Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5KC2

Negative stain structure of Vps15/Vps34 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0000011	biological_process	vacuole inheritance
B	0000139	cellular_component	Golgi membrane
B	0000166	molecular_function	nucleotide binding
B	0000329	cellular_component	fungal-type vacuole membrane
B	0000425	biological_process	pexophagy
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005770	cellular_component	late endosome
B	0005794	cellular_component	Golgi apparatus
B	0006468	biological_process	protein phosphorylation
B	0006623	biological_process	protein targeting to vacuole
B	0006914	biological_process	autophagy
B	0010008	cellular_component	endosome membrane
B	0015031	biological_process	protein transport
B	0016236	biological_process	macroautophagy
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
B	0034045	cellular_component	phagophore assembly site membrane
B	0034271	cellular_component	phosphatidylinositol 3-kinase complex, class III, type I
B	0034272	cellular_component	phosphatidylinositol 3-kinase complex, class III, type II
B	0043130	molecular_function	ubiquitin binding
B	0045053	biological_process	protein retention in Golgi apparatus
B	0045324	biological_process	late endosome to vacuole transport
B	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
B	0051365	biological_process	cellular response to potassium ion starvation
B	0071561	cellular_component	nucleus-vacuole junction
B	0072665	biological_process	protein localization to vacuole
B	0106310	molecular_function	protein serine kinase activity
B	0120095	cellular_component	vacuole-isolation membrane contact site
C	0000045	biological_process	autophagosome assembly
C	0000139	cellular_component	Golgi membrane
C	0000166	molecular_function	nucleotide binding
C	0000329	cellular_component	fungal-type vacuole membrane
C	0000407	cellular_component	phagophore assembly site
C	0000425	biological_process	pexophagy
C	0004672	molecular_function	protein kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005768	cellular_component	endosome
C	0005777	cellular_component	peroxisome
C	0005794	cellular_component	Golgi apparatus
C	0005829	cellular_component	cytosol
C	0006897	biological_process	endocytosis
C	0006914	biological_process	autophagy
C	0010008	cellular_component	endosome membrane
C	0015031	biological_process	protein transport
C	0016020	cellular_component	membrane
C	0016236	biological_process	macroautophagy
C	0016301	molecular_function	kinase activity
C	0016303	molecular_function	1-phosphatidylinositol-3-kinase activity
C	0016740	molecular_function	transferase activity
C	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
C	0033554	biological_process	cellular response to stress
C	0034045	cellular_component	phagophore assembly site membrane
C	0034271	cellular_component	phosphatidylinositol 3-kinase complex, class III, type I
C	0034272	cellular_component	phosphatidylinositol 3-kinase complex, class III, type II
C	0036092	biological_process	phosphatidylinositol-3-phosphate biosynthetic process
C	0045324	biological_process	late endosome to vacuole transport
C	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
C	0048015	biological_process	phosphatidylinositol-mediated signaling
C	0051365	biological_process	cellular response to potassium ion starvation
C	0071561	cellular_component	nucleus-vacuole junction

Functional Information from PROSITE/UniProt

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHgDIKteNILV

Chain	Residue	Details
B	ILE143-VAL155

site_id	PS00915
Number of Residues	15
Details	PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKvg.DDLRQDqlvvQ

Chain	Residue	Details
C	PHE623-GLN637

site_id	PS00916
Number of Residues	21
Details	PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVitYILgVgDRHldN

Chain	Residue	Details
C	SER716-ASN736

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	174
Details	Domain: {"description":"C2 PI3K-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00880","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	266
Details	Domain: {"description":"PI3K/PI4K catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	21
Details	Region: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	37
Details	Repeat: {"description":"HEAT 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	37
Details	Repeat: {"description":"HEAT 3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	37
Details	Repeat: {"description":"HEAT 4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	40
Details	Repeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	39
Details	Repeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	39
Details	Repeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	40
Details	Repeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	38
Details	Repeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	32
Details	Repeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)