PRTB_YEAST - dbPTM
PRTB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRTB_YEAST
UniProt AC P09232
Protein Name Cerevisin
Gene Name PRB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 635
Subcellular Localization Vacuole.
Protein Description Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase..
Protein Sequence MKLENTLFTLGALGSISAALVIPNLENAADHHELINKEDHHERPRKVEFTKDDDEEPSDSEDKEHGKFHKKGRKGQDKESPEFNGKRASGSHGSAHEGGKGMKPKHESSNDDDNDDKKKKPHHKGGCHENKVEEKKMKGKKVKGKKHHEKTLEKGRHHNRLAPLVSTAQFNPDAISKIIPNRYIIVFKRGAPQEEIDFHKENVQQAQLQSVENLSAEDAFFISTKDTSLSTSEAGGIQDSFNIDNLFSGYIGYFTQEIVDLIRQNPLVDFVERDSIVEATEFDTQNSAPWGLARISHRERLNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKHYGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPGSDSEFFELGQDSLTPQQLKKKLIHYSTKDILFDIPEDTPNVLIYNGGGQDLSAFWNDTKKSHSSGFKQELNMDEFIGSKTDLIFDQVRDILDKLNII
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
58PhosphorylationKDDDEEPSDSEDKEH
CCCCCCCCCCCCHHC		57.9825521595
60PhosphorylationDDEEPSDSEDKEHGK
CCCCCCCCCCHHCCC		52.6222890988
177UbiquitinationFNPDAISKIIPNRYI
CCHHHHHHHCCCEEE		38.2417644757
188UbiquitinationNRYIIVFKRGAPQEE
CEEEEEEECCCCHHH		38.7417644757
305PhosphorylationRERLNLGSFNKYLYD
HHCCCCCCCCCEEEC		28.8922369663
308AcetylationLNLGSFNKYLYDDDA
CCCCCCCCEEECCCC		34.3224489116
308UbiquitinationLNLGSFNKYLYDDDA
CCCCCCCCEEECCCC		34.3217644757
333UbiquitinationTGVNINHKDFEKRAI
CCCCCCCHHHHHHHC		60.6717644757
337AcetylationINHKDFEKRAIWGKT
CCCHHHHHHHCCCEE		47.3124489116
343AcetylationEKRAIWGKTIPLNDE
HHHHCCCEEEECCCH		28.4324489116
374UbiquitinationSKHYGVAKNANVVAV
HCCCCCCCCCCEEEE		54.9417644757
382UbiquitinationNANVVAVKVLRSNGS
CCCEEEEEEEECCCC		26.3017644757
389PhosphorylationKVLRSNGSGTMSDVV
EEEECCCCCCHHHHH		35.0327214570
397UbiquitinationGTMSDVVKGVEYAAK
CCHHHHHHHHHHHHH		58.0217644757
594N-linked_GlycosylationQDLSAFWNDTKKSHS
CCHHHHHHCCCCCCC		40.39-
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 PRTB_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRTB_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 PRTB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PBN1_YEASTPBN1physical
9649520
CBPY_YEASTPRC1genetic
17899065
YBQ6_YEASTYBR056Wgenetic
20093466
CHK1_YEASTCHK1genetic
20093466
RV161_YEASTRVS161genetic
20093466
BUD31_YEASTBUD31genetic
20093466
HOSC_YEASTLYS20genetic
20093466
VMS1_YEASTVMS1genetic
20093466
SWI5_YEASTSWI5genetic
20093466
VPS74_YEASTVPS74genetic
20093466
LSM6_YEASTLSM6genetic
20093466
RPOM_YEASTRPO41genetic
20093466
MSH4_YEASTMSH4genetic
20093466
RRT6_YEASTRRT6genetic
20093466
OPI1_YEASTOPI1genetic
20093466
VPS29_YEASTVPS29genetic
20093466
SLT2_YEASTSLT2genetic
20093466
SAE3_YEASTSAE3genetic
20093466
WSS1_YEASTWSS1genetic
20093466
STM1_YEASTSTM1genetic
20093466
GSF2_YEASTGSF2genetic
20093466
MVP1_YEASTMVP1genetic
20093466
SAM37_YEASTSAM37genetic
20093466
GBLP_YEASTASC1genetic
20093466
OCA2_YEASTOCA2genetic
20093466
MSN1_YEASTMSN1genetic
20093466
SHE4_YEASTSHE4genetic
