STM1_YEAST - dbPTM
STM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STM1_YEAST
UniProt AC P39015
Protein Name Suppressor protein STM1
Gene Name STM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 273
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, perinuclear region. Concentrated in the perinuclear region.
Protein Description Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death..
Protein Sequence MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA
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
2Acetylation------MSNPFDLLG
------CCCHHHHCC		53.89-
2Phosphorylation------MSNPFDLLG
------CCCHHHHCC		53.8922369663
23SuccinylationDVVVLPPKEIVKSNT
CEEEECHHHHHCCCC		59.1223954790
27SuccinylationLPPKEIVKSNTSSKK
ECHHHHHCCCCCCCC		43.5823954790
27AcetylationLPPKEIVKSNTSSKK
ECHHHHHCCCCCCCC		43.5825381059
272-HydroxyisobutyrylationLPPKEIVKSNTSSKK
ECHHHHHCCCCCCCC		43.58-
28PhosphorylationPPKEIVKSNTSSKKA
CHHHHHCCCCCCCCC		34.1523749301
30PhosphorylationKEIVKSNTSSKKADV
HHHHCCCCCCCCCCC		41.2821440633
31PhosphorylationEIVKSNTSSKKADVP
HHHCCCCCCCCCCCC		44.4028889911
32PhosphorylationIVKSNTSSKKADVPP
HHCCCCCCCCCCCCC		35.8228889911
34UbiquitinationKSNTSSKKADVPPPS
CCCCCCCCCCCCCCC		52.3323749301
41PhosphorylationKADVPPPSADPSKAR
CCCCCCCCCCHHHHH		51.5921440633
45PhosphorylationPPPSADPSKARKNRP
CCCCCCHHHHHCCCC		39.2223749301
46UbiquitinationPPSADPSKARKNRPR
CCCCCHHHHHCCCCC		58.5622106047
46AcetylationPPSADPSKARKNRPR
CCCCCHHHHHCCCCC		58.5624489116
49UbiquitinationADPSKARKNRPRPSG
CCHHHHHCCCCCCCC		63.2717644757
55PhosphorylationRKNRPRPSGNEGAIR
HCCCCCCCCCCCCCC		56.3722369663
73PhosphorylationAGRRNNRSKDVTDSA
CCCCCCCCCCCCCCC		35.0221082442
74AcetylationGRRNNRSKDVTDSAT
CCCCCCCCCCCCCCC		53.6424489116
742-HydroxyisobutyrylationGRRNNRSKDVTDSAT
CCCCCCCCCCCCCCC		53.64-
74UbiquitinationGRRNNRSKDVTDSAT
CCCCCCCCCCCCCCC		53.6423749301
77PhosphorylationNNRSKDVTDSATTKK
CCCCCCCCCCCCCCC		34.0828889911
79PhosphorylationRSKDVTDSATTKKSN
CCCCCCCCCCCCCCC		20.3928889911
81PhosphorylationKDVTDSATTKKSNTR
CCCCCCCCCCCCCCC		43.0028889911
82PhosphorylationDVTDSATTKKSNTRR
CCCCCCCCCCCCCCC		35.8728889911
83AcetylationVTDSATTKKSNTRRA
CCCCCCCCCCCCCCC		50.2624489116
83SuccinylationVTDSATTKKSNTRRA
CCCCCCCCCCCCCCC		50.2623954790
85PhosphorylationDSATTKKSNTRRATD
CCCCCCCCCCCCCHH		45.0127017623
114AcetylationNQGWGDDKKELSAEK
HCCCCCCHHHHCHHH		53.5424489116
115AcetylationQGWGDDKKELSAEKE
CCCCCCHHHHCHHHH		71.5224489116
118PhosphorylationGDDKKELSAEKEAQA
CCCHHHHCHHHHHHH		35.1617330950
121AcetylationKKELSAEKEAQADAA
HHHHCHHHHHHHHHH		59.0524489116
121UbiquitinationKKELSAEKEAQADAA
