SHE2_YEAST - dbPTM
SHE2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHE2_YEAST
UniProt AC P36068
Protein Name SWI5-dependent HO expression protein 2
Gene Name SHE2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 246
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and cytoplasm and is exported in an mRNA-dependent manner (PubMed:12499354, PubMed:14561888) (PubMed:18566598). The presence in the nucleus is essential for PUF6 and LOC1 to bind the ASH1 mRNA.
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. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA..
Protein Sequence MSKDKDIKVTPGTCELVEQILALLSRYLSSYIHVLNKFISHLRRVATLRFERTTLIKFVKKLRFYNDCVLSYNASEFINEGKNELDPEADSFDKVILPIASMFVKCVETFDLLNYYLTQSLQKEILSKTLNEDLTLTAESILAIDDTYNHFVKFSQWMIESLRIGSNLLDLEVVQFAIKCADEDGTNIGETDNIFLQEILPVNSEEEFQTLSAAWHSILDGKLSALDEEFDVVATKWHDKFGKLKN
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
27PhosphorylationILALLSRYLSSYIHV
HHHHHHHHHHHHHHH		13.9424930733
29PhosphorylationALLSRYLSSYIHVLN
HHHHHHHHHHHHHHH		16.5024930733
30PhosphorylationLLSRYLSSYIHVLNK
HHHHHHHHHHHHHHH		26.0524930733
31PhosphorylationLSRYLSSYIHVLNKF
HHHHHHHHHHHHHHH		7.5324930733
109PhosphorylationMFVKCVETFDLLNYY
HHHHHHHHHHHHHHH		11.3130377154
115PhosphorylationETFDLLNYYLTQSLQ
HHHHHHHHHHHHHHH		10.3827017623
166PhosphorylationIESLRIGSNLLDLEV
HHHCCCCCCCCCHHH		23.1817563356
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 SHE2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHE2_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 SHE2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHE3_YEASTSHE3physical
11101531
SHE3_YEASTSHE3physical
11032818
ASH1_YEASTASH1physical
10792032
SHE2_YEASTSHE2physical
15537539
MYO4_YEASTMYO4physical
16429126
IMDH4_YEASTIMD4physical
16429126
SHE3_YEASTSHE3physical
14561888
ASH1_YEASTASH1physical
14561888
IST2_YEASTIST2physical
14561888
ASH1_YEASTASH1physical
17339339
SRO7_YEASTSRO7physical
17339339
SRO77_YEASTSRO77physical
17339339
SEC4_YEASTSEC4physical
17339339
CDC42_YEASTCDC42physical
17339339
EXO84_YEASTEXO84physical
17339339
SEC1_YEASTSEC1physical
17339339
SEC3_YEASTSEC3physical
17339339
RHO3_YEASTRHO3physical
17339339
SHE2_YEASTSHE2physical
17922018
SHE3_YEASTSHE3physical
17922018
MYO4_YEASTMYO4physical
17922018
MYO2_YEASTMYO2physical
17922018
ACT_YEASTACT1physical
17922018
ERG2_YEASTERG2physical
17922018
PRY2_YEASTPRY2physical
17922018
ASH1_YEASTASH1physical
17922018
SRL1_YEASTSRL1physical
17922018
AIM34_YEASTAIM34physical
17922018
YSP2_YEASTYSP2physical
17922018
PFD3_YEASTPAC10physical
17922018
WSC2_YEASTWSC2physical
17922018
MMR1_YEASTMMR1physical
17922018
BUD8_YEASTBUD8physical
17922018
GPP1_YEASTGPP1physical
17922018
CG22_YEASTCLB2physical
17922018
NTF2_YEASTNTF2physical
17922018
PMT2_YEASTPMT2physical
17922018
ACBP_YEASTACB1physical
17922018
MID2_YEASTMID2physical
17922018
IST2_YEASTIST2physical
17922018
SUI1_YEASTSUI1physical
17922018
YL413_YEASTINA1physical
17922018
TCB2_YEASTTCB2physical
17922018
CYS3_YEASTCYS3physical
17922018
CBPS_YEASTCPS1physical
17922018
LCB1_YEASTLCB1physical
17922018
C1TC_YEASTADE3physical
17922018
TAM41_YEASTTAM41physical
17922018
IRC8_YEASTIRC8physical
17922018
TKT1_YEASTTKL1physical
17922018
SCY1_YEASTSCY1physical
17922018
EF3A_YEASTYEF3physical
17922018
SUN4_YEASTSUN4physical
17922018
DHAS_YEASTHOM2physical
17922018
CIS3_YEASTCIS3physical
17922018
PRY1_YEASTPRY1physical
17922018
SYFA_YEASTFRS2physical
17922018
MAK21_YEASTMAK21physical
17922018
SYNC_YEASTDED81physical
17922018
EF1G2_YEASTTEF4physical
17922018
YL179_YEASTYLR179Cphysical
17922018
STM1_YEASTSTM1physical
17922018
ASH1_YEASTASH1physical
15537539
ASH1_YEASTASH1physical
18791219
IF4F1_YEASTTIF4631genetic
19061648
ASH1_YEASTASH1physical
18566598
SHE3_YEASTSHE3physical
19429778
ASH1_YEASTASH1physical
19429778
SHE2_YEASTSHE2physical
19710186
SHE3_YEASTSHE3physical
19710186
IMA1_YEASTSRP1physical
19244342
ASH1_YEASTASH1physical
19244342
SHE2_YEASTSHE2physical
20457760
ASH1_YEASTASH1physical
20844764
RPB1_YEASTRPO21physical
20713510
MYO4_YEASTMYO4physical
22084309
SHE3_YEASTSHE3physical
22084309
STE7_YEASTSTE7physical
22832273
FUS3_YEASTFUS3physical
22832273
KAR3_YEASTKAR3physical
22832273
PUF2_YEASTPUF2genetic
23904265
INV2_YEASTSUC2physical
23904265
ASH1_YEASTASH1physical
23904265
SC61A_YEASTSEC61physical
24056370
ASH1_YEASTASH1physical
24445806
LOC1_YEASTLOC1physical
25013181
PUF6_YEASTPUF6physical
25013181
MIM1_YEASTMIM1physical
23959800
ASH1_YEASTASH1physical
24368805
LOC1_YEASTLOC1physical
24324176
ASH1_YEASTASH1physical
24324176
SHE3_YEASTSHE3physical
25535369
MYO4_YEASTMYO4physical
25482893
SHE3_YEASTSHE3physical
25482893
SHE3_YEASTSHE3physical
28092367
ASH1_YEASTASH1physical
28092367
ASH1_YEASTASH1physical
25306441
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SHE2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-166, AND MASSSPECTROMETRY.

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