INP52_YEAST - dbPTM
INP52_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INP52_YEAST
UniProt AC P50942
Protein Name Polyphosphatidylinositol phosphatase INP52
Gene Name INP52
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1183
Subcellular Localization Cytoplasm, cytoskeleton, actin patch .
Protein Description Dephosphorylates a number of phosphatidylinositols (PIs) like phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Controls the cellular levels and subcellular distribution of phosphatidylinositol 3-phosphate and phosphatidylinositol 4,5-bisphosphate. Specifically functions within the early endocytic pathway and actin organization..
Protein Sequence MKILLSKQQTRKIAIVSETHGLVFRPINSKNSRRSTCAVELVPKAELNGNGFRRLSNHEIYGFIGLIEIEGLMFIATITGKSKVAQPIPNKTVNKIYAVDFFCLNNSKWDFMDIDSSGYPIVTNDGDFAISSPPSISTHSSRSSLRSSSSRSLNAQEQAPKHPCHELRKLLSNGSFYYSTDFDLTCTLQKRGFTEHSLSFDDFDREFMWNSFLMDEIITYRDRLDVTAKELLDQRGFLTTVIRGFAETIFSYINRLKVGLTIISRQSWKRAGTRFNARGIDDDGHVANFVETEMIMYSSQYCYAFTQIRGSLPIFWEQDTSLISPKIQITRSVEATQPTFDEHFIRLFKKYGPVHIINLLSTKSSEIQLSRRYKEQLKNSEKMKIGRDVFLTSFDFHRETSQDGFAAASRIIPKIRNTILDAGYFSYDVKEGRLISEQDGVFRTNCLDCLDRTNLIQQTISLAVFKLFLEDFRLVKPSSFIDDNEFVQKVNALWADNGDQISQIYTGTNALKSSYSRKGKMSFSGALSDATKSVSRMYINNFVDKGKQQNIDTLLGKLPHQQVVELYDPICEYVNERLLESEEKFTTHSNINLFVGTFNVNGNSRRADLSKWLFPIGDKFKPDVVVLGLQEVIELTAGSILNADYTKSSFWETMVTDCLNQYEEKYLLLRVEQMSSLLILFFARSDRAYNIKEVGGSTKKTGFGGITGNKGAVAIRFDYGATSFCFVNTHLSAGASNIDERRNDYNNIYRNITFPRSKTIPHHDSLFWLGDLNYRITLTNDEVRRELRAQKDGYIDRLLQYDQLTQEINEGVVFQGFKEPTLQFRPTYKYDYGTDNYDTSEKARTPSWTDRIIYKGENLHPLAYSDAPLKISDHKPVYAAYRANVKFVDEKEKLNLVEKLYAEYKNTHPEALTTGPDELSHARMEKQKESIPLDATVQSAGIKLIDLDDTSSCVSPLLSGPSPQPSVVGPGGLSNVSPDKSKLNVLPPPPPTSRHNKEPSSKLLSPTKEISIVSVSPRKGESNLPALERHSTPKPLPPVPALSLSKPVSLQKSSSELQHAKETIDNGKIVPRPCPPIRRKSSTAPDEISTSTKNSGVSTTEDPEPAKASTKPEKPPVVKKPHYLSVAANKLNTSQEHSIKVSPSNSKSEEELPCKKKSKPKVPAKNPELEKLSVHPLKPCDPN
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
91UbiquitinationVAQPIPNKTVNKIYA
CCCCCCCCCCCEEEE		48.7923749301
147PhosphorylationSSRSSLRSSSSRSLN
CCHHHHCCCCCCCCC		39.6122369663
148PhosphorylationSRSSLRSSSSRSLNA
CHHHHCCCCCCCCCH		26.3722369663
149PhosphorylationRSSLRSSSSRSLNAQ
HHHHCCCCCCCCCHH		30.9022369663
150PhosphorylationSSLRSSSSRSLNAQE
HHHCCCCCCCCCHHH		28.0322369663
152PhosphorylationLRSSSSRSLNAQEQA
HCCCCCCCCCHHHHC		28.1122369663
444PhosphorylationEQDGVFRTNCLDCLD
CCCCCEECCHHHHHC		20.8617563356
522PhosphorylationYSRKGKMSFSGALSD
CCCCCCCCCHHHCCH		21.5321440633
524PhosphorylationRKGKMSFSGALSDAT
CCCCCCCHHHCCHHC		18.8219779198
791UbiquitinationRRELRAQKDGYIDRL
HHHHHHCCCCHHHHH		52.7323749301
828NitrationTLQFRPTYKYDYGTD
CEEECCEEECCCCCC		15.38-
842AcetylationDNYDTSEKARTPSWT
CCCCCCCCCCCCCCC		42.8224489116
842UbiquitinationDNYDTSEKARTPSWT
CCCCCCCCCCCCCCC		42.8223749301
952PhosphorylationIDLDDTSSCVSPLLS
EECCCCCCCCHHHHC		22.1928889911
955PhosphorylationDDTSSCVSPLLSGPS
CCCCCCCHHHHCCCC		17.7319779198
962PhosphorylationSPLLSGPSPQPSVVG
HHHHCCCCCCCCCCC		39.4328889911
977PhosphorylationPGGLSNVSPDKSKLN
CCCCCCCCCCHHHCC		31.4720377248
1005PhosphorylationEPSSKLLSPTKEISI
CCCHHCCCCCCEEEE		40.7417330950
1007PhosphorylationSSKLLSPTKEISIVS
CHHCCCCCCEEEEEE		37.6219684113
1011PhosphorylationLSPTKEISIVSVSPR
CCCCCEEEEEEECCC		20.3015665377
1014PhosphorylationTKEISIVSVSPRKGE
CCEEEEEEECCCCCC		18.4024909858
