RRP15_HUMAN - dbPTM
RRP15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP15_HUMAN
UniProt AC Q9Y3B9
Protein Name RRP15-like protein
Gene Name RRP15
Organism Homo sapiens (Human).
Sequence Length 282
Subcellular Localization
Protein Description
Protein Sequence MAAAAPDSRVSEEENLKKTPKKKMKMVTGAVASVLEDEATDTSDSEGSCGSEKDHFYSDDDAIEADSEGDAEPCDKENENDGESSVGTNMGWADAMAKVLNKKTPESKPTILVKNKKLEKEKEKLKQERLEKIKQRDKRLEWEMMCRVKPDVVQDKETERNLQRIATRGVVQLFNAVQKHQKNVDEKVKEAGSSMRKRAKLISTVSKKDFISVLRGMDGSTNETASSRKKPKAKQTEVKSEEGPGWTILRDDFMMGASMKDWDKESDGPDDSRPESASDSDT
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
2Acetylation------MAAAAPDSR
------CCCCCCCCC		13.0521406692
8PhosphorylationMAAAAPDSRVSEEEN
CCCCCCCCCCCHHHH		33.2623401153
9CitrullinationAAAAPDSRVSEEENL
CCCCCCCCCCHHHHH		43.28-
9CitrullinationAAAAPDSRVSEEENL
CCCCCCCCCCHHHHH		43.28-
11PhosphorylationAAPDSRVSEEENLKK
CCCCCCCCHHHHHHC		37.8729255136
17AcetylationVSEEENLKKTPKKKM
CCHHHHHHCCCHHHH		67.2125953088
19PhosphorylationEEENLKKTPKKKMKM
HHHHHHCCCHHHHHH		38.4626055452
33PhosphorylationMVTGAVASVLEDEAT
HHHHHHHHHHHCCCC		22.1920873877
40PhosphorylationSVLEDEATDTSDSEG
HHHHCCCCCCCCCCC		37.4528348404
42PhosphorylationLEDEATDTSDSEGSC
HHCCCCCCCCCCCCC		30.0328348404
43PhosphorylationEDEATDTSDSEGSCG
HCCCCCCCCCCCCCC		41.7828348404
45PhosphorylationEATDTSDSEGSCGSE
CCCCCCCCCCCCCCC		43.5628348404
48PhosphorylationDTSDSEGSCGSEKDH
CCCCCCCCCCCCCCC		15.9720873877
51PhosphorylationDSEGSCGSEKDHFYS
CCCCCCCCCCCCCCC		45.8925159151
57PhosphorylationGSEKDHFYSDDDAIE
CCCCCCCCCCCHHCC		14.0522617229
58PhosphorylationSEKDHFYSDDDAIEA
CCCCCCCCCCHHCCC		33.3526503892
67PhosphorylationDDAIEADSEGDAEPC
CHHCCCCCCCCCCCC		50.9926503892
84PhosphorylationENENDGESSVGTNMG
CCCCCCCCCCCCHHH		35.5325159151
85PhosphorylationNENDGESSVGTNMGW
CCCCCCCCCCCHHHH		21.9228985074
88PhosphorylationDGESSVGTNMGWADA
CCCCCCCCHHHHHHH		21.6327251275
102AcetylationAMAKVLNKKTPESKP
HHHHHHCCCCCCCCC		54.597340243
103AcetylationMAKVLNKKTPESKPT
HHHHHCCCCCCCCCE		69.147340253
104PhosphorylationAKVLNKKTPESKPTI
HHHHCCCCCCCCCEE		33.6229255136
107PhosphorylationLNKKTPESKPTILVK
HCCCCCCCCCEEEEE		45.1725159151
108SumoylationNKKTPESKPTILVKN
CCCCCCCCCEEEEEC		44.5128112733
108AcetylationNKKTPESKPTILVKN
CCCCCCCCCEEEEEC		44.5123954790
108UbiquitinationNKKTPESKPTILVKN
CCCCCCCCCEEEEEC		44.5133845483
110PhosphorylationKTPESKPTILVKNKK
CCCCCCCEEEEECHH		30.5823927012
114AcetylationSKPTILVKNKKLEKE
CCCEEEEECHHHHHH		60.6526051181
149UbiquitinationWEMMCRVKPDVVQDK
HHHHHCCCCCCCCCH		19.0229967540
156AcetylationKPDVVQDKETERNLQ
CCCCCCCHHHHHHHH		49.8225953088
156UbiquitinationKPDVVQDKETERNLQ
CCCCCCCHHHHHHHH		49.8224816145
179UbiquitinationQLFNAVQKHQKNVDE
HHHHHHHHHHCCHHH		41.2123000965
179SumoylationQLFNAVQKHQKNVDE
HHHHHHHHHHCCHHH		41.2128112733
179AcetylationQLFNAVQKHQKNVDE
HHHHHHHHHHCCHHH		41.2125953088
182UbiquitinationNAVQKHQKNVDEKVK
HHHHHHHCCHHHHHH		59.6723000965
193PhosphorylationEKVKEAGSSMRKRAK
HHHHHHHHHHHHHHH		28.1924732914
194PhosphorylationKVKEAGSSMRKRAKL
