STE50_YEAST - dbPTM
STE50_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STE50_YEAST
UniProt AC P25344
Protein Name Protein STE50
Gene Name STE50
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 346
Subcellular Localization
Protein Description Involved in growth arrest during conjugation. May interact with the G protein alpha subunit..
Protein Sequence MEDGKQAINEGSNDASPDLDVNGTILMNNEDFSQWSVDDVITWCISTLEVEETDPLCQRLRENDIVGDLLPELCLQDCQDLCDGDLNKAIKFKILINKMRDSKLEWKDDKTQEDMITVLKNLYTTTSAKLQEFQSQYTRLRMDVLDVMKTSSSSSPINTHGVSTTVPSSNNTIIPSSDGVSLSQTDYFDTVHNRQSPSRRESPVTVFRQPSLSHSKSLHKDSKNKVPQISTNQSHPSAVSTANTPGPSPNEALKQLRASKEDSCERILKNAMKRHNLADQDWRQYVLVICYGDQERLLELNEKPVIIFKNLKQQGLHPAIMLRRRGDFEEVAMMNGSDNVTPGGRL
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
42PhosphorylationWSVDDVITWCISTLE
CCHHHHHHHHHHHCC		17.7114555477
126PhosphorylationLKNLYTTTSAKLQEF
HHHHHHHCHHHHHHH		20.9121440633
127PhosphorylationKNLYTTTSAKLQEFQ
HHHHHHCHHHHHHHH		22.7021440633
138PhosphorylationQEFQSQYTRLRMDVL
HHHHHHHHHHHHHHH		18.6521551504
150PhosphorylationDVLDVMKTSSSSSPI
HHHHHHHCCCCCCCC		18.7521440633
154PhosphorylationVMKTSSSSSPINTHG
HHHCCCCCCCCCCCC		41.9219779198
155PhosphorylationMKTSSSSSPINTHGV
HHCCCCCCCCCCCCC		31.5728889911
159PhosphorylationSSSSPINTHGVSTTV
CCCCCCCCCCCCCEE		22.2619779198
163PhosphorylationPINTHGVSTTVPSSN
CCCCCCCCCEECCCC		23.9730377154
196PhosphorylationDTVHNRQSPSRRESP
CCCCCCCCCCCCCCC		22.9328889911
202PhosphorylationQSPSRRESPVTVFRQ
CCCCCCCCCEEEEEC		23.9022369663
205PhosphorylationSRRESPVTVFRQPSL
CCCCCCEEEEECCCC		19.8128132839
211PhosphorylationVTVFRQPSLSHSKSL
EEEEECCCCCCCCCC		33.8822369663
213PhosphorylationVFRQPSLSHSKSLHK
EEECCCCCCCCCCCC		30.0121440633
215PhosphorylationRQPSLSHSKSLHKDS
ECCCCCCCCCCCCCC		22.1422369663
230PhosphorylationKNKVPQISTNQSHPS
CCCCCCCCCCCCCCC		18.9623749301
231PhosphorylationNKVPQISTNQSHPSA
CCCCCCCCCCCCCCC		38.6219823750
234PhosphorylationPQISTNQSHPSAVST
CCCCCCCCCCCCCCC		39.1619823750
237PhosphorylationSTNQSHPSAVSTANT
CCCCCCCCCCCCCCC		35.5624961812
240PhosphorylationQSHPSAVSTANTPGP
CCCCCCCCCCCCCCC		22.8619684113
241PhosphorylationSHPSAVSTANTPGPS
CCCCCCCCCCCCCCC		19.8224603354
244PhosphorylationSAVSTANTPGPSPNE
CCCCCCCCCCCCHHH		27.4517330950
248PhosphorylationTANTPGPSPNEALKQ
CCCCCCCCHHHHHHH		46.3917330950
303AcetylationRLLELNEKPVIIFKN
HHHHHCCCCEEEEEC		43.4424489116
309AcetylationEKPVIIFKNLKQQGL
CCCEEEEECHHHCCC		51.4624489116
312UbiquitinationVIIFKNLKQQGLHPA
EEEEECHHHCCCCHH		50.3923749301
337PhosphorylationEVAMMNGSDNVTPGG
HHHCCCCCCCCCCCC		22.4722369663
341PhosphorylationMNGSDNVTPGGRL--
CCCCCCCCCCCCC--		23.5922369663
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
42TPhosphorylationKinaseYCK1P23291
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STE50_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 STE50_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STE11_YEASTSTE11physical
9738877
STE11_YEASTSTE11physical
10397774
STE11_YEASTSTE11physical
11370856
STE50_YEASTSTE50physical
11370856
STE11_YEASTSTE11physical
9742096
STE11_YEASTSTE11physical
9148934
GBB_YEASTSTE4physical
9148934
STE11_YEASTSTE11physical
8793874
GBB_YEASTSTE4physical
8793874
STE11_YEASTSTE11physical
14573615
STE11_YEASTSTE11physical
15544813
STE11_YEASTSTE11physical
15689513
STE5_YEASTSTE5physical
8816472
STE11_YEASTSTE11physical
8816472
STE11_YEASTSTE11physical
9636180
STE5_YEASTSTE5physical
9636180
STE11_YEASTSTE11genetic
10397774
SSK2_YEASTSSK2genetic
9742096
SSK22_YEASTSSK22genetic
9742096
MBA1_YEASTMBA1physical
16554755
ARI1_YEASTARI1physical
16554755
STE11_YEASTSTE11physical
16429126
CDC42_YEASTCDC42physical
16428446
SHO1_YEASTSHO1physical
16778768
