PPZ2_YEAST - dbPTM
PPZ2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPZ2_YEAST
UniProt AC P33329
Protein Name Serine/threonine-protein phosphatase PP-Z2
Gene Name PPZ2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 710
Subcellular Localization
Protein Description Essential for the maintenance of cell size and integrity in response to osmotic stress..
Protein Sequence MGNSGSKQHTKHNSKKDDHDGDRKKTLDLPPLTKSDTTHSLKSSRSLRSLRSKRSEASLASNVQAQTQPLSRRSSTLGNGNRNHRRSNNAPITPPNNHYLTSHPSSSRRLSSSSRRSSMGNNNNSELPPSMIQMEPKSPILKNSTSMHSTSSFNSYENALTDDDDDRGDDGGESPSMAKVTRINTSSSADRGSKRTPLRRHNSLQPEKGVTGFSSTSSKLRRRSDNTLPASYPLNAEAGGNGSDYFSNRSNSHASSRKSSFGSTGNTAYSTPLHSPALRKMSSRDNDDSGDNVNGRGTSPIPNLNIDKPSPSASSASKREYLSAYPTLAHRDSSSSLSPRGKGQRSSSSSSSSQRIYVSPPSPTGDFVHGSCADGDNGSRTNTMVEMKRKKPVRPVDIDEIIQRLLDAGYAAKRTKNVCLKNSEIIQICHKARELFLAQPALLELSPSVKIVGDVHGQYADLLRLFTKCGFPPMANYLFLGDYVDRGKQSLETILLLLCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWKTFVDTFNTLPLAAIVTGKIFCVHGGLSPVLNSMDEIRHVSRPTDVPDFGLINDLLWSDPTDSSNEWEDNERGVSFCYNKVAINKFLNKFGFDLVCRAHMVVEDGYEFFNDRSLVTVFSAPNYCGEFDNWGAVMTVSEGLLCSFELLDPLDSTALKQVMKKGRQERKLANR
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
2Myristoylation------MGNSGSKQH
------CCCCCCCCC
36.69-
35PhosphorylationDLPPLTKSDTTHSLK
CCCCCCCCCCCCHHH
34.6528889911
37PhosphorylationPPLTKSDTTHSLKSS
CCCCCCCCCCHHHHH
33.2427214570
38PhosphorylationPLTKSDTTHSLKSSR
CCCCCCCCCHHHHHH
17.9228889911
40PhosphorylationTKSDTTHSLKSSRSL
CCCCCCCHHHHHHHH
35.0927214570
43PhosphorylationDTTHSLKSSRSLRSL
CCCCHHHHHHHHHHH
35.9630377154
44PhosphorylationTTHSLKSSRSLRSLR
CCCHHHHHHHHHHHH
25.0530377154
46PhosphorylationHSLKSSRSLRSLRSK
CHHHHHHHHHHHHHH
30.0421440633
49PhosphorylationKSSRSLRSLRSKRSE
HHHHHHHHHHHHHCH
33.1721440633
52PhosphorylationRSLRSLRSKRSEASL
HHHHHHHHHHCHHHH
37.4019779198
55PhosphorylationRSLRSKRSEASLASN
HHHHHHHCHHHHHHH
41.0529136822
58PhosphorylationRSKRSEASLASNVQA
HHHHCHHHHHHHHHH
22.0329136822
61PhosphorylationRSEASLASNVQAQTQ
HCHHHHHHHHHHHCC
42.7123749301
71PhosphorylationQAQTQPLSRRSSTLG
HHHCCCCCCCCCCCC
32.1229136822
74PhosphorylationTQPLSRRSSTLGNGN
CCCCCCCCCCCCCCC
26.9427214570
75PhosphorylationQPLSRRSSTLGNGNR
CCCCCCCCCCCCCCC
26.3227214570
76PhosphorylationPLSRRSSTLGNGNRN
CCCCCCCCCCCCCCC
39.6730377154
87PhosphorylationGNRNHRRSNNAPITP
CCCCCCCCCCCCCCC
34.1023749301
93PhosphorylationRSNNAPITPPNNHYL
CCCCCCCCCCCCCCC
31.4729136822
99PhosphorylationITPPNNHYLTSHPSS
CCCCCCCCCCCCCCC
17.5023749301
106PhosphorylationYLTSHPSSSRRLSSS
CCCCCCCCCCCCCCC
32.1123749301
107PhosphorylationLTSHPSSSRRLSSSS
CCCCCCCCCCCCCCC
26.2523749301
117PhosphorylationLSSSSRRSSMGNNNN
CCCCCCCCCCCCCCC
24.4623749301
118PhosphorylationSSSSRRSSMGNNNNS
CCCCCCCCCCCCCCC
28.9723749301
125PhosphorylationSMGNNNNSELPPSMI
CCCCCCCCCCCHHHH
42.5119779198
138PhosphorylationMIQMEPKSPILKNST
HHCCCCCCCCCCCCC
28.0823749301
151PhosphorylationSTSMHSTSSFNSYEN
CCCCCCCCCCCCHHC