HHHHHHHHHHHHHHH		22.9924732914
200AcetylationSSMRKRAKLISTVSK
HHHHHHHHHHHHCCH		50.8425953088
200UbiquitinationSSMRKRAKLISTVSK
HHHHHHHHHHHHCCH		50.8433845483
203PhosphorylationRKRAKLISTVSKKDF
HHHHHHHHHCCHHHH		32.9426434776
204PhosphorylationKRAKLISTVSKKDFI
HHHHHHHHCCHHHHH		23.0828387310
206PhosphorylationAKLISTVSKKDFISV
HHHHHHCCHHHHHHH		33.7926434776
207UbiquitinationKLISTVSKKDFISVL
HHHHHCCHHHHHHHH		52.6123000965
2072-HydroxyisobutyrylationKLISTVSKKDFISVL
HHHHHCCHHHHHHHH		52.61-
207AcetylationKLISTVSKKDFISVL
HHHHHCCHHHHHHHH		52.6125953088
208UbiquitinationLISTVSKKDFISVLR
HHHHCCHHHHHHHHC		50.8223000965
208SumoylationLISTVSKKDFISVLR
HHHHCCHHHHHHHHC		50.8228112733
208AcetylationLISTVSKKDFISVLR
HHHHCCHHHHHHHHC		50.8291183
212PhosphorylationVSKKDFISVLRGMDG
CCHHHHHHHHCCCCC		18.3228387310
220PhosphorylationVLRGMDGSTNETASS
HHCCCCCCCCCCHHH		24.6429255136
221PhosphorylationLRGMDGSTNETASSR
HCCCCCCCCCCHHHC		42.4729255136
224PhosphorylationMDGSTNETASSRKKP
CCCCCCCCHHHCCCC		33.6329255136
226PhosphorylationGSTNETASSRKKPKA
CCCCCCHHHCCCCCC		37.7929255136
227PhosphorylationSTNETASSRKKPKAK
CCCCCHHHCCCCCCC		45.7325262027
234UbiquitinationSRKKPKAKQTEVKSE
HCCCCCCCCCCCCCC		64.9722817900
239SumoylationKAKQTEVKSEEGPGW
CCCCCCCCCCCCCCC		46.0125114211
239UbiquitinationKAKQTEVKSEEGPGW
CCCCCCCCCCCCCCC		46.0122817900
239SumoylationKAKQTEVKSEEGPGW
CCCCCCCCCCCCCCC		46.01-
240PhosphorylationAKQTEVKSEEGPGWT
CCCCCCCCCCCCCCE		46.1621815630
258PhosphorylationDDFMMGASMKDWDKE
CCCCCCCCCCCCCCC		22.1921815630
266PhosphorylationMKDWDKESDGPDDSR
CCCCCCCCCCCCCCC		54.3221082442
272PhosphorylationESDGPDDSRPESASD
CCCCCCCCCCCCCCC		58.0523927012
276PhosphorylationPDDSRPESASDSDT-
CCCCCCCCCCCCCC-		35.4425159151
278PhosphorylationDSRPESASDSDT---
CCCCCCCCCCCC---		47.1025159151
280PhosphorylationRPESASDSDT-----
CCCCCCCCCC-----		40.4328355574
282PhosphorylationESASDSDT-------
CCCCCCCC-------		44.4525159151
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 RRP15_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP15_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 RRP15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DDX27_HUMANDDX27physical
26344197
DDX54_HUMANDDX54physical
26344197
MK67I_HUMANNIFKphysical
26344197
PK1IP_HUMANPAK1IP1physical
26344197
RBM28_HUMANRBM28physical
26344197
RPF2_HUMANRPF2physical
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 RRP15_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS 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-11; SER-67; THR-104;SER-107 AND SER-226, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS 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 THR-104; SER-266; SER-276;SER-278 AND SER-280, AND MASS 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-11; SER-67; THR-104;SER-107 AND SER-226, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ANDMASS SPECTROMETRY.
"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-280, AND MASSSPECTROMETRY.

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