NRBP_HUMAN - dbPTM
NRBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRBP_HUMAN
UniProt AC Q9UHY1
Protein Name Nuclear receptor-binding protein
Gene Name NRBP1
Organism Homo sapiens (Human).
Sequence Length 535
Subcellular Localization Cytoplasm, cell cortex . Endomembrane system . Cell projection, lamellipodium . Colocalizes with activated RAC3 to endomembranes and at the cell periphery in lamellipodia.
Protein Description May play a role in subcellular trafficking between the endoplasmic reticulum and Golgi apparatus through interactions with the Rho-type GTPases. Binding to the NS3 protein of dengue virus type 2 appears to subvert this activity into the alteration of the intracellular membrane structure associated with flaviviral replication..
Protein Sequence MSEGESQTVLSSGSDPKVESSSSAPGLTSVSPPVTSTTSAASPEEEEESEDESEILEESPCGRWQKRREEVNQRNVPGIDSAYLAMDTEEGVEVVWNEVQFSERKNYKLQEEKVRAVFDNLIQLEHLNIVKFHKYWADIKENKARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCDPPIIHGNLTCDTIFIQHNGLIKIGSVAPDTINNHVKTCREEQKNLHFFAPEYGEVTNVTTAVDIYSFGMCALEMAVLEIQGNGESSYVPQEAISSAIQLLEDPLQREFIQKCLQSEPARRPTARELLFHPALFEVPSLKLLAAHCIVGHQHMIPENALEEITKNMDTSAVLAEIPAGPGREPVQTLYSQSPALELDKFLEDVRNGIYPLTAFGLPRPQQPQQEEVTSPVVPPSVKTPTPEPAEVETRKVVLMQCNIESVEEGVKHHLTLLLKLEDKLNRHLSCDLMPNENIPELAAELVQLGFISEADQSRLTSLLEETLNKFNFARNSTLNSAAVTVSS
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
2Acetylation------MSEGESQTV
------CCCCCCCEE		55.0719413330
2Phosphorylation------MSEGESQTV
------CCCCCCCEE		55.0729255136
6Phosphorylation--MSEGESQTVLSSG
--CCCCCCCEECCCC		41.8422167270
8PhosphorylationMSEGESQTVLSSGSD
CCCCCCCEECCCCCC		32.4722167270
11PhosphorylationGESQTVLSSGSDPKV
CCCCEECCCCCCCCC		28.4629255136
12PhosphorylationESQTVLSSGSDPKVE
CCCEECCCCCCCCCC		37.8529255136
14PhosphorylationQTVLSSGSDPKVESS
CEECCCCCCCCCCCC		53.3329255136
20PhosphorylationGSDPKVESSSSAPGL
CCCCCCCCCCCCCCC		38.2120873877
21PhosphorylationSDPKVESSSSAPGLT
CCCCCCCCCCCCCCC		18.1427251275
22PhosphorylationDPKVESSSSAPGLTS
CCCCCCCCCCCCCCC		39.5427251275
23PhosphorylationPKVESSSSAPGLTSV
CCCCCCCCCCCCCCC		40.1927251275
28PhosphorylationSSSAPGLTSVSPPVT
CCCCCCCCCCCCCCC		32.7520873877
29PhosphorylationSSAPGLTSVSPPVTS
CCCCCCCCCCCCCCC		26.1620873877
31PhosphorylationAPGLTSVSPPVTSTT
CCCCCCCCCCCCCCC		24.2130576142
35PhosphorylationTSVSPPVTSTTSAAS
CCCCCCCCCCCCCCC		26.5720873877
36PhosphorylationSVSPPVTSTTSAASP
CCCCCCCCCCCCCCH		29.8920873877
37PhosphorylationVSPPVTSTTSAASPE
CCCCCCCCCCCCCHH		18.5320873877
38PhosphorylationSPPVTSTTSAASPEE
CCCCCCCCCCCCHHH		19.0130576142
39PhosphorylationPPVTSTTSAASPEEE
CCCCCCCCCCCHHHH		23.1720873877
42PhosphorylationTSTTSAASPEEEEES
CCCCCCCCHHHHCCC		32.3430576142
49PhosphorylationSPEEEEESEDESEIL
CHHHHCCCCCHHHHH		54.3426657352
53PhosphorylationEEESEDESEILEESP
HCCCCCHHHHHHHCC		42.1130576142
59PhosphorylationESEILEESPCGRWQK
HHHHHHHCCCCHHHH		19.0027251275
134UbiquitinationLNIVKFHKYWADIKE
CCHHEEHHHHHHHHH		45.6919608861
134AcetylationLNIVKFHKYWADIKE
CCHHEEHHHHHHHHH		45.6919608861
150PhosphorylationKARVIFITEYMSSGS
