RPF2_HUMAN - dbPTM
RPF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPF2_HUMAN
UniProt AC Q9H7B2
Protein Name Ribosome production factor 2 homolog
Gene Name RPF2
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization Nucleus, nucleolus . Associated with the nucleolus in an RNA-dependent manner.
Protein Description Involved in ribosomal large subunit assembly. May regulate the localization of the 5S RNP/5S ribonucleoprotein particle to the nucleolus..
Protein Sequence MDTLDRVVKPKTKRAKRFLEKREPKLNENIKNAMLIKGGNANATVTKVLKDVYALKKPYGVLYKKKNITRPFEDQTSLEFFSKKSDCSLFMFGSHNKKRPNNLVIGRMYDYHVLDMIELGIENFVSLKDIKNSKCPEGTKPMLIFAGDDFDVTEDYRRLKSLLIDFFRGPTVSNIRLAGLEYVLHFTALNGKIYFRSYKLLLKKSGCRTPRIELEEMGPSLDLVLRRTHLASDDLYKLSMKMPKALKPKKKKNISHDTFGTTYGRIHMQKQDLSKLQTRKMKGLKKRPAERITEDHEKKSKRIKKN
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
1Acetylation-------MDTLDRVV
-------CCHHHHHC		8.84-
6Methylation--MDTLDRVVKPKTK
--CCHHHHHCCCCCH		37.94-
13UbiquitinationRVVKPKTKRAKRFLE
HHCCCCCHHHHHHHH		57.3924816145
20UbiquitinationKