VPS15_YEAST - dbPTM
VPS15_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS15_YEAST
UniProt AC P22219
Protein Name Serine/threonine-protein kinase VPS15
Gene Name VPS15
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1454
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Lipid-anchor . Endosome membrane
Lipid-anchor .
Protein Description Serine/threonine-protein kinase required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Is also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3-kinase complex II. This second complex is required for the endosome-to-Golgi retrieval of PEP1 and KEX2, and the recruitment of VPS5 and VPS7, two components of the retromer complex, to endosomal membranes (probably through the synthesis of a specific pool of phosphatidylinositol 3-phosphate recruiting the retromer to the endosomes). By regulating VPS34 kinase activity, VPS15 appears to be essential for the efficient delivery of soluble hydrolases to the yeast vacuole..
Protein Sequence MGAQLSLVVQASPSIAIFSYIDVLEEVHYVSQLNSSRFLKTCKALDPNGEIVIKVFIKPKDQYSLRPFLQRIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNPGEFLFYFDTSKRRTCYLAPERFNSKLYQDGKSNNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLNKYRGIFFPDYFYTFIYDYFRNLVTMTTSTPISDNTCTNSTLEDNVKLLDETTEKIYRDFSQICHCLDFPLIKDGGEIGSDPPILESYKIEIEISRFLNTNLYFPQNYHLVLQQFTKVSEKIKSVKEECALLFISYLSHSIRSIVSTATKLKNLELLAVFAQFVSDENKIDRVVPYFVCCFEDSDQDVQALSLLTLIQVLTSVRKLNQLNENIFVDYLLPRLKRLLISNRQNTNYLRIVFANCLSDLAIIINRFQEFTFAQHCNDNSMDNNTEIMESSTKYSAKLIQSVEDLTVSFLTDNDTYVKMALLQNILPLCKFFGRERTNDIILSHLITYLNDKDPALRVSLIQTISGISILLGTVTLEQYILPLLIQTITDSEELVVISVLQSLKSLFKTGLIRKKYYIDISKTTSPLLLHPNNWIRQFTLMIIIEIINKLSKAEVYCILYPIIRPFFEFDVEFNFKSMISCCKQPVSRSVYNLLCSWSVRASKSLFWKKIITNHVDSFGNNRIEFITKNYSSKNYGFNKRDTKSSSSLKGIKTSSTVYSHDNKEIPLTAEDRNWIDKFHIIGLTEKDIWKIVALRGYVIRTARVMAANPDFPYNNSNYRPLVQNSPPNLNLTNIMPRNIFFDVEFAEESTSEGQDSNLENQQIYKYDESEKDSNKLNINGSKQLSTVMDINGSLIFKNKSIATTTSNLKNVFVQLEPTSYHMHSPNHGLKDNANVKPERKVVVSNSYEGDVESIEKFLSTFKILPPLRDYKEFGPIQEIVRSPNMGNLRGKLIATLMENEPNSITSSAVSPGETPYLITGSDQGVIKIWNLKEIIVGEVYSSSLTYDCSSTVTQITMIPNFDAFAVSSKDGQIIVLKVNHYQQESEVKFLNCECIRKINLKNFGKNEYAVRMRAFVNEEKSLLVALTNLSRVIIFDIRTLERLQIIENSPRHGAVSSICIDEECCVLILGTTRGIIDIWDIRFNVLIRSWSFGDHAPITHVEVCQFYGKNSVIVVGGSSKTFLTIWNFVKGHCQYAFINSDEQPSMEHFLPIEKGLEELNFCGIRSLNALSTISVSNDKILLTDEATSSIVMFSLNELSSSKAVISPSRFSDVFIPTQVTANLTMLLRKMKRTSTHSVDDSLYHHDIINSISTCEVDETPLLVACDNSGLIGIFQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGAQLSLVV
------CCCCEEEEE		33.08-
2Myristoylation------MGAQLSLVV
------CCCCEEEEE		33.081756716
110PhosphorylationQHLKNNLYDRLSLRP
HHHHHCHHHHHCCHH		10.9227017623
205UbiquitinationAPERFNSKLYQDGKS
CCHHHCCHHCCCCCC		52.9323749301
211UbiquitinationSKLYQDGKSNNGRLT
CHHCCCCCCCCCCCC		59.3023749301
411PhosphorylationLQQFTKVSEKIKSVK
HHHHHHHHHHHHHHH		34.4328889911
416PhosphorylationKVSEKIKSVKEECAL
HHHHHHHHHHHHHHH		41.7328889911
427PhosphorylationECALLFISYLSHSIR
HHHHHHHHHHHHHHH		16.8227017623
428PhosphorylationCALLFISYLSHSIRS
HHHHHHHHHHHHHHH		13.8627017623
520PhosphorylationRLKRLLISNRQNTNY
HHHHHHHCCCCCCCC		26.4028889911
695PhosphorylationTGLIRKKYYIDISKT
HCCCCEEEEEEECCC		14.5328889911
696PhosphorylationGLIRKKYYIDISKTT
CCCCEEEEEEECCCC		10.8628889911
700PhosphorylationKKYYIDISKTTSPLL
EEEEEEECCCCCCEE		21.8728889911
702PhosphorylationYYIDISKTTSPLLLH
EEEEECCCCCCEEEC		26.2228889911
703PhosphorylationYIDISKTTSPLLLHP
EEEECCCCCCEEECC		31.8928889911
826PhosphorylationRDTKSSSSLKGIKTS