35.6321440633
155PhosphorylationHSTSSFNSYENALTD
CCCCCCCCHHCCCCC
31.6421551504
156PhosphorylationSTSSFNSYENALTDD
CCCCCCCHHCCCCCC
17.8221440633
161PhosphorylationNSYENALTDDDDDRG
CCHHCCCCCCCCCCC
34.6621440633
174PhosphorylationRGDDGGESPSMAKVT
CCCCCCCCCCCEEEE
26.0828889911
181PhosphorylationSPSMAKVTRINTSSS
CCCCEEEEEEECCCC
25.7321551504
185PhosphorylationAKVTRINTSSSADRG
EEEEEEECCCCCCCC
27.8423749301
186PhosphorylationKVTRINTSSSADRGS
EEEEEECCCCCCCCC
20.1519823750
187PhosphorylationVTRINTSSSADRGSK
EEEEECCCCCCCCCC
27.7524603354
188PhosphorylationTRINTSSSADRGSKR
EEEECCCCCCCCCCC
33.6819823750
193PhosphorylationSSSADRGSKRTPLRR
CCCCCCCCCCCCCCC
21.6221551504
203PhosphorylationTPLRRHNSLQPEKGV
CCCCCCCCCCCCCCC
23.4321082442
224PhosphorylationSSKLRRRSDNTLPAS
CHHHHHCCCCCCCCC
33.1428889911
227PhosphorylationLRRRSDNTLPASYPL
HHHCCCCCCCCCCCC
38.8319779198
231PhosphorylationSDNTLPASYPLNAEA
CCCCCCCCCCCCCCC
25.9119779198
232PhosphorylationDNTLPASYPLNAEAG
CCCCCCCCCCCCCCC
17.5319779198
243PhosphorylationAEAGGNGSDYFSNRS
CCCCCCCCCCCCCCC
32.8928889911
245PhosphorylationAGGNGSDYFSNRSNS
CCCCCCCCCCCCCCC
15.5919779198
247PhosphorylationGNGSDYFSNRSNSHA
CCCCCCCCCCCCCCC
25.7119779198
259PhosphorylationSHASSRKSSFGSTGN
CCCCCCCCCCCCCCC
29.7722369663
260PhosphorylationHASSRKSSFGSTGNT
CCCCCCCCCCCCCCC
36.3423749301
263PhosphorylationSRKSSFGSTGNTAYS
CCCCCCCCCCCCCCC
31.0022369663
264PhosphorylationRKSSFGSTGNTAYST
CCCCCCCCCCCCCCC
34.5322369663
267PhosphorylationSFGSTGNTAYSTPLH
CCCCCCCCCCCCCCC
28.4622369663
269PhosphorylationGSTGNTAYSTPLHSP
CCCCCCCCCCCCCCH
15.8422369663
270PhosphorylationSTGNTAYSTPLHSPA
CCCCCCCCCCCCCHH
22.5322369663
271PhosphorylationTGNTAYSTPLHSPAL
CCCCCCCCCCCCHHH
19.7322369663
275PhosphorylationAYSTPLHSPALRKMS
CCCCCCCCHHHHHHH
21.3922369663
282PhosphorylationSPALRKMSSRDNDDS
CHHHHHHHCCCCCCC
25.8424909858
283PhosphorylationPALRKMSSRDNDDSG
HHHHHHHCCCCCCCC
39.9124909858
289PhosphorylationSSRDNDDSGDNVNGR
HCCCCCCCCCCCCCC
51.4119795423
298PhosphorylationDNVNGRGTSPIPNLN
CCCCCCCCCCCCCCC
29.9322369663
299PhosphorylationNVNGRGTSPIPNLNI
CCCCCCCCCCCCCCC
24.5322369663
310PhosphorylationNLNIDKPSPSASSAS
CCCCCCCCCCCCCHH
36.9122369663
312PhosphorylationNIDKPSPSASSASKR
CCCCCCCCCCCHHHH
45.1622369663
314PhosphorylationDKPSPSASSASKREY
CCCCCCCCCHHHHHH
30.6722369663
315PhosphorylationKPSPSASSASKREYL
CCCCCCCCHHHHHHH
35.9622369663
317PhosphorylationSPSASSASKREYLSA
CCCCCCHHHHHHHHH
33.9122369663
321PhosphorylationSSASKREYLSAYPTL
CCHHHHHHHHHCCCC
15.2519823750
323PhosphorylationASKREYLSAYPTLAH
HHHHHHHHHCCCCCC
25.5119823750
325PhosphorylationKREYLSAYPTLAHRD
HHHHHHHCCCCCCCC
8.0619823750
327PhosphorylationEYLSAYPTLAHRDSS
HHHHHCCCCCCCCCC
24.7321440633
333PhosphorylationPTLAHRDSSSSLSPR
CCCCCCCCCCCCCCC
31.8821440633
334PhosphorylationTLAHRDSSSSLSPRG
CCCCCCCCCCCCCCC
28.3819823750
335PhosphorylationLAHRDSSSSLSPRGK
CCCCCCCCCCCCCCC
38.9719823750
