SST2_YEAST - dbPTM
SST2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SST2_YEAST
UniProt AC P11972
Protein Name Protein SST2
Gene Name SST2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 698
Subcellular Localization
Protein Description Desensitization to alpha-factor pheromone. Is involved in regulating the signaling pathway for responding to mating pheromone..
Protein Sequence MVDKNRTLHELSSKNFSRTPNGLIFTNDLKTVYSIFLICLDLKEKKHSSDTKSFLLTAFTKHFHFTFTYQEAIKAMGQLELKVDMNTTCINVSYNIKPSLARHLLTLFMSSKLLHTPQDRTRGEPKEKVLFQPTPKGVAVLQKYVRDIGLKTMPDILLSSFNSMKLFTFERSSVTDSIIHSDYLIHILFIKMMGAKPNVWSPTNADDPLPCLSSLLEYTNNDDTFTFEKSKPEQGWQAQIGNIDINDLERVSPLAHRFFTNPDSESHTQYYVSNAGIRLFENKTFGTSKKIVIKYTFTTKAIWQWIMDCTDIMHVKEAVSLAALFLKTGLIVPVLLQPSRTDKKKFQISRSSFFTLSKRGWDLVSWTGCKSNNIRAPNGSTIDLDFTLRGHMTVRDEKKTLDDSEGFSQDMLISSSNLNKLDYVLTDPGMRYLFRRHLEKELCVENLDVFIEIKRFLKKMTILKKLIDSKHCDKKSNTSTSKNNIVKTIDSALMKQANECLEMAYHIYSSYIMIGSPYQLNIHHNLRQNISDIMLHPHSPLSEHFPTNLYDPSPASAESAASSISSTEADTLGEPPEVSLKPSKNLSNENCSFKKQGFKHQLKEYKPAPLTLAETHSPNASVENSHTIVRYGMDNTQNDTKSVESFPATLKVLRKLYPLFEIVSNEMYRLMNNDSFQKFTQSDVYKDASALIEIQEKC
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
88PhosphorylationLKVDMNTTCINVSYN
EEEECCCEEEEEEEE		13.3428889911
93PhosphorylationNTTCINVSYNIKPSL
CCEEEEEEEECCHHH		14.1528889911
143AcetylationKGVAVLQKYVRDIGL
CHHHHHHHHHHHCCC		41.3624489116
252PhosphorylationINDLERVSPLAHRFF
HHHHHHHCCCCCCCC		22.0317330950
260PhosphorylationPLAHRFFTNPDSESH
CCCCCCCCCCCCCCC		43.0330377154
380PhosphorylationNIRAPNGSTIDLDFT
CEECCCCCEEECEEE		28.9122369663
381PhosphorylationIRAPNGSTIDLDFTL
EECCCCCEEECEEEE		21.6529734811
400PhosphorylationTVRDEKKTLDDSEGF
EECCCCCCCCCCCCC		46.6230377154
404PhosphorylationEKKTLDDSEGFSQDM
CCCCCCCCCCCCHHH		39.0130377154
408PhosphorylationLDDSEGFSQDMLISS
CCCCCCCCHHHEECC		35.8128889911
414PhosphorylationFSQDMLISSSNLNKL
CCHHHEECCCCCCCC		24.6130377154
479PhosphorylationCDKKSNTSTSKNNIV
CCCCCCCCCCCHHHH		34.6323749301
487AcetylationTSKNNIVKTIDSALM
CCCHHHHHHHHHHHH		35.6524489116
539PhosphorylationDIMLHPHSPLSEHFP
HHHCCCCCCHHHCCC		31.8015924435
587PhosphorylationLKPSKNLSNENCSFK
CCCCCCCCCCCCCCH		52.0322369663
592PhosphorylationNLSNENCSFKKQGFK
CCCCCCCCCHHCCHH		52.2422369663
611PhosphorylationEYKPAPLTLAETHSP
HCCCCCCEEEECCCC		23.9028152593
615PhosphorylationAPLTLAETHSPNASV
CCCEEEECCCCCCCC		23.2617330950
617PhosphorylationLTLAETHSPNASVEN
CEEEECCCCCCCCCC		27.5417330950
621PhosphorylationETHSPNASVENSHTI
ECCCCCCCCCCCCEE		36.2817330950
625PhosphorylationPNASVENSHTIVRYG
