NOP56_MOUSE - dbPTM
NOP56_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOP56_MOUSE
UniProt AC Q9D6Z1
Protein Name Nucleolar protein 56
Gene Name Nop56
Organism Mus musculus (Mouse).
Sequence Length 580
Subcellular Localization Nucleus, nucleolus. Cytoplasm . Nucleus, nucleoplasm.
Protein Description Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (By similarity)..
Protein Sequence MVLLHVLFEHAVGYALLALKEVEEISLLLPQVEECVLNLGKFHNVVRLVAFCPFSSSQVALENANAVSEGVVHEDLRLLLETYLPSKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIVNDNATYCRLAQFIGNRRELNEEKLEKLEEITMDGAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAKYPASTVQILGAEKALFRALKTRGNTPKYGLIFHSTFIGRAAAKNKGRISRYLANKCSIASRIDCFSEVPTSVFGEKLREQVEERLSFYETGEIPRKNLDVMKEAVVQAEEAAAEITRKLEKQEKKRLKKEKKRLAALALASSENSSTPEECEEVNEKSKKKKKLKPQENGMEDPPVSLPKSKKKKAPKEELASDLEEMATSSAKRKKSSPKEEVASEPEEAASPTTPKKKRKFSEEPEVAANFTKSSTKKKKKSQKAQED
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
52GlutathionylationVVRLVAFCPFSSSQV
HHHHEEECCCCCHHH		2.1024333276
87MalonylationLETYLPSKKKKVLLG
HHHHCCCCCCEEEEC		67.6726320211
90MalonylationYLPSKKKKVLLGVGD
HCCCCCCEEEECCCC		47.1726320211
134AcetylationLHFHNLVKGLTDLSA
HHHHHHHHHCCHHHH		51.9022826441
143UbiquitinationLTDLSACKAQLGLGH
CCHHHHHHHHHCCCC		38.59-
158MalonylationSYSRAKVKFNVNRVD
CCCCCEEEECHHHHH		30.4326320211
227AcetylationRRELNEEKLEKLEEI
CHHCCHHHHHHHHHH		56.6323954790
250PhosphorylationAILDASRSSMGMDIS
HHHHHHHHCCCCCCH		23.37-
275PhosphorylationSSRVVSLSEYRQSLH
CCCCCCHHHHHHHHH		25.69-
314PhosphorylationRLIAHAGSLTNLAKY
HHHHCCCCCHHHHHC		32.5725159016
316PhosphorylationIAHAGSLTNLAKYPA
HHCCCCCHHHHHCCH		29.8625159016
320AcetylationGSLTNLAKYPASTVQ
CCCHHHHHCCHHHHH		55.7422826441
320UbiquitinationGSLTNLAKYPASTVQ
CCCHHHHHCCHHHHH		55.74-
333UbiquitinationVQILGAEKALFRALK
HHHHCHHHHHHHHHH		50.27-
359MethylationFHSTFIGRAAAKNKG
EEHHHHHHHHHCCCC		19.0830988667
375UbiquitinationISRYLANKCSIASRI
HHHHHHHHCCHHHHC		24.61-
384GlutathionylationSIASRIDCFSEVPTS
CHHHHCCCCCCCCHH		3.6324333276
406PhosphorylationEQVEERLSFYETGEI
HHHHHHHCHHHCCCC		31.8128066266
436PhosphorylationEEAAAEITRKLEKQE
HHHHHHHHHHHHHHH		17.1620139300
461PhosphorylationLAALALASSENSSTP
HHHHHHHCCCCCCCH		38.7522942356
462PhosphorylationAALALASSENSSTPE
HHHHHHCCCCCCCHH		34.8827087446
465PhosphorylationALASSENSSTPEECE
HHHCCCCCCCHHHHH		31.3825521595
466PhosphorylationLASSENSSTPEECEE
HHCCCCCCCHHHHHH		60.6125521595
467PhosphorylationASSENSSTPEECEEV
HCCCCCCCHHHHHHH		34.2425521595
497PhosphorylationGMEDPPVSLPKSKKK
CCCCCCCCCCHHHCC		44.7329550500
513PhosphorylationAPKEELASDLEEMAT
CCHHHHHHHHHHHHH		56.1827087446
520PhosphorylationSDLEEMATSSAKRKK
HHHHHHHHHHHHHCC		23.1524925903
521PhosphorylationDLEEMATSSAKRKKS
HHHHHHHHHHHHCCC		20.8224925903
522PhosphorylationLEEMATSSAKRKKSS
HHHHHHHHHHHCCCC		33.1924925903
528PhosphorylationSSAKRKKSSPKEEVA
HHHHHCCCCCHHHHC		55.7127087446
529PhosphorylationSAKRKKSSPKEEVAS
HHHHCCCCCHHHHCC		49.2027087446
536PhosphorylationSPKEEVASEPEEAAS
CCHHHHCCCHHHHCC		59.8827087446
543PhosphorylationSEPEEAASPTTPKKK
CCHHHHCCCCCCHHH		29.8124925903
545PhosphorylationPEEAASPTTPKKKRK
HHHHCCCCCCHHHCC		53.9224925903
546PhosphorylationEEAASPTTPKKKRKF
HHHCCCCCCHHHCCC		36.1724925903
552AcetylationTTPKKKRKFSEEPEV
CCCHHHCCCCCCHHH		63.2223806337
554PhosphorylationPKKKRKFSEEPEVAA
CHHHCCCCCCHHHHH		44.0527087446
564PhosphorylationPEVAANFTKSSTKKK
HHHHHHCCCCCCHHH		29.8028725479
565AcetylationEVAANFTKSSTKKKK
HHHHHCCCCCCHHHH		37.9723806337
566PhosphorylationVAANFTKSSTKKKKK
HHHHCCCCCCHHHHH		39.9325619855
567PhosphorylationAANFTKSSTKKKKKS
HHHCCCCCCHHHHHH		45.8925619855
568PhosphorylationANFTKSSTKKKKKSQ
HHCCCCCCHHHHHHH		54.7125619855
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 NOP56_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOP56_MOUSE !!
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 NOP56_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NOP56_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOP56_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 ANDSER-543, AND MASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 ANDSER-554, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 ANDSER-554, AND MASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-467; SER-529;SER-536 AND SER-543, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 ANDTHR-545, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, ANDMASS SPECTROMETRY.

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