NOP12_YEAST - dbPTM
NOP12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOP12_YEAST
UniProt AC Q08208
Protein Name Nucleolar protein 12
Gene Name NOP12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 459
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in pre-25S rRNA processing..
Protein Sequence MSSAIDNLFGNIDEKKIESSVDKLFSSSCGPINKLEVKSKTRTVLPDSKKRERAAEADQEEKEASKPDVSDEQTEEVALPKVKKAKKSKRNDEDEDLEARYYAKLLNEEAEAEDDKPTVTKTDETSVPLTSAAKKVDFKEDELEKAERTVFIGNILSTVITSKKVYKEFKKLFGTNPIAETEESGNEKEEESSKKSDNNEFAIESIRFRSISFDEALPRKVAFVQQKFHKSRDTINAYIVYKNKSAVRKICSNLNAVVFQDHHLRVDSVAHPAPHDKKRSIFVGNLDFEEIEESLWKHFEPCGDIEYVRIIRDSKTNMGKGFAYVQFKDLQSVNKALLLNEKPMKSQKQEDENTKKPTKKARKLRVSRCKNMKKGTTIGTGLDRNGLTDSQRTRAGRAKKILGKADRATLGQEITIEGLRAKKGEGSTHLKKKKQRSATGRVTKRSIAFKKAQAEKSKK
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
2Phosphorylation------MSSAIDNLF
------CCHHHHHHH
28.6030377154
3Phosphorylation-----MSSAIDNLFG
-----CCHHHHHHHC
28.1330377154
16AcetylationFGNIDEKKIESSVDK
HCCCCHHHHHHHHHH
50.0524489116
23AcetylationKIESSVDKLFSSSCG
HHHHHHHHHHHCCCC
49.6422865919
26PhosphorylationSSVDKLFSSSCGPIN
HHHHHHHHCCCCCCC
31.6030377154
27PhosphorylationSVDKLFSSSCGPINK
HHHHHHHCCCCCCCE
23.4730377154
28PhosphorylationVDKLFSSSCGPINKL
HHHHHHCCCCCCCEE
23.1530377154
34AcetylationSSCGPINKLEVKSKT
CCCCCCCEEEECCCC
46.9024489116
62AcetylationAEADQEEKEASKPDV
HHHHHHHHHHHCCCC
58.8024489116
65PhosphorylationDQEEKEASKPDVSDE
HHHHHHHHCCCCCHH
45.9022369663
70PhosphorylationEASKPDVSDEQTEEV
HHHCCCCCHHHHHHH
42.6922369663
74PhosphorylationPDVSDEQTEEVALPK
CCCCHHHHHHHHHHH
31.8725521595
104AcetylationLEARYYAKLLNEEAE
HHHHHHHHHHCHHHH
37.0724489116
116AcetylationEAEAEDDKPTVTKTD
HHHHCCCCCCCCCCC
55.7124489116
121AcetylationDDKPTVTKTDETSVP
CCCCCCCCCCCCCCC
50.0324489116
125PhosphorylationTVTKTDETSVPLTSA
CCCCCCCCCCCCCHH
37.5221440633
126PhosphorylationVTKTDETSVPLTSAA
CCCCCCCCCCCCHHH
21.4927214570
175PhosphorylationEFKKLFGTNPIAETE
HHHHHHCCCCCCCCC
30.4122890988
181PhosphorylationGTNPIAETEESGNEK
CCCCCCCCCCCCCHH
35.7125521595
184PhosphorylationPIAETEESGNEKEEE
CCCCCCCCCCHHHHH
40.4622369663
192PhosphorylationGNEKEEESSKKSDNN
CCHHHHHHHCCCCCC
51.2222369663
193PhosphorylationNEKEEESSKKSDNNE
CHHHHHHHCCCCCCC
47.5922369663
212PhosphorylationSIRFRSISFDEALPR
HEEEEECCCCHHHHH
28.0825752575
227AcetylationKVAFVQQKFHKSRDT
HHHHHHHHHHCCCCC
32.1424489116
252PhosphorylationSAVRKICSNLNAVVF
HHHHHHHHCCCCEEE
48.0728889911
342AcetylationKALLLNEKPMKSQKQ
HHHHHCCCCCCCCCC
49.7124489116
367PhosphorylationKARKLRVSRCKNMKK
HHHHHHHHHHCCCCC
26.0619795423
390PhosphorylationDRNGLTDSQRTRAGR
CCCCCCHHHHHHHHH
19.1423749301
404AcetylationRAKKILGKADRATLG
HHHHHHCCCCHHCCC
43.6025381059
427PhosphorylationRAKKGEGSTHLKKKK
HCCCCCCCCHHCHHH
14.3530377154
443PhosphorylationRSATGRVTKRSIAFK
CCCCCCCCHHHHHHH
21.2728889911