HHHHCHHHHHHHHHH		59.0524961812
121SuccinylationKKELSAEKEAQADAA
HHHHCHHHHHHHHHH		59.0523954790
143UbiquitinationAEAEDAGKPKTAQLS
HHHHHCCCCCEEHHH		45.0924961812
143AcetylationAEAEDAGKPKTAQLS
HHHHHCCCCCEEHHH		45.0924489116
145UbiquitinationAEDAGKPKTAQLSLQ
HHHCCCCCEEHHHHH		61.0424961812
146PhosphorylationEDAGKPKTAQLSLQD
HHCCCCCEEHHHHHH		28.3221440633
150PhosphorylationKPKTAQLSLQDYLNQ
CCCEEHHHHHHHHHH		16.3528889911
154PhosphorylationAQLSLQDYLNQQANN
EHHHHHHHHHHHHHH		8.4519779198
165AcetylationQANNQFNKVPEAKKV
HHHHCCCCCCHHHCC		61.5324489116
165UbiquitinationQANNQFNKVPEAKKV
HHHHCCCCCCHHHCC		61.5323749301
1702-HydroxyisobutyrylationFNKVPEAKKVELDAE
CCCCCHHHCCCCCHH		56.54-
170AcetylationFNKVPEAKKVELDAE
CCCCCHHHCCCCCHH		56.5424489116
170UbiquitinationFNKVPEAKKVELDAE
CCCCCHHHCCCCCHH		56.5422817900
171AcetylationNKVPEAKKVELDAER
CCCCHHHCCCCCHHH		48.2522865919
171UbiquitinationNKVPEAKKVELDAER
CCCCHHHCCCCCHHH		48.2523749301
181PhosphorylationLDAERIETAEKEAYV
CCHHHHHHHHHHHCC		37.4320377248
184AcetylationERIETAEKEAYVPAT
HHHHHHHHHHCCCCH		45.2224489116
184UbiquitinationERIETAEKEAYVPAT
HHHHHHHHHHCCCCH		45.2223749301
1842-HydroxyisobutyrylationERIETAEKEAYVPAT
HHHHHHHHHHCCCCH		45.22-
192UbiquitinationEAYVPATKVKNVKSK
HHCCCCHHCCCCCCC		54.0023749301
1922-HydroxyisobutyrylationEAYVPATKVKNVKSK
HHCCCCHHCCCCCCC		54.00-
192AcetylationEAYVPATKVKNVKSK
HHCCCCHHCCCCCCC		54.0025381059
2202-HydroxyisobutyrylationFVESNTRKNFGDRNN
EECCCCCCCCCCCCC		55.37-
229PhosphorylationFGDRNNNSRNNFNNR
CCCCCCCCCCCCCCC		38.2122369663
244UbiquitinationRGGRGARKGNNTANA
CCCCCCCCCCCCCCC		66.5123749301
248PhosphorylationGARKGNNTANATNSA
CCCCCCCCCCCCCCC		25.8622369663
252PhosphorylationGNNTANATNSANTVQ
CCCCCCCCCCCCHHH		29.5222369663
254PhosphorylationNTANATNSANTVQKN
CCCCCCCCCCHHHHC		20.6725521595
257PhosphorylationNATNSANTVQKNRNI
CCCCCCCHHHHCCCC		24.8322369663
260AcetylationNSANTVQKNRNIDVS
CCCCHHHHCCCCCHH		54.2425381059
260UbiquitinationNSANTVQKNRNIDVS
CCCCHHHHCCCCCHH		54.2423749301
267PhosphorylationKNRNIDVSNLPSLA-
HCCCCCHHHCCCCC-		28.9721440633
271PhosphorylationIDVSNLPSLA-----
CCHHHCCCCC-----		39.8421440633
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 STM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STM1_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 STM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ETT1_YEASTETT1physical
15044472
RLA0_YEASTRPP0physical
15044472
RL5_YEASTRPL5physical
15044472
RS2_YEASTRPS2physical
15044472
RS3_YEASTRPS3physical
15044472
RL10_YEASTRPL10physical
15044472
RL16A_YEASTRPL16Aphysical
15044472
YKT6_YEASTYKT6physical
15044472
RL17A_YEASTRPL17Aphysical
