NUD1_YEAST - dbPTM
NUD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUD1_YEAST
UniProt AC P32336
Protein Name Protein NUD1
Gene Name NUD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 851
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Nucleus envelope . Localizes to the meiotic outer plaque of the SPB, at the end of the meiotic spindles.
Protein Description Involved in astral microtubule organization by binding SCP72 to the outer plaque in a cell-cycle dependent manner. Required for the mitotic exit by facilitating the binding of TEMP1 to CDC15. Also involved in the pathway that organizes the shaping and sizing of the prospore membrane (PSM) during sporulation..
Protein Sequence MDMDTQEAELSSQLENLTINSPRKLRSNAHSNSGKVFKEYESNHDFQDSNFTSQVVEPAISDSVKKPPTMTVLNNYSTVHQKVPSGFSGTTATSHQEAQWKQYFPGIGSGGGTNFGGAVGTANKVPESDLIVSDLVKDLSGVLETNTFKRHLDMKNKTTTMQTHENHDTISISHSKDFFNAEKVSSSFSDDSDSGPAAEAHDVFDGILQKQKSNYLVGSYPSNSNNKNNNNNNNNNNNNSININNKDNARTKEEDEEDTSNSFEFSSSSSMSSSQTQSGRKSKVLKKPPLNTISPGQLGYQFNHTHGAWDPPLNQGLDVSSSHSLDNTSSNQSQFATMVPTGDNHTNGKAPSILDKKAYELTSTKPGDVGYRQKKIQEEENLANSDDTPLDTPKFNDLFTKNGTRAKVKGQMRTSRSISNSNLLEAHKKLKTFPAERVEDITSISEVNTSFNETEKQLISILTSKLSGSPSYDSDWEKILKVDLSRGKLKNMFGMQRLLPNVLVLNLSDNEMNTLEGIPSNVVQLFCSNNKITSAHCSLAGFHDLECLDLSYNLLNTSLKFLSLCHHLQEVNLSYNSIQSLEGIGSSRMKKLNLSNNEINGIIDFEQLILTNNSVVGGWLTVEVLDLSNNNIIGVRNINCLPRLKVLNLNGNPLVSIVESSKMENGTLRALSIKNTGGALSKLQNYKLDDQFTFPYQNLKILKLDGFAQLSKWQKWPATLQILEINGGLASSLPRFSSLKSTNLYSLTIANVRDFTHLPVDLSKELPFLQELHLPGNNLQNAHKLTKTLPRQSVKFLDLRNNPITTPRHDRASTSLHYRQLLQLAGLCQQQCPALATLWLDDTPAPTATNL
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
11PhosphorylationDTQEAELSSQLENLT
HHHHHHHHHHHHHCC		13.9324961812
12PhosphorylationTQEAELSSQLENLTI
HHHHHHHHHHHHCCC		51.9524961812
18PhosphorylationSSQLENLTINSPRKL
HHHHHHCCCCCCHHH		29.6924961812
21PhosphorylationLENLTINSPRKLRSN
HHHCCCCCCHHHHCC		23.4128152593
33PhosphorylationRSNAHSNSGKVFKEY
HCCCCCCCCCCHHHH		42.9021700874
35AcetylationNAHSNSGKVFKEYES
CCCCCCCCCHHHHHC		44.3023572591
40PhosphorylationSGKVFKEYESNHDFQ
CCCCHHHHHCCCCCC		25.8321700874
42PhosphorylationKVFKEYESNHDFQDS
CCHHHHHCCCCCCCC		38.2621700874
49PhosphorylationSNHDFQDSNFTSQVV
CCCCCCCCCCHHCCC		24.0621700874
52PhosphorylationDFQDSNFTSQVVEPA
CCCCCCCHHCCCCCH		23.6221700874
53PhosphorylationFQDSNFTSQVVEPAI
CCCCCCHHCCCCCHH		19.4821700874
61PhosphorylationQVVEPAISDSVKKPP
CCCCCHHCCCCCCCC		26.4121700874
63PhosphorylationVEPAISDSVKKPPTM
CCCHHCCCCCCCCCE		29.1021700874
71PhosphorylationVKKPPTMTVLNNYST
CCCCCCEEEECCCCC		25.0721700874
76PhosphorylationTMTVLNNYSTVHQKV
CEEEECCCCCCEECC		12.4921700874
77PhosphorylationMTVLNNYSTVHQKVP
EEEECCCCCCEECCC		26.5221700874
78PhosphorylationTVLNNYSTVHQKVPS
EEECCCCCCEECCCC		16.2028889911
