PLP2_YEAST - dbPTM
PLP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLP2_YEAST
UniProt AC Q12017
Protein Name Phosducin-like protein 2
Gene Name PLP2 {ECO:0000312|SGD:S000005807}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 286
Subcellular Localization Cytoplasm .
Protein Description Essential for cell growth. Inhibits early G-protein signaling events following pheromone stimulation..
Protein Sequence MQNEPMFQVQVDESEDSEWNDILRAKGVIPERAPSPTAKLEEALEEAIAKQHENRLEDKDLSDLEELEDDEDEDFLEAYKIKRLNEIRKLQERSKFGEVFHINKPEYNKEVTLASQGKKYEGAQTNDNGEEDDGGVYVFVHLSLQSKLQSRILSHLFQSAACKFREIKFVEIPANRAIENYPESNCPTLIVYYRGEVIKNMITLLELGGNNSKMEDFEDFMVKVGAVAEGDNRLIMNRDDEESREERKLHYGEKKSIRSGIRGKFNVGIGGNDDGNINDDDDGFFD
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
14PhosphorylationFQVQVDESEDSEWND
EEEECCCCCCCHHHH		42.0930377154
17PhosphorylationQVDESEDSEWNDILR
ECCCCCCCHHHHHHH		40.2230377154
35PhosphorylationVIPERAPSPTAKLEE
CCCCCCCCCCCHHHH		33.6222369663
37PhosphorylationPERAPSPTAKLEEAL
CCCCCCCCCHHHHHH		40.5422369663
62PhosphorylationRLEDKDLSDLEELED
HCCCCCCHHHHHHCC		50.7322369663
109AcetylationINKPEYNKEVTLASQ
ECCCCCCCEEEEECC		53.3024489116
243PhosphorylationMNRDDEESREERKLH
CCCCCHHHHHHHHHC		42.8328889911
254AcetylationRKLHYGEKKSIRSGI
HHHCCCCHHHHHCCC		47.6725381059
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 PLP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLP2_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 PLP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPB_YEASTCCT2physical
16429126
TCPD_YEASTCCT4physical
16429126
TCPZ_YEASTCCT6physical
16429126
TCPH_YEASTCCT7physical
16429126
TCPQ_YEASTCCT8physical
16429126
VHS2_YEASTVHS2genetic
17429077
VHS3_YEASTVHS3genetic
17429077
PP2C2_YEASTPTC2genetic
17429077
PP2C3_YEASTPTC3genetic
17429077
YAP7_YEASTYAP7genetic
17429077
HAL5_YEASTHAL5genetic
17429077
SIS2_YEASTSIS2genetic
17429077
CG13_YEASTCLN3genetic
17429077
ACT_YEASTACT1physical
19501098
GYP5_YEASTGYP5physical
22875988
RE104_YEASTREC104genetic
27708008
SWE1_YEASTSWE1genetic
27708008
BFA1_YEASTBFA1genetic
27708008
ARPC1_YEASTARC40genetic
27708008
TECR_YEASTTSC13genetic
27708008
ARP2_YEASTARP2genetic
27708008
TCPD_YEASTCCT4genetic
27708008
DAD1_YEASTDAD1genetic
27708008
SC61G_YEASTSSS1genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
TCPA_YEASTTCP1genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
ARPC5_YEASTARC15genetic
27708008
TCPE_YEASTCCT5genetic
27708008
FIP1_YEASTFIP1genetic
27708008
HIR1_YEASTHIR1genetic
27708008
DSE2_YEASTDSE2genetic
27708008
HOS4_YEASTHOS4genetic
27708008
MOG1_YEASTMOG1genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
PFD6_YEASTYKE2genetic
27708008
TDA1_YEASTTDA1genetic
27708008
PFD4_YEASTGIM3genetic
27708008
AGA1_YEASTAGA1genetic
27708008
TBCC_YEASTCIN2genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
AXL1_YEASTAXL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLP2_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-35 AND SER-62, 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 SER-35 AND SER-62, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
"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 SER-35 AND SER-62, AND MASSSPECTROMETRY.
"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-35, AND MASSSPECTROMETRY.

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