NOP58_MOUSE - dbPTM
NOP58_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOP58_MOUSE
UniProt AC Q6DFW4
Protein Name Nucleolar protein 58
Gene Name Nop58
Organism Mus musculus (Mouse).
Sequence Length 536
Subcellular Localization Nucleus, nucleolus. Nucleus, nucleoplasm.
Protein Description Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (By similarity)..
Protein Sequence MLVLFETSVGYAIFKVLNEKKLQEVDSLWKEFETPEKANKIVKLKHFEKFQDTAEALAAFTALMEGKINKQLKKVLKKIVKEAHEPLAVADAKLGGVIKEKLNLSCIHSPVVNELMRGIRSQMDGLIPGVEPREMAAMCLGLAHSLSRYRLKFSADKVDTMIVQAISLLDDLDKELNNYIMRCREWYGWHFPELGKIISDNLTYCKCLQKVGDRKNYASASLSEFLSEEVEAEVKAAAEISMGTEVSEEDICNILHLCTQVIEISEYRTQLYEYLQNRMMAIAPNVTVMVGELVGARLIAHAGSLLNLAKHAASTVQILGAEKALFRALKSRRDTPKYGLIYHASLVGQSSPKHKGKISRMLAAKTVLAIRYDAFGEDSSSAMGIENRAKLEARLRILEDRGIRKISGTGKALAKAEKYEHKSEVKTYDPSGDSTLPTCSKKRKIEEVDKEDEITEKKAKKAKIKIKAEVEEEMEEEEAEEEQVVEEEPTVKKKKKKDKKKHIKEEPLSEEEPCTSTAVPSPEKKKKKKKKKDAED
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
34PhosphorylationSLWKEFETPEKANKI
HHHHHCCCHHHHHHH
41.9128066266
67AcetylationFTALMEGKINKQLKK
HHHHHHCCHHHHHHH
29.7823954790
70UbiquitinationLMEGKINKQLKKVLK
HHHCCHHHHHHHHHH
61.55-
81MalonylationKVLKKIVKEAHEPLA
HHHHHHHHHHCCCHH
53.2926320211
93MalonylationPLAVADAKLGGVIKE
CHHHCCCCCCCHHHH
48.4926320211
101MalonylationLGGVIKEKLNLSCIH
CCCHHHHHCCCHHCC
37.3626320211
105PhosphorylationIKEKLNLSCIHSPVV
HHHHCCCHHCCHHHH
15.2225159016
106S-palmitoylationKEKLNLSCIHSPVVN
HHHCCCHHCCHHHHH
3.5128526873
106GlutathionylationKEKLNLSCIHSPVVN
HHHCCCHHCCHHHHH
3.5124333276
109PhosphorylationLNLSCIHSPVVNELM
CCCHHCCHHHHHHHH
10.2425159016
121PhosphorylationELMRGIRSQMDGLIP
HHHHHHHHHHCCCCC
28.1222817900
206UbiquitinationSDNLTYCKCLQKVGD
HCCCHHHHHHHHHCC
27.8022790023
217PhosphorylationKVGDRKNYASASLSE
HHCCCCCHHHCHHHH
12.6422802335
223PhosphorylationNYASASLSEFLSEEV
CHHHCHHHHHHHHHH
24.6522802335
304PhosphorylationRLIAHAGSLLNLAKH
HHHHHHHHHHHHHHH
30.39-
342PhosphorylationTPKYGLIYHASLVGQ
CCCCEEEEEHHHCCC
9.0725159016
345PhosphorylationYGLIYHASLVGQSSP
CEEEEEHHHCCCCCC
15.4125159016
350PhosphorylationHASLVGQSSPKHKGK
EHHHCCCCCCCCCCH
42.5526239621
351PhosphorylationASLVGQSSPKHKGKI
HHHCCCCCCCCCCHH
30.0422942356
405AcetylationLEDRGIRKISGTGKA
HHHCCCEECCCCCHH
39.026569155
407PhosphorylationDRGIRKISGTGKALA
HCCCEECCCCCHHHH
33.0829514104
409PhosphorylationGIRKISGTGKALAKA
CCEECCCCCHHHHHH
28.81-
411MalonylationRKISGTGKALAKAEK
EECCCCCHHHHHHHH
39.8126320211
411AcetylationRKISGTGKALAKAEK
EECCCCCHHHHHHHH
39.816568357
419PhosphorylationALAKAEKYEHKSEVK
HHHHHHHCCCCCCCC
18.1228576409
434PhosphorylationTYDPSGDSTLPTCSK
EECCCCCCCCCCCCC
35.0629176673
435PhosphorylationYDPSGDSTLPTCSKK
ECCCCCCCCCCCCCC
41.3129176673
438PhosphorylationSGDSTLPTCSKKRKI
CCCCCCCCCCCCCCH
32.3129176673
440PhosphorylationDSTLPTCSKKRKIEE
CCCCCCCCCCCCHHH
43.6329176673
441MalonylationSTLPTCSKKRKIEEV
CCCCCCCCCCCHHHC
59.7626320211
441AcetylationSTLPTCSKKRKIEEV
CCCCCCCCCCCHHHC
59.76133337
509PhosphorylationHIKEEPLSEEEPCTS
CCCCCCCCCCCCCCC
54.3927087446
515PhosphorylationLSEEEPCTSTAVPSP
CCCCCCCCCCCCCCH
39.5724925903
516PhosphorylationSEEEPCTSTAVPSPE
CCCCCCCCCCCCCHH
22.5324925903
517PhosphorylationEEEPCTSTAVPSPEK
CCCCCCCCCCCCHHH
17.3324925903
521PhosphorylationCTSTAVPSPEKKKKK
CCCCCCCCHHHHHHH
38.8124925903

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 NOP58_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOP58_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 NOP58_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NOP58_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOP58_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-509, AND MASSSPECTROMETRY.
"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-509 AND SER-521, 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-509 AND SER-521, ANDMASS 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-509 AND SER-521, ANDMASS SPECTROMETRY.

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