MPP10_YEAST - dbPTM
MPP10_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP10_YEAST
UniProt AC P47083
Protein Name U3 small nucleolar RNA-associated protein MPP10
Gene Name MPP10
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 593
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA. Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing..
Protein Sequence MSELFGVLKSNAGRIILKDPSATSKDVKAYIDSVINTCKNGSITKKAELDEITVDGLDANQVWWQVKLVLDSIDGDLIQGIQELKDVVTPSHNLSDGSTLNSSSGEESELEEAESVFKEKQMLSADVSEIEEQSNDSLSENDEEPSMDDEKTSAEAAREEFAEEKRISSGQDERHSSPDPYGINDKFFDLEKFNRDTLAAEDSNEASEGSEDEDIDYFQDMPSDDEEEEAIYYEDFFDKPTKEPVKKHSDVKDPKEDEELDEEEHDSAMDKVKLDLFADEEDEPNAEGVGEASDKNLSSFEKQQIEIRKQIEQLENEAVAEKKWSLKGEVKAKDRPEDALLTEELEFDRTAKPVPVITSEVTESLEDMIRRRIQDSNFDDLQRRTLLDITRKSQRPQFELSDVKSSKSLAEIYEDDYTRAEDESALSEELQKAHSEISELYANLVYKLDVLSSVHFVPKPASTSLEIRVETPTISMEDAQPLYMSNASSLAPQEIYNVGKAEKDGEIRLKNGVAMSKEELTREDKNRLRRALKRKRSKANLPNVNKRSKRNDVVDTLSKAKNITVINQKGEKKDVSGKTKKSRSGPDSTNIKL
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------MSELFGVLK
------CCHHHHHHH		42.9022814378
18AcetylationNAGRIILKDPSATSK
CCCCEEECCCCCCCH		58.1322865919
98PhosphorylationSHNLSDGSTLNSSSG
CCCCCCCCCCCCCCC		34.4119795423
99PhosphorylationHNLSDGSTLNSSSGE
CCCCCCCCCCCCCCC		35.1719795423
102PhosphorylationSDGSTLNSSSGEESE
CCCCCCCCCCCCHHH		29.0621440633
103PhosphorylationDGSTLNSSSGEESEL
CCCCCCCCCCCHHHH		41.0920377248
104PhosphorylationGSTLNSSSGEESELE
CCCCCCCCCCHHHHH		50.4720377248
108PhosphorylationNSSSGEESELEEAES
CCCCCCHHHHHHHHH		43.0820377248
124PhosphorylationFKEKQMLSADVSEIE
HHHHHHHHCCHHHHH		19.6521440633
146PhosphorylationSENDEEPSMDDEKTS
CCCCCCCCCCHHHHH		37.8221440633
152PhosphorylationPSMDDEKTSAEAARE
CCCCHHHHHHHHHHH		30.9929136822
153PhosphorylationSMDDEKTSAEAAREE
CCCHHHHHHHHHHHH		34.8729136822
168PhosphorylationFAEEKRISSGQDERH
HHHHHCCCCCCCCCC		32.2322369663
169PhosphorylationAEEKRISSGQDERHS
HHHHCCCCCCCCCCC		37.7922369663
176PhosphorylationSGQDERHSSPDPYGI
CCCCCCCCCCCCCCC		50.1922369663
177PhosphorylationGQDERHSSPDPYGIN
CCCCCCCCCCCCCCC		27.4822369663
181PhosphorylationRHSSPDPYGINDKFF
CCCCCCCCCCCHHHC		37.7122369663
186AcetylationDPYGINDKFFDLEKF
CCCCCCHHHCCHHHH		43.3624489116
192AcetylationDKFFDLEKFNRDTLA
HHHCCHHHHCHHHCC		56.0624489116
267PhosphorylationLDEEEHDSAMDKVKL
CCHHHHHHHHHHHHH		27.6625521595
293PhosphorylationAEGVGEASDKNLSSF
CCCCCCCCCCCCHHH		44.8328889911
295AcetylationGVGEASDKNLSSFEK
CCCCCCCCCCHHHHH		58.2424489116
298PhosphorylationEASDKNLSSFEKQQI
CCCCCCCHHHHHHHH		42.2328889911
299PhosphorylationASDKNLSSFEKQQIE
CCCCCCHHHHHHHHH		40.3625752575
309AcetylationKQQIEIRKQIEQLEN
HHHHHHHHHHHHHHH		62.3824489116
322AcetylationENEAVAEKKWSLKGE
HHHHHHHHCCCCCCE		50.2122865919
333AcetylationLKGEVKAKDRPEDAL
CCCEECCCCCCCCCC		48.8624489116
401PhosphorylationQRPQFELSDVKSSKS
CCCCCCHHHCCCCHH		32.9121440633
405PhosphorylationFELSDVKSSKSLAEI
CCHHHCCCCHHHHHH		42.7327017623
406PhosphorylationELSDVKSSKSLAEIY
