ZDS1_YEAST - dbPTM
ZDS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZDS1_YEAST
UniProt AC P50111
Protein Name Protein ZDS1
Gene Name ZDS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 915
Subcellular Localization Cytoplasm . Concentrated at incipient bud site of unbudded cells and at the bud tip of small and medium-sized buds.
Protein Description Has a role in establishing cell polarity. Together with cAMP-dependent protein kinase regulatory subunit BCY1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1. In heat-stressed cells appears to play a role in localizing BCY1 to the cytoplasm. Seems to interact with, and down-regulate, CDC42. Also acts as a suppressor of PKC1. May act as an integration point for distinct signaling pathways helping to maintain a balance among these different pathways.; When associated with DBP5, GFD1 and nucleoporins at the cytosolic fibrils of the nuclear pore complex, is required for mRNA export form the nucleus..
Protein Sequence MSNRDNESMLRTTSSDKAIASQRDKRKSEVLIAAQSLDNEIRSVKNLKRLSIGSMDLLIDPELDIKFGGESSGRRSWSGTTSSSASMPSDTTTVNNTRYSDPTPLENLHGRGNSGIESSNKTKQGNYLGIKKGVHSPSRKLNANVLKKNLLWVPANQHPNVKPDNFLELVQDTLQNIQLSDNGEDNDGNSNENNDIEDNGEDKESQSYENKENNTINLNRGLSRHGNASLIRRPSTLRRSYTEFDDNEDDDNKGDSASETVNKVEERISKIKERPVSLRDITEELTKISNSAGLTDNDAITLARTLSMAGSYSDKKDQPQPEGHYDEGDIGFSTSQANTLDDGEFASNMPINNTMTWPERSSLRRSRFNTYRIRSQEQEKEVEQSVDEMKNDDEERLKLTKNTIKVEIDPHKSPFRQQDEDSENMSSPGSIGDFQDIYNHYRQSSGEWEQEMGIEKEAEEVPVKVRNDTVEQDLELREGTTDMVKPSATDDNKETKRHRRRNGWTWLNNKMSREDDNEENQGDDENEENVDSQRMELDNSKKHYISLFNGGEKTEVSNKEEMNNSSTSTATSQTRQKIEKTFANLFRRKPHHKHDASSSPSSSPSSSPSIPNNDAVHVRVRKSKKLGNKSGREPVEPIVLRNRPRPHRHHHSRHGSQKISVKTLKDSQPQQQIPLQPQLEGAIEIEKKEESDSESLPQLQPAVSVSSTKSNSRDREEEEAKKKNKKRSNTTEISNQQHSKHVQKENTDEQKAQLQAPAQEQVQTSVPVQASAPVQNSAPVQTSAPVEASAQTQAPAAPPLKHTSILPPRKLTFADVKKPDKPNSPVQFTDSAFGFPLPLLTVSTVIMFDHRLPINVERAIYRLSHLKLSNSKRGLREQVLLSNFMYAYLNLVNHTLYMEQVAHDKEQQQQQQQQP
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
8PhosphorylationMSNRDNESMLRTTSS
CCCCCCHHHCCCCCH		29.3924909858
12PhosphorylationDNESMLRTTSSDKAI
CCHHHCCCCCHHHHH		27.3730377154
13PhosphorylationNESMLRTTSSDKAIA
CHHHCCCCCHHHHHH		21.5721551504
14PhosphorylationESMLRTTSSDKAIAS
HHHCCCCCHHHHHHH		35.6123749301
15PhosphorylationSMLRTTSSDKAIASQ
HHCCCCCHHHHHHHH		40.8323749301
21PhosphorylationSSDKAIASQRDKRKS
CHHHHHHHHHHHHHH		21.4521551504
28PhosphorylationSQRDKRKSEVLIAAQ
HHHHHHHHHHHHHHH		36.6528889911
51PhosphorylationVKNLKRLSIGSMDLL
HHHHCCCCCCCCCEE		29.0119823750
54PhosphorylationLKRLSIGSMDLLIDP
HCCCCCCCCCEEECC		13.8821440633
78PhosphorylationSSGRRSWSGTTSSSA
CCCCCCCCCCCCCCC		27.7519779198
86PhosphorylationGTTSSSASMPSDTTT
CCCCCCCCCCCCCCC		32.9219779198
93PhosphorylationSMPSDTTTVNNTRYS
CCCCCCCCCCCCCCC		24.2719779198
99PhosphorylationTTVNNTRYSDPTPLE
CCCCCCCCCCCCCHH		18.5225704821
100PhosphorylationTVNNTRYSDPTPLEN
CCCCCCCCCCCCHHH		33.5528132839
103PhosphorylationNTRYSDPTPLENLHG
CCCCCCCCCHHHCCC		45.5628132839
136PhosphorylationGIKKGVHSPSRKLNA
CCCCCCCCCCCCCCH		23.3628889911
229PhosphorylationLSRHGNASLIRRPST
HHHCCCCHHHCCCHH		28.4717330950
240PhosphorylationRPSTLRRSYTEFDDN
CCHHCCCCEEECCCC		29.9428889911
