NOB1_HUMAN - dbPTM
NOB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOB1_HUMAN
UniProt AC Q9ULX3
Protein Name RNA-binding protein NOB1
Gene Name NOB1
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Nucleus .
Protein Description May play a role in mRNA degradation..
Protein Sequence MAPVEHVVADAGAFLRHAALQDIGKNIYTIREVVTEIRDKATRRRLAVLPYELRFKEPLPEYVRLVTEFSKKTGDYPSLSATDIQVLALTYQLEAEFVGVSHLKQEPQKVKVSSSIQHPETPLHISGFHLPYKPKPPQETEKGHSACEPENLEFSSFMFWRNPLPNIDHELQELLIDRGEDVPSEEEEEEENGFEDRKDDSDDDGGGWITPSNIKQIQQELEQCDVPEDVRVGCLTTDFAMQNVLLQMGLHVLAVNGMLIREARSYILRCHGCFKTTSDMSRVFCSHCGNKTLKKVSVTVSDDGTLHMHFSRNPKVLNPRGLRYSLPTPKGGKYAINPHLTEDQRFPQLRLSQKARQKTNVFAPDYIAGVSPFVENDISSRSATLQVRDSTLGAGRRRLNPNASRKKFVKKR
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
25UbiquitinationAALQDIGKNIYTIRE
HHHHHHHHHCEEHHH		40.2721906983
29PhosphorylationDIGKNIYTIREVVTE
HHHHHCEEHHHHHHH		15.1224719451
35PhosphorylationYTIREVVTEIRDKAT
EEHHHHHHHHHHHHH		30.76-
35UbiquitinationYTIREVVTEIRDKAT
EEHHHHHHHHHHHHH		30.7621890473
40UbiquitinationVVTEIRDKATRRRLA
HHHHHHHHHHHHHEE		41.63-
42PhosphorylationTEIRDKATRRRLAVL
HHHHHHHHHHHEEEC		30.37-
51PhosphorylationRRLAVLPYELRFKEP
HHEEECCEEEECCCC		24.3528152594
56UbiquitinationLPYELRFKEPLPEYV
CCEEEECCCCCHHHH		52.5727667366
62PhosphorylationFKEPLPEYVRLVTEF
CCCCCHHHHHHHHHH		6.7421406692
71UbiquitinationRLVTEFSKKTGDYPS
HHHHHHHHHHCCCCC		60.7329967540
71AcetylationRLVTEFSKKTGDYPS
HHHHHHHHHHCCCCC		60.7325953088
72UbiquitinationLVTEFSKKTGDYPSL
HHHHHHHHHCCCCCC		57.45-
111UbiquitinationKQEPQKVKVSSSIQH
CCCCCEEEEECCCCC		43.3629967540
121PhosphorylationSSIQHPETPLHISGF
CCCCCCCCCCEECEE		35.2825159151
126PhosphorylationPETPLHISGFHLPYK
CCCCCEECEECCCCC		25.3429759185
133UbiquitinationSGFHLPYKPKPPQET
CEECCCCCCCCCCCC		44.6229967540
135UbiquitinationFHLPYKPKPPQETEK
ECCCCCCCCCCCCCC		66.2429967540
140PhosphorylationKPKPPQETEKGHSAC
CCCCCCCCCCCCCCC		37.4420860994
184PhosphorylationDRGEDVPSEEEEEEE
HCCCCCCCHHHHHHH		58.4522167270
201PhosphorylationFEDRKDDSDDDGGGW
CCCCCCCCCCCCCCC		53.7422167270
210PhosphorylationDDGGGWITPSNIKQI
CCCCCCCCHHHHHHH		17.7323927012
212PhosphorylationGGGWITPSNIKQIQQ
CCCCCCHHHHHHHHH		42.4023927012
275MethylationLRCHGCFKTTSDMSR
HHHCCCCCCCCCHHH		55.78115974101
275UbiquitinationLRCHGCFKTTSDMSR
HHHCCCCCCCCCHHH		55.78-
286PhosphorylationDMSRVFCSHCGNKTL
CHHHHHHHHCCCCEE		15.45-
291UbiquitinationFCSHCGNKTLKKVSV
HHHHCCCCEEEEEEE		40.2829967540
292PhosphorylationCSHCGNKTLKKVSVT
HHHCCCCEEEEEEEE		48.05-
294UbiquitinationHCGNKTLKKVSVTVS
HCCCCEEEEEEEEEC		57.25-
295UbiquitinationCGNKTLKKVSVTVSD
CCCCEEEEEEEEECC		42.74-
315UbiquitinationMHFSRNPKVLNPRGL
