UTP11_HUMAN - dbPTM
UTP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP11_HUMAN
UniProt AC Q9Y3A2
Protein Name Probable U3 small nucleolar RNA-associated protein 11
Gene Name UTP11 {ECO:0000312|HGNC:HGNC:24329}
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Nucleus, nucleolus.
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA..
Protein Sequence MAAAFRKAAKSRQREHRERSQPGFRKHLGLLEKKKDYKLRADDYRKKQEYLKALRKKALEKNPDEFYYKMTRVKLQDGVHIIKETKEEVTPEQLKLMRTQDVKYIEMKRVAEAKKIERLKSELHLLDFQGKQQNKHVFFFDTKKEVEQFDVATHLQTAPELVDRVFNRPRIETLQKEKVKGVTNQTGLKRIAKERQKQYNCLTQRIEREKKLFVIAQKIQTRKDLMDKTQKVKVKKETVNSPAIYKFQSRRKR
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
26UbiquitinationRSQPGFRKHLGLLEK
HCCCHHHHHHHHHHH		40.70-
26SumoylationRSQPGFRKHLGLLEK
HCCCHHHHHHHHHHH		40.70-
26SumoylationRSQPGFRKHLGLLEK
HCCCHHHHHHHHHHH		40.70-
26UbiquitinationRSQPGFRKHLGLLEK
HCCCHHHHHHHHHHH		40.7029967540
33UbiquitinationKHLGLLEKKKDYKLR
HHHHHHHHHCCCCCC		66.16-
332-HydroxyisobutyrylationKHLGLLEKKKDYKLR
HHHHHHHHHCCCCCC		66.16-
33UbiquitinationKHLGLLEKKKDYKLR
HHHHHHHHHCCCCCC		66.1629967540
34UbiquitinationHLGLLEKKKDYKLRA
HHHHHHHHCCCCCCH		41.31-
34UbiquitinationHLGLLEKKKDYKLRA
HHHHHHHHCCCCCCH		41.31-
35UbiquitinationLGLLEKKKDYKLRAD
HHHHHHHCCCCCCHH		76.88-
35UbiquitinationLGLLEKKKDYKLRAD
HHHHHHHCCCCCCHH		76.88-
37PhosphorylationLLEKKKDYKLRADDY
HHHHHCCCCCCHHHH		22.32-
44PhosphorylationYKLRADDYRKKQEYL
CCCCHHHHHHHHHHH		25.53-
46UbiquitinationLRADDYRKKQEYLKA
CCHHHHHHHHHHHHH		53.2122817900
50PhosphorylationDYRKKQEYLKALRKK
HHHHHHHHHHHHHHH		15.8222817900
51UbiquitinationYRKKQEYLKALRKKA
HHHHHHHHHHHHHHH		2.2921890473
52UbiquitinationRKKQEYLKALRKKAL
HHHHHHHHHHHHHHH		44.4632015554
61UbiquitinationLRKKALEKNPDEFYY
HHHHHHHHCHHHHHH		74.71-
61UbiquitinationLRKKALEKNPDEFYY
HHHHHHHHCHHHHHH		74.7129967540
62UbiquitinationRKKALEKNPDEFYYK
HHHHHHHCHHHHHHH		39.6222817900
66UbiquitinationLEKNPDEFYYKMTRV
HHHCHHHHHHHHHEE		12.0122817900
67PhosphorylationEKNPDEFYYKMTRVK
HHCHHHHHHHHHEEE		10.50-
68PhosphorylationKNPDEFYYKMTRVKL
HCHHHHHHHHHEEEC		10.29-
74UbiquitinationYYKMTRVKLQDGVHI
HHHHHEEECCCCCEE		36.82-
74SumoylationYYKMTRVKLQDGVHI
HHHHHEEECCCCCEE		36.82-
74SumoylationYYKMTRVKLQDGVHI
HHHHHEEECCCCCEE		36.8228112733
74UbiquitinationYYKMTRVKLQDGVHI
HHHHHEEECCCCCEE		36.8229967540
83SumoylationQDGVHIIKETKEEVT
CCCCEEECCCCCCCC		59.7428112733
85PhosphorylationGVHIIKETKEEVTPE
CCEEECCCCCCCCHH		38.4620860994
86UbiquitinationVHIIKETKEEVTPEQ
CEEECCCCCCCCHHH		53.63-
86SumoylationVHIIKETKEEVTPEQ
CEEECCCCCCCCHHH		53.63-
86SumoylationVHIIKETKEEVTPEQ