241PhosphorylationPSTLRRSYTEFDDNE
CHHCCCCEEECCCCC		14.4219779198
242PhosphorylationSTLRRSYTEFDDNED
HHCCCCEEECCCCCC		31.2728889911
277PhosphorylationKIKERPVSLRDITEE
HHHHCCCCHHHHHHH		21.9921440633
282PhosphorylationPVSLRDITEELTKIS
CCCHHHHHHHHHHHH		27.9124961812
286PhosphorylationRDITEELTKISNSAG
HHHHHHHHHHHHCCC		29.6119779198
307PhosphorylationITLARTLSMAGSYSD
HHHHHHHHHHCCCCC		13.1328889911
413PhosphorylationVEIDPHKSPFRQQDE
EEECCCCCCCCCCCC		26.6625704821
422PhosphorylationFRQQDEDSENMSSPG
CCCCCCCCCCCCCCC		28.9028889911
426PhosphorylationDEDSENMSSPGSIGD
CCCCCCCCCCCCHHH		44.9919779198
430PhosphorylationENMSSPGSIGDFQDI
CCCCCCCCHHHHHHH		27.1228889911
444PhosphorylationIYNHYRQSSGEWEQE
HHHHHHHCCCHHHHH		31.1728889911
445PhosphorylationYNHYRQSSGEWEQEM
HHHHHHCCCHHHHHH		32.1824909858
456UbiquitinationEQEMGIEKEAEEVPV
HHHHCCCCCCEECCC		61.3723749301
464UbiquitinationEAEEVPVKVRNDTVE
CCEECCCEEECCCHH		29.4323749301
559UbiquitinationEKTEVSNKEEMNNSS
CEEECCCHHHHCCCC		47.7723749301
565PhosphorylationNKEEMNNSSTSTATS
CHHHHCCCCCCCCHH		29.9527017623
569PhosphorylationMNNSSTSTATSQTRQ
HCCCCCCCCHHHHHH		33.7627017623
571PhosphorylationNSSTSTATSQTRQKI
CCCCCCCHHHHHHHH		22.8127017623
597PhosphorylationPHHKHDASSSPSSSP
CCCCCCCCCCCCCCC		37.0927017623
598PhosphorylationHHKHDASSSPSSSPS
CCCCCCCCCCCCCCC		48.2529136822
599PhosphorylationHKHDASSSPSSSPSS
CCCCCCCCCCCCCCC		26.7219779198
601PhosphorylationHDASSSPSSSPSSSP
CCCCCCCCCCCCCCC		45.4529136822
602PhosphorylationDASSSPSSSPSSSPS
CCCCCCCCCCCCCCC		50.0519779198
603PhosphorylationASSSPSSSPSSSPSI
CCCCCCCCCCCCCCC		32.8929136822
605PhosphorylationSSPSSSPSSSPSIPN
CCCCCCCCCCCCCCC		45.4529136822
606PhosphorylationSPSSSPSSSPSIPNN
CCCCCCCCCCCCCCC		50.0529136822
607PhosphorylationPSSSPSSSPSIPNND
CCCCCCCCCCCCCCC		27.3129136822
691PhosphorylationEIEKKEESDSESLPQ
EEEECCCCCCCCCCC		47.7522369663
693PhosphorylationEKKEESDSESLPQLQ
EECCCCCCCCCCCCC		38.0625521595
695PhosphorylationKEESDSESLPQLQPA
CCCCCCCCCCCCCCC		49.6720377248
704PhosphorylationPQLQPAVSVSSTKSN
CCCCCCEECCCCCCC		20.5622369663
706PhosphorylationLQPAVSVSSTKSNSR
CCCCEECCCCCCCCC		25.4522369663
707PhosphorylationQPAVSVSSTKSNSRD
CCCEECCCCCCCCCH		37.3820377248
708PhosphorylationPAVSVSSTKSNSRDR
CCEECCCCCCCCCHH		30.8720377248
710PhosphorylationVSVSSTKSNSRDREE
EECCCCCCCCCHHHH		39.8817287358
712PhosphorylationVSSTKSNSRDREEEE
CCCCCCCCCHHHHHH		42.5217287358
728PhosphorylationKKKNKKRSNTTEISN
HHHHHHCCCHHHHHH		47.6221082442
730PhosphorylationKNKKRSNTTEISNQQ
HHHHCCCHHHHHHHH		27.3517287358
812PhosphorylationILPPRKLTFADVKKP
CCCCCCCCCCCCCCC		21.5828889911
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 ZDS1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZDS1_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 ZDS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOS2_YEASTHOS2physical
11805826
IMB1_YEASTKAP95physical
11805826
PP2A2_YEASTPPH22physical
11805826
SIF2_YEASTSIF2physical
11805826
IMA1_YEASTSRP1physical
11805826
SNT1_YEASTSNT1physical
11805826
HOS4_YEASTHOS4physical
11805826
SET3_YEASTSET3physical
11805826
SIR2_YEASTSIR2physical
10398844
SIR3_YEASTSIR3physical
10398844
