MSC3_YEAST - dbPTM
MSC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSC3_YEAST
UniProt AC Q05812
Protein Name Meiotic sister-chromatid recombination protein 3
Gene Name MSC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 728
Subcellular Localization Cell membrane
Peripheral membrane protein . Cell periphery.
Protein Description May be involved in the control of meiotic sister-chromatid recombination..
Protein Sequence MVFGFTKRDRRVPDLSRYDYYYQNHEDYNKSPQLSAAAASAASAASPDRTNYSRSHSLVSHAPSIPRQRSSVKSPGRRLSTSSAAPPTSRAAAKQYSQKTYSLRSQRSGEYHLHPPGYTTNGSRMNSMTSGANVRRNYGKNKSTAGNNNDSRANSITVKTTQVTDPSGRTQSITKKTIRKINGYEYVETTTTTKNLVPLGDSQRHFDEFSENYMLQDDDILEEQASDNIHDIIEENETDNEKPYSPVSESHLQDDSELNVEKPDFPLGSYFHHKYSTDVMPLEEESSLSNFSDALDYIPPTHQTSSKYIHNKRKQASTTRRKKRPPAVKNAEAEAKKPLTEAEMYLKALEVAKRNVYHTDAASDNASAPLGSNKSRKSRMGQKMTLRSSSDSPTATANLVKSNVEVQPKRFTSSFFSRNTKSAPHEVHNHSVSTHFKSNKAVDPVPEPKSANTGLTDKEMYDQALKIAQARYYNSHGIQPEAVDNSTTAAKPRQVGVSHLGSTGSIPPNEQHYLGDSEIPVQSEVHEYEPIPLQKTKTTGSSKNKFKTMFDKVLQFSQENYGYQHKKEQGEQTPVTRNAEESFPAASISEGVTTAKPSSNEGVMTNPVVTDSPSPLQQQIDSTTASSNGQSQGNVPTSAVASTTRTRSPELQDNLKSSSSLLQDQTPQRQEDATDPTTSSTNELSAAEPTMVTSTHATKTIQAQTQDPPTKHKKSSFFTKLFKKKSSR
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
31PhosphorylationNHEDYNKSPQLSAAA
CCCHHCCCHHHHHHH
17.7824909858
35PhosphorylationYNKSPQLSAAAASAA
HCCCHHHHHHHHHHH
15.6019779198
40PhosphorylationQLSAAAASAASAASP
HHHHHHHHHHHHCCC
21.4619779198
43PhosphorylationAAAASAASAASPDRT
HHHHHHHHHCCCCCC
24.8819779198
46PhosphorylationASAASAASPDRTNYS
HHHHHHCCCCCCCCC
27.3528889911
50PhosphorylationSAASPDRTNYSRSHS
HHCCCCCCCCCCCCC
45.9823749301
52PhosphorylationASPDRTNYSRSHSLV
CCCCCCCCCCCCCHH
12.5927017623
53PhosphorylationSPDRTNYSRSHSLVS
CCCCCCCCCCCCHHH
29.4023749301
55PhosphorylationDRTNYSRSHSLVSHA
CCCCCCCCCCHHHCC
16.1022369663
57PhosphorylationTNYSRSHSLVSHAPS
CCCCCCCCHHHCCCC
31.5422369663
60PhosphorylationSRSHSLVSHAPSIPR
CCCCCHHHCCCCCCC
21.1622369663
64PhosphorylationSLVSHAPSIPRQRSS
CHHHCCCCCCCCCCC
46.1122369663
74PhosphorylationRQRSSVKSPGRRLST
CCCCCCCCCCCCCCC
30.3619823750
80PhosphorylationKSPGRRLSTSSAAPP
CCCCCCCCCCCCCCC
25.1622369663
81PhosphorylationSPGRRLSTSSAAPPT
CCCCCCCCCCCCCCC
31.1522369663
82PhosphorylationPGRRLSTSSAAPPTS
CCCCCCCCCCCCCCC
18.0122369663
83PhosphorylationGRRLSTSSAAPPTSR
CCCCCCCCCCCCCCH
28.6522369663
88PhosphorylationTSSAAPPTSRAAAKQ
CCCCCCCCCHHHHHH
29.7722890988
89PhosphorylationSSAAPPTSRAAAKQY
CCCCCCCCHHHHHHH
26.2022890988
99AcetylationAAKQYSQKTYSLRSQ
HHHHHCCCCCCCCCC
43.4122865919
100PhosphorylationAKQYSQKTYSLRSQR
HHHHCCCCCCCCCCC
15.6522369663
101PhosphorylationKQYSQKTYSLRSQRS
HHHCCCCCCCCCCCC
16.8522369663
102PhosphorylationQYSQKTYSLRSQRSG
HHCCCCCCCCCCCCC
23.6522369663
105PhosphorylationQKTYSLRSQRSGEYH
CCCCCCCCCCCCCCC
34.9322369663
108PhosphorylationYSLRSQRSGEYHLHP
CCCCCCCCCCCCCCC
28.4822369663
111PhosphorylationRSQRSGEYHLHPPGY
