RRP36_HUMAN - dbPTM
RRP36_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP36_HUMAN
UniProt AC Q96EU6
Protein Name Ribosomal RNA processing protein 36 homolog
Gene Name RRP36
Organism Homo sapiens (Human).
Sequence Length 259
Subcellular Localization Nucleus, nucleolus . Concentrated in the fibrillar region of the nucleolus.
Protein Description Involved in the early processing steps of the pre-rRNA in the maturation pathway leading to the 18S rRNA..
Protein Sequence MPGANYRAGAGAGAGARRPRGARDREEDGGGLEPAAVARDLLRGTSNMSFEELLELQSQVGTKTYKQLVAGNSPKKQASRPPIQNACVADKHRPLEMSAKIRVPFLRQVVPISKKVARDPRFDDLSGEYNPEVFDKTYQFLNDIRAKEKELVKKQLKKHLSGEEHEKLQQLLQRMEQQEMAQQERKQQQELHLALKQERRAQAQQGHRPYFLKKSEQRQLALAEKFKELKRSKKLENFLSRKRRRNAGKDRRHLPLSKE
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
7Methylation-MPGANYRAGAGAGA
-CCCCCCCCCCCCCC
26.76115492937
45PhosphorylationARDLLRGTSNMSFEE
HHHHHHCCCCCCHHH
15.5326074081
46PhosphorylationRDLLRGTSNMSFEEL
HHHHHCCCCCCHHHH
33.1026074081
49PhosphorylationLRGTSNMSFEELLEL
HHCCCCCCHHHHHHH
33.4826074081
58PhosphorylationEELLELQSQVGTKTY
HHHHHHHHHHCCCHH
39.1826074081
62PhosphorylationELQSQVGTKTYKQLV
HHHHHHCCCHHHHHH
22.7426074081
64PhosphorylationQSQVGTKTYKQLVAG
HHHHCCCHHHHHHCC
35.4726074081
65PhosphorylationSQVGTKTYKQLVAGN
HHHCCCHHHHHHCCC
9.7826074081
73PhosphorylationKQLVAGNSPKKQASR
HHHHCCCCCCCCCCC
36.8629255136
79PhosphorylationNSPKKQASRPPIQNA
CCCCCCCCCCCCCCC
42.7126074081
98PhosphorylationKHRPLEMSAKIRVPF
CCCCCCCCCEECCCC
19.6222210691
100UbiquitinationRPLEMSAKIRVPFLR
CCCCCCCEECCCCHH
24.6029967540
114AcetylationRQVVPISKKVARDPR
HHHHCCCHHHCCCCC
52.5725953088
115UbiquitinationQVVPISKKVARDPRF
HHHCCCHHHCCCCCC
34.04-
129PhosphorylationFDDLSGEYNPEVFDK
CCCCCCCCCHHHHHH
39.2727642862
136UbiquitinationYNPEVFDKTYQFLND
CCHHHHHHHHHHHHH
37.3529967540
137PhosphorylationNPEVFDKTYQFLNDI
CHHHHHHHHHHHHHH
25.1326546556
138PhosphorylationPEVFDKTYQFLNDIR
HHHHHHHHHHHHHHH
11.7427642862
158AcetylationLVKKQLKKHLSGEEH
HHHHHHHHHCCHHHH
59.377932663
161PhosphorylationKQLKKHLSGEEHEKL
HHHHHHCCHHHHHHH
43.8328985074
167UbiquitinationLSGEEHEKLQQLLQR
CCHHHHHHHHHHHHH
54.2029967540
167AcetylationLSGEEHEKLQQLLQR
CCHHHHHHHHHHHHH
54.2026051181
208UbiquitinationAQAQQGHRPYFLKKS
HHHHCCCCCCCCCHH
34.1429967540
213UbiquitinationGHRPYFLKKSEQRQL
CCCCCCCCHHHHHHH
44.3429967540
219 (in isoform 2)Ubiquitination-30.6821890473
220UbiquitinationKKSEQRQLALAEKFK
CHHHHHHHHHHHHHH
4.6121890473
222UbiquitinationSEQRQLALAEKFKEL
HHHHHHHHHHHHHHH
9.5822817900
225UbiquitinationRQLALAEKFKELKRS
HHHHHHHHHHHHHHH
57.0122817900
225AcetylationRQLALAEKFKELKRS
HHHHHHHHHHHHHHH
57.0125953088
225 (in isoform 1)Ubiquitination-57.0121890473
227UbiquitinationLALAEKFKELKRSKK
HHHHHHHHHHHHHHH
73.5322817900
229UbiquitinationLAEKFKELKRSKKLE
HHHHHHHHHHHHHHH
6.0229967540
230UbiquitinationAEKFKELKRSKKLEN
HHHHHHHHHHHHHHH
56.5722817900
234UbiquitinationKELKRSKKLENFLSR
HHHHHHHHHHHHHHH
63.3829967540
234AcetylationKELKRSKKLENFLSR
HHHHHHHHHHHHHHH
63.3826051181
240PhosphorylationKKLENFLSRKRRRNA
HHHHHHHHHHHHHHC
31.45-

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 RRP36_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP36_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 RRP36_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRP12_HUMANRRP12physical
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 RRP36_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-73, 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-73, 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 SER-73, AND MASSSPECTROMETRY.

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