CDC42_YEASTCDC42genetic
16778768
STE11_YEASTSTE11physical
11283351
ATG17_YEASTATG17physical
11283351
PDE2_YEASTPDE2genetic
17318632
STE11_YEASTSTE11genetic
9738877
STE50_YEASTSTE50physical
18431466
TPS1_YEASTTPS1genetic
19269370
FNTB_YEASTRAM1genetic
19269370
PTP3_YEASTPTP3genetic
19269370
STE20_YEASTSTE20genetic
19269370
KHSE_YEASTTHR1genetic
19269370
PVH1_YEASTYVH1genetic
19269370
PRR1_YEASTPRR1genetic
19269370
ATG17_YEASTATG17genetic
19269370
NPR1_YEASTNPR1genetic
19269370
6P22_YEASTPFK27genetic
19269370
CET1_YEASTCET1genetic
19269370
PLC1_YEASTPLC1genetic
19269370
RHO5_YEASTRHO5genetic
18621925
OPY2_YEASTOPY2physical
19846660
OPY2_YEASTOPY2physical
19369942
OPY2_YEASTOPY2physical
20932477
STE11_YEASTSTE11physical
20932477
PTP2_YEASTPTP2genetic
20932477
MSB2_YEASTMSB2genetic
20932477
HKR1_YEASTHKR1genetic
20932477
RCK2_YEASTRCK2genetic
22242015
OPY2_YEASTOPY2physical
22904036
HSP71_YEASTSSA1physical
22875988
QDR3_YEASTQDR3physical
22875988
MUM2_YEASTMUM2physical
22875988
AKL1_YEASTAKL1physical
22875988
SGF29_YEASTSGF29physical
22875988
VAM6_YEASTVAM6physical
22875988
NOP14_YEASTNOP14physical
22875988
SCC2_YEASTSCC2physical
22875988
IVY1_YEASTIVY1physical
22875988
NACB2_YEASTBTT1physical
22875988
YAP6_YEASTYAP6physical
22875988
SP110_YEASTSPC110physical
22875988
LRS4_YEASTLRS4physical
22875988
TLG1_YEASTTLG1physical
22875988
PSP1_YEASTPSP1physical
22875988
VAB2_YEASTVAB2physical
22875988
SPC25_YEASTSPC25physical
22875988
VAM7_YEASTVAM7physical
22875988
SYV_YEASTVAS1physical
22875988
CCM1_YEASTCCM1physical
22875988
KEL2_YEASTKEL2physical
22875988
MGA1_YEASTMGA1physical
22875988
TBP7_YEASTYTA7physical
22875988
MYO1_YEASTMYO1physical
22875988
LAM4_YEASTYHR080Cphysical
22875988
MSH1_YEASTMSH1physical
22875988
SKN7_YEASTSKN7physical
22875988
MPS3_YEASTMPS3physical
22875988
VPS53_YEASTVPS53physical
22875988
PFD1_YEASTPFD1physical
22875988
LAA1_YEASTLAA1physical
22875988
RE107_YEASTREC107physical
22875988
EAF6_YEASTEAF6physical
22875988
ATP7_YEASTATP7physical
22875988
YKF0_YEASTYKL050Cphysical
22875988
HSK3_YEASTHSK3physical
22875988
EBP2_YEASTEBP2physical
22875988
DYHC_YEASTDYN1physical
22875988
DAD2_YEASTDAD2physical
22875988
HSP72_YEASTSSA2physical
22875988
SED5_YEASTSED5physical
22875988
BOS1_YEASTBOS1physical
22875988
VTA1_YEASTVTA1physical
22875988
ENT2_YEASTENT2physical
22875988
NKP2_YEASTNKP2physical
22875988
ATG17_YEASTATG17physical
22875988
RCF1_YEASTRCF1physical
22875988
MDM1_YEASTMDM1physical
22875988
FAR3_YEASTFAR3physical
22875988
VPS20_YEASTVPS20physical
22875988
SPC24_YEASTSPC24physical
22875988
CBF3B_YEASTCEP3physical
22875988
END3_YEASTEND3physical
22875988
CBK1_YEASTCBK1physical
22875988
RM50_YEASTMRPL50physical
22875988
CTR9_YEASTCTR9physical
22875988
YO223_YEASTDSC3physical
22875988
SNF2_YEASTSNF2physical
22875988
YO304_YEASTBIL1physical
22875988
SCD5_YEASTSCD5physical
22875988
SKS1_YEASTSKS1physical
22875988
LGE1_YEASTLGE1physical
22875988
TBP6_YEASTYTA6physical
22875988
GCR1_YEASTGCR1physical
22875988
ATPF_YEASTATP4physical
22875988
SPC29_YEASTSPC29physical
22875988
NIP80_YEASTNIP100physical
22875988
GYP5_YEASTGYP5physical
22875988
MCM16_YEASTMCM16physical
22875988
STE11_YEASTSTE11physical
23658712
STE50_YEASTSTE50physical
8816472
SHO1_YEASTSHO1physical
25898136
STE11_YEASTSTE11physical
25898136
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STE50_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-202 AND SER-248, ANDMASS 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-202, 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-202 AND SER-248, ANDMASS SPECTROMETRY.

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