CCCCCCCCCEEEEEC		14.4321440633
627PhosphorylationASVENSHTIVRYGMD
CCCCCCCEEEEECCC		22.4624961812
657PhosphorylationLKVLRKLYPLFEIVS
HHHHHHHHHHHHHHC		10.8321551504
664PhosphorylationYPLFEIVSNEMYRLM
HHHHHHHCHHHHHHH		32.5021551504
675PhosphorylationYRLMNNDSFQKFTQS
HHHHCCHHHHHHCHH		31.5330377154
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
539SPhosphorylationKinaseMAPK-FAMILY-GPS
539SPhosphorylationKinaseMAPK-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SST2_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 SST2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPT5_YEASTMPT5physical
9154842
BNR1_YEASTBNR1physical
11940600
IKS1_YEASTIKS1physical
11940600
KEL1_YEASTKEL1physical
11940600
KSS1_YEASTKSS1physical
11940600
MVP1_YEASTMVP1physical
11940600
NBP1_YEASTNBP1physical
11940600
PEP12_YEASTPEP12physical
11940600
SHO1_YEASTSHO1physical
11940600
TLG2_YEASTTLG2physical
11940600
VPS36_YEASTVPS36physical
11940600
YD180_YEASTYDL180Wphysical
11940600
YD186_YEASTYDL186Wphysical
11940600
YFT2_YEASTYFT2physical
11940600
YIP1_YEASTYIP1physical
11940600
YMD8_YEASTYMD8physical
11940600
MPT5_YEASTMPT5physical
11779797
GPA1_YEASTGPA1physical
10705368
GPA1_YEASTGPA1physical
9537998
GPA1_YEASTGPA1physical
9488712
GPA1_YEASTGPA1physical
8756677
CSN10_YEASTRRI2genetic
12446563
CSN9_YEASTCSN9genetic
12446563
CSI1_YEASTCSI1genetic
12446563
KSS1_YEASTKSS1genetic
2673544
STE50_YEASTSTE50genetic
1494345
YEC5_YEASTYEL025Cphysical
16554755
TBA1_YEASTTUB1physical
16554755
EGT2_YEASTEGT2physical
16554755
GCN20_YEASTGCN20physical
16429126
GFA1_YEASTGFA1physical
16429126
YHI0_YEASTYHR020Wphysical
16429126
KEL1_YEASTKEL1physical
18719252
SSB1_YEASTSSB1physical
19536198
NPC1_YEASTNCR1genetic
19547744
GPX2_YEASTGPX2genetic
20093466
VBA2_YEASTVBA2genetic
20093466
KAR4_YEASTKAR4genetic
20093466
SNT1_YEASTSNT1genetic
20093466
RL35A_YEASTRPL35Agenetic
20093466
RL35B_YEASTRPL35Agenetic
20093466
STF1_YEASTSTF1genetic
20093466
RPN4_YEASTRPN4genetic
20093466
TMS1_YEASTTMS1genetic
20093466
TRM1_YEASTTRM1genetic
20093466
SWM1_YEASTSWM1genetic
20093466
SSD1_YEASTSSD1genetic
20093466
MSN5_YEASTMSN5genetic
20093466
LSM6_YEASTLSM6genetic
20093466
LCMT1_YEASTPPM1genetic
20093466
EMI2_YEASTEMI2genetic
20093466
AK_YEASTHOM3genetic
20093466
UBP3_YEASTUBP3genetic
20093466
SPT2_YEASTSPT2genetic
20093466
BCK2_YEASTBCK2genetic
20093466
RT31_YEASTYMR31genetic
20093466
SHE10_YEASTSHE10genetic
20093466
HOS2_YEASTHOS2genetic
20093466
YG036_YEASTYGL036Wgenetic
20093466