1016PhosphorylationEISIVSVSPRKGESN
EEEEEEECCCCCCCC		16.1022369663
1022PhosphorylationVSPRKGESNLPALER
ECCCCCCCCCCHHHC		52.9521440633
1031PhosphorylationLPALERHSTPKPLPP
CCHHHCCCCCCCCCC		53.2621440633
1032PhosphorylationPALERHSTPKPLPPV
CHHHCCCCCCCCCCC		29.2517330950
1053PhosphorylationKPVSLQKSSSELQHA
CCCCCCCCHHHHHHH		26.5728889911
1055PhosphorylationVSLQKSSSELQHAKE
CCCCCCHHHHHHHHH		49.7930377154
1081PhosphorylationCPPIRRKSSTAPDEI
CCCCCCCCCCCCCCC		30.9822369663
1082PhosphorylationPPIRRKSSTAPDEIS
CCCCCCCCCCCCCCC		31.4622369663
1083PhosphorylationPIRRKSSTAPDEIST
CCCCCCCCCCCCCCC		49.6622369663
1089PhosphorylationSTAPDEISTSTKNSG
CCCCCCCCCCCCCCC		17.7922369663
1090PhosphorylationTAPDEISTSTKNSGV
CCCCCCCCCCCCCCC		46.1822369663
1091PhosphorylationAPDEISTSTKNSGVS
CCCCCCCCCCCCCCC		30.5022369663
1092PhosphorylationPDEISTSTKNSGVST
CCCCCCCCCCCCCCC		34.0422369663
1095PhosphorylationISTSTKNSGVSTTED
CCCCCCCCCCCCCCC		41.97-
1133PhosphorylationVAANKLNTSQEHSIK
EECCCCCCCCCCCEE		42.0728889911
1142PhosphorylationQEHSIKVSPSNSKSE
CCCCEEECCCCCCCC		20.0121440633
1144PhosphorylationHSIKVSPSNSKSEEE
CCEEECCCCCCCCCC		46.3522369663
1146PhosphorylationIKVSPSNSKSEEELP
EEECCCCCCCCCCCC		41.7320377248
1147UbiquitinationKVSPSNSKSEEELPC
EECCCCCCCCCCCCC		67.1623749301
1148PhosphorylationVSPSNSKSEEELPCK
ECCCCCCCCCCCCCC		50.4922369663
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 INP52_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INP52_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 INP52_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VDAC1_YEASTPOR1physical
11805837
SA190_YEASTSAP190physical
11805837
RNQ1_YEASTRNQ1physical
11805837
RNH2B_YEASTRNH202physical
11805837
FHP_YEASTYHB1physical
11805837
ADK_YEASTADO1physical
11805837
IF4A_YEASTTIF2physical
11805837
BSP1_YEASTBSP1physical
12606027
ABP1_YEASTABP1physical
15798181
INP53_YEASTINP53genetic
9560389
INP51_YEASTINP51genetic
9788876
INP53_YEASTINP53genetic
9788876
INP53_YEASTINP53genetic
10029994
PRTB_YEASTPRB1physical
16554755
CLH_YEASTCHC1physical
16406366
SSB1_YEASTSSB1physical
19536198
UBP3_YEASTUBP3genetic
18931302
RV161_YEASTRVS161genetic
18931302
ATC1_YEASTPMR1genetic
18931302
MNN10_YEASTMNN10genetic
18931302
SLX5_YEASTSLX5genetic
18931302
RAD18_YEASTRAD18genetic
18931302
FEN1_YEASTRAD27genetic
18931302
SGF73_YEASTSGF73genetic
18931302
PMP3_YEASTPMP3genetic
18931302
VPS24_YEASTVPS24genetic
18931302
NGG1_YEASTNGG1genetic
18931302
BIM1_YEASTBIM1genetic
18931302
MRC1_YEASTMRC1genetic
18931302
DCC1_YEASTDCC1genetic
18931302
BRE2_YEASTBRE2genetic
18931302
INP53_YEASTINP53genetic
11854411
INP53_YEASTINP53genetic
12686590
BECN1_YEASTVPS30genetic
16306222
KPC1_YEASTPKC1genetic
16306222
SAC7_YEASTSAC7genetic
16306222
MSG5_YEASTMSG5genetic
16306222
OSH7_YEASTOSH7genetic
16306222
YPT1_YEASTYPT1genetic
16306222
VAM6_YEASTVAM6genetic
16306222
ROY1_YEASTROY1genetic
16306222
ARF3_YEASTARF3genetic
16306222
RME1_YEASTRME1genetic
16306222
AZF1_YEASTAZF1genetic
16306222
ATG21_YEASTATG21genetic
16306222
ELP4_YEASTELP4genetic
16306222
SCS2_YEASTSCS2genetic
16306222
GLO3_YEASTGLO3genetic
16306222
HMRA1_YEASTHMRA1genetic
16306222
SSB1_YEASTSSB1genetic
16306222
ROM2_YEASTROM2genetic
16306222
RIC1_YEASTRIC1genetic
20526336
RV161_YEASTRVS161genetic
20526336
PIL1_YEASTPIL1genetic
20526336
