CNM67_YEAST - dbPTM
CNM67_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNM67_YEAST
UniProt AC P53865
Protein Name Chaotic nuclear migration protein 67
Gene Name CNM67
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 581
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
Protein Description Involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation. Required for the proper formation of the spindle pole body (SPB) outer plaque. May connect the outer plaque to the central plaque embedded in the nuclear envelope..
Protein Sequence MTDFDLMNFPFHERLDSPVSENGEIKDGEPIPQNWLNENHVGKSILPLFVNPEDVINCNFSNARDSYEENKSPSMDQMNYARNTSYQESPGLQERPKNEKDKSPIGTDVHKKDVPNFIHSTPRENSSKHFTRANEQASAQPTDEHTSPDISIEDCNGAKIFLQNSLSKEDFRMLENVILGYQKKVIELGRDNLRQEERANSLQKELEAATKSNDKTLDNKKKIEEQTVLIENLTKDLSLNKEMLEKANDTIQTKHTALLSLTDSLRKAELFEIPIGILFFDLYDSEENSSKLDHILQEKYPNIKGFLCASQQEELSRISQRFKNAKAEAEDLRNELENKKIEIQTMREKNNTLIGTNKTLSKQNKILCDKFDKLTIDEKEILKGCNEEIKIKLERLNERLGSWEKSKEKYETSLKDKEKMLADAEKKTNTLSKELDNLRSRFGNLEGNTSERITIKNILQSRPDISAEECNFLMVEQIDSANLTTLQNTVKEIVLAVGIPYPKLRRKIPLLAIKLKYENIMLSNFAQRLHRQVYSQEMNLKKFTDQAYYDFMSTRRMDSIDHHLERCLDHLYDHILEKMVK
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------MTDFDLMNF
------CCCCCCCCC		45.4319823750
17PhosphorylationPFHERLDSPVSENGE
CHHHCCCCCCCCCCC		31.6222369663
20PhosphorylationERLDSPVSENGEIKD
HCCCCCCCCCCCCCC		28.8222369663
61PhosphorylationDVINCNFSNARDSYE
HHCCCCCCCCCCCCC		18.6521440633
66PhosphorylationNFSNARDSYEENKSP
CCCCCCCCCCCCCCC		28.9629136822
67PhosphorylationFSNARDSYEENKSPS
CCCCCCCCCCCCCCC		31.3929136822
72PhosphorylationDSYEENKSPSMDQMN
CCCCCCCCCCHHHHH		33.5117563356
74PhosphorylationYEENKSPSMDQMNYA
CCCCCCCCHHHHHHH		41.9229136822
80PhosphorylationPSMDQMNYARNTSYQ
CCHHHHHHHHHCCCC		11.1221440633
84PhosphorylationQMNYARNTSYQESPG
HHHHHHHCCCCCCCC		24.2122369663
85PhosphorylationMNYARNTSYQESPGL
HHHHHHCCCCCCCCC		28.5022369663
86PhosphorylationNYARNTSYQESPGLQ
HHHHHCCCCCCCCCC		17.7922369663
89PhosphorylationRNTSYQESPGLQERP
HHCCCCCCCCCCCCC		14.5622369663
103PhosphorylationPKNEKDKSPIGTDVH
CCCCCCCCCCCCCCC		31.7019823750
107PhosphorylationKDKSPIGTDVHKKDV
CCCCCCCCCCCCCCC		35.2519795423
120PhosphorylationDVPNFIHSTPRENSS
CCCCCCCCCCCCCCC		34.9819823750
121PhosphorylationVPNFIHSTPRENSSK
CCCCCCCCCCCCCCH		16.5319823750
126PhosphorylationHSTPRENSSKHFTRA
CCCCCCCCCHHCHHH		35.6921440633
127PhosphorylationSTPRENSSKHFTRAN
CCCCCCCCHHCHHHH		41.5521700874
128AcetylationTPRENSSKHFTRANE
CCCCCCCHHCHHHHH		42.4323572591
138PhosphorylationTRANEQASAQPTDEH
HHHHHHHCCCCCCCC		27.4223749301
142PhosphorylationEQASAQPTDEHTSPD
HHHCCCCCCCCCCCC		41.7729136822
146PhosphorylationAQPTDEHTSPDISIE
CCCCCCCCCCCCCHH		39.6529136822