CCEEEEEEEECCCCC		15.4323663014
152PhosphorylationRVIFITEYMSSGSLK
EEEEEEEECCCCCHH		8.1423663014
154PhosphorylationIFITEYMSSGSLKQF
EEEEEECCCCCHHHH		30.5523663014
155PhosphorylationFITEYMSSGSLKQFL
EEEEECCCCCHHHHH		18.8323663014
157PhosphorylationTEYMSSGSLKQFLKK
EEECCCCCHHHHHHH		34.0523663014
220PhosphorylationNGLIKIGSVAPDTIN
CCEEEECCCCCHHHH		20.6928857561
225PhosphorylationIGSVAPDTINNHVKT
ECCCCCHHHHHHHHH		25.2523403867
231UbiquitinationDTINNHVKTCREEQK
HHHHHHHHHHHHHHC		34.06-
232PhosphorylationTINNHVKTCREEQKN
HHHHHHHHHHHHHCC		18.7325849741
306UbiquitinationLQREFIQKCLQSEPA
HHHHHHHHHHCCCCC		31.90-
362PhosphorylationEITKNMDTSAVLAEI
HHHHCCCCCCEEEEC		14.0725627689
363PhosphorylationITKNMDTSAVLAEIP
HHHCCCCCCEEEECC		16.4721815630
380PhosphorylationPGREPVQTLYSQSPA
CCCCCHHHHHCCCCC		28.0927732954
383PhosphorylationEPVQTLYSQSPALEL
CCHHHHHCCCCCHHH		27.5627732954
385PhosphorylationVQTLYSQSPALELDK
HHHHHCCCCCHHHHH		13.2427732954
392UbiquitinationSPALELDKFLEDVRN
CCCHHHHHHHHHHHC		65.55-
402PhosphorylationEDVRNGIYPLTAFGL
HHHHCCCCCHHHCCC		8.1226074081
405PhosphorylationRNGIYPLTAFGLPRP
HCCCCCHHHCCCCCC		18.5526074081
421PhosphorylationQPQQEEVTSPVVPPS
CCCCCCCCCCCCCCC		30.5029255136
422PhosphorylationPQQEEVTSPVVPPSV
CCCCCCCCCCCCCCC		22.3729255136
428PhosphorylationTSPVVPPSVKTPTPE
CCCCCCCCCCCCCCC		30.1228348404
430UbiquitinationPVVPPSVKTPTPEPA
CCCCCCCCCCCCCCC		53.80-
431PhosphorylationVVPPSVKTPTPEPAE
CCCCCCCCCCCCCCC		30.1819664994
433PhosphorylationPPSVKTPTPEPAEVE
CCCCCCCCCCCCCCC		45.5819664994
441PhosphorylationPEPAEVETRKVVLMQ
CCCCCCCCCEEEEEE		40.7523927012
471UbiquitinationLLLKLEDKLNRHLSC
HHHHHHHHHHHHCCC		37.98-
505O-linked_GlycosylationFISEADQSRLTSLLE
CCCHHHHHHHHHHHH		29.7930059200
517UbiquitinationLLEETLNKFNFARNS
HHHHHHHHHCHHCCC		44.8121890473
532O-linked_GlycosylationTLNSAAVTVSS----
CCCCCEEECCC----		15.2230059200
534O-linked_GlycosylationNSAAVTVSS------
CCCEEECCC------		22.4430059200
534PhosphorylationNSAAVTVSS------
CCCEEECCC------		22.4425159151
535O-linked_GlycosylationSAAVTVSS-------
CCEEECCC-------		39.6530059200
535PhosphorylationSAAVTVSS-------
CCEEECCC-------		39.6525159151
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 NRBP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRBP_HUMAN !!
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 NRBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
T22D4_HUMANTSC22D4physical
16189514
LRIF1_HUMANLRIF1physical
16169070
ELOB_HUMANTCEB2physical
18187417
ELOC_HUMANTCEB1physical
18187417
CSN5_HUMANCOPS5physical
17052710
SART3_HUMANSART3physical
22863883
T22D4_HUMANTSC22D4physical
25416956
T22D4_HUMANTSC22D4physical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRBP_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-134, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-431 AND THR-433,AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431 AND THR-433, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASSSPECTROMETRY.

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