INP53_YEASTINP53genetic
20526336
SWA2_YEASTSWA2genetic
20526336
SCS7_YEASTSCS7genetic
20526336
VPS8_YEASTVPS8genetic
21987634
NUM1_YEASTNUM1genetic
21987634
SWA2_YEASTSWA2genetic
21987634
ATO3_YEASTATO3genetic
21987634
RV167_YEASTRVS167genetic
21987634
ERG4_YEASTERG4genetic
21987634
PIL1_YEASTPIL1genetic
21987634
ARP1_YEASTARP1genetic
21987634
INP51_YEASTINP51genetic
21987634
RIC1_YEASTRIC1genetic
21987634
CCW12_YEASTCCW12genetic
21987634
YPT6_YEASTYPT6genetic
21987634
DYN3_YEASTDYN3genetic
21987634
PFD4_YEASTGIM3genetic
21987634
PEP12_YEASTPEP12genetic
21987634
VATA_YEASTVMA1physical
22940862
RAV1_YEASTRAV1physical
22940862
VATH_YEASTVMA13physical
22940862
VATB_YEASTVMA2physical
22940862
ICS2_YEASTICS2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
NBP2_YEASTNBP2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
VAM7_YEASTVAM7genetic
27708008
MAL12_YEASTMAL12genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
BFA1_YEASTBFA1genetic
27708008
MPCP_YEASTMIR1genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
MCR1_YEASTMCR1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
PDR8_YEASTPDR8genetic
27708008
SEI1_YEASTFLD1genetic
27708008
ATP18_YEASTATP18genetic
27708008
GRP78_YEASTKAR2genetic
27708008
ESS1_YEASTESS1genetic
27708008
RSC9_YEASTRSC9genetic
27708008
ESA1_YEASTESA1genetic
27708008
ARP7_YEASTARP7genetic
27708008
GEM1_YEASTGEM1genetic
27708008
TPS1_YEASTTPS1genetic
27708008
MTC4_YEASTMTC4genetic
27708008
REI1_YEASTREI1genetic
27708008
YB8B_YEASTYBR287Wgenetic
27708008
DCC1_YEASTDCC1genetic
27708008
RV161_YEASTRVS161genetic
27708008
PAT1_YEASTPAT1genetic
27708008
YD121_YEASTYDL121Cgenetic
27708008
ATG9_YEASTATG9genetic
27708008
NUM1_YEASTNUM1genetic
27708008
H2A1_YEASTHTA1genetic
27708008
ASPG1_YEASTASP1genetic
27708008
SAC7_YEASTSAC7genetic
27708008
DLDH_YEASTLPD1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
PIL1_YEASTPIL1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
HTD2_YEASTHTD2genetic
27708008
PTH_YEASTPTH1genetic
27708008
ACA2_YEASTCST6genetic
27708008
AIM21_YEASTAIM21genetic
27708008
PBS2_YEASTPBS2genetic
27708008
HOC1_YEASTHOC1genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
FEN1_YEASTRAD27genetic
27708008
HOG1_YEASTHOG1genetic
27708008
MMS22_YEASTMMS22genetic
27708008
PALI_YEASTRIM9genetic
27708008
MOT3_YEASTMOT3genetic
27708008
TDA1_YEASTTDA1genetic
27708008
INP53_YEASTINP53genetic
27708008
LIPA_YEASTLIP5genetic
27708008
PALA_YEASTRIM20genetic
27708008
SPS4_YEASTSPS4genetic
27708008
THP3_YEASTTHP3genetic
27708008
MSS18_YEASTMSS18genetic
27708008
CSK22_YEASTCKA2genetic
25268174
MYO5_YEASTMYO5genetic
25268174
RBD2_YEASTRBD2genetic
25694450
PP2B1_YEASTCNA1physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INP52_YEAST

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Related Literatures of Post-Translational Modification
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-149; SER-152; SER-952;SER-962; SER-1082; THR-1083; THR-1133; SER-1146 AND SER-1148, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-444; SER-1081; SER-1082AND THR-1083, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005 AND SER-1011, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, AND MASSSPECTROMETRY.

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