CCCCCCCCCCCCCCC
17.1323749301
118PhosphorylationYHLHPPGYTTNGSRM
CCCCCCCCCCCCCCC
19.0322369663
119PhosphorylationHLHPPGYTTNGSRMN
CCCCCCCCCCCCCCC
21.5022369663
120PhosphorylationLHPPGYTTNGSRMNS
CCCCCCCCCCCCCCC
29.1522369663
123PhosphorylationPGYTTNGSRMNSMTS
CCCCCCCCCCCCCCC
30.3522369663
127PhosphorylationTNGSRMNSMTSGANV
CCCCCCCCCCCCHHC
17.6922369663
129PhosphorylationGSRMNSMTSGANVRR
CCCCCCCCCCHHCHH
24.6722369663
130PhosphorylationSRMNSMTSGANVRRN
CCCCCCCCCHHCHHH
27.5422369663
143PhosphorylationRNYGKNKSTAGNNND
HHCCCCCCCCCCCCC
32.6522890988
144PhosphorylationNYGKNKSTAGNNNDS
HCCCCCCCCCCCCCH
39.9522890988
151PhosphorylationTAGNNNDSRANSITV
CCCCCCCHHCCEEEE
35.1022369663
155PhosphorylationNNDSRANSITVKTTQ
CCCHHCCEEEEEEEE
20.7422369663
157PhosphorylationDSRANSITVKTTQVT
CHHCCEEEEEEEEEE
18.7722890988
159UbiquitinationRANSITVKTTQVTDP
HCCEEEEEEEEEECC
36.8923749301
161PhosphorylationNSITVKTTQVTDPSG
CEEEEEEEEEECCCC
18.4821440633
164PhosphorylationTVKTTQVTDPSGRTQ
EEEEEEEECCCCCCE
32.1621440633
167PhosphorylationTTQVTDPSGRTQSIT
EEEEECCCCCCEEEE
43.6622369663
170PhosphorylationVTDPSGRTQSITKKT
EECCCCCCEEEEHHH
30.1422369663
172PhosphorylationDPSGRTQSITKKTIR
CCCCCCEEEEHHHHH
31.4522369663
174PhosphorylationSGRTQSITKKTIRKI
CCCCEEEEHHHHHHC
31.5620377248
180UbiquitinationITKKTIRKINGYEYV
EEHHHHHHCCCEEEE
36.3523749301
275PhosphorylationGSYFHHKYSTDVMPL
HHHCCCCCCCCCCCC
16.6721551504
286PhosphorylationVMPLEEESSLSNFSD
CCCCCCCHHCCCHHH
39.6020377248
287PhosphorylationMPLEEESSLSNFSDA
CCCCCCHHCCCHHHH
38.8121440633
289PhosphorylationLEEESSLSNFSDALD
CCCCHHCCCHHHHHH
37.4621440633
292PhosphorylationESSLSNFSDALDYIP
CHHCCCHHHHHHCCC
26.6521440633
357PhosphorylationEVAKRNVYHTDAASD
HHHHHHCCCCCCCCC
11.5329136822
359PhosphorylationAKRNVYHTDAASDNA
HHHHCCCCCCCCCCC
15.0529136822
363PhosphorylationVYHTDAASDNASAPL
CCCCCCCCCCCCCCC
32.8722369663
367PhosphorylationDAASDNASAPLGSNK
CCCCCCCCCCCCCCC
36.3522369663
372PhosphorylationNASAPLGSNKSRKSR
CCCCCCCCCCCHHCC
49.0921440633
378PhosphorylationGSNKSRKSRMGQKMT
CCCCCHHCCCCCCCE
26.7928889911
385PhosphorylationSRMGQKMTLRSSSDS
CCCCCCCEECCCCCC
26.5122369663
388PhosphorylationGQKMTLRSSSDSPTA
CCCCEECCCCCCCCH
36.9922890988
389PhosphorylationQKMTLRSSSDSPTAT
CCCEECCCCCCCCHH
31.5625521595
390PhosphorylationKMTLRSSSDSPTATA
CCEECCCCCCCCHHH
43.2725521595
392PhosphorylationTLRSSSDSPTATANL
EECCCCCCCCHHHHH
26.5422369663
394PhosphorylationRSSSDSPTATANLVK
CCCCCCCCHHHHHHH
40.3622890988
396PhosphorylationSSDSPTATANLVKSN
CCCCCCHHHHHHHCC
20.6822890988
413PhosphorylationVQPKRFTSSFFSRNT
ECCCCCCHHHHCCCC
23.5730377154
414PhosphorylationQPKRFTSSFFSRNTK
CCCCCCHHHHCCCCC
27.5330377154
458UbiquitinationANTGLTDKEMYDQAL
CCCCCCCHHHHHHHH
38.8623749301
466UbiquitinationEMYDQALKIAQARYY
HHHHHHHHHHHHHHH
38.7224961812
486PhosphorylationQPEAVDNSTTAAKPR
CHHHCCCCCCCCCCC
23.7519779198
487PhosphorylationPEAVDNSTTAAKPRQ
