UTP18_HUMAN - dbPTM
UTP18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP18_HUMAN
UniProt AC Q9Y5J1
Protein Name U3 small nucleolar RNA-associated protein 18 homolog
Gene Name UTP18
Organism Homo sapiens (Human).
Sequence Length 556
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA..
Protein Sequence MPPERRRRMKLDRRTGAKPKRKPGMRPDWKAGAGPGGPPQKPAPSSQRKPPARPSAAAAAIAVAAAEEERRLRQRNRLRLEEDKPAVERCLEELVFGDVENDEDALLRRLRGPRVQEHEDSGDSEVENEAKGNFPPQKKPVWVDEEDEDEEMVDMMNNRFRKDMMKNASESKLSKDNLKKRLKEEFQHAMGGVPAWAETTKRKTSSDDESEEDEDDLLQRTGNFISTSTSLPRGILKMKNCQHANAERPTVARISSVQFHPGAQIVMVAGLDNAVSLFQVDGKTNPKIQSIYLERFPIFKACFSANGEEVLATSTHSKVLYVYDMLAGKLIPVHQVRGLKEKIVRSFEVSPDGSFLLINGIAGYLHLLAMKTKELIGSMKINGRVAASTFSSDSKKVYASSGDGEVYVWDVNSRKCLNRFVDEGSLYGLSIATSRNGQYVACGSNCGVVNIYNQDSCLQETNPKPIKAIMNLVTGVTSLTFNPTTEILAIASEKMKEAVRLVHLPSCTVFSNFPVIKNKNISHVHTMDFSPRSGYFALGNEKGKALMYRLHHYSDF
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
41UbiquitinationGPGGPPQKPAPSSQR
CCCCCCCCCCCHHHC		49.2527667366
41AcetylationGPGGPPQKPAPSSQR
CCCCCCCCCCCHHHC		49.2525953088
45PhosphorylationPPQKPAPSSQRKPPA
CCCCCCCHHHCCCCC		41.0125849741
46PhosphorylationPQKPAPSSQRKPPAR
CCCCCCHHHCCCCCC		32.7130266825
55PhosphorylationRKPPARPSAAAAAIA
CCCCCCHHHHHHHHH		25.6120068231
84SumoylationRLRLEEDKPAVERCL
CCCHHCCCHHHHHHH		37.8528112733
84SumoylationRLRLEEDKPAVERCL
CCCHHCCCHHHHHHH		37.85-
84UbiquitinationRLRLEEDKPAVERCL
CCCHHCCCHHHHHHH		37.8524816145
121PhosphorylationRVQEHEDSGDSEVEN
CCCCCCCCCCCHHCH		41.3329255136
124PhosphorylationEHEDSGDSEVENEAK
CCCCCCCCHHCHHHC		47.2529255136
172SumoylationMKNASESKLSKDNLK
HHHHCHHHCCHHHHH		53.37-
172SumoylationMKNASESKLSKDNLK
HHHHCHHHCCHHHHH		53.37-
172UbiquitinationMKNASESKLSKDNLK
HHHHCHHHCCHHHHH		53.3733845483
1722-HydroxyisobutyrylationMKNASESKLSKDNLK
HHHHCHHHCCHHHHH		53.37-
172AcetylationMKNASESKLSKDNLK
HHHHCHHHCCHHHHH		53.3725953088
175SumoylationASESKLSKDNLKKRL
HCHHHCCHHHHHHHH		62.16-
175UbiquitinationASESKLSKDNLKKRL
HCHHHCCHHHHHHHH		62.1624816145
175SumoylationASESKLSKDNLKKRL
HCHHHCCHHHHHHHH		62.16-
183AcetylationDNLKKRLKEEFQHAM
HHHHHHHHHHHHHHC		60.2726051181
183SumoylationDNLKKRLKEEFQHAM
HHHHHHHHHHHHHHC		60.27-
183SumoylationDNLKKRLKEEFQHAM
HHHHHHHHHHHHHHC		60.2728112733
183UbiquitinationDNLKKRLKEEFQHAM
HHHHHHHHHHHHHHC		60.2729967540
199PhosphorylationGVPAWAETTKRKTSS
CCCCHHHHCCCCCCC		29.8528555341
201UbiquitinationPAWAETTKRKTSSDD
CCHHHHCCCCCCCCC		60.3529967540
201SumoylationPAWAETTKRKTSSDD
CCHHHHCCCCCCCCC		60.3528112733
204PhosphorylationAETTKRKTSSDDESE
HHHCCCCCCCCCCCC		37.1822167270
205PhosphorylationETTKRKTSSDDESEE
HHCCCCCCCCCCCCC		34.5022167270
206PhosphorylationTTKRKTSSDDESEED
HCCCCCCCCCCCCCC		55.0729255136
210PhosphorylationKTSSDDESEEDEDDL
CCCCCCCCCCCHHHH		53.9629255136
221PhosphorylationEDDLLQRTGNFISTS
HHHHHHHHCCCCCCC		24.4228112733
226PhosphorylationQRTGNFISTSTSLPR
HHHCCCCCCCCCCCC		16.5020068231
227PhosphorylationRTGNFISTSTSLPRG
HHCCCCCCCCCCCCC		31.0720068231
228PhosphorylationTGNFISTSTSLPRGI
HCCCCCCCCCCCCCE		14.8120068231
229PhosphorylationGNFISTSTSLPRGIL
CCCCCCCCCCCCCEE		34.0820068231
230PhosphorylationNFISTSTSLPRGILK
CCCCCCCCCCCCEEH		35.8220068231
239UbiquitinationPRGILKMKNCQHANA
CCCEEHHCCCCCCCC		53.6529967540
283UbiquitinationSLFQVDGKTNPKIQS
EEEEECCCCCHHHEE		40.4423000965
287UbiquitinationVDGKTNPKIQSIYLE
ECCCCCHHHEEEEEE		56.2823000965
287AcetylationVDGKTNPKIQSIYLE
ECCCCCHHHEEEEEE		56.2826051181
290PhosphorylationKTNPKIQSIYLERFP
CCCHHHEEEEEECCH		19.3720068231