85PhosphorylationTVHQKVPSGFSGTTA
CCEECCCCCCCCCCC		56.3021700874
88PhosphorylationQKVPSGFSGTTATSH
ECCCCCCCCCCCCCC		38.4621700874
93PhosphorylationGFSGTTATSHQEAQW
CCCCCCCCCCCHHHH		25.3421440633
94PhosphorylationFSGTTATSHQEAQWK
CCCCCCCCCCHHHHH		22.2521440633
109PhosphorylationQYFPGIGSGGGTNFG
HHCCCCCCCCCCCCC		32.1321440633
133PhosphorylationPESDLIVSDLVKDLS
CHHHHHHHHHHHHHH		20.4521700874
140PhosphorylationSDLVKDLSGVLETNT
HHHHHHHHHHHHHCH		36.6719823750
145PhosphorylationDLSGVLETNTFKRHL
HHHHHHHHCHHHHHH		35.0823749301
147PhosphorylationSGVLETNTFKRHLDM
HHHHHHCHHHHHHCC		37.6423749301
149UbiquitinationVLETNTFKRHLDMKN
HHHHCHHHHHHCCCC		36.5523749301
169PhosphorylationQTHENHDTISISHSK
EEECCCCEEEEECCH		14.7421440633
171PhosphorylationHENHDTISISHSKDF
ECCCCEEEEECCHHC		21.8221440633
173PhosphorylationNHDTISISHSKDFFN
CCCEEEEECCHHCCC		18.2124961812
175PhosphorylationDTISISHSKDFFNAE
CEEEEECCHHCCCCH		27.4221440633
185PhosphorylationFFNAEKVSSSFSDDS
CCCCHHHHCCCCCCC		31.1919795423
186PhosphorylationFNAEKVSSSFSDDSD
CCCHHHHCCCCCCCC		38.0919795423
187PhosphorylationNAEKVSSSFSDDSDS
CCHHHHCCCCCCCCC		22.6619823750
189PhosphorylationEKVSSSFSDDSDSGP
HHHHCCCCCCCCCCC		42.3228152593
192PhosphorylationSSSFSDDSDSGPAAE
HCCCCCCCCCCCHHH		38.3719823750
194PhosphorylationSFSDDSDSGPAAEAH
CCCCCCCCCCHHHHH		51.1020377248
213PhosphorylationGILQKQKSNYLVGSY
HHHHHCCCCCCCCCC		28.3619823750
215PhosphorylationLQKQKSNYLVGSYPS
HHHCCCCCCCCCCCC		15.1721440633
219PhosphorylationKSNYLVGSYPSNSNN
CCCCCCCCCCCCCCC		26.7921700874
220PhosphorylationSNYLVGSYPSNSNNK
CCCCCCCCCCCCCCC		12.5419823750
222PhosphorylationYLVGSYPSNSNNKNN
CCCCCCCCCCCCCCC		44.6628152593
224PhosphorylationVGSYPSNSNNKNNNN
CCCCCCCCCCCCCCC		46.2321700874
240PhosphorylationNNNNNNNSININNKD
CCCCCCCCCCCCCCC		21.0922369663
246UbiquitinationNSININNKDNARTKE
CCCCCCCCCCCCCCC		48.1223749301
259PhosphorylationKEEDEEDTSNSFEFS
CCCCCCCCCCCEEEC		32.8421700874
262PhosphorylationDEEDTSNSFEFSSSS
CCCCCCCCEEECCCC		26.3921700874
267PhosphorylationSNSFEFSSSSSMSSS
CCCEEECCCCCCCCC		39.2921700874
357UbiquitinationAPSILDKKAYELTST
CCCHHHHHHHHCCCC		56.7323749301
359PhosphorylationSILDKKAYELTSTKP
CHHHHHHHHCCCCCC		21.9821700874
362PhosphorylationDKKAYELTSTKPGDV
HHHHHHCCCCCCCCC		23.5521440633
363PhosphorylationKKAYELTSTKPGDVG
HHHHHCCCCCCCCCC		47.2423749301
365UbiquitinationAYELTSTKPGDVGYR
HHHCCCCCCCCCCHH		46.9323749301
375UbiquitinationDVGYRQKKIQEEENL
CCCHHHHHHHHHHHH		41.0823749301
385PhosphorylationEEENLANSDDTPLDT
HHHHHCCCCCCCCCC		31.1221440633
388PhosphorylationNLANSDDTPLDTPKF
HHCCCCCCCCCCCCH		30.6420377248
392PhosphorylationSDDTPLDTPKFNDLF
CCCCCCCCCCHHHHC		35.7420377248
400PhosphorylationPKFNDLFTKNGTRAK
CCHHHHCCCCCCCCE		30.7828889911
404PhosphorylationDLFTKNGTRAKVKGQ