336PhosphorylationAHRDSSSSLSPRGKG
CCCCCCCCCCCCCCC
34.5117330950
338PhosphorylationRDSSSSLSPRGKGQR
CCCCCCCCCCCCCCC
17.9425752575
357PhosphorylationSSSSQRIYVSPPSPT
CCCCCCEEECCCCCC
9.3229136822
359PhosphorylationSSQRIYVSPPSPTGD
CCCCEEECCCCCCCC
17.7029136822
362PhosphorylationRIYVSPPSPTGDFVH
CEEECCCCCCCCCCC
38.1821082442
364PhosphorylationYVSPPSPTGDFVHGS
EECCCCCCCCCCCCC
54.4429136822
371PhosphorylationTGDFVHGSCADGDNG
CCCCCCCCCCCCCCC
7.4029136822
379PhosphorylationCADGDNGSRTNTMVE
CCCCCCCCCCCCCEE
42.0319779198
381PhosphorylationDGDNGSRTNTMVEMK
CCCCCCCCCCCEEEE
36.4223749301
383PhosphorylationDNGSRTNTMVEMKRK
CCCCCCCCCEEEECC
23.2130377154
413UbiquitinationLDAGYAAKRTKNVCL
HHHHHHHHHCCCEEC
53.0523749301
503UbiquitinationLLLCYKIKYPENFFL
HHHHHHCCCCCCEEE
51.0723749301
567PhosphorylationFCVHGGLSPVLNSMD
EEECCCHHHHHCCHH
19.0823749301
628UbiquitinationAINKFLNKFGFDLVC
HHHHHHHHCCCCCEE
49.3523749301

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 PPZ2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPZ2_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 PPZ2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SDS22_YEASTSDS22physical
11805837
GLC8_YEASTGLC8physical
11805837
VHS3_YEASTVHS3physical
11805837
SLT2_YEASTSLT2genetic
14871941
PPZ1_YEASTPPZ1genetic
8395014
SIS2_YEASTSIS2physical
18467557
CAB3_YEASTCAB3physical
18467557
PFD5_YEASTGIM5genetic
19269370
CAB3_YEASTCAB3physical
20489023
HAL1_YEASTHAL1physical
20489023
PPZ1_YEASTPPZ1physical
20489023
SDS22_YEASTSDS22physical
20489023
SIS2_YEASTSIS2physical
20489023
VHS3_YEASTVHS3physical
20489023
YPI1_YEASTYPI1physical
20489023
TRK2_YEASTTRK2genetic
21143561
TRK1_YEASTTRK1genetic
21143561
SLT2_YEASTSLT2genetic
21143561
HCM1_YEASTHCM1genetic
21127252
DUN1_YEASTDUN1genetic
21127252
UME6_YEASTUME6genetic
21127252
UPC2_YEASTUPC2genetic
21127252
NHP10_YEASTNHP10genetic
21127252
IPMK_YEASTARG82genetic
21127252
SIS2_YEASTSIS2genetic
23275495
PDC2_YEASTPDC2genetic
27708008
MED14_YEASTRGR1genetic
27708008
RPB1_YEASTRPO21genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SPC19_YEASTSPC19genetic
27708008
RSP5_YEASTRSP5genetic
27708008
COG3_YEASTCOG3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
MCE1_YEASTCEG1genetic
27708008
CDC45_YEASTCDC45genetic
27708008
NEP1_YEASTEMG1genetic
27708008
TEM1_YEASTTEM1genetic
27708008
ORC1_YEASTORC1genetic
27708008
RSC9_YEASTRSC9genetic
27708008
RNA1_YEASTRNA1genetic
27708008
CET1_YEASTCET1genetic
27708008
ASA1_YEASTASA1genetic
27708008
UBI4P_YEASTUBI4genetic
29130884

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPZ2_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-299; SER-310 ANDSER-362, AND MASS SPECTROMETRY.
"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-362, 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-188 AND SER-203, ANDMASS SPECTROMETRY.

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