CEEECCCCCCCCHHH		53.6328112733
86UbiquitinationVHIIKETKEEVTPEQ
CEEECCCCCCCCHHH		53.63-
90PhosphorylationKETKEEVTPEQLKLM
CCCCCCCCHHHHHHH		25.1230266825
95UbiquitinationEVTPEQLKLMRTQDV
CCCHHHHHHHHHCCC		39.67-
95SumoylationEVTPEQLKLMRTQDV
CCCHHHHHHHHHCCC		39.67-
95SumoylationEVTPEQLKLMRTQDV
CCCHHHHHHHHHCCC		39.67-
95UbiquitinationEVTPEQLKLMRTQDV
CCCHHHHHHHHHCCC		39.6729967540
99PhosphorylationEQLKLMRTQDVKYIE
HHHHHHHHCCCCHHH		18.3721406692
103UbiquitinationLMRTQDVKYIEMKRV
HHHHCCCCHHHHHHH		49.12-
103SumoylationLMRTQDVKYIEMKRV
HHHHCCCCHHHHHHH		49.12-
103SumoylationLMRTQDVKYIEMKRV
HHHHCCCCHHHHHHH		49.1228112733
103UbiquitinationLMRTQDVKYIEMKRV
HHHHCCCCHHHHHHH		49.12-
104PhosphorylationMRTQDVKYIEMKRVA
HHHCCCCHHHHHHHH		11.2721406692
108MethylationDVKYIEMKRVAEAKK
CCCHHHHHHHHHHHH		30.82-
114MethylationMKRVAEAKKIERLKS
HHHHHHHHHHHHHHH		45.87-
115UbiquitinationKRVAEAKKIERLKSE
HHHHHHHHHHHHHHH		57.7722817900
120UbiquitinationAKKIERLKSELHLLD
HHHHHHHHHHHHHHH		48.3721890473
120SumoylationAKKIERLKSELHLLD
HHHHHHHHHHHHHHH		48.37-
120AcetylationAKKIERLKSELHLLD
HHHHHHHHHHHHHHH		48.3726051181
120SumoylationAKKIERLKSELHLLD
HHHHHHHHHHHHHHH		48.3728112733
120UbiquitinationAKKIERLKSELHLLD
HHHHHHHHHHHHHHH		48.3721906983
121PhosphorylationKKIERLKSELHLLDF
HHHHHHHHHHHHHHC		50.4028555341
131UbiquitinationHLLDFQGKQQNKHVF
HHHHCCCCCCCEEEE		37.62-
131UbiquitinationHLLDFQGKQQNKHVF
HHHHCCCCCCCEEEE		37.6222817900
135UbiquitinationFQGKQQNKHVFFFDT
CCCCCCCEEEEEEEC		36.49-
135UbiquitinationFQGKQQNKHVFFFDT
CCCCCCCEEEEEEEC		36.4922817900
143SumoylationHVFFFDTKKEVEQFD
EEEEEECHHHHHHHC		49.10-
1432-HydroxyisobutyrylationHVFFFDTKKEVEQFD
EEEEEECHHHHHHHC		49.10-
143SumoylationHVFFFDTKKEVEQFD
EEEEEECHHHHHHHC		49.1028112733
144SumoylationVFFFDTKKEVEQFDV
EEEEECHHHHHHHCH		69.9128112733
144UbiquitinationVFFFDTKKEVEQFDV
EEEEECHHHHHHHCH		69.9129967540
176SumoylationPRIETLQKEKVKGVT
CHHHHHHHHHCCCCC		63.72-
176SumoylationPRIETLQKEKVKGVT
CHHHHHHHHHCCCCC		63.72-
176UbiquitinationPRIETLQKEKVKGVT
CHHHHHHHHHCCCCC		63.7229967540
177UbiquitinationRIETLQKEKVKGVTN
HHHHHHHHHCCCCCC		50.5521890473
178UbiquitinationIETLQKEKVKGVTNQ
HHHHHHHHCCCCCCH		57.17-
180SumoylationTLQKEKVKGVTNQTG
HHHHHHCCCCCCHHH		59.75-
180SumoylationTLQKEKVKGVTNQTG
HHHHHHCCCCCCHHH		59.7528112733
180UbiquitinationTLQKEKVKGVTNQTG
HHHHHHCCCCCCHHH		59.7529967540
189SumoylationVTNQTGLKRIAKERQ
CCCHHHHHHHHHHHH		43.00-
189AcetylationVTNQTGLKRIAKERQ
CCCHHHHHHHHHHHH		43.0025953088
189SumoylationVTNQTGLKRIAKERQ
CCCHHHHHHHHHHHH		43.00-
189UbiquitinationVTNQTGLKRIAKERQ
