GAL83_YEAST - dbPTM
GAL83_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAL83_YEAST
UniProt AC Q04739
Protein Name SNF1 protein kinase subunit beta-3
Gene Name GAL83
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 417
Subcellular Localization Cytoplasm . Nucleus . Resides in the cytosol during growth on fermentable carbon sources and relocalizes rapidly to the nucleus in response to carbon stress.
Protein Description Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Promotes the relocalization of the SNF1 kinase complex to the nucleus upon shift to nonfermentable carbon sources..
Protein Sequence MAGDNPENKDASMLDVSDAASNTTINGKHSADSTNEASLAYTFSQMNVDNPNELEPQHPLRHKSSLIFNDDDDDEIPPYSNHAENGSGETFDSDDDIDASSSSSIDSNEGDIHDADMTGNTLQKMDYQPSQQPDSLQNQGFQQQQEQQQGTVEGKKGRAMMFPVDITWQQGGNKVYVTGSFTGWRKMIGLVPVPGQPGLMHVKLQLPPGTHRFRFIVDNELRFSDYLPTATDQMGNFVNYMEVSAPPDWGNEPQQHLAEKKANHVDDSKLSKRPMSARSRIALEIEKEPDDMGDGYTRFHDETPAKPNLEYTQDIPAVFTDPNVMEQYYLTLDQQQNNHQNMAWLTPPQLPPHLENVILNSYSNAQTDNTSGALPIPNHVILNHLATSSIKHNTLCVASIVRYKQKYVTQILYTPLQ
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
12PhosphorylationNPENKDASMLDVSDA
CCCCCCCCCCCHHHH		29.9722369663
17PhosphorylationDASMLDVSDAASNTT
CCCCCCHHHHHCCCE		22.6222369663
21PhosphorylationLDVSDAASNTTINGK
CCHHHHHCCCEECCC		36.1122369663
23PhosphorylationVSDAASNTTINGKHS
HHHHHCCCEECCCCC		26.9322369663
24PhosphorylationSDAASNTTINGKHSA
HHHHCCCEECCCCCC		19.3920377248
30PhosphorylationTTINGKHSADSTNEA
CEECCCCCCCCCCHH		36.9422369663
33PhosphorylationNGKHSADSTNEASLA
CCCCCCCCCCHHHHH		32.6122369663
34PhosphorylationGKHSADSTNEASLAY
CCCCCCCCCHHHHHH		37.3122369663
38PhosphorylationADSTNEASLAYTFSQ
CCCCCHHHHHHEHHH		13.8322369663
41PhosphorylationTNEASLAYTFSQMNV
CCHHHHHHEHHHCCC		17.3822369663
42PhosphorylationNEASLAYTFSQMNVD
CHHHHHHEHHHCCCC		15.9422369663
44PhosphorylationASLAYTFSQMNVDNP
HHHHHEHHHCCCCCC		22.2622369663
64PhosphorylationQHPLRHKSSLIFNDD
CCCCCCCCCEEECCC		25.0119897735
65PhosphorylationHPLRHKSSLIFNDDD
CCCCCCCCEEECCCC		30.2219897735
87PhosphorylationSNHAENGSGETFDSD
CCCCCCCCCCCCCCC		45.0719897735
90PhosphorylationAENGSGETFDSDDDI
CCCCCCCCCCCCCCC		35.9519897735
93PhosphorylationGSGETFDSDDDIDAS
CCCCCCCCCCCCCCC		38.4519897735
130PhosphorylationQKMDYQPSQQPDSLQ
HHCCCCCCCCCCHHH		26.3923749301
135PhosphorylationQPSQQPDSLQNQGFQ
CCCCCCCHHHHHCHH		38.2423749301
178PhosphorylationGGNKVYVTGSFTGWR
CCCEEEEEECCCCCH		14.9324961812
180PhosphorylationNKVYVTGSFTGWRKM
CEEEEEECCCCCHHE		15.4022369663
182PhosphorylationVYVTGSFTGWRKMIG
EEEEECCCCCHHEEE		37.2221440633
276PhosphorylationKLSKRPMSARSRIAL
HHCCCCCCHHHHEEE		24.1817287358
279PhosphorylationKRPMSARSRIALEIE
CCCCCHHHHEEEEEE		27.9617287358
287UbiquitinationRIALEIEKEPDDMGD
HEEEEEECCCCCCCC		79.0023749301
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 GAL83_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAL83_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 GAL83_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNF1_YEASTSNF1physical
9121458
AAKG_YEASTSNF4physical
9121458
REG1_YEASTREG1genetic
8293971
SIP1_YEASTSIP1genetic
8293971
SIP1_YEASTSIP1genetic
8088514
SIP2_YEASTSIP2genetic
8293971
NRG1_YEASTNRG1genetic
12556493
NRG2_YEASTNRG2genetic
12556493
SIP1_YEASTSIP1genetic
12556493
SIP1_YEASTSIP1genetic
15340085
SIP2_YEASTSIP2genetic
15340085
REG1_YEASTREG1physical
16554755
BMH2_YEASTBMH2physical
16554755
SAK1_YEASTSAK1physical
16554755
RAD4_YEASTRAD4physical
16554755
AAKG_YEASTSNF4physical
16554755
6P22_YEASTPFK27physical
17828247
REE1_YEASTREE1physical
18851946
REG1_YEASTREG1genetic
19269370
SIP1_YEASTSIP1genetic
19269370
GDA1_YEASTGDA1genetic
19269370
GET2_YEASTGET2genetic
19269370
KHSE_YEASTTHR1genetic
19269370
PP2C7_YEASTPTC7genetic
19269370
CBT1_YEASTCBT1genetic
19269370
RIC1_YEASTRIC1genetic
19269370
YPT6_YEASTYPT6genetic
19269370
PPZ1_YEASTPPZ1genetic
19269370
DSS1_YEASTDSS1genetic
19269370
CLA4_YEASTCLA4genetic
19269370
PHO88_YEASTPHO88genetic
23891562
TIR2_YEASTTIR2genetic
23891562
KAPB_YEASTTPK2genetic
23495665
SLX5_YEASTSLX5genetic
27708008
SIP1_YEASTSIP1genetic
27708008
MSH4_YEASTMSH4genetic
27708008
MED5_YEASTNUT1genetic
27708008
CHO2_YEASTCHO2genetic
27708008
MED20_YEASTSRB2genetic
27708008
ILM1_YEASTILM1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
PEX13_YEASTPEX13genetic
27708008
EIF3J_YEASTHCR1genetic
27708008
GSF2_YEASTGSF2genetic
27708008
OCA1_YEASTOCA1genetic
27708008
SFL1_YEASTSFL1genetic
27708008
SYH1_YEASTSYH1genetic
27708008
SPEE_YEASTSPE3genetic
27708008
PSK1_YEASTPSK1physical
25428989
SIP1_YEASTSIP1genetic
27592031
SIP2_YEASTSIP2genetic
27592031
SNF1_YEASTSNF1physical
23184934
AAKG_YEASTSNF4physical
23184934
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GAL83_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-12; SER-17; SER-21;THR-23 AND SER-44, AND MASS SPECTROMETRY.
"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-276 AND SER-279, ANDMASS SPECTROMETRY.

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