CCCCCCCCCCCCCCC		35.7328889911
904PhosphorylationYRPLVQNSPPNLNLT
CCCCCCCCCCCCCCC		25.3328889911
964PhosphorylationINGSKQLSTVMDING
CCCCCCCEEEEEECC		19.2319823750
965PhosphorylationNGSKQLSTVMDINGS
CCCCCCEEEEEECCC		28.5719823750
972PhosphorylationTVMDINGSLIFKNKS
EEEEECCCEEECCCC		17.5019823750
979PhosphorylationSLIFKNKSIATTTSN
CEEECCCCEEECCCC		27.1819823750
982PhosphorylationFKNKSIATTTSNLKN
ECCCCEEECCCCCEE		29.0119823750
983PhosphorylationKNKSIATTTSNLKNV
CCCCEEECCCCCEEE		21.1419823750
984PhosphorylationNKSIATTTSNLKNVF
CCCEEECCCCCEEEE		15.9719823750
985PhosphorylationKSIATTTSNLKNVFV
CCEEECCCCCEEEEE		37.7619823750
1385PhosphorylationSSSKAVISPSRFSDV
CCCCCEECHHHCCCC		15.3821126336
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of VPS15_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS15_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of VPS15_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RV167_YEASTRVS167physical
16554755
GPA1_YEASTGPA1physical
16839886
DAK2_YEASTDAK2physical
18467557
GPA1_YEASTGPA1physical
19445518
ATG14_YEASTATG14physical
19445518
VPS34_YEASTVPS34genetic
14731957
VPS34_YEASTVPS34physical
20489023
SEC22_YEASTSEC22physical
23904270
YOP1_YEASTYOP1physical
23904270
YPT52_YEASTYPT52physical
23904270
BET1_YEASTBET1physical
23904270
TMEDA_YEASTERV25physical
23904270
ATC7_YEASTNEO1physical
23904270
PIL1_YEASTPIL1physical
23904270
COPG_YEASTSEC21physical
23904270
SEC23_YEASTSEC23physical
23904270
SFT1_YEASTSFT1physical
23904270
STV1_YEASTSTV1physical
23904270
KC13_YEASTYCK3physical
23904270
EMP24_YEASTEMP24physical
23904270
SVP26_YEASTSVP26physical
23904270
TVP38_YEASTTVP38physical
23904270
YPT31_YEASTYPT31physical
23904270
DID4_YEASTDID4physical
23904270
ATC5_YEASTDNF1physical
23904270
VPS10_YEASTPEP1physical
23904270
YPT7_YEASTYPT7physical
23904270
ATG14_YEASTATG14physical
23904270
EMP47_YEASTEMP47physical
23904270
SEC17_YEASTSEC17physical
23904270
SEC4_YEASTSEC4physical
23904270
AKR1_YEASTAKR1physical
23904270
CDC48_YEASTCDC48physical
23904270
GOSR1_YEASTGOS1physical
23904270
SNF7_YEASTSNF7physical
23904270
VPS1_YEASTVPS1physical
23904270
VPS21_YEASTVPS21physical
23904270
YPT1_YEASTYPT1physical
23904270
PEP12_YEASTPEP12physical
23904270
SS120_YEASTSSP120physical
23904270
ATC1_YEASTPMR1physical
23904270
SFT2_YEASTSFT2physical
23904270
PRA1_YEASTYIP3physical
23904270
DID2_YEASTDID2physical
23904270
SSO1_YEASTSSO1physical
23904270
VTI1_YEASTVTI1physical
23904270
CASP_YEASTCOY1physical
23904270
VPS38_YEASTVPS38physical
23904270
FKS1_YEASTFKS1physical
23904270
VPS34_YEASTVPS34physical
23904270
BECN1_YEASTVPS30physical
23904270
VPS15_YEASTVPS15physical
23904270
YHJ3_YEASTYHR033Wgenetic
27708008
ENT5_YEASTENT5genetic
27708008
SUM1_YEASTSUM1genetic
27708008
NNF2_YEASTNNF2genetic
27708008
THP3_YEASTTHP3genetic
27708008
VPS34_YEASTVPS34physical
27630019
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPS15_YEAST

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"A genetic and structural analysis of the yeast Vps15 protein kinase:evidence for a direct role of Vps15p in vacuolar protein delivery.";
Herman P.K., Stack J.H., Emr S.D.;
EMBO J. 10:4049-4060(1991).
Cited for: FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF GLY-2; LYS-54; ASP-147;LYS-149 AND GLU-151, AND MYRISTOYLATION AT GLY-2.
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904, AND MASSSPECTROMETRY.

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