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 NOP12_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOP12_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 NOP12_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL8B_YEASTRPL8Bphysical
14759368
BRX1_YEASTBRX1physical
14759368
NOP12_YEASTNOP12physical
14759368
PWP1_YEASTPWP1physical
14759368
NOP2_YEASTNOP2genetic
11452019
RL15A_YEASTRPL15Aphysical
16429126
RL4B_YEASTRPL4Bphysical
16429126
RRP5_YEASTRRP5physical
16429126
HAS1_YEASTHAS1physical
16429126
RL7B_YEASTRPL7Bphysical
16429126
DBP3_YEASTDBP3genetic
19061648
AIR1_YEASTAIR1genetic
19061648
TMA23_YEASTTMA23genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
RRP8_YEASTRRP8genetic
19061648
RS8A_YEASTRPS8Agenetic
19061648
RS8B_YEASTRPS8Agenetic
19061648
MRM2_YEASTMRM2genetic
19061648
PSA3_YEASTPRE9genetic
19061648
IF2A_YEASTSUI2genetic
19061648
NMD5_YEASTNMD5genetic
19061648
LTV1_YEASTLTV1genetic
19061648
URB1_YEASTURB1genetic
19061648
MRT4_YEASTMRT4genetic
19061648
BUD21_YEASTBUD21genetic
19061648
UAF30_YEASTUAF30genetic
19061648
FKBP_YEASTFPR1genetic
19061648
YAJ9_YEASTYAR029Wgenetic
20093466
YBQ6_YEASTYBR056Wgenetic
20093466
YPT10_YEASTYPT10genetic
20093466
ELO2_YEASTELO2genetic
20093466
ODO2_YEASTKGD2genetic
20093466
FAR7_YEASTFAR7genetic
20093466
PIH1_YEASTPIH1genetic
20093466
SSF1_YEASTSSF1genetic
20093466
THP2_YEASTTHP2genetic
20093466
AIR1_YEASTAIR1genetic
20093466
MDV1_YEASTMDV1genetic
20093466
DPH4_YEASTJJJ3genetic
20093466
LTHAD_YEASTSRY1genetic
20093466
PXA2_YEASTPXA2genetic
20093466
GPT2_YEASTGPT2genetic
20093466
SRP40_YEASTSRP40genetic
20093466
RL8B_YEASTRPL8Bgenetic
20093466
GBLP_YEASTASC1genetic
20093466
TMA23_YEASTTMA23genetic
20093466
DYN3_YEASTDYN3genetic
20093466
ALG5_YEASTALG5genetic
20093466
TRE1_YEASTTRE1genetic
20093466
SRS2_YEASTSRS2genetic
21459050
NOP4_YEASTNOP4physical
25877921
LOC1_YEASTLOC1physical
25877921
EBP2_YEASTEBP2physical
25877921
NOP12_YEASTNOP12physical
25877921
ARP6_YEASTARP6genetic
27708008
ACE2_YEASTACE2genetic
27708008
MAK16_YEASTMAK16genetic
27708008
CDK1_YEASTCDC28genetic
27708008
MAK21_YEASTMAK21genetic
27708008
RRP1_YEASTRRP1genetic
27708008
ERF3_YEASTSUP35genetic
27708008
PESC_YEASTNOP7genetic
27708008
CDC12_YEASTCDC12genetic
27708008
NOP56_YEASTNOP56genetic
27708008
DBP9_YEASTDBP9genetic
27708008
RLP7_YEASTRLP7genetic
27708008
NOP2_YEASTNOP2genetic
27708008
DCP2_YEASTDCP2genetic
27708008
GRPE_YEASTMGE1genetic
27708008
DBP3_YEASTDBP3genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RL26B_YEASTRPL26Bgenetic
27708008
SSF1_YEASTSSF1genetic
27708008
AIR1_YEASTAIR1genetic
27708008
DBR1_YEASTDBR1genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
ERG3_YEASTERG3genetic
27708008
SIC1_YEASTSIC1genetic
27708008
GBLP_YEASTASC1genetic
27708008
TMA23_YEASTTMA23genetic
27708008
NOP4_YEASTNOP4physical
27077951

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOP12_YEAST

loading...

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-70; THR-181; SER-184;SER-192; SER-212 AND SER-252, 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-70 AND SER-184, 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-184, 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-70 AND SER-184, AND MASSSPECTROMETRY.

TOP