15044472
RL25_YEASTRPL25physical
15044472
RL27A_YEASTRPL27Aphysical
15044472
RS26A_YEASTRPS26Aphysical
15044472
EF3A_YEASTYEF3genetic
19666721
PIF1_YEASTPIF1genetic
19704012
GPR1_YEASTGPR1genetic
27708008
LSM6_YEASTLSM6genetic
27708008
MRM2_YEASTMRM2genetic
27708008
PEF1_YEASTPEF1genetic
27708008
OSH3_YEASTOSH3genetic
27708008
SNX4_YEASTSNX4genetic
27708008
MNS1_YEASTMNS1genetic
27708008
COG8_YEASTCOG8genetic
27708008
IRA2_YEASTIRA2genetic
27708008
NAT5_YEASTNAT5genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
ATC3_YEASTDRS2genetic
27708008
SLA1_YEASTSLA1genetic
27708008
HAP3_YEASTHAP3genetic
27708008
AIM4_YEASTAIM4genetic
27708008
SNF5_YEASTSNF5genetic
27708008
BUD31_YEASTBUD31genetic
27708008
MTU1_YEASTSLM3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
RM01_YEASTMRPL1genetic
27708008
RV167_YEASTRVS167genetic
27708008
VPS60_YEASTVPS60genetic
27708008
PEX14_YEASTPEX14genetic
27708008
ATG1_YEASTATG1genetic
27708008
RTG2_YEASTRTG2genetic
27708008
SPR3_YEASTSPR3genetic
27708008
SLX9_YEASTSLX9genetic
27708008
DBF2_YEASTDBF2genetic
27708008
PTH_YEASTPTH1genetic
27708008
YIH7_YEASTYIL077Cgenetic
27708008
VPS53_YEASTVPS53genetic
27708008
SIP4_YEASTSIP4genetic
27708008
ASF1_YEASTASF1genetic
27708008
RPA34_YEASTRPA34genetic
27708008
YJ00_YEASTYJR030Cgenetic
27708008
HOC1_YEASTHOC1genetic
27708008
YJ85_YEASTYJR115Wgenetic
27708008
YJ94_YEASTYJR124Cgenetic
27708008
BLI1_YEASTBLI1genetic
27708008
SA190_YEASTSAP190genetic
27708008
MTD1_YEASTMTD1genetic
27708008
VPS38_YEASTVPS38genetic
27708008
CDC73_YEASTCDC73genetic
27708008
NU188_YEASTNUP188genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MOT3_YEASTMOT3genetic
27708008
CRZ1_YEASTCRZ1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
HOL1_YEASTHOL1genetic
27708008
TLG2_YEASTTLG2genetic
27708008
RTG1_YEASTRTG1genetic
27708008
EXO1_YEASTEXO1genetic
27708008
VPS21_YEASTVPS21genetic
27708008
IES4_YEASTIES4genetic
27708008
TEA1_YEASTTEA1genetic
27708008
LGE1_YEASTLGE1genetic
27708008
AIM44_YEASTAIM44genetic
27708008
CUP9_YEASTCUP9genetic
27708008
NEW1_YEASTNEW1genetic
27708008
UBA3_YEASTUBA3genetic
27708008
VPS4_YEASTVPS4genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STM1_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-73 AND SER-118, AND MASSSPECTROMETRY.
"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-73 AND SER-118, 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 SER-55; THR-181 AND SER-229,AND MASS SPECTROMETRY.
"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-118, AND MASSSPECTROMETRY.

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