292PhosphorylationNPKIQSIYLERFPIF
CHHHEEEEEECCHHH		14.0420068231
304UbiquitinationPIFKACFSANGEEVL
HHHHHHHCCCCCEEE		22.2521890473
313PhosphorylationNGEEVLATSTHSKVL
CCCEEEEECCCCCEE		29.9628787133
321PhosphorylationSTHSKVLYVYDMLAG
CCCCCEEHHHHHHCC		10.43-
329UbiquitinationVYDMLAGKLIPVHQV
HHHHHCCCEEEHHHH		37.3223000965
340UbiquitinationVHQVRGLKEKIVRSF
HHHHCCCHHHHHEEE		60.8424816145
346UbiquitinationLKEKIVRSFEVSPDG
CHHHHHEEEEECCCC		18.1821890473
354PhosphorylationFEVSPDGSFLLINGI
EEECCCCCEEEECCH		21.80-
364PhosphorylationLINGIAGYLHLLAMK
EECCHHHHHHHHHHH		5.07-
372PhosphorylationLHLLAMKTKELIGSM
HHHHHHHHHHHHCCC		19.3729759185
373UbiquitinationHLLAMKTKELIGSMK
HHHHHHHHHHHCCCE		45.0329967540
389PhosphorylationNGRVAASTFSSDSKK
CCEEEEEEECCCCCE		23.8620860994
3952-HydroxyisobutyrylationSTFSSDSKKVYASSG
EEECCCCCEEEEECC		51.77-
395UbiquitinationSTFSSDSKKVYASSG
EEECCCCCEEEEECC		51.7721906983
396UbiquitinationTFSSDSKKVYASSGD
EECCCCCEEEEECCC		44.4229967540
412UbiquitinationEVYVWDVNSRKCLNR
CEEEEECCCCHHHHH		33.3621890473
425PhosphorylationNRFVDEGSLYGLSIA
HHHCCCCCEEEEEEE		19.1728152594
427PhosphorylationFVDEGSLYGLSIATS
HCCCCCEEEEEEEEC		20.0928152594
430PhosphorylationEGSLYGLSIATSRNG
CCCEEEEEEEECCCC		13.0528152594
433PhosphorylationLYGLSIATSRNGQYV
EEEEEEEECCCCCEE		26.9228152594
434PhosphorylationYGLSIATSRNGQYVA
EEEEEEECCCCCEEE		18.0928152594
517UbiquitinationFSNFPVIKNKNISHV
ECCCCEEECCCCCCE		63.2032015554
517AcetylationFSNFPVIKNKNISHV
ECCCCEEECCCCCCE		63.2026051181
517SumoylationFSNFPVIKNKNISHV
ECCCCEEECCCCCCE		63.2028112733
519UbiquitinationNFPVIKNKNISHVHT
CCCEEECCCCCCEEE		51.1333845483
530PhosphorylationHVHTMDFSPRSGYFA
CEEECCCCCCCCEEE		18.3520873877
535PhosphorylationDFSPRSGYFALGNEK
CCCCCCCEEEECCHH		6.21-
536UbiquitinationFSPRSGYFALGNEKG
CCCCCCEEEECCHHH		5.3021890473
542AcetylationYFALGNEKGKALMYR
EEEECCHHHHHHHHH		70.4826051181
542UbiquitinationYFALGNEKGKALMYR
EEEECCHHHHHHHHH		70.4829967540
554PhosphorylationMYRLHHYSDF-----
HHHHHCCCCC-----		28.3420873877
559UbiquitinationHYSDF----------
CCCCC----------		21890473
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP18_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 UTP18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_HUMANMPHOSPH10physical
26344197
RBM19_HUMANRBM19physical
26344197
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 UTP18_HUMAN

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Related Literatures of Post-Translational Modification
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-121; SER-124; THR-204;SER-205; SER-206 AND SER-210, AND MASS 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 THR-204; SER-205; SER-206AND SER-210, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, ANDMASS SPECTROMETRY.
"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-121; SER-124; THR-204;SER-205; SER-206 AND SER-210, AND MASS SPECTROMETRY.
"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 SER-121 AND SER-124, ANDMASS SPECTROMETRY.
"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-121 AND SER-124, ANDMASS SPECTROMETRY.
"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 SER-121 AND SER-124, 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 SER-121 AND SER-124, ANDMASS SPECTROMETRY.
"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-121 AND SER-124, ANDMASS SPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, ANDMASS SPECTROMETRY.

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