CIS3_YEAST - dbPTM
CIS3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CIS3_YEAST
UniProt AC P47001
Protein Name Cell wall mannoprotein CIS3
Gene Name CIS3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 227
Subcellular Localization Secreted, cell wall . Covalently attached to the cell wall. Localizes predominantly on the surface of growing buds.
Protein Description Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents..
Protein Sequence MQFKNVALAASVAALSATASAEGYTPGEPWSTLTPTGSISCGAAEYTTTFGIAVQAITSSKAKRDVISQIGDGQVQATSAATAQATDSQAQATTTATPTSSEKISSSASKTSTNATSSSCATPSLKDSSCKNSGTLELTLKDGVLTDAKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSITEDGYLALGDSDVFYQCLSGNFYNLYDQNVAEQCSAIHLEAVSLVDC
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
68O-linked_GlycosylationKAKRDVISQIGDGQV
CCCHHHHHHHCCCCE		18.6516495216
78O-linked_GlycosylationGDGQVQATSAATAQA
CCCCEEECCEEECCC		11.2116495216
93PhosphorylationTDSQAQATTTATPTS
CCCCHHHHCCCCCCC		16.7628889911
105O-linked_GlycosylationPTSSEKISSSASKTS
CCCCHHHCCCCCCCC		29.3412776183
106O-linked_GlycosylationTSSEKISSSASKTST
CCCHHHCCCCCCCCC		33.1412776183
107O-linked_GlycosylationSSEKISSSASKTSTN
CCHHHCCCCCCCCCC		29.7612776183
109O-linked_GlycosylationEKISSSASKTSTNAT
HHHCCCCCCCCCCCC		38.1112776183
110UbiquitinationKISSSASKTSTNATS
HHCCCCCCCCCCCCC		46.3323749301
111O-linked_GlycosylationISSSASKTSTNATSS
HCCCCCCCCCCCCCC		37.9812776183
112O-linked_GlycosylationSSSASKTSTNATSSS
CCCCCCCCCCCCCCC		24.3312776183
113O-linked_GlycosylationSSASKTSTNATSSSC
CCCCCCCCCCCCCCC		33.8212776183
114N-linked_GlycosylationSASKTSTNATSSSCA
CCCCCCCCCCCCCCC		40.77-
116O-linked_GlycosylationSKTSTNATSSSCATP
CCCCCCCCCCCCCCC		31.0712776183
117O-linked_GlycosylationKTSTNATSSSCATPS
CCCCCCCCCCCCCCC		20.1712776183
118O-linked_GlycosylationTSTNATSSSCATPSL
CCCCCCCCCCCCCCC		25.6912776183
126UbiquitinationSCATPSLKDSSCKNS
CCCCCCCCCCCCCCC		60.9623749301
141AcetylationGTLELTLKDGVLTDA
CEEEEEEECCEEECC		47.3924489116
146PhosphorylationTLKDGVLTDAKGRIG
EEECCEEECCCCCEE		31.3527017623
149UbiquitinationDGVLTDAKGRIGSIV
CCEEECCCCCEEEEE		52.0823749301
149SuccinylationDGVLTDAKGRIGSIV
CCEEECCCCCEEEEE		52.0823954790
154PhosphorylationDAKGRIGSIVANRQF
CCCCCEEEEEECCEE		16.1225752575
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 CIS3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CIS3_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 CIS3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS150_YEASTHSP150genetic
10407261
PIR1_YEASTPIR1genetic
14734022
HS150_YEASTHSP150genetic
14734022
PIR3_YEASTPIR3genetic
14734022
GUP1_YEASTGUP1genetic
20526336
TOR2_YEASTTOR2genetic
20526336
ARV1_YEASTARV1genetic
23891562
GAS1_YEASTGAS1genetic
23891562
CCW12_YEASTCCW12genetic
23891562
VPS41_YEASTVPS41genetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
YM46_YEASTYMR181Cgenetic
27708008
ATG3_YEASTATG3genetic
27708008
NTH1_YEASTNTG1genetic
27708008
TOD6_YEASTTOD6genetic
27708008
ADH5_YEASTADH5genetic
27708008
YC01A_YEASTYCL001W-Agenetic
27708008
NHP10_YEASTNHP10genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
ACK1_YEASTACK1genetic
27708008
BAP3_YEASTBAP3genetic
27708008
OCA6_YEASTOCA6genetic
27708008
SWI5_YEASTSWI5genetic
27708008
ENT5_YEASTENT5genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
MDS3_YEASTMDS3genetic
27708008
RME1_YEASTRME1genetic
27708008
CRH1_YEASTCRH1genetic
27708008
SNG1_YEASTSNG1genetic
27708008
TNA1_YEASTTNA1genetic
27708008
OPI1_YEASTOPI1genetic
27708008
SNL1_YEASTSNL1genetic
27708008
YIF5_YEASTYIL055Cgenetic
27708008
THIK_YEASTPOT1genetic
27708008
ALLA_YEASTDAL3genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
PAN3_YEASTPAN3genetic
27708008
RT109_YEASTRTT109genetic
27708008
YL032_YEASTYLL032Cgenetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
YL257_YEASTYLR257Wgenetic
27708008
YL278_YEASTYLR278Cgenetic
27708008
EFM7_YEASTNNT1genetic
27708008
FKS1_YEASTFKS1genetic
27708008
AP1_YEASTYAP1genetic
27708008
PSP2_YEASTPSP2genetic
27708008
SOK2_YEASTSOK2genetic
27708008
GAS1_YEASTGAS1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
PHO23_YEASTPHO23genetic
27708008
OCA1_YEASTOCA1genetic
27708008
MSB4_YEASTMSB4genetic
27708008
MSA1_YEASTMSA1genetic
27708008
SFL1_YEASTSFL1genetic
27708008
PMT3_YEASTPMT3genetic
27708008
MED1_YEASTMED1genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
VPS4_YEASTVPS4genetic
27708008
HDA3_YEASTHDA3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CIS3_YEAST

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Related Literatures of Post-Translational Modification
O-linked Glycosylation
ReferencePubMed
"Pir proteins of Saccharomyces cerevisiae are attached to beta-1,3-glucan by a new protein-carbohydrate linkage.";
Ecker M., Deutzmann R., Lehle L., Mrsa V., Tanner W.;
J. Biol. Chem. 281:11523-11529(2006).
Cited for: PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION AT SER-68 AND THR-78,MUTAGENESIS OF ASP-65; SER-68; GLN-69; ASP-72; GLN-74; GLN-76; THR-78;SER-79 AND THR-82, CELL WALL ATTACHMENT SITE, AND MASS SPECTROMETRY.
"O-mannosylation precedes and potentially controls the N-glycosylationof a yeast cell wall glycoprotein.";
Ecker M., Mrsa V., Hagen I., Deutzmann R., Strahl S., Tanner W.;
EMBO Rep. 4:628-632(2003).
Cited for: PROTEIN SEQUENCE OF 65-118, AND GLYCOSYLATION AT SER-105; SER-106;SER-107; SER-109; THR-111; SER-112; THR-113; THR-116; SER-117 ANDSER-118.
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-93, AND MASSSPECTROMETRY.

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