20093466
VPS17_YEASTVPS17genetic
20093466
LIPA_YEASTLIP5genetic
20093466
FABD_YEASTMCT1genetic
20093466
DGAT2_YEASTDGA1genetic
20093466
VPH1_YEASTVPH1genetic
20093466
CAF20_YEASTCAF20genetic
20093466
YO304_YEASTBIL1genetic
20093466
TGS1_YEASTTGS1genetic
20093466
CARP_YEASTPEP4genetic
20093466
ODC1_YEASTODC1genetic
20093466
GSHR_YEASTGLR1genetic
20093466
SUR1_YEASTSUR1genetic
20093466
YME1_YEASTYME1genetic
20093466
PACC_YEASTRIM101genetic
20641016
HSP71_YEASTSSA1physical
22940862
VPS51_YEASTVPS51genetic
23169651
CHK1_YEASTCHK1genetic
22282571
SLT2_YEASTSLT2genetic
22282571
H3_YEASTHHT1physical
24587380
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
YME1_YEASTYME1genetic
27708008
LCB2_YEASTLCB2genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRP18_YEASTPRP18genetic
27708008
MOB1_YEASTMOB1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
LCB1_YEASTLCB1genetic
27708008
LST8_YEASTLST8genetic
27708008
HRP1_YEASTHRP1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
MED10_YEASTNUT2genetic
27708008
DEP1_YEASTDEP1genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
MUM2_YEASTMUM2genetic
27708008
RV161_YEASTRVS161genetic
27708008
ELO2_YEASTELO2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
PAT1_YEASTPAT1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
SLX5_YEASTSLX5genetic
27708008
HOSC_YEASTLYS20genetic
27708008
MAF1_YEASTMAF1genetic
27708008
VMS1_YEASTVMS1genetic
27708008
PAA1_YEASTPAA1genetic
27708008
SWI5_YEASTSWI5genetic
27708008
VPS74_YEASTVPS74genetic
27708008
LSM6_YEASTLSM6genetic
27708008
MSH4_YEASTMSH4genetic
27708008
MRM2_YEASTMRM2genetic
27708008
PEF1_YEASTPEF1genetic
27708008
VPS29_YEASTVPS29genetic
27708008
SLT2_YEASTSLT2genetic
27708008
HTD2_YEASTHTD2genetic
27708008
WSS1_YEASTWSS1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
YJE9_YEASTYJL049Wgenetic
27708008
YJH0_YEASTYJL070Cgenetic
27708008
BCK1_YEASTBCK1genetic
27708008
VPS35_YEASTVPS35genetic
27708008
YJ24_YEASTKCH1genetic
27708008
BLI1_YEASTBLI1genetic
27708008
FLO10_YEASTFLO10genetic
27708008
GST2_YEASTGTT2genetic
27708008
STM1_YEASTSTM1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
VPS38_YEASTVPS38genetic
27708008
SRR1L_YEASTBER1genetic
27708008
PSP2_YEASTPSP2genetic
27708008
GSF2_YEASTGSF2genetic
27708008
GTR1_YEASTGTR1genetic
27708008
MVP1_YEASTMVP1genetic
27708008
SAM37_YEASTSAM37genetic
27708008
GBLP_YEASTASC1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
LSM7_YEASTLSM7genetic
27708008
PFA4_YEASTPFA4genetic
27708008
MSN1_YEASTMSN1genetic
27708008
VPS17_YEASTVPS17genetic
27708008
FABD_YEASTMCT1genetic
27708008
GSHR_YEASTGLR1genetic
27708008
ODC1_YEASTODC1genetic
27708008
CARP_YEASTPEP4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRTB_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-58, 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-58, AND MASSSPECTROMETRY.

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