PP2B2_YEAST - dbPTM
PP2B2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PP2B2_YEAST
UniProt AC P14747
Protein Name Serine/threonine-protein phosphatase 2B catalytic subunit A2
Gene Name CMP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 604
Subcellular Localization
Protein Description Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin..
Protein Sequence MSSDAIRNTEQINAAIKIIENKTERPQSSTTPIDSKASTVAAANSTATETSRDLTQYTLDDGRVVSTNRRIMNKVPAITSHVPTDEELFQPNGIPRHEFLRDHFKREGKLSAAQAARIVTLATELFSKEPNLISVPAPITVCGDIHGQYFDLLKLFEVGGDPATTSYLFLGDYVDRGSFSFECLIYLYSLKLNFNDHFWLLRGNHECKHLTSYFTFKNEMLHKYNLDIYEKCCESFNNLPLAALMNGQYLCVHGGISPELNSLQDINNLNRFREIPSHGLMCDLLWADPIEEYDEVLDKDLTEEDIVNSKTMVPHHGKMAPSRDMFVPNSVRGCSYAFTYRAACHFLQETGLLSIIRAHEAQDAGYRMYKNTKTLGFPSLLTLFSAPNYLDTYNNKAAILKYENNVMNIRQFNMTPHPYWLPDFMDVFTWSLPFVGEKVTEMLVAILNICTEDELENDTPVIEELVGTDKKLPQAGKSEATPQPATSASPKHASILDDEHRRKALRNKILAVAKVSRMYSVLREETNKVQFLKDHNSGVLPRGALSNGVKGLDEALSTFERARKHDLINEKLPPSLDELKNENKKYYEKVWQKVHEHDAKNDSK
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
17UbiquitinationEQINAAIKIIENKTE
HHHHHHHHHHHCCCC		32.6717644757
22UbiquitinationAIKIIENKTERPQSS
HHHHHHCCCCCCCCC		38.6823749301
23PhosphorylationIKIIENKTERPQSST
HHHHHCCCCCCCCCC		49.1322890988
28PhosphorylationNKTERPQSSTTPIDS
CCCCCCCCCCCCCCC		32.1322890988
29PhosphorylationKTERPQSSTTPIDSK
CCCCCCCCCCCCCCH		30.9322890988
30PhosphorylationTERPQSSTTPIDSKA
CCCCCCCCCCCCCHH		41.6722369663
31PhosphorylationERPQSSTTPIDSKAS
CCCCCCCCCCCCHHH		21.8622369663
35PhosphorylationSSTTPIDSKASTVAA
CCCCCCCCHHHHHHH		30.7322890988
36UbiquitinationSTTPIDSKASTVAAA
CCCCCCCHHHHHHHC		42.4823749301
38PhosphorylationTPIDSKASTVAAANS
CCCCCHHHHHHHCCC		27.4428889911
39PhosphorylationPIDSKASTVAAANST
CCCCHHHHHHHCCCC		21.0128889911
51PhosphorylationNSTATETSRDLTQYT
CCCCCCCCCCCCCCC		19.9827017623
109UbiquitinationDHFKREGKLSAAQAA
HHHHHCCCCCHHHHH		34.2223749301
120PhosphorylationAQAARIVTLATELFS
HHHHHHHHHHHHHHC		14.3322369663
123PhosphorylationARIVTLATELFSKEP
HHHHHHHHHHHCCCC		36.0122369663
127PhosphorylationTLATELFSKEPNLIS
HHHHHHHCCCCCCEE		49.0522369663
215PhosphorylationKHLTSYFTFKNEMLH
CCCCEEEEECHHHHH		26.0124930733
302PhosphorylationEVLDKDLTEEDIVNS
HHHCCCCCHHHHCCC		47.6825315811
477UbiquitinationKKLPQAGKSEATPQP
CCCCCCCCCCCCCCC		48.4123749301
478PhosphorylationKLPQAGKSEATPQPA
CCCCCCCCCCCCCCC		31.3922369663
481PhosphorylationQAGKSEATPQPATSA
CCCCCCCCCCCCCCC		20.5722369663
486PhosphorylationEATPQPATSASPKHA
CCCCCCCCCCCHHCH		31.3522369663
487PhosphorylationATPQPATSASPKHAS
CCCCCCCCCCHHCHH		28.9322369663
489PhosphorylationPQPATSASPKHASIL
CCCCCCCCHHCHHHC		33.9622369663
520PhosphorylationAKVSRMYSVLREETN
HHHHHHHHHHHHHHC		12.82-
533UbiquitinationTNKVQFLKDHNSGVL
HCCCHHHCCCCCCCC		59.2217644757
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 PP2B2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PP2B2_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 PP2B2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALM_YEASTCMD1physical
11805837
CANB_YEASTCNB1physical
11805837
IDH1_YEASTIDH1physical
11805837
EF1G2_YEASTTEF4physical
11805837
RPN7_YEASTRPN7physical
11805837
RFC3_YEASTRFC3physical
11805837
HSP82_YEASTHSP82physical
11094077
HSC82_YEASTHSC82physical
11094077
STD1_YEASTSTD1genetic
9725828
FKS1_YEASTFKS1genetic
7510323
CALM_YEASTCMD1physical
16554755
SLM2_YEASTSLM2physical
11283351
GCN2_YEASTGCN2genetic
19269370
ISC1_YEASTISC1genetic
19269370
MON1_YEASTMON1genetic
19269370
CAX4_YEASTCAX4genetic
19269370
YPT6_YEASTYPT6genetic
19269370
IPYR2_YEASTPPA2genetic
19269370
CANB_YEASTCNB1physical
20489023
RUVB2_YEASTRVB2physical
20489023
RGC1_YEASTRGC1physical
20489023
TSC10_YEASTTSC10genetic
20526336
SCS7_YEASTSCS7genetic
20526336
RTG3_YEASTRTG3genetic
21127252
ATG1_YEASTATG1genetic
21127252
MMS22_YEASTMMS22genetic
21127252
PKH3_YEASTPKH3genetic
21127252
YPT6_YEASTYPT6genetic
21987634
LIC4_YEASTATC1genetic
10102375
LIC4_YEASTATC1physical
10102375
CSG2_YEASTCSG2genetic
23891562
PP2B1_YEASTCNA1genetic
23891562
INP53_YEASTINP53physical
25518934
CSN12_YEASTYJR084Wgenetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
AVT5_YEASTAVT5genetic
27708008
SEA4_YEASTSEA4genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
RXT2_YEASTRXT2genetic
27708008
SIF2_YEASTSIF2genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
PYC2_YEASTPYC2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
PER1_YEASTPER1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
NDH2_YEASTNDE2genetic
27708008
NUR1_YEASTNUR1genetic
27708008
RL35A_YEASTRPL35Agenetic
27708008
RL35B_YEASTRPL35Agenetic
27708008
TGL2_YEASTTGL2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
MRB1_YEASTPHO92genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
GIP2_YEASTGIP2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
SA155_YEASTSAP155genetic
27708008
MRM2_YEASTMRM2genetic
27708008
ASK10_YEASTASK10genetic
27708008
CHO2_YEASTCHO2genetic
27708008
KEL1_YEASTKEL1genetic
27708008
SOL3_YEASTSOL3genetic
27708008
ATG7_YEASTATG7genetic
27708008
YJ24_YEASTKCH1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PP2B2_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 THR-30; THR-31 AND SER-489,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 THR-31, AND MASSSPECTROMETRY.

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