SHE3_YEAST - dbPTM
SHE3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHE3_YEAST
UniProt AC P38272
Protein Name SWI5-dependent HO expression protein 3
Gene Name SHE3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 425
Subcellular Localization Endoplasmic reticulum membrane
Peripheral membrane protein .
Protein Description RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud..
Protein Sequence MSDQDNTQTSSSKLAPHHNIFMANLESSPTKDRNTSSQNASSSRVIESLHDQIDMLTKTNLQLTTQSQNLLSKLELAQSKESKLLENLNLLKNENENLNSIFERKNKKLKELEKDYSELSNRYNEQKEKMDQLSKLAKNSSAIEQSCSEKLQNMEVNYNSLLESQNLYRDHYSDEISKLNEKIGLLELELSNQNLNYGSDTSSNSDIELNLNKFNDSVKDLKSLETEKDSKLSKIITHSLDELNLQSWLNLYQTNENLISTFAEKMDLKDVLKRNDEKISNKGAVVQTLKKNVQTQVESNNADALSSNNAQDMLPIKMVKLRKTPNTNDSSSNGNSSNNKRRSFYTASPLLSSGSIPKSASPVLPGVKRTASVRKPSSSSSKTNVTHNNDPSTSPTISVPPGVTRTVSSTHKKKGNSMVVHGAQS
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
2Phosphorylation------MSDQDNTQT
------CCCCCCCCC
43.9330377154
9PhosphorylationSDQDNTQTSSSKLAP
CCCCCCCCCCCCCCC
28.6530377154
10PhosphorylationDQDNTQTSSSKLAPH
CCCCCCCCCCCCCCC
23.8530377154
12PhosphorylationDNTQTSSSKLAPHHN
CCCCCCCCCCCCCCC
31.3030377154
27PhosphorylationIFMANLESSPTKDRN
EEEECCCCCCCCCCC
44.7925521595
28PhosphorylationFMANLESSPTKDRNT
EEECCCCCCCCCCCC
27.4922369663
30PhosphorylationANLESSPTKDRNTSS
ECCCCCCCCCCCCCC
47.7422369663
37PhosphorylationTKDRNTSSQNASSSR
CCCCCCCCCCHHHHH
25.9721082442
100PhosphorylationNENENLNSIFERKNK
CCCHHHHHHHHHHHH
31.6424961812
114AcetylationKKLKELEKDYSELSN
HHHHHHHHHHHHHHH
74.6824489116
123PhosphorylationYSELSNRYNEQKEKM
HHHHHHHHHHHHHHH
27.5728889911
140PhosphorylationLSKLAKNSSAIEQSC
HHHHHHCHHHHHHHH
22.0527017623
148PhosphorylationSAIEQSCSEKLQNME
HHHHHHHHHHHHCCC
42.9127017623
178AcetylationHYSDEISKLNEKIGL
HCHHHHHHHHHHHCC
62.0824489116
203PhosphorylationNYGSDTSSNSDIELN
CCCCCCCCCCCCEEH
42.3121440633
217PhosphorylationNLNKFNDSVKDLKSL
HHHHHCHHHHHHHHC
31.9723749301
219UbiquitinationNKFNDSVKDLKSLET
HHHCHHHHHHHHCCC
62.3823749301
228UbiquitinationLKSLETEKDSKLSKI
HHHCCCHHHHHHHHH
74.7923749301
295PhosphorylationTLKKNVQTQVESNNA
HHHHHHHHHHHHCCC
30.2428889911
299PhosphorylationNVQTQVESNNADALS
HHHHHHHHCCCCHHH
36.2128889911
306PhosphorylationSNNADALSSNNAQDM
HCCCCHHHCCCHHHH
32.5128889911
307PhosphorylationNNADALSSNNAQDML
CCCCHHHCCCHHHHC
34.6528889911
324PhosphorylationKMVKLRKTPNTNDSS
EEEEEECCCCCCCCC
18.4828889911
327PhosphorylationKLRKTPNTNDSSSNG
EEECCCCCCCCCCCC
41.4228889911
332PhosphorylationPNTNDSSSNGNSSNN
CCCCCCCCCCCCCCC
53.3528889911
336PhosphorylationDSSSNGNSSNNKRRS
CCCCCCCCCCCCCCC
35.5228889911
337PhosphorylationSSSNGNSSNNKRRSF
CCCCCCCCCCCCCCE
48.7128889911
343PhosphorylationSSNNKRRSFYTASPL
CCCCCCCCEEECCHH
27.0017330950
345PhosphorylationNNKRRSFYTASPLLS
CCCCCCEEECCHHHC
11.5722890988
346PhosphorylationNKRRSFYTASPLLSS
CCCCCEEECCHHHCC
20.7428132839
348PhosphorylationRRSFYTASPLLSSGS
CCCEEECCHHHCCCC
14.3119823750
352PhosphorylationYTASPLLSSGSIPKS
EECCHHHCCCCCCCC
40.0919823750
353PhosphorylationTASPLLSSGSIPKSA
ECCHHHCCCCCCCCC
36.2119823750
355PhosphorylationSPLLSSGSIPKSASP
CHHHCCCCCCCCCCC
37.3522890988
359PhosphorylationSSGSIPKSASPVLPG
CCCCCCCCCCCCCCC
28.7322890988
361PhosphorylationGSIPKSASPVLPGVK
CCCCCCCCCCCCCCE
23.7222369663
370PhosphorylationVLPGVKRTASVRKPS
CCCCCEEEEECCCCC
19.9819684113
372PhosphorylationPGVKRTASVRKPSSS
CCCEEEEECCCCCCC
23.1124909858
377PhosphorylationTASVRKPSSSSSKTN
EEECCCCCCCCCCCC
45.9819823750
378PhosphorylationASVRKPSSSSSKTNV
EECCCCCCCCCCCCC
42.6519779198
379PhosphorylationSVRKPSSSSSKTNVT
ECCCCCCCCCCCCCC
42.8619823750
380PhosphorylationVRKPSSSSSKTNVTH
CCCCCCCCCCCCCCC
37.4919823750
381PhosphorylationRKPSSSSSKTNVTHN
CCCCCCCCCCCCCCC
45.5121440633
383PhosphorylationPSSSSSKTNVTHNND
CCCCCCCCCCCCCCC
36.5522369663
386PhosphorylationSSSKTNVTHNNDPST
CCCCCCCCCCCCCCC
22.4322369663
392PhosphorylationVTHNNDPSTSPTISV
CCCCCCCCCCCCEEC
44.3622369663
393PhosphorylationTHNNDPSTSPTISVP
CCCCCCCCCCCEECC
44.0822369663
394PhosphorylationHNNDPSTSPTISVPP
CCCCCCCCCCEECCC
25.1222369663
396PhosphorylationNDPSTSPTISVPPGV
CCCCCCCCEECCCCC
26.1722369663
398PhosphorylationPSTSPTISVPPGVTR
CCCCCCEECCCCCEE
30.9220377248
404PhosphorylationISVPPGVTRTVSSTH
EECCCCCEEEECCCC
26.9120377248
406PhosphorylationVPPGVTRTVSSTHKK
CCCCCEEEECCCCCC
18.5121440633
408PhosphorylationPGVTRTVSSTHKKKG
CCCEEEECCCCCCCC
28.9820377248
409PhosphorylationGVTRTVSSTHKKKGN
CCEEEECCCCCCCCC
30.1428889911
410PhosphorylationVTRTVSSTHKKKGNS
CEEEECCCCCCCCCE
30.1521440633
417PhosphorylationTHKKKGNSMVVHGAQ
CCCCCCCEEEEECCC
22.9423749301
425PhosphorylationMVVHGAQS-------
EEEECCCC-------
41.4728889911

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 SHE3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHE3_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 SHE3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO4_YEASTMYO4physical
11805826
MLC1_YEASTMLC1physical
11805826
SHE2_YEASTSHE2physical
11805826
ERF1_YEASTSUP45physical
11805837
MLC1_YEASTMLC1physical
11805837
MYO4_YEASTMYO4physical
11805837
SUL2_YEASTSUL2physical
11805837
MYO4_YEASTMYO4physical
11032818
MYO4_YEASTMYO4physical
10792032
ASH1_YEASTASH1physical
10792032
SHE2_YEASTSHE2physical
15328357
MYO4_YEASTMYO4physical
16554755
CALM_YEASTCMD1physical
16554755
MLC1_YEASTMLC1physical
16554755
SHE2_YEASTSHE2physical
16554755
MLC1_YEASTMLC1physical
16429126
MYO4_YEASTMYO4physical
16429126
SHE2_YEASTSHE2physical
16429126
MYO4_YEASTMYO4physical
18056806
TPM2_YEASTTPM2physical
18467557
SHE2_YEASTSHE2physical
18467557
SHE3_YEASTSHE3physical
18467557
POP7_YEASTPOP7genetic
19061648
XRN1_YEASTXRN1genetic
19061648
EAF6_YEASTEAF6genetic
19061648
THP2_YEASTTHP2genetic
19061648
EAF5_YEASTEAF5genetic
19061648
MYO4_YEASTMYO4physical
19429778
SHE2_YEASTSHE2physical
19429778
ASH1_YEASTASH1physical
19429778
SHE2_YEASTSHE2physical
19244342
MYO4_YEASTMYO4physical
20439999
SHE2_YEASTSHE2physical
21526221
MYO4_YEASTMYO4physical
22084309
TPM2_YEASTTPM2physical
22615397
ATG17_YEASTATG17physical
22875988
MYO4_YEASTMYO4physical
24368805
SHE2_YEASTSHE2physical
25535369
MYO4_YEASTMYO4physical
25482893
RL22A_YEASTRPL22Agenetic
27708008
RV161_YEASTRVS161genetic
27708008
BUD31_YEASTBUD31genetic
27708008
VPS53_YEASTVPS53genetic
27708008
TOK1_YEASTTOK1genetic
27708008
CTK1_YEASTCTK1genetic
27708008
TAL1_YEASTTAL1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
GYP1_YEASTGYP1genetic
27708008
WDR6_YEASTRTT10genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHE3_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-28; SER-217; SER-343;SER-348; SER-361; THR-393 AND SER-394, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-394, ANDMASS 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-28, 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-343, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-394, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-123, AND MASSSPECTROMETRY.

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