KSS1_YEASTKSS1genetic
20093466
TRS65_YEASTTRS65genetic
20093466
PSD2_YEASTPSD2genetic
20093466
YOR1_YEASTYOR1genetic
20093466
SNF6_YEASTSNF6genetic
20093466
TCD1_YEASTTCD1genetic
20093466
INM1_YEASTINM1genetic
20093466
PEX18_YEASTPEX18genetic
20093466
AP18A_YEASTYAP1801genetic
20093466
PBS2_YEASTPBS2genetic
20093466
STE24_YEASTSTE24genetic
20093466
FRMSR_YEASTYKL069Wgenetic
20093466
VPS24_YEASTVPS24genetic
20093466
TCD2_YEASTTCD2genetic
20093466
TOF2_YEASTTOF2genetic
20093466
SA190_YEASTSAP190genetic
20093466
UTH1_YEASTUTH1genetic
20093466
GLG1_YEASTGLG1genetic
20093466
ALAM_YEASTALT1genetic
20093466
HOG1_YEASTHOG1genetic
20093466
VTA1_YEASTVTA1genetic
20093466
NKP2_YEASTNKP2genetic
20093466
NUP2_YEASTNUP2genetic
20093466
SUB1_YEASTSUB1genetic
20093466
MOT3_YEASTMOT3genetic
20093466
GBLP_YEASTASC1genetic
20093466
HLJ1_YEASTHLJ1genetic
20093466
BCH1_YEASTBCH1genetic
20093466
SCS7_YEASTSCS7genetic
20093466
LSM7_YEASTLSM7genetic
20093466
MEP2_YEASTMEP2genetic
20093466
FKBP_YEASTFPR1genetic
20093466
MSG5_YEASTMSG5genetic
20093466
SSK2_YEASTSSK2genetic
20093466
BRE5_YEASTBRE5genetic
20093466
TOP1_YEASTTOP1genetic
20093466
CSK2C_YEASTCKB2genetic
20093466
LEU9_YEASTLEU9genetic
20093466
MCP1_YEASTMCP1genetic
20093466
KAR9_YEASTKAR9genetic
20093466
EAF3_YEASTEAF3genetic
20093466
YOP1_YEASTYOP1genetic
20093466
YP098_YEASTYPR098Cgenetic
20093466
GPA1_YEASTGPA1genetic
7791771
VPS27_YEASTVPS27genetic
20526336
VPS4_YEASTVPS4genetic
20526336
GPA1_YEASTGPA1genetic
3113738
POG1_YEASTPOG1genetic
9927449
CSN5_YEASTRRI1genetic
12446563
CSN12_YEASTYJR084Wgenetic
12446563
PBS2_YEASTPBS2genetic
22282571
HOG1_YEASTHOG1genetic
22282571
SSK2_YEASTSSK2genetic
22282571
ROD1_YEASTROD1genetic
24820415
ROG3_YEASTROG3genetic
24820415
KASH5_HUMANCCDC155physical
27107014
CEP55_HUMANCEP55physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SST2_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-380; SER-408; SER-539;SER-587; SER-592 AND SER-617, 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-587, 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-252 AND SER-587, ANDMASS SPECTROMETRY.
"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-380; SER-587 ANDSER-592, AND MASS SPECTROMETRY.
"Feedback phosphorylation of an RGS protein by MAP kinase in yeast.";
Garrison T.R., Zhang Y., Pausch M., Apanovitch D., Aebersold R.,Dohlman H.G.;
J. Biol. Chem. 274:36387-36391(1999).
Cited for: PHOSPHORYLATION AT SER-539.

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