CHA4_YEAST - dbPTM
CHA4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHA4_YEAST
UniProt AC P43634
Protein Name Activatory protein CHA4
Gene Name CHA4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 648
Subcellular Localization Nucleus .
Protein Description Activates the CHA1 gene for L-serine dehydratase. Binds to the DNA sequence 5'-GVGGARAYRTRATTCCRC-3'..
Protein Sequence MMLEPSPPPLTTTVTPSLPSSLKKSVTDNDQNNNNVPRKRKLACQNCRRRRRKCNMEKPCSNCIKFRTECVFTQQDLRNKRYSTTYVEALQSQIRSLKEQLQILSSSSSTIASNALSSLKNNSDHGDAPNEKILKYGETAQSALPSSESNDENESDAFTKKMPSESPPPVGTNSIYPSNSLSIIKKKTDGSTRYQQQQVSLKNLSRSPLILRSLSLFFKWLYPGHYLFIHRETFLSAFFGDTNTKSYYCSEELVFAIAALGSLISYKSETELFQQSEVFYQRAKTIVLKKIFQLEDSSLAESSSSSKLAIIQTLLCLAFYDIGSGENPMAWYLSGLAFRIAHEIGLHLNPEAWSNVYEDELSIMDFEVRSRIYWGCYIADHLIAILFGRSTSLRLSNSTVPETDELPEIETGIEEYIYDPKVILSTANPLKKLIVLSRITEIFASKIFSPNETLLQRSEYLAKFNLEVYNWRRDLPPELQWTKRSLMEMTDFNPTIAYVWFHYYIVLISYNKPFIYEIKQSRELVEGYVDELYYLLKVWKNKFKTFEKATIYMIYSAILAIQCMKSNLIKKDRKQDFLNFLSAPTLNYELARKFIENSEDALHNSETMDLLGTLSHGNDFALEYNFDFTLLNEIDMLIGGNTNDGLSK
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
6Phosphorylation--MMLEPSPPPLTTT
--CCCCCCCCCCCCC		40.4325752575
11PhosphorylationEPSPPPLTTTVTPSL
CCCCCCCCCCCCCCC		26.6228152593
12PhosphorylationPSPPPLTTTVTPSLP
CCCCCCCCCCCCCCC		27.2728152593
17PhosphorylationLTTTVTPSLPSSLKK
CCCCCCCCCCHHHCC		43.4728152593
20PhosphorylationTVTPSLPSSLKKSVT
CCCCCCCHHHCCCCC		54.3028152593
21PhosphorylationVTPSLPSSLKKSVTD
CCCCCCHHHCCCCCC		42.1228152593
25PhosphorylationLPSSLKKSVTDNDQN
CCHHHCCCCCCCCCC		28.7622369663
27PhosphorylationSSLKKSVTDNDQNNN
HHHCCCCCCCCCCCC		35.8521551504
123PhosphorylationLSSLKNNSDHGDAPN
HHHHHCCCCCCCCCC		40.1428889911
146PhosphorylationTAQSALPSSESNDEN
HHHHHCCCCCCCCCC		47.8121551504
147PhosphorylationAQSALPSSESNDENE
HHHHCCCCCCCCCCC		43.0028889911
149PhosphorylationSALPSSESNDENESD
HHCCCCCCCCCCCCC		52.0823749301
155PhosphorylationESNDENESDAFTKKM
CCCCCCCCCHHHCCC		45.9123749301
159PhosphorylationENESDAFTKKMPSES
CCCCCHHHCCCCCCC		31.3223749301
164PhosphorylationAFTKKMPSESPPPVG
HHHCCCCCCCCCCCC		47.4022369663
166PhosphorylationTKKMPSESPPPVGTN
HCCCCCCCCCCCCCC		47.2322369663
172PhosphorylationESPPPVGTNSIYPSN
CCCCCCCCCCCCCCC		26.4822369663
174PhosphorylationPPPVGTNSIYPSNSL
CCCCCCCCCCCCCCC		24.2822369663
176PhosphorylationPVGTNSIYPSNSLSI
CCCCCCCCCCCCCCE		10.6322369663
178PhosphorylationGTNSIYPSNSLSIIK
CCCCCCCCCCCCEEE		23.2919823750
180PhosphorylationNSIYPSNSLSIIKKK
CCCCCCCCCCEEEEC		28.0319823750
182PhosphorylationIYPSNSLSIIKKKTD
CCCCCCCCEEEECCC		23.3019823750
302PhosphorylationEDSSLAESSSSSKLA
CCCCCCCCCCHHHHH		29.8827017623
305PhosphorylationSLAESSSSSKLAIIQ
CCCCCCCHHHHHHHH		33.1827017623
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 CHA4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHA4_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 CHA4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BUD21_YEASTBUD21genetic
20093466
HMO1_YEASTHMO1genetic
20959818
SODC_YEASTSOD1genetic
20959818
SNT1_YEASTSNT1genetic
20959818
HAP5_YEASTHAP5genetic
20959818
SUB1_YEASTSUB1genetic
20959818
UBP3_YEASTUBP3genetic
20959818
NU133_YEASTNUP133genetic
21127252
KAPC_YEASTTPK3genetic
21127252
NRG1_YEASTNRG1genetic
21127252
PHD1_YEASTPHD1genetic
21127252
EAF5_YEASTEAF5genetic
21127252
RAD51_YEASTRAD51genetic
21127252
MDS3_YEASTMDS3genetic
21127252
BUB1_YEASTBUB1genetic
21127252
CTK1_YEASTCTK1genetic
21127252
ADR1_YEASTADR1genetic
21127252
ELM1_YEASTELM1genetic
21127252
KAPA_YEASTTPK1genetic
21127252
RTG3_YEASTRTG3genetic
21127252
HAL4_YEASTSAT4genetic
21127252
FUS3_YEASTFUS3genetic
21127252
SNF5_YEASTSNF5genetic
27708008
THRC_YEASTTHR4genetic
27708008
IMG2_YEASTIMG2genetic
27708008
AAD3_YEASTAAD3genetic
27708008
YD186_YEASTYDL186Wgenetic
27708008
MCM21_YEASTMCM21genetic
27708008
RV167_YEASTRVS167genetic
27708008
CBT1_YEASTCBT1genetic
27708008
SSO2_YEASTSSO2genetic
27708008
LSM7_YEASTLSM7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHA4_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-6, 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-164, AND MASSSPECTROMETRY.

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