HHHCCCCCCCCCCCE
27.0619779198
491AcetylationDNSTTAAKPRQVGVS
CCCCCCCCCCEECCC
37.9624489116
491UbiquitinationDNSTTAAKPRQVGVS
CCCCCCCCCCEECCC
37.9623749301
503PhosphorylationGVSHLGSTGSIPPNE
CCCCCCCCCCCCCCC
32.9021551504
505PhosphorylationSHLGSTGSIPPNEQH
CCCCCCCCCCCCCCC
31.8220377248
566AcetylationENYGYQHKKEQGEQT
HHHCHHCCHHCCCCC
42.3424489116
573PhosphorylationKKEQGEQTPVTRNAE
CHHCCCCCCCCCCHH
18.5423749301
576PhosphorylationQGEQTPVTRNAEESF
CCCCCCCCCCHHHHC
21.2924961812
582PhosphorylationVTRNAEESFPAASIS
CCCCHHHHCCCCEEC
28.2124961812
587PhosphorylationEESFPAASISEGVTT
HHHCCCCEECCCCCC
28.8424909858
589PhosphorylationSFPAASISEGVTTAK
HCCCCEECCCCCCCC
26.2924909858
593PhosphorylationASISEGVTTAKPSSN
CEECCCCCCCCCCCC
31.7124961812
594PhosphorylationSISEGVTTAKPSSNE
EECCCCCCCCCCCCC
30.2224961812
646PhosphorylationAVASTTRTRSPELQD
HHHHCCCCCCHHHHH
33.1522369663
648PhosphorylationASTTRTRSPELQDNL
HHCCCCCCHHHHHHH
23.3222369663
657PhosphorylationELQDNLKSSSSLLQD
HHHHHHHCCHHHHCC
38.3222369663
658PhosphorylationLQDNLKSSSSLLQDQ
HHHHHHCCHHHHCCC
23.5122369663
659PhosphorylationQDNLKSSSSLLQDQT
HHHHHCCHHHHCCCC
31.9022369663
660PhosphorylationDNLKSSSSLLQDQTP
HHHHCCHHHHCCCCC
34.7422369663
666PhosphorylationSSLLQDQTPQRQEDA
HHHHCCCCCCCCCCC
29.6722890988
674PhosphorylationPQRQEDATDPTTSST
CCCCCCCCCCCCCCH
55.6322369663
677PhosphorylationQEDATDPTTSSTNEL
CCCCCCCCCCCHHHH
41.9620377248
678PhosphorylationEDATDPTTSSTNELS
CCCCCCCCCCHHHHC
26.5222369663
679PhosphorylationDATDPTTSSTNELSA
CCCCCCCCCHHHHCC
37.3322369663
680PhosphorylationATDPTTSSTNELSAA
CCCCCCCCHHHHCCC
32.9122369663
681PhosphorylationTDPTTSSTNELSAAE
CCCCCCCHHHHCCCC
32.2622369663
685PhosphorylationTSSTNELSAAEPTMV
CCCHHHHCCCCCEEE
21.1824909858
690PhosphorylationELSAAEPTMVTSTHA
HHCCCCCEEEEECCC
18.7722369663
693PhosphorylationAAEPTMVTSTHATKT
CCCCEEEEECCCCCE
19.6522369663
694PhosphorylationAEPTMVTSTHATKTI
CCCEEEEECCCCCEE
13.5422369663
695PhosphorylationEPTMVTSTHATKTIQ
CCEEEEECCCCCEEE
13.2322369663
698PhosphorylationMVTSTHATKTIQAQT
EEEECCCCCEEECCC
22.5522369663

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 MSC3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSC3_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 MSC3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSP1_YEASTLSP1physical
18719252

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSC3_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-390; THR-646; SER-648;SER-658; SER-659; SER-660 AND THR-681, 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-648 AND SER-679, 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-151; SER-155 ANDSER-172, 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-151; SER-155 ANDSER-363, 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-80, AND MASSSPECTROMETRY.

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