EEECCCCCCCCCCCC		64.0024816145
315AcetylationMHFSRNPKVLNPRGL
EEECCCCCCCCCCCC		64.0025953088
324PhosphorylationLNPRGLRYSLPTPKG
CCCCCCCCCCCCCCC		21.4328450419
325PhosphorylationNPRGLRYSLPTPKGG
CCCCCCCCCCCCCCC		22.8025159151
328PhosphorylationGLRYSLPTPKGGKYA
CCCCCCCCCCCCEEC		42.8126055452
330UbiquitinationRYSLPTPKGGKYAIN
CCCCCCCCCCEECCC		80.7833845483
333UbiquitinationLPTPKGGKYAINPHL
CCCCCCCEECCCCCC		39.9333845483
333AcetylationLPTPKGGKYAINPHL
CCCCCCCEECCCCCC		39.9319608861
334PhosphorylationPTPKGGKYAINPHLT
CCCCCCEECCCCCCC		18.9126074081
341PhosphorylationYAINPHLTEDQRFPQ
ECCCCCCCCCCCCCH		34.1928152594
343UbiquitinationINPHLTEDQRFPQLR
CCCCCCCCCCCCHHH		39.4521890473
345MethylationPHLTEDQRFPQLRLS
CCCCCCCCCCHHHHH		58.49115485227
352PhosphorylationRFPQLRLSQKARQKT
CCCHHHHHHHHHHHC		24.1723401153
354UbiquitinationPQLRLSQKARQKTNV
CHHHHHHHHHHHCCC		42.0122817900
358UbiquitinationLSQKARQKTNVFAPD
HHHHHHHHCCCCCCH		36.1921963094
359PhosphorylationSQKARQKTNVFAPDY
HHHHHHHCCCCCCHH		28.4230257219
366PhosphorylationTNVFAPDYIAGVSPF
CCCCCCHHHCCCCHH		7.5121552520
368UbiquitinationVFAPDYIAGVSPFVE
CCCCHHHCCCCHHCC		13.2021890473
371PhosphorylationPDYIAGVSPFVENDI
CHHHCCCCHHCCCCC		16.2328348404
379PhosphorylationPFVENDISSRSATLQ
HHCCCCCCCCCEEEE		23.6728122231
380PhosphorylationFVENDISSRSATLQV
HCCCCCCCCCEEEEE		30.5028122231
382PhosphorylationENDISSRSATLQVRD
CCCCCCCCEEEEEEC		27.7927251275
384PhosphorylationDISSRSATLQVRDST
CCCCCCEEEEEECCC		20.9728857561
390PhosphorylationATLQVRDSTLGAGRR
EEEEEECCCCCCCCC		18.2428857561
391PhosphorylationTLQVRDSTLGAGRRR
EEEEECCCCCCCCCC		33.2430257219
396MethylationDSTLGAGRRRLNPNA
CCCCCCCCCCCCCCC		21.73115485221
404PhosphorylationRRLNPNASRKKFVKK
CCCCCCCHHHHHHCC		51.8027251275
410UbiquitinationASRKKFVKKR-----
CHHHHHHCCC-----		46.0624816145
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
121TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOB1_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 NOB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
NOG2_HUMANGNL2physical
26344197
TSR1_HUMANTSR1physical
26344197
KLH22_HUMANKLHL22physical
28514442
ANKH1_HUMANANKHD1physical
28514442
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 NOB1_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-333, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-184 AND SER-201, ANDMASS SPECTROMETRY.
"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-201, 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 SER-184; SER-201 ANDSER-352, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-201, ANDMASS SPECTROMETRY.

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