CCCHHHHHHHHHHHH		43.0029967540
197AcetylationRIAKERQKQYNCLTQ
HHHHHHHHHHCHHHH		62.0526051181
197UbiquitinationRIAKERQKQYNCLTQ
HHHHHHHHHHCHHHH		62.0529967540
199PhosphorylationAKERQKQYNCLTQRI
HHHHHHHHCHHHHHH		18.1928152594
211SumoylationQRIEREKKLFVIAQK
HHHHHHHHHHHHHHH		42.26-
211SumoylationQRIEREKKLFVIAQK
HHHHHHHHHHHHHHH		42.2628112733
211UbiquitinationQRIEREKKLFVIAQK
HHHHHHHHHHHHHHH		42.2629967540
218AcetylationKLFVIAQKIQTRKDL
HHHHHHHHHHCCHHH		27.9726051181
218SumoylationKLFVIAQKIQTRKDL
HHHHHHHHHHCCHHH		27.9728112733
218UbiquitinationKLFVIAQKIQTRKDL
HHHHHHHHHHCCHHH		27.97-
228AcetylationTRKDLMDKTQKVKVK
CCHHHHHHHHCCEEE		38.6091167
228UbiquitinationTRKDLMDKTQKVKVK
CCHHHHHHHHCCEEE		38.6030230243
231AcetylationDLMDKTQKVKVKKET
HHHHHHHCCEEEHHH		49.6291171
231UbiquitinationDLMDKTQKVKVKKET
HHHHHHHCCEEEHHH		49.62-
233AcetylationMDKTQKVKVKKETVN
HHHHHCCEEEHHHCC		56.2091175
235SumoylationKTQKVKVKKETVNSP
HHHCCEEEHHHCCCH		38.89-
235SumoylationKTQKVKVKKETVNSP
HHHCCEEEHHHCCCH		38.8928112733
236SumoylationTQKVKVKKETVNSPA
HHCCEEEHHHCCCHH		62.7028112733
236UbiquitinationTQKVKVKKETVNSPA
HHCCEEEHHHCCCHH		62.7029967540
238PhosphorylationKVKVKKETVNSPAIY
CCEEEHHHCCCHHHH		33.5930266825
241PhosphorylationVKKETVNSPAIYKFQ
EEHHHCCCHHHHHCH		16.0423401153
245PhosphorylationTVNSPAIYKFQSRRK
HCCCHHHHHCHHHCC		14.0924732914
246UbiquitinationVNSPAIYKFQSRRKR
CCCHHHHHCHHHCCC		30.7121890473
246SumoylationVNSPAIYKFQSRRKR
CCCHHHHHCHHHCCC		30.71-
246AcetylationVNSPAIYKFQSRRKR
CCCHHHHHCHHHCCC		30.7126051181
246SumoylationVNSPAIYKFQSRRKR
CCCHHHHHCHHHCCC		30.7128112733
246UbiquitinationVNSPAIYKFQSRRKR
CCCHHHHHCHHHCCC		30.7121906983
249PhosphorylationPAIYKFQSRRKR---
HHHHHCHHHCCC---		36.8719845377
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 UTP11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP11_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 UTP11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP70_HUMANCEP70physical
25416956
THNS1_HUMANTHNSL1physical
26186194
KLH41_HUMANKLHL41physical
26186194
SPRR3_HUMANSPRR3physical
26186194
CRNN_HUMANCRNNphysical
26186194
RRP15_HUMANRRP15physical
26344197
KLH41_HUMANKLHL41physical
28514442
THNS1_HUMANTHNSL1physical
28514442
CRNN_HUMANCRNNphysical
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 UTP11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-241, 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-241, 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 TYR-50, AND MASSSPECTROMETRY.

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