CHHHCCCCHHHHHHH		22.1321440633
407AcetylationLSDVKSSKSLAEIYE
HHHCCCCHHHHHHHH		57.4925381059
408PhosphorylationSDVKSSKSLAEIYED
HHCCCCHHHHHHHHC		34.4622369663
413PhosphorylationSKSLAEIYEDDYTRA
CHHHHHHHHCCCCHH		12.5722369663
427PhosphorylationAEDESALSEELQKAH
HHCHHHHHHHHHHHH		28.8328889911
435PhosphorylationEELQKAHSEISELYA
HHHHHHHHHHHHHHH		41.2930377154
438PhosphorylationQKAHSEISELYANLV
HHHHHHHHHHHHHHH		19.9330377154
453PhosphorylationYKLDVLSSVHFVPKP
HHHHHCEEEEEECCC		18.5630377154
464PhosphorylationVPKPASTSLEIRVET
ECCCCCCCEEEEEEC		22.8530377154
471PhosphorylationSLEIRVETPTISMED
CEEEEEECCCCCHHH		23.9127214570
473PhosphorylationEIRVETPTISMEDAQ
EEEEECCCCCHHHCC		32.8627214570
503AcetylationYNVGKAEKDGEIRLK
HCCCCCCCCCCEEEE		75.7325381059
516PhosphorylationLKNGVAMSKEELTRE
EECCEECCHHHHCHH		27.4630377154
537PhosphorylationRALKRKRSKANLPNV
HHHHHHHHHCCCCCC		38.8730377154
556PhosphorylationKRNDVVDTLSKAKNI
HCCCHHHHHHHHCCE		22.7119779198
576PhosphorylationKGEKKDVSGKTKKSR
CCCEECCCCCCCCCC		44.7127017623
579PhosphorylationKKDVSGKTKKSRSGP
EECCCCCCCCCCCCC		47.4327017623
589PhosphorylationSRSGPDSTNIKL---
CCCCCCCCCCCC---		48.6321440633
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 MPP10_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP10_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 MPP10_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMP3_YEASTIMP3physical
10409734
IMP4_YEASTIMP4physical
10409734
UTP18_YEASTUTP18physical
15590835
NOC4_YEASTNOC4physical
15590835
UTP20_YEASTUTP20physical
15590835
UTP21_YEASTUTP21physical
15590835
UTP22_YEASTUTP22physical
15590835
NEP1_YEASTEMG1physical
15590835
KRR1_YEASTKRR1physical
15590835
UTP23_YEASTUTP23physical
16769905
FCF1_YEASTFCF1physical
16769905
PEX5_YEASTPEX5genetic
20093466
RT103_YEASTRTT103genetic
20093466
ASK10_YEASTASK10genetic
20093466
REE1_YEASTREE1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
ELF1_YEASTELF1genetic
20093466
SIC1_YEASTSIC1genetic
20093466
RAS2_YEASTRAS2genetic
20093466
FABD_YEASTMCT1genetic
20093466
YP089_YEASTYPR089Wgenetic
20093466
SAS10_YEASTSAS10physical
20884785
UTP8_YEASTUTP8physical
20884785
UTP18_YEASTUTP18physical
20884785
RRP9_YEASTRRP9physical
20884785
NOL10_YEASTENP2physical
24357410
BFR2_YEASTBFR2physical
24357410
FCF1_YEASTFCF1genetic
27708008
UTP6_YEASTUTP6genetic
27708008
GBP2_YEASTGBP2genetic
27708008
BIK1_YEASTBIK1genetic
27708008
NAA38_YEASTMAK31genetic
27708008
NOP6_YEASTNOP6genetic
27708008
HBS1_YEASTHBS1genetic
27708008
CMS1_YEASTCMS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MPP10_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-176; SER-177; SER-293AND SER-299, 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-176 AND SER-177, 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-168; SER-176 ANDSER-177, 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-176 AND SER-177, ANDMASS SPECTROMETRY.

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