SIR4_YEASTSIR4physical
10398844
ZDS2_YEASTZDS2physical
11489916
DBP5_YEASTDBP5physical
15619606
GFD1_YEASTGFD1physical
15619606
ZDS2_YEASTZDS2genetic
10398844
ZDS2_YEASTZDS2genetic
9443973
ZDS2_YEASTZDS2genetic
8816438
MCK1_YEASTMCK1genetic
11230131
SWE1_YEASTSWE1genetic
9521328
CANB_YEASTCNB1genetic
9521328
SLT2_YEASTSLT2genetic
9521328
PP2B2_YEASTCMP2genetic
9521328
ZDS2_YEASTZDS2genetic
8816439
MEX67_YEASTMEX67genetic
15619606
ZDS2_YEASTZDS2genetic
15619606
CG12_YEASTCLN2genetic
16141237
RHO1_YEASTRHO1genetic
16141237
HOS2_YEASTHOS2physical
16429126
HOS4_YEASTHOS4physical
16429126
IMB1_YEASTKAP95physical
16429126
PP2A2_YEASTPPH22physical
16429126
SET3_YEASTSET3physical
16429126
SIF2_YEASTSIF2physical
16429126
SNT1_YEASTSNT1physical
16429126
AP1_YEASTYAP1genetic
16485023
ERF3_YEASTSUP35genetic
19061648
PRP19_YEASTPRP19genetic
19061648
PRP11_YEASTPRP11genetic
19061648
EI2BA_YEASTGCN3genetic
19061648
CLU_YEASTCLU1genetic
19061648
BUB1_YEASTBUB1genetic
19269370
STE20_YEASTSTE20genetic
19269370
RAS2_YEASTRAS2genetic
19269370
2ABA_YEASTCDC55physical
18762578
2AAA_YEASTTPD3physical
18762578
ZDS2_YEASTZDS2genetic
18762578
ESP1_YEASTESP1physical
18762578
HSP72_YEASTSSA2physical
19536198
SSB1_YEASTSSB1physical
19536198
PP2C1_YEASTPTC1genetic
20093466
SWI5_YEASTSWI5genetic
20093466
NBP2_YEASTNBP2genetic
20093466
BEM2_YEASTBEM2genetic
20093466
SMI1_YEASTSMI1genetic
20093466
IMPX_YEASTIMP2genetic
20093466
FMC1_YEASTFMC1genetic
20093466
HOC1_YEASTHOC1genetic
20093466
HSL1_YEASTHSL1genetic
20093466
ELM1_YEASTELM1genetic
20093466
MEH1_YEASTMEH1genetic
20093466
ZDS2_YEASTZDS2genetic
20093466
BUB3_YEASTBUB3genetic
20093466
ZDS2_YEASTZDS2genetic
20980617
2ABA_YEASTCDC55genetic
20980617
AIM3_YEASTAIM3genetic
21035341
ZDS2_YEASTZDS2genetic
21119008
2ABA_YEASTCDC55physical
21119008
2AAA_YEASTTPD3physical
21119008
PP2A1_YEASTPPH21physical
21119008
PP2A2_YEASTPPH22physical
21119008
2ABA_YEASTCDC55genetic
21536748
SWE1_YEASTSWE1genetic
21536748
LTE1_YEASTLTE1genetic
21536748
SIR3_YEASTSIR3genetic
21712379
CANB_YEASTCNB1genetic
21712379
SCH9_YEASTSCH9physical
22428880
KPC1_YEASTPKC1genetic
16141237
KPC1_YEASTPKC1genetic
11554924
2ABA_YEASTCDC55physical
22427694
SWE1_YEASTSWE1genetic
14623082
2ABA_YEASTCDC55physical
23861665
SIR4_YEASTSIR4genetic
25454064
IGO1_YEASTIGO1genetic
24800822
2ABA_YEASTCDC55genetic
24800822
BUD31_YEASTBUD31genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
NBP2_YEASTNBP2genetic
27708008
DOT1_YEASTDOT1genetic
27708008
SMI1_YEASTSMI1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
FMC1_YEASTFMC1genetic
27708008
IMPX_YEASTIMP2genetic
27708008
ELM1_YEASTELM1genetic
27708008
HSL1_YEASTHSL1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
ZDS2_YEASTZDS2genetic
27708008
AIM34_YEASTAIM34genetic
27708008
AIM44_YEASTAIM44genetic
27708008
RHO1_YEASTRHO1genetic
26728856
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZDS1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-229, AND MASSSPECTROMETRY.
"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 THR-730, AND MASSSPECTROMETRY.

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