ACM1_YEAST - dbPTM
ACM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACM1_YEAST
UniProt AC Q08981
Protein Name APC/C-CDH1 modulator 1
Gene Name ACM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 209
Subcellular Localization
Protein Description Negative regulator of GDH1, the activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C), and which is required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1..
Protein Sequence MISPSKKRTILSSKNINQKPRAVVKGNELRSPSKRRSQIDTDYALRRSPIKTIQISKAAQFMLYEETAEERNIAVHRHNEIYNNNNSVSNENNPSQVKENLSPAKICPYERAFLREGGRIALKDLSVDEFKGYIQDPLTDETIPLTLPLGDKKISLPSFITPPRNSKISIFFTSKHQGQNPETKISRSTDDVSEKKVVRKLSFHVYEDE
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
3Phosphorylation-----MISPSKKRTI
-----CCCHHHCCEE		23.0927717283
5Phosphorylation---MISPSKKRTILS
---CCCHHHCCEECC		43.9827738172
25UbiquitinationQKPRAVVKGNELRSP
CCCCEEECCCCCCCC		49.7923749301
31PhosphorylationVKGNELRSPSKRRSQ
ECCCCCCCCCHHHHH		46.2625752575
33PhosphorylationGNELRSPSKRRSQID
CCCCCCCCHHHHHCC		39.7919823750
37PhosphorylationRSPSKRRSQIDTDYA
CCCCHHHHHCCCCHH		35.2017287358
41PhosphorylationKRRSQIDTDYALRRS
HHHHHCCCCHHHHHC		32.3217287358
43PhosphorylationRSQIDTDYALRRSPI
HHHCCCCHHHHHCCC		15.0421440633
48PhosphorylationTDYALRRSPIKTIQI
CCHHHHHCCCCEEEC		25.2517287358
57UbiquitinationIKTIQISKAAQFMLY
CCEEECHHHHHHHHH		49.7417644757
87PhosphorylationEIYNNNNSVSNENNP
CHHCCCCCCCCCCCH		29.1023749301
89PhosphorylationYNNNNSVSNENNPSQ
HCCCCCCCCCCCHHH		37.9428889911
95PhosphorylationVSNENNPSQVKENLS
CCCCCCHHHHHHHCC		50.1323749301
102PhosphorylationSQVKENLSPAKICPY
HHHHHHCCHHHCCHH		34.1025752575
105UbiquitinationKENLSPAKICPYERA
HHHCCHHHCCHHHHH		48.5023749301
123AcetylationEGGRIALKDLSVDEF
CCCEEEEEECCHHHH		47.8324489116
126PhosphorylationRIALKDLSVDEFKGY
EEEEEECCHHHHCCC		37.3422369663
153UbiquitinationTLPLGDKKISLPSFI
EEECCCCEECCCCCC		42.1217644757
155PhosphorylationPLGDKKISLPSFITP
ECCCCEECCCCCCCC		43.0122369663
158PhosphorylationDKKISLPSFITPPRN
CCEECCCCCCCCCCC		34.2822369663
161PhosphorylationISLPSFITPPRNSKI
ECCCCCCCCCCCCCE		25.8222369663
166PhosphorylationFITPPRNSKISIFFT
CCCCCCCCCEEEEEE		32.4220377248
173PhosphorylationSKISIFFTSKHQGQN
CCEEEEEEECCCCCC		26.5628889911
174PhosphorylationKISIFFTSKHQGQNP
CEEEEEEECCCCCCC		24.0021440633
183PhosphorylationHQGQNPETKISRSTD
CCCCCCCCCCCCCCC		34.6328889911
186PhosphorylationQNPETKISRSTDDVS
CCCCCCCCCCCCCCC		23.0217563356
188PhosphorylationPETKISRSTDDVSEK
CCCCCCCCCCCCCHH		29.4217287358
189PhosphorylationETKISRSTDDVSEKK
CCCCCCCCCCCCHHH		34.8017563356
193PhosphorylationSRSTDDVSEKKVVRK
CCCCCCCCHHHHHHE		51.1727717283
202PhosphorylationKKVVRKLSFHVYEDE
HHHHHEEEEEEECCC		19.1522369663
206PhosphorylationRKLSFHVYEDE----
HEEEEEEECCC----		14.7522369663
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
-KUbiquitinationE3 ubiquitin ligaseCDC20P26309
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseCDH1P53197
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACM1_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 ACM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDH1_YEASTCDH1physical
17178718
BMH1_YEASTBMH1physical
17178718
CDC14_YEASTCDC14physical
18287090
CDH1_YEASTCDH1physical
18498748
CDC5_YEASTCDC5genetic
18500339
CDH1_YEASTCDH1genetic
18500339
BMH2_YEASTBMH2physical
18719252
RDS1_YEASTRDS1physical
18719252
CDH1_YEASTCDH1physical
21460798
CDH1_YEASTCDH1genetic
22189709
HSL1_YEASTHSL1genetic
22189709
CDH1_YEASTCDH1physical
23049888
YAJ9_YEASTYAR029Wgenetic
27708008
CCZ1_YEASTCCZ1genetic
27708008
ICS2_YEASTICS2genetic
27708008
THRC_YEASTTHR4genetic
27708008
H2A1_YEASTHTA1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
TFS2_YEASTDST1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
ELP2_YEASTELP2genetic
27708008
AIM18_YEASTAIM18genetic
27708008
GSH1_YEASTGSH1genetic
27708008
ELM1_YEASTELM1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
UPS1_YEASTUPS1genetic
27708008
COA4_YEASTCOA4genetic
27708008
SEI1_YEASTFLD1genetic
27708008
PET8_YEASTPET8genetic
27708008
EAF7_YEASTEAF7genetic
27708008
PT127_YEASTPET127genetic
27708008
DIA2_YEASTDIA2genetic
27708008
HAP5_YEASTHAP5genetic
27708008
FRE3_YEASTFRE3genetic
27708008
1433E_HUMANYWHAEphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACM1_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-126; THR-161; SER-188AND SER-202, 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 THR-161; SER-186 ANDTHR-189, AND MASS 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-37; THR-41; SER-48;THR-161; SER-188 AND SER-202, AND MASS 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-202, AND MASSSPECTROMETRY.

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