147PhosphorylationQPTDEHTSPDISIED
CCCCCCCCCCCCHHC		23.6029136822
151PhosphorylationEHTSPDISIEDCNGA
CCCCCCCCHHCCCCC		27.5729136822
168AcetylationFLQNSLSKEDFRMLE
EECCCCCHHHHHHHH		67.6024489116
210PhosphorylationQKELEAATKSNDKTL
HHHHHHHHHCCCCCC		41.8928889911
410PhosphorylationWEKSKEKYETSLKDK
HHHHHHHHHCCHHHH		26.0717287358
412PhosphorylationKSKEKYETSLKDKEK
HHHHHHHCCHHHHHH		35.9517287358
413PhosphorylationSKEKYETSLKDKEKM
HHHHHHCCHHHHHHH		22.8317287358
432PhosphorylationEKKTNTLSKELDNLR
HHHHHHHHHHHHHHH		23.2619779198
433AcetylationKKTNTLSKELDNLRS
HHHHHHHHHHHHHHH		66.4623572591
534PhosphorylationQRLHRQVYSQEMNLK
HHHHHHHHHCCCCHH		9.0421700874
544PhosphorylationEMNLKKFTDQAYYDF
CCCHHHHCHHHHHHH		35.7627017623
548PhosphorylationKKFTDQAYYDFMSTR
HHHCHHHHHHHHHCC		9.6427017623
549PhosphorylationKFTDQAYYDFMSTRR
HHCHHHHHHHHHCCC		13.0127017623
553PhosphorylationQAYYDFMSTRRMDSI
HHHHHHHHCCCCHHH		20.8227017623
554PhosphorylationAYYDFMSTRRMDSID
HHHHHHHCCCCHHHH		15.5427017623
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 CNM67_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNM67_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 CNM67_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFI1_YEASTAFI1physical
14515169
CNM67_YEASTCNM67physical
10339566
SPC42_YEASTSPC42physical
10339566
NUD1_YEASTNUD1physical
10339566
ADY4_YEASTADY4physical
12796288
MPC70_YEASTSPO21physical
11742972
MPC70_YEASTSPO21physical
10899120
CALM_YEASTCMD1physical
15872084
SPC29_YEASTSPC29physical
15872084
CDK1_YEASTCDC28physical
16580990
SPC42_YEASTSPC42physical
20826607
CNM67_YEASTCNM67physical
21454609
CG22_YEASTCLB2genetic
21321099
BFA1_YEASTBFA1genetic
21321099
CDC5_YEASTCDC5physical
15509790
CDC5_YEASTCDC5genetic
15509790
SWE1_YEASTSWE1genetic
15509790
KIN3_YEASTKIN3physical
22875988
LUC7_YEASTLUC7physical
22875988
NOT3_YEASTNOT3physical
22875988
NNF1_YEASTNNF1physical
22875988
HMS2_YEASTHMS2physical
22875988
FMP27_YEASTFMP27physical
22875988
MDM1_YEASTMDM1physical
22875988
STV1_YEASTSTV1physical
22875988
END3_YEASTEND3physical
22875988
AF9_YEASTYAF9physical
22875988
CTF19_YEASTCTF19physical
22875988
YP216_YEASTYPL216Wphysical
22875988
EAF7_YEASTEAF7physical
23572591
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNM67_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-17; SER-20; SER-72;SER-85 AND SER-89, 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-72 AND SER-89, 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-120; TYR-410; THR-412AND SER-413, 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-17 AND SER-20, AND MASSSPECTROMETRY.

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