FKS2_YEAST - dbPTM
FKS2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKS2_YEAST
UniProt AC P40989
Protein Name 1,3-beta-glucan synthase component GSC2
Gene Name GSC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1895
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS). Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall. Required for spore wall assembly. Negative regulation of activity by SMK1 is important for spore wall deposition. Activity is positively regulated by RHO1..
Protein Sequence MSYNDPNLNGQYYSNGDGTGDGNYPTYQVTQDQSAYDEYGQPIYTQNQLDDGYYDPNEQYVDGTQFPQGQDPSQDQGPYNNDASYYNQPPNMMNPSSQDGENFSDFSSYGPPSGTYPNDQYTPSQMSYPDQDGSSGASTPYGNGVVNGNGQYYDPNAIEMALPNDPYPAWTADPQSPLPIEQIEDIFIDLTNKFGFQRDSMRNMFDHFMTLLDSRSSRMSPEQALLSLHADYIGGDTANYKKWYFAAQLDMDDEIGFRNMKLGKLSRKARKAKKKNKKAMQEASPEDTEETLNQIEGDNSLEAADFRWKSKMNQLSPFEMVRQIALFLLCWGEANQVRFTPECLCFIYKCASDYLDSAQCQQRPDPLPEGDFLNRVITPLYRFIRSQVYEIVDGRYVKSEKDHNKVIGYDDVNQLFWYPEGIAKIVMEDGTRLIDLPAEERYLKLGEIPWDDVFFKTYKETRSWLHLVTNFNRIWIMHISVYWMYCAYNAPTFYTHNYQQLVDNQPLAAYKWATAALGGTVASLIQVAATLCEWSFVPRKWAGAQHLSRRFWFLCVIMGINLGPVIFVFAYDKDTVYSTAAHVVGAVMFFVAVATLVFFSVMPLGGLFTSYMKKSTRSYVASQTFTASFAPLHGLDRWMSYLVWVTVFAAKYAESYFFLILSLRDPIRILSTTSMRCTGEYWWGNKICKVQPKIVLGLMIATDFILFFLDTYLWYIVVNTVFSVGKSFYLGISILTPWRNIFTRLPKRIYSKILATTDMEIKYKPKVLISQIWNAIIISMYREHLLAIDHVQKLLYHQVPSEIEGKRTLRAPTFFVSQDDNNFETEFFPRDSEAERRISFFAQSLSTPIPEPLPVDNMPTFTVLTPHYAERILLSLREIIREDDQFSRVTLLEYLKQLHPVEWDCFVKDTKILAEETAAYENNEDEPEKEDALKSQIDDLPFYCIGFKSAAPEYTLRTRIWASLRSQTLYRTISGFMNYSRAIKLLYRVENPEIVQMFGGNADGLERELEKMARRKFKFLVSMQRLAKFKPHELENAEFLLRAYPDLQIAYLDEEPPLNEGEEPRIYSALIDGHCEILENGRRRPKFRVQLSGNPILGDGKSDNQNHALIFYRGEYIQLIDANQDNYLEECLKIRSVLAEFEELGIEQIHPYTPGLKYEDQSTNHPVAIVGAREYIFSENSGVLGDVAAGKEQTFGTLFARTLAQIGGKLHYGHPDFINATFMTTRGGVSKAQKGLHLNEDIYAGMNAVLRGGRIKHCEYYQCGKGRDLGFGTILNFTTKIGAGMGEQMLSREYYYLGTQLPIDRFLTFYYAHPGFHLNNLFIQLSLQMFMLTLVNLHALAHESILCVYDRDKPITDVLYPIGCYNFHPAIDWVRRYTLSIFIVFWIAFVPIVVQELIERGLWKATQRFFRHILSLSPMFEVFAGQIYSSALLSDIAVGGARYISTGRGFATSRIPFSILYSRFAGSAIYMGSRSMLMLLFGTVAHWQAPLLWFWASLSALIFAPFIFNPHQFAWEDFFLDYRDYIRWLSRGNNKYHRNSWIGYVRMSRSRVTGFKRKLVGDESEKSAGDASRAHRTNLIMAEIIPCAIYAAGCFIAFTFINAQTGVKTTDEDRVNSTLRIIICTLAPIVIDIGVLFFCMGLSCCSGPLLGMCCKKTGSVMAGIAHGIAVVVHIVFFIVMWVLEGFSFVRMLIGVVTCIQCQRLIFHCMTVLLLTREFKNDHANTAFWTGKWYSTGLGYMAWTQPTRELTAKVIELSEFAADFVLGHVILIFQLPVICIPKIDKFHSIMLFWLKPSRQIRPPIYSLKQARLRKRMVRRYCSLYFLVLIIFAGCIVGPAVASAHVPKDLGSGLTGTFHNLVQPRNVSNNDTGSQMSTYKSHYYTHTPSLKTWSTIK
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
278UbiquitinationKAKKKNKKAMQEASP
HHHHHCHHHHHHCCC		59.4923749301
284PhosphorylationKKAMQEASPEDTEET
HHHHHHCCCCHHHHH		28.2427214570
288PhosphorylationQEASPEDTEETLNQI
HHCCCCHHHHHHHHH		33.78-
291PhosphorylationSPEDTEETLNQIEGD
CCCHHHHHHHHHCCC		25.44-
349UbiquitinationECLCFIYKCASDYLD
HHHHHHHHHHHHHHH		20.6417644757
405UbiquitinationKSEKDHNKVIGYDDV
ECCCCCCCEECCCCH		31.6317644757
424UbiquitinationWYPEGIAKIVMEDGT
CCCCCCEEEEEECCC		33.6317644757
444UbiquitinationPAEERYLKLGEIPWD
CHHHHHHHCCCCCHH		45.5717644757
456UbiquitinationPWDDVFFKTYKETRS
CHHHCCCHHHHHHHH		39.2117644757
756PhosphorylationIYSKILATTDMEIKY
HHHHHHHCCCCCCCC		21.6327017623
793UbiquitinationLAIDHVQKLLYHQVP
HHHHHHHHHHHCCCC		39.0922106047
806UbiquitinationVPSEIEGKRTLRAPT
CCCHHCCCCEEECCE		29.4423749301
813PhosphorylationKRTLRAPTFFVSQDD
CCEEECCEEEEECCC		28.8127017623
887PhosphorylationIREDDQFSRVTLLEY
HHCCCCCCHHHHHHH		21.8721177495
