NRP1_YEAST - dbPTM
NRP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRP1_YEAST
UniProt AC P32770
Protein Name Asparagine-rich protein
Gene Name NRP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 719
Subcellular Localization
Protein Description
Protein Sequence MHYVVLELQVAHLPDTPKDQCRIANIAFQIVNAETLVCHYGTNSLPSIEVNGTTKSLESAMVQLDKDIHDVIGNDDFVLVSLYSTWHIRVTLPRQARDDGFILTSYLQHPKVFDLWKEFDRWCVNHPEILGQKKAISNNNCNTKSISINAAKNTKDLDEIVRILEVSIPTEEAGSVPEIYSLLKRTTDILIQLHKKCTSPEDMESVLTKPYDSHTDIRAFLQEKSKILYMNNLPPDTTQSELESWFTQYGVRPVGFWTVKNIVEDTSNVNNNWSLNNSPYVEDQDSISGFVVFQTHEEATEVLALNGRSILSNLANTKQPRVVEHVLELQPSSTGVLDKAQEILSPFPQSKNKPRPGDWNCPSCGFSNFQRRTACFRCSFPAPSNSQIHTANSNNNVNSSRNNLNNRVNSGSSSNISNTAANHPYGAPEFNMIANNTPAALTYNRAHFPAITPLSRQNSLNMAPSNSGSPIIIADHFSGNNNIAPNYRYNNNINNNNNNINNMTNNRYNINNNINGNGNGNGNNSNNNNNHNNNHNNNHHNGSINSNSNTNNNNNNNNGNNSNNCNSNIGMGGCGSNMPFRAGDWKCSTCTYHNFAKNVVCLRCGGPKSISGDASETNHYIDSSTFGPASRTPSNNNISVNTNGGSNAGRTDGNDNKGRDISLMEFMSPPLSMATKSMKEGDGNGSSFNEFKSDKANVNFSNVGDNSAFGNGFNSSIRW
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
339UbiquitinationSSTGVLDKAQEILSP
CCCCHHHHHHHHHCC
48.0515699485
345PhosphorylationDKAQEILSPFPQSKN
HHHHHHHCCCCCCCC
30.1021551504
351UbiquitinationLSPFPQSKNKPRPGD
HCCCCCCCCCCCCCC
64.8415699485
384PhosphorylationRCSFPAPSNSQIHTA
EECCCCCCCCCCCCC
51.7419779198
393PhosphorylationSQIHTANSNNNVNSS
CCCCCCCCCCCCCCC
38.1719779198
410PhosphorylationNLNNRVNSGSSSNIS
CCCCCCCCCCCCCCC
36.8821440633
412PhosphorylationNNRVNSGSSSNISNT
CCCCCCCCCCCCCCC
30.3428889911
414PhosphorylationRVNSGSSSNISNTAA
CCCCCCCCCCCCCCC
39.6225752575
417PhosphorylationSGSSSNISNTAANHP
CCCCCCCCCCCCCCC
32.1723749301
419PhosphorylationSSSNISNTAANHPYG
CCCCCCCCCCCCCCC
21.9830377154
425PhosphorylationNTAANHPYGAPEFNM
CCCCCCCCCCCCHHC
20.5428889911
437PhosphorylationFNMIANNTPAALTYN
HHCCCCCCCCHHEEC
17.7030377154
452PhosphorylationRAHFPAITPLSRQNS
HHHCCCCCCCCCCCC
21.9322369663
455PhosphorylationFPAITPLSRQNSLNM
CCCCCCCCCCCCCCC
32.7822369663
459PhosphorylationTPLSRQNSLNMAPSN
CCCCCCCCCCCCCCC
16.8725752575
465PhosphorylationNSLNMAPSNSGSPII
CCCCCCCCCCCCCEE
33.8019779198
467PhosphorylationLNMAPSNSGSPIIIA
CCCCCCCCCCCEEEE
45.0123749301
469PhosphorylationMAPSNSGSPIIIADH
CCCCCCCCCEEEEEC
16.8523749301
478PhosphorylationIIIADHFSGNNNIAP
EEEEECCCCCCCCCC
36.8730377154
630PhosphorylationSSTFGPASRTPSNNN
CCCCCCCCCCCCCCC
39.5625704821
632PhosphorylationTFGPASRTPSNNNIS
CCCCCCCCCCCCCEE
28.6822369663
634PhosphorylationGPASRTPSNNNISVN
CCCCCCCCCCCEEEE
52.1322369663
639PhosphorylationTPSNNNISVNTNGGS
CCCCCCEEEECCCCC
16.0719779198
651PhosphorylationGGSNAGRTDGNDNKG
CCCCCCCCCCCCCCC
47.5527017623
668PhosphorylationISLMEFMSPPLSMAT
CCHHHHCCCCHHHHC
28.7828889911
686PhosphorylationKEGDGNGSSFNEFKS
CCCCCCCCCHHHHHC
35.4430377154
687PhosphorylationEGDGNGSSFNEFKSD
CCCCCCCCHHHHHCC
33.2330377154

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 NRP1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRP1_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 NRP1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YBI1_YEASTYBL081Wphysical
11283351
NGR1_YEASTNGR1physical
11283351
PAT1_YEASTPAT1genetic
19061648
SWD3_YEASTSWD3genetic
19061648
XRN1_YEASTXRN1genetic
19061648
LSM1_YEASTLSM1genetic
19061648
EBP2_YEASTEBP2genetic
19061648
MED1_YEASTMED1genetic
19061648
SN309_YEASTSNT309genetic
19061648
ECM1_YEASTECM1genetic
19061648
ERF3_YEASTSUP35genetic
19061648
POP8_YEASTPOP8genetic
19061648
DBP5_YEASTDBP5genetic
19061648
UAF30_YEASTUAF30genetic
19061648
AEP3_YEASTAEP3genetic
19061648
PRP4_YEASTPRP4genetic
19061648
NRP1_YEASTNRP1physical
19345193
COQ1_YEASTCOQ1genetic
15641941
YPK9_YEASTYPK9genetic
22457822
SIS1_YEASTSIS1physical
22718905
MCM7_YEASTMCM7genetic
27708008
PDC2_YEASTPDC2genetic
27708008
ERF3_YEASTSUP35genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
CDC4_YEASTCDC4genetic
27708008
ACT_YEASTACT1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
SSL1_YEASTSSL1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
TIM23_YEASTTIM23genetic
27708008
PROF_YEASTPFY1genetic
27708008
ULP1_YEASTULP1genetic
27708008
SEC62_YEASTSEC62genetic
27708008
PSB5_YEASTPRE2genetic
27708008
IWS1_YEASTSPN1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRP1_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-345; SER-455 ANDSER-634, 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-455, AND MASSSPECTROMETRY.
"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-455, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND MASSSPECTROMETRY.

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