UTP18_MOUSE - dbPTM
UTP18_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP18_MOUSE
UniProt AC Q5SSI6
Protein Name U3 small nucleolar RNA-associated protein 18 homolog
Gene Name Utp18
Organism Mus musculus (Mouse).
Sequence Length 552
Subcellular Localization Nucleus, nucleolus.
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA..
Protein Sequence MPPERKSRTRRDRRAGATPGRKARPGSGSTPAKAARSSQRTQPAEPRAAPSAGSAAAAAEEEESRLRQRNRLTLEDDKPAAERCLEQLVFGDVEDDEDALLQRLRSSRGQLHGSSDESEVENEAKDIFSQKKKQPVWVDEDDEDEEIVDMSNNRFRKDIMKNASESKLSKDKLQKRLKEEFQHAMGGVPDWAEAGSKRRTSSDDESEEDEDDLLQRTGNFISTSTSLPRGILKMKNCRPANAERPTTARISSVQFHPGAQVVMVSGVDNAISLFQVDGKTNPKIQSIYLEKFPIFKACFSANGEEVLATSMHSKVLYVYDMLAGKLIPVHQVRGLKEKTVKQFEVSPDGSFLLISGIAGFSHLLSMKTKELIGSMKINGRIAASTFSSDSKRIYTYSENGEVYVWDVNSRKCMNRFLDEGSLCGLSIAASKNGQYVACGSKSGVVNIYNQDSCLQQTNPKPIKAIMNLVTGVTSLAFNPTTEILAVASRKMKEAVRLVHLPSCTVFSNFPVFKKSTLSRVQTMDFSPRGGYFALGNEKGRALMYRLHHYSDF
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
27PhosphorylationGRKARPGSGSTPAKA
CCCCCCCCCCCHHHH		32.0526824392
29PhosphorylationKARPGSGSTPAKAAR
CCCCCCCCCHHHHHH		32.6829899451
30PhosphorylationARPGSGSTPAKAARS
CCCCCCCCHHHHHHH		30.6924453211
51PhosphorylationAEPRAAPSAGSAAAA
CCCCCCCCHHHHHHH		40.3030635358
54PhosphorylationRAAPSAGSAAAAAEE
CCCCCHHHHHHHHHH		17.9125619855
64PhosphorylationAAAEEEESRLRQRNR
HHHHHHHHHHHHHHC		39.6430635358
73PhosphorylationLRQRNRLTLEDDKPA
HHHHHCCCCCCCHHH		25.5125159016
106PhosphorylationALLQRLRSSRGQLHG
HHHHHHHHCCCCCCC		29.0423984901
107PhosphorylationLLQRLRSSRGQLHGS
HHHHHHHCCCCCCCC		33.7123984901
114PhosphorylationSRGQLHGSSDESEVE
CCCCCCCCCCHHHHH		24.7027087446
115PhosphorylationRGQLHGSSDESEVEN
CCCCCCCCCHHHHHH		50.4127087446
118PhosphorylationLHGSSDESEVENEAK
CCCCCCHHHHHHHHH		52.5127087446
129PhosphorylationNEAKDIFSQKKKQPV
HHHHHHHHCCCCCCE		41.2325367039
200PhosphorylationEAGSKRRTSSDDESE
HHCCCCCCCCCCCCC		36.2925521595
201PhosphorylationAGSKRRTSSDDESEE
HCCCCCCCCCCCCCC		29.9225521595
202PhosphorylationGSKRRTSSDDESEED
CCCCCCCCCCCCCCC		48.7625521595
206PhosphorylationRTSSDDESEEDEDDL
CCCCCCCCCCCHHHH		53.9625521595
217PhosphorylationEDDLLQRTGNFISTS
HHHHHHHHCCCCCCC		24.4228066266
222PhosphorylationQRTGNFISTSTSLPR
HHHCCCCCCCCCCCC		16.5028066266
288PhosphorylationNPKIQSIYLEKFPIF
CCCCEEEEEEECHHH		17.6625367039
325UbiquitinationVYDMLAGKLIPVHQV
HHHHHCCCEEEHHHC		37.32-
387PhosphorylationRIAASTFSSDSKRIY
EEEEEECCCCCCEEE		33.0720531401
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 UTP18_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP18_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 UTP18_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UTP18_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP18_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-114; SER-115 ANDSER-118, 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-114; SER-115; SER-118AND SER-206, 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-114; SER-115; SER-118AND SER-206, AND MASS 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-114; SER-115 ANDSER-206, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-115; SER-201;SER-202 AND SER-206, AND MASS SPECTROMETRY.

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