HHCCCCCCCCEEEEE		36.5321700874
414PhosphorylationKVKGQMRTSRSISNS
EEEEEECCCCCCCCC		24.1321440633
415PhosphorylationVKGQMRTSRSISNSN
EEEEECCCCCCCCCC		17.4221700874
417PhosphorylationGQMRTSRSISNSNLL
EEECCCCCCCCCCHH		30.0922369663
419PhosphorylationMRTSRSISNSNLLEA
ECCCCCCCCCCHHHH		35.1422369663
421PhosphorylationTSRSISNSNLLEAHK
CCCCCCCCCHHHHHH		23.2822890988
442PhosphorylationAERVEDITSISEVNT
HHHHCCCCCHHHCCC		32.1221700874
443PhosphorylationERVEDITSISEVNTS
HHHCCCCCHHHCCCC		25.1721700874
445PhosphorylationVEDITSISEVNTSFN
HCCCCCHHHCCCCCC		34.9523749301
449PhosphorylationTSISEVNTSFNETEK
CCHHHCCCCCCHHHH		39.6121700874
450PhosphorylationSISEVNTSFNETEKQ
CHHHCCCCCCHHHHH		22.3723749301
454PhosphorylationVNTSFNETEKQLISI
CCCCCCHHHHHHHHH		49.9721700874
460PhosphorylationETEKQLISILTSKLS
HHHHHHHHHHHHHCC		21.8221440633
467PhosphorylationSILTSKLSGSPSYDS
HHHHHHCCCCCCCCC		40.7521700874
469PhosphorylationLTSKLSGSPSYDSDW
HHHHCCCCCCCCCCH		13.8028152593
471PhosphorylationSKLSGSPSYDSDWEK
HHCCCCCCCCCCHHH		43.1821700874
667PhosphorylationSSKMENGTLRALSIK
CCCCCCCCEEEEEEE		25.3421700874
676PhosphorylationRALSIKNTGGALSKL
EEEEEECCCCHHHHH		31.8021700874
681PhosphorylationKNTGGALSKLQNYKL
ECCCCHHHHHHCCCC		30.6821700874
805PhosphorylationDLRNNPITTPRHDRA
ECCCCCCCCCCCCCC		31.8221700874
806PhosphorylationLRNNPITTPRHDRAS
CCCCCCCCCCCCCCC		21.0321700874
813PhosphorylationTPRHDRASTSLHYRQ
CCCCCCCCCHHHHHH		21.3021700874
815PhosphorylationRHDRASTSLHYRQLL
CCCCCCCHHHHHHHH		15.6221700874
843PhosphorylationATLWLDDTPAPTATN
HEEECCCCCCCCCCC		22.4821700874
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 NUD1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUD1_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 NUD1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNM67_YEASTCNM67physical
11101520
SPC72_YEASTSPC72physical
11101520
CNM67_YEASTCNM67physical
10339566
SP110_YEASTSPC110physical
10339566
SPC42_YEASTSPC42physical
10339566
SPC72_YEASTSPC72physical
10339566
NUD1_YEASTNUD1physical
10339566
ADY4_YEASTADY4physical
12796288
MPC70_YEASTSPO21physical
10899120
CDC14_YEASTCDC14genetic
11101520
SPO12_YEASTSPO12genetic
11101520
CDC15_YEASTCDC15genetic
11101520
CDC5_YEASTCDC5genetic
11101520
SIC1_YEASTSIC1genetic
11101520
CNM67_YEASTCNM67genetic
21321099
TEM1_YEASTTEM1genetic
21321099
DYHC_YEASTDYN1genetic
22385961
CG24_YEASTCLB4genetic
22385961
CDC5_YEASTCDC5physical
15509790
BFA1_YEASTBFA1physical
27159239
MOB1_YEASTMOB1physical
23579499
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUD1_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-419 AND SER-469, 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-417 AND SER-419, ANDMASS SPECTROMETRY.

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