NUR1_YEAST - dbPTM
NUR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUR1_YEAST
UniProt AC Q12066
Protein Name Nuclear rim protein 1
Gene Name NUR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 484
Subcellular Localization Nucleus membrane
Multi-pass membrane protein .
Protein Description Member of a perinuclear network that controls recombination at multiple loci to maintain genome stability. Required for rDNA repeat stability..
Protein Sequence MGSNDLINEAYDDSEVVGEERESKSAWMKRWYQLLTSPLDLQLVINEKLEMINWDAYAKSLAKPLGNFLTILFFIIRLLQDNLIKPNYYKLNVKSGAFDLSKSNKLKEFDYLWEISSSFQNNNQFYAFQSWYFVTLRFLNNLFRFTIFILLSLNLYVSCKFMFGYFKTYNLFHLKKEFNSPNLTKHNLKDLSKEYYEDIYKQSLWSMLKHFFRGSRDDGPHVNQNEDEIFFQLRKWIPTNFMINLFVSFSPTAIVFLSFSDVSFTSAIAIVFHQYILDYIITKRFQRSVDDDLILSSAALQEYEDKHIMARINQCSNIDTLSSAMGTRSKTPRIFTTHSLCGEEIREVYNYEKREFEALPKMTESVPGSRETRIKDYGGISQVSDHQSHPIGFHYSPRMSPYYRDKVLDNNLAQSSSNENLEKGGAYLPNQDQNRPSKSLSPLRKTPLSARQKRFEGSEFNVLNKNDINSILRSPKKKKNYHKR
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
3Phosphorylation-----MGSNDLINEA
-----CCCCHHHHHH		26.3528889911
14PhosphorylationINEAYDDSEVVGEER
HHHHCCCCCCCCCHH		29.4123749301
306UbiquitinationALQEYEDKHIMARIN
HHHHHHHHHHHHHHH		24.0817644757
365PhosphorylationALPKMTESVPGSRET
CCCCCCCCCCCCCCC		25.1721440633
369PhosphorylationMTESVPGSRETRIKD
CCCCCCCCCCCCCCC		22.3724961812
372PhosphorylationSVPGSRETRIKDYGG
CCCCCCCCCCCCCCC		36.2627717283
375UbiquitinationGSRETRIKDYGGISQ
CCCCCCCCCCCCCCC		41.4217644757
388PhosphorylationSQVSDHQSHPIGFHY
CCCCCCCCCCCCCCC		28.0124961812
395PhosphorylationSHPIGFHYSPRMSPY
CCCCCCCCCCCCCHH		20.3617330950
396PhosphorylationHPIGFHYSPRMSPYY
CCCCCCCCCCCCHHH		9.4728889911
400PhosphorylationFHYSPRMSPYYRDKV
CCCCCCCCHHHHHHH		15.8424961812
402PhosphorylationYSPRMSPYYRDKVLD
CCCCCCHHHHHHHHC		12.1124961812
403PhosphorylationSPRMSPYYRDKVLDN
CCCCCHHHHHHHHCC		18.7324961812
406UbiquitinationMSPYYRDKVLDNNLA
CCHHHHHHHHCCCCC		35.3823749301
415PhosphorylationLDNNLAQSSSNENLE
HCCCCCCCCCCCCHH		30.0822369663
416PhosphorylationDNNLAQSSSNENLEK
CCCCCCCCCCCCHHH		25.7122369663
417PhosphorylationNNLAQSSSNENLEKG
CCCCCCCCCCCHHHC		54.1022369663
437PhosphorylationNQDQNRPSKSLSPLR
CCCCCCCCCCCCCCC		31.4719779198
439PhosphorylationDQNRPSKSLSPLRKT
CCCCCCCCCCCCCCC		38.1217287358
441PhosphorylationNRPSKSLSPLRKTPL
CCCCCCCCCCCCCCC		29.0419823750
446PhosphorylationSLSPLRKTPLSARQK
CCCCCCCCCCCHHHH		24.0321440633
449PhosphorylationPLRKTPLSARQKRFE
CCCCCCCCHHHHHHC		23.7019779198
470PhosphorylationLNKNDINSILRSPKK
CCHHHHHHHHHCCCC		24.2721440633
474PhosphorylationDINSILRSPKKKKNY
HHHHHHHCCCCCCCC		37.3125521595
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 NUR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUR1_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 NUR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUR1_YEASTNUR1physical
10688190
PEX30_YEASTPEX30physical
10688190
CSM1_YEASTCSM1physical
11283351
RTN1_YEASTRTN1physical
11283351
PEX30_YEASTPEX30physical
11283351
ERG6_YEASTERG6physical
11283351
YOP1_YEASTYOP1physical
11283351
RLI1_YEASTRLI1genetic
19061648
LSM7_YEASTLSM7genetic
19061648
DBP5_YEASTDBP5genetic
19061648
RNH2A_YEASTRNH201genetic
19061648
EF3B_YEASTHEF3genetic
19061648
EAF5_YEASTEAF5genetic
19061648
PFD2_YEASTGIM4genetic
19061648
SRC1_YEASTSRC1physical
18997772
CSM1_YEASTCSM1physical
18997772
NET1_YEASTNET1physical
18997772
SEC66_YEASTSEC66genetic
20093466
APQ12_YEASTAPQ12genetic
20093466
ACA2_YEASTCST6genetic
20093466
YPT52_YEASTYPT52genetic
20093466
TOM70_YEASTTOM70genetic
20093466
PHO23_YEASTPHO23genetic
20093466
YPT52_YEASTYPT52genetic
27708008
NPL4_YEASTNPL4genetic
27708008
SEC66_YEASTSEC66genetic
27708008
THIK_YEASTPOT1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
NU188_YEASTNUP188genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUR1_YEAST

loading...

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-3; SER-416 AND SER-417,AND MASS 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-439 AND SER-441, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory