NDD1_YEAST - dbPTM
NDD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NDD1_YEAST
UniProt AC Q08887
Protein Name Nuclear division defective protein 1
Gene Name NDD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 554
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Transcription activator involved in G2/M transcription through its association with FKH2..
Protein Sequence MDRDISYQQNYTSTGATATSSRQPSTDNNADTNFLKVMSEFKYNFNSPLPTTTQFPTPYSSNQYQQTQDHFANTDAHNSSSNESSLVENSILPHHQQIQQQQQQQQQQQQQQQALGSLVPPAVTRTDTSETLDDINVQPSSVLQFGNSLPSEFLVASPEQFKEFLLDSPSTNFNFFHKTPAKTPLRFVTDSNGAQQSTTENPGQQQNVFSNVDLNNLLKSNGKTPSSSCTGAFSRTPLSKIDMNLMFNQPLPTSPSKRFSSLSLTPYGRKILNDVGTPYAKALISSNSALVDFQKARKDITTNATSIGLENANNILQRTPLRSNNKKLFIKTPQDTINSTSTLTKDNENKQDIYGSSPTTIQLNSSITKSISKLDNSRIPLLASRSDNILDSNVDDQLFDLGLTRLPLSPTPNCNSLHSTTTGTSALQIPELPKMGSFRSDTGINPISSSNTVSFKSKSGNNNSKGRIKKNGKKPSKFQIIVANIDQFNQDTSSSSLSSSLNASSSAGNSNSNVTKKRASKLKRSQSLLSDSGSKSQARKSCNSKSNGNLFNSQ
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
25PhosphorylationATSSRQPSTDNNADT
CCCCCCCCCCCCCCC		39.8023810556
85PhosphorylationNSSSNESSLVENSIL
CCCCCHHHHHHCCCH		30.2028889911
168PhosphorylationFKEFLLDSPSTNFNF
HHHHHHCCCCCCCCC		22.2528132839
179PhosphorylationNFNFFHKTPAKTPLR
CCCCCCCCCCCCCEE		21.6521440633
224PhosphorylationLLKSNGKTPSSSCTG
HHHHCCCCCCCCCCC		29.7823749301
227PhosphorylationSNGKTPSSSCTGAFS
HCCCCCCCCCCCCCC		30.5428889911
253PhosphorylationMFNQPLPTSPSKRFS
HCCCCCCCCCCHHCC		62.0428132839
254PhosphorylationFNQPLPTSPSKRFSS
CCCCCCCCCCHHCCC		25.8228152593
256PhosphorylationQPLPTSPSKRFSSLS
CCCCCCCCHHCCCCC		35.9121440633
257UbiquitinationPLPTSPSKRFSSLSL
CCCCCCCHHCCCCCC		61.9323749301
263PhosphorylationSKRFSSLSLTPYGRK
CHHCCCCCCCHHHHH		31.9521440633
265PhosphorylationRFSSLSLTPYGRKIL
HCCCCCCCHHHHHHH		15.8728889911
267PhosphorylationSSLSLTPYGRKILND
CCCCCCHHHHHHHHC		25.0727017623
277PhosphorylationKILNDVGTPYAKALI
HHHHCCCCHHHHHHH		16.9928889911
279PhosphorylationLNDVGTPYAKALISS
HHCCCCHHHHHHHHC		22.1421440633
298UbiquitinationVDFQKARKDITTNAT
CCHHHHHCCCCCCCH		59.3417644757
301PhosphorylationQKARKDITTNATSIG
HHHHCCCCCCCHHHC		24.9122369663
302PhosphorylationKARKDITTNATSIGL
HHHCCCCCCCHHHCH		24.1622369663
305PhosphorylationKDITTNATSIGLENA
CCCCCCCHHHCHHHH		23.9722369663
306PhosphorylationDITTNATSIGLENAN
CCCCCCHHHCHHHHH		16.5522369663
319PhosphorylationANNILQRTPLRSNNK
HHHHHHHCCCCCCCC		17.4522369663
323PhosphorylationLQRTPLRSNNKKLFI
HHHCCCCCCCCEEEE		53.0624961812
331UbiquitinationNNKKLFIKTPQDTIN
CCCEEEEECCCHHCC		46.9817644757
332PhosphorylationNKKLFIKTPQDTINS
CCEEEEECCCHHCCC		22.7425752575
339PhosphorylationTPQDTINSTSTLTKD
CCCHHCCCCCCCCCC		21.6427017623
342PhosphorylationDTINSTSTLTKDNEN
HHCCCCCCCCCCCCC		38.2427017623
344PhosphorylationINSTSTLTKDNENKQ
CCCCCCCCCCCCCCC		36.1227017623
345UbiquitinationNSTSTLTKDNENKQD
CCCCCCCCCCCCCCC		62.7617644757
356PhosphorylationNKQDIYGSSPTTIQL
CCCCCCCCCCCEEEE		19.0327017623
357PhosphorylationKQDIYGSSPTTIQLN
CCCCCCCCCCEEEEC		23.1523749301
359PhosphorylationDIYGSSPTTIQLNSS
CCCCCCCCEEEECCH		38.1823810556
365PhosphorylationPTTIQLNSSITKSIS
CCEEEECCHHHHHHH		31.5427017623
370PhosphorylationLNSSITKSISKLDNS
ECCHHHHHHHHHCCC		24.3628889911
384PhosphorylationSRIPLLASRSDNILD
CCCCEEECCCCCCCC		32.0827017623
386PhosphorylationIPLLASRSDNILDSN
CCEEECCCCCCCCCC		32.3028132839
409PhosphorylationGLTRLPLSPTPNCNS
CCCCCCCCCCCCCCC		25.4523749301
416PhosphorylationSPTPNCNSLHSTTTG
CCCCCCCCCCCCCCC		29.6523810556
442PhosphorylationMGSFRSDTGINPISS
CCCCCCCCCCCCCCC		41.0021440633
448PhosphorylationDTGINPISSSNTVSF
CCCCCCCCCCCEEEE		29.0423810556
449PhosphorylationTGINPISSSNTVSFK
CCCCCCCCCCEEEEE		28.4723810556
450PhosphorylationGINPISSSNTVSFKS
CCCCCCCCCEEEEEE		29.7227017623
454PhosphorylationISSSNTVSFKSKSGN
CCCCCEEEEEECCCC		25.5623810556
525PhosphorylationRASKLKRSQSLLSDS
HHHHHHHHHHHHCCC		23.6422369663
527PhosphorylationSKLKRSQSLLSDSGS
HHHHHHHHHHCCCCC		32.3122369663
530PhosphorylationKRSQSLLSDSGSKSQ
HHHHHHHCCCCCHHH		34.7221440633
532PhosphorylationSQSLLSDSGSKSQAR
HHHHHCCCCCHHHHH		41.4119823750
534PhosphorylationSLLSDSGSKSQARKS
HHHCCCCCHHHHHHH		32.8423810556
546PhosphorylationRKSCNSKSNGNLFNS
HHHHCCCCCCCCCCC		50.1922369663
553PhosphorylationSNGNLFNSQ------
CCCCCCCCC------		29.9021440633
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
319TPhosphorylationKinaseCDC28P00546
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
319TPhosphorylation

12865300
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 NDD1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FKH2_YEASTFKH2physical
12865300
FKH2_YEASTFKH2physical
15509804
ISW1_YEASTISW1genetic
17283050
ISW2_YEASTISW2genetic
17283050
FKH2_YEASTFKH2genetic
10894549
CG22_YEASTCLB2physical
27555611
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NDD1_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-254; THR-319; SER-527AND SER-530, AND MASS SPECTROMETRY.
"Recruitment of Thr 319-phosphorylated Ndd1p to the FHA domain ofFkh2p requires Clb kinase activity: a mechanism for CLB cluster geneactivation.";
Reynolds D., Shi B.J., McLean C., Katsis F., Kemp B., Dalton S.;
Genes Dev. 17:1789-1802(2003).
Cited for: FUNCTION, INTERACTION WITH FKH2, PHOSPHORYLATION AT THR-319, ANDMUTAGENESIS OF THR-319.

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