896UbiquitinationVTLLEYLKQLHPVEW
HHHHHHHHHHCCCCC		50.3317644757
929UbiquitinationNNEDEPEKEDALKSQ
CCCCCCHHHHHHHHH		72.1623749301
934UbiquitinationPEKEDALKSQIDDLP
CHHHHHHHHHHCCCC		41.8724961812
935PhosphorylationEKEDALKSQIDDLPF
HHHHHHHHHHCCCCE		32.9722369663
948UbiquitinationPFYCIGFKSAAPEYT
CEEEEEECCCCCCCC		33.6923749301
972PhosphorylationRSQTLYRTISGFMNY
HHHHHHHHHHHHCCH		13.1122369663
974PhosphorylationQTLYRTISGFMNYSR
HHHHHHHHHHCCHHH		25.9322369663
979PhosphorylationTISGFMNYSRAIKLL
HHHHHCCHHHHHHHH		6.4322369663
980PhosphorylationISGFMNYSRAIKLLY
HHHHCCHHHHHHHHH		15.3822369663
984UbiquitinationMNYSRAIKLLYRVEN
CCHHHHHHHHHHCCC		31.3023749301
1018UbiquitinationKMARRKFKFLVSMQR
HHHHHHHHHHHHHHH		40.6017644757
1028UbiquitinationVSMQRLAKFKPHELE
HHHHHHHCCCHHHHH		59.5223749301
1030UbiquitinationMQRLAKFKPHELENA
HHHHHCCCHHHHHCH		44.7723749301
1086UbiquitinationENGRRRPKFRVQLSG
HCCCCCCCEEEEECC		43.9517644757
1092PhosphorylationPKFRVQLSGNPILGD
CCEEEEECCCCCCCC		21.3121440633
1101UbiquitinationNPILGDGKSDNQNHA
CCCCCCCCCCCCCEE		60.4223749301
1133UbiquitinationNYLEECLKIRSVLAE
CHHHHHHHHHHHHHH		47.9717644757
1191UbiquitinationLGDVAAGKEQTFGTL
CCCHHCCCCCCHHHH		41.7523749301
1209UbiquitinationTLAQIGGKLHYGHPD
HHHHHCCEEECCCHH		27.2017644757
1221PhosphorylationHPDFINATFMTTRGG
CHHHCCEEEEECCCC		14.9524930733
1224PhosphorylationFINATFMTTRGGVSK
HCCEEEEECCCCCCH		14.7824930733
1234UbiquitinationGGVSKAQKGLHLNED
CCCCHHHCCCCCCCC		69.1917644757
1256UbiquitinationVLRGGRIKHCEYYQC
HHCCCCCCCCEEEEC		40.6217644757
1265UbiquitinationCEYYQCGKGRDLGFG
CEEEECCCCCCCCCC		59.4017644757
1280UbiquitinationTILNFTTKIGAGMGE
HHHEEECCCCCCCCH		35.7617644757
1461PhosphorylationRIPFSILYSRFAGSA
CCCHHHHHHHCCCCC		8.9827017623
1467PhosphorylationLYSRFAGSAIYMGSR
HHHHCCCCCEEECCH		14.2027017623
1473PhosphorylationGSAIYMGSRSMLMLL
CCCEEECCHHHHHHH		12.4927017623
1540PhosphorylationNNKYHRNSWIGYVRM
CCCCCCCCCEEEEEE		21.7428889911
1556UbiquitinationRSRVTGFKRKLVGDE
HHHCCCCEEECCCCH		50.3922817900
1558UbiquitinationRVTGFKRKLVGDESE
HCCCCEEECCCCHHH		48.3823749301
1566UbiquitinationLVGDESEKSAGDASR
CCCCHHHCCCCCHHH		55.6823749301
1735PhosphorylationWTGKWYSTGLGYMAW
EECCCEECCCCCCCC		22.2630377154
1746PhosphorylationYMAWTQPTRELTAKV
CCCCCCCCHHHHHHH		27.2730377154
1846UbiquitinationVASAHVPKDLGSGLT
HHCCCCCCCCCCCCC		65.5817644757
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 FKS2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKS2_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 FKS2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FKS1_YEASTFKS1genetic
14764870
SCW4_YEASTSCW4genetic
15470100
SCW10_YEASTSCW10genetic
15470100
LRG1_YEASTLRG1genetic
11447600
FKS1_YEASTFKS1genetic
17158736
FKS1_YEASTFKS1genetic
15166135
HKR1_YEASTHKR1genetic
20526336
SMI1_YEASTSMI1genetic
23891562
ARO1_YEASTARO1genetic
27708008
YPS7_YEASTYPS7genetic
27708008
SMI1_YEASTSMI1genetic
27708008
YPT6_YEASTYPT6genetic
27708008
FKS1_YEASTFKS1genetic
27708008
ARPC3_YEASTARC18genetic
27708008
VPS9_YEASTVPS9genetic
27708008
MSC1_YEASTMSC1genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
ZDS1_YEASTZDS1genetic
26728856
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FKS2_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-974, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-806, AND MASSSPECTROMETRY.

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