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5KC2

Negative stain structure of Vps15/Vps34 complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0000011biological_processvacuole inheritance
B0000139cellular_componentGolgi membrane
B0000329cellular_componentfungal-type vacuole membrane
B0000425biological_processpexophagy
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005768cellular_componentendosome
B0005770cellular_componentlate endosome
B0005794cellular_componentGolgi apparatus
B0006468biological_processprotein phosphorylation
B0006623biological_processprotein targeting to vacuole
B0006914biological_processautophagy
B0010008cellular_componentendosome membrane
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016236biological_processmacroautophagy
B0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
B0034045cellular_componentphagophore assembly site membrane
B0034271cellular_componentphosphatidylinositol 3-kinase complex, class III, type I
B0034272cellular_componentphosphatidylinositol 3-kinase complex, class III, type II
B0043130molecular_functionubiquitin binding
B0045053biological_processprotein retention in Golgi apparatus
B0045324biological_processlate endosome to vacuole transport
B0046854biological_processphosphatidylinositol phosphate biosynthetic process
B0051365biological_processcellular response to potassium ion starvation
B0071561cellular_componentnucleus-vacuole junction
B0106310molecular_functionprotein serine kinase activity
B0120095cellular_componentvacuole-isolation membrane contact site
C0000045biological_processautophagosome assembly
C0000139cellular_componentGolgi membrane
C0000329cellular_componentfungal-type vacuole membrane
C0000407cellular_componentphagophore assembly site
C0000425biological_processpexophagy
C0004672molecular_functionprotein kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005768cellular_componentendosome
C0005777cellular_componentperoxisome
C0005794cellular_componentGolgi apparatus
C0005829cellular_componentcytosol
C0006897biological_processendocytosis
C0006914biological_processautophagy
C0010008cellular_componentendosome membrane
C0015031biological_processprotein transport
C0016020cellular_componentmembrane
C0016236biological_processmacroautophagy
C0016301molecular_functionkinase activity
C0016303molecular_function1-phosphatidylinositol-3-kinase activity
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
C0034045cellular_componentphagophore assembly site membrane
C0034271cellular_componentphosphatidylinositol 3-kinase complex, class III, type I
C0034272cellular_componentphosphatidylinositol 3-kinase complex, class III, type II
C0036092biological_processphosphatidylinositol-3-phosphate biosynthetic process
C0045324biological_processlate endosome to vacuole transport
C0046854biological_processphosphatidylinositol phosphate biosynthetic process
C0048015biological_processphosphatidylinositol-mediated signaling
C0051365biological_processcellular response to potassium ion starvation
C0071561cellular_componentnucleus-vacuole junction
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHgDIKteNILV
ChainResidueDetails
BILE143-VAL155

site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKvg.DDLRQDqlvvQ
ChainResidueDetails
CPHE623-GLN637

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVitYILgVgDRHldN
ChainResidueDetails
CSER716-ASN736

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BASP147

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU33
BLYS54

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:1756716
ChainResidueDetails
BGLY2

220113

PDB entries from 2024-05-22

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