardiac muscle cell proliferation
A	2000774	biological_process	positive regulation of cellular senescence
B	0000139	cellular_component	Golgi membrane
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005515	molecular_function	protein binding
B	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
B	0005547	molecular_function	phosphatidylinositol-3,4,5-trisphosphate binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005741	cellular_component	mitochondrial outer membrane
B	0005764	cellular_component	lysosome
B	0005765	cellular_component	lysosomal membrane
B	0005769	cellular_component	early endosome
B	0005770	cellular_component	late endosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005794	cellular_component	Golgi apparatus
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0007010	biological_process	cytoskeleton organization
B	0019901	molecular_function	protein kinase binding
B	0021762	biological_process	substantia nigra development
B	0030307	biological_process	positive regulation of cell growth
B	0031267	molecular_function	small GTPase binding
B	0031669	biological_process	cellular response to nutrient levels
B	0031901	cellular_component	early endosome membrane
B	0031902	cellular_component	late endosome membrane
B	0031932	cellular_component	TORC2 complex
B	0032869	biological_process	cellular response to insulin stimulus
B	0038203	biological_process	TORC2 signaling
B	0043066	biological_process	negative regulation of apoptotic process
B	0043325	molecular_function	phosphatidylinositol-3,4-bisphosphate binding
B	0046580	biological_process	negative regulation of Ras protein signal transduction
B	0046627	biological_process	negative regulation of insulin receptor signaling pathway
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0060090	molecular_function	molecular adaptor activity
B	0070300	molecular_function	phosphatidic acid binding
B	0080025	molecular_function	phosphatidylinositol-3,5-bisphosphate binding
B	0140767	molecular_function	enzyme-substrate adaptor activity
B	1900407	biological_process	regulation of cellular response to oxidative stress

Functional Information from PROSITE/UniProt

site_id	PS00307
Number of Residues	7
Details	LECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVDLDS

Chain	Residue	Details
B	VAL333-SER339

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BKH7","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Motif: {"description":"Effector region"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22431598","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22566140","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34380736","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"35522713","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylmethionine; in GTPase KRas; alternate","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N-acetylthreonine; in GTPase KRas, N-terminally processed","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22711838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL","evidences":[{"source":"PubMed","id":"19744486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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