NSR1_YEAST - dbPTM
NSR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSR1_YEAST
UniProt AC P27476
Protein Name Nuclear localization sequence-binding protein
Gene Name NSR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 414
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in pre-rRNA processing. Specifically binds nuclear localization sequences. Candidate for a receptor at the nucleus that may be involved in both RNA and protein transport. Binds telomeric sequences of the type (TG[1-3])n in vitro..
Protein Sequence MAKTTKVKGNKKEVKASKQAKEEKAKAVSSSSSESSSSSSSSSESESESESESESSSSSSSSDSESSSSSSSDSESEAETKKEESKDSSSSSSDSSSDEEEEEEKEETKKEESKESSSSDSSSSSSSDSESEKEESNDKKRKSEDAEEEEDEESSNKKQKNEETEEPATIFVGRLSWSIDDEWLKKEFEHIGGVIGARVIYERGTDRSRGYGYVDFENKSYAEKAIQEMQGKEIDGRPINCDMSTSKPAGNNDRAKKFGDTPSEPSDTLFLGNLSFNADRDAIFELFAKHGEVVSVRIPTHPETEQPKGFGYVQFSNMEDAKKALDALQGEYIDNRPVRLDFSSPRPNNDGGRGGSRGFGGRGGGRGGNRGFGGRGGARGGRGGFRPSGSGANTAPLGRSRNTASFAGSKKTFD
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
92PhosphorylationSKDSSSSSSDSSSDE
CCCCCCCCCCCCCHH		39.8628889911
93PhosphorylationKDSSSSSSDSSSDEE
CCCCCCCCCCCCHHH		43.3821551504
95PhosphorylationSSSSSSDSSSDEEEE
CCCCCCCCCCHHHHH		33.4219795423
96PhosphorylationSSSSSDSSSDEEEEE
CCCCCCCCCHHHHHH		46.9628132839
97PhosphorylationSSSSDSSSDEEEEEE
CCCCCCCCHHHHHHH		53.6619795423
124PhosphorylationSSSDSSSSSSSDSES
CCCCCCCCCCCCCHH		35.8727717283
125PhosphorylationSSDSSSSSSSDSESE
CCCCCCCCCCCCHHH		35.4927717283
126PhosphorylationSDSSSSSSSDSESEK
CCCCCCCCCCCHHHH		39.8628889911
127PhosphorylationDSSSSSSSDSESEKE
CCCCCCCCCCHHHHH		47.2923749301
129PhosphorylationSSSSSSDSESEKEES
CCCCCCCCHHHHHHH		44.9923749301
131PhosphorylationSSSSDSESEKEESND
CCCCCCHHHHHHHHH		58.9027717283
143PhosphorylationSNDKKRKSEDAEEEE
HHHHHHHHHHHHHHH		44.7529136822
154PhosphorylationEEEEDEESSNKKQKN
HHHHHHHHHCHHHHC		36.8425521595
155PhosphorylationEEEDEESSNKKQKNE
HHHHHHHHCHHHHCC		56.8229136822
157AcetylationEDEESSNKKQKNEET
HHHHHHCHHHHCCCC		59.5425381059
176PhosphorylationTIFVGRLSWSIDDEW
EEEEEEEECCCCHHH		19.8819779198
186AcetylationIDDEWLKKEFEHIGG
CCHHHHHHHHHHHHC		66.5224489116
219AcetylationGYVDFENKSYAEKAI
CEEECCCHHHHHHHH		37.3324489116
219SuccinylationGYVDFENKSYAEKAI
CEEECCCHHHHHHHH		37.3323954790
224AcetylationENKSYAEKAIQEMQG
CCHHHHHHHHHHHCC		42.4924489116
244PhosphorylationRPINCDMSTSKPAGN
CCCCCCCCCCCCCCC		19.1121082442
245PhosphorylationPINCDMSTSKPAGNN
CCCCCCCCCCCCCCC		33.8521082442
246PhosphorylationINCDMSTSKPAGNND
CCCCCCCCCCCCCCH		29.3621082442
275PhosphorylationTLFLGNLSFNADRDA
EEEECEECCCCCHHH		22.0630377154
308AcetylationHPETEQPKGFGYVQF
CCCCCCCCCCCCEEE		67.5724489116
323AcetylationSNMEDAKKALDALQG
CCHHHHHHHHHHHCC		56.7724489116
343PhosphorylationRPVRLDFSSPRPNND
CCEEEECCCCCCCCC		38.8224909858
344PhosphorylationPVRLDFSSPRPNNDG
CEEEECCCCCCCCCC		25.5621082442
353Asymmetric dimethylarginineRPNNDGGRGGSRGFG
CCCCCCCCCCCCCCC		52.40-
353MethylationRPNNDGGRGGSRGFG
CCCCCCCCCCCCCCC		52.4012756332
362Asymmetric dimethylarginineGSRGFGGRGGGRGGN
CCCCCCCCCCCCCCC		40.75-
362MethylationGSRGFGGRGGGRGGN
CCCCCCCCCCCCCCC		40.7512756332
366Asymmetric dimethylarginineFGGRGGGRGGNRGFG
CCCCCCCCCCCCCCC		53.79-
366MethylationFGGRGGGRGGNRGFG
CCCCCCCCCCCCCCC		53.7912756332
375Asymmetric dimethylarginineGNRGFGGRGGARGGR
CCCCCCCCCCCCCCC		40.53-
375MethylationGNRGFGGRGGARGGR
CCCCCCCCCCCCCCC		40.5312756332
379Asymmetric dimethylarginineFGGRGGARGGRGGFR
CCCCCCCCCCCCCCC		51.91-
379MethylationFGGRGGARGGRGGFR
CCCCCCCCCCCCCCC		51.9112756332
382MethylationRGGARGGRGGFRPSG
CCCCCCCCCCCCCCC		44.9012756332
382Asymmetric dimethylarginineRGGARGGRGGFRPSG
CCCCCCCCCCCCCCC		44.90-
388PhosphorylationGRGGFRPSGSGANTA
CCCCCCCCCCCCCCC		41.1428132839
390PhosphorylationGGFRPSGSGANTAPL
CCCCCCCCCCCCCCC		38.7828132839
394PhosphorylationPSGSGANTAPLGRSR
CCCCCCCCCCCCCCC		29.1727017623
400PhosphorylationNTAPLGRSRNTASFA
CCCCCCCCCCCHHHC		28.2530377154
403PhosphorylationPLGRSRNTASFAGSK
CCCCCCCCHHHCCCC		23.6728889911
405PhosphorylationGRSRNTASFAGSKKT
CCCCCCHHHCCCCCC		17.3724909858
409PhosphorylationNTASFAGSKKTFD--
CCHHHCCCCCCCC--		27.7828889911
410AcetylationTASFAGSKKTFD---
CHHHCCCCCCCC---		55.7225381059
411AcetylationASFAGSKKTFD----
HHHCCCCCCCC----		57.0025381059
412PhosphorylationSFAGSKKTFD-----
HHCCCCCCCC-----		36.4523749301
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 NSR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSR1_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 NSR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DBP3_YEASTDBP3physical
14759368
NOP58_YEASTNOP58physical
14759368
NSR1_YEASTNSR1physical
14759368
CBF5_YEASTCBF5physical
14759368
NOP56_YEASTNOP56physical
14759368
FBRL_YEASTNOP1physical
14759368
DED1_YEASTDED1physical
14759368
PABP_YEASTPAB1physical
14759368
IF2B_YEASTSUI3physical
14759368
TOP1_YEASTTOP1physical
10967121
DBP2_YEASTDBP2physical
18467557
GAR1_YEASTGAR1physical
18467557
RTC6_YEASTRTC6genetic
20691087
SRS2_YEASTSRS2genetic
21459050
DBP2_YEASTDBP2physical
22615397
LOC1_YEASTLOC1physical
25877921
NOP4_YEASTNOP4physical
25877921
SEPT6_HUMANSEPT6physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSR1_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-344 AND SER-405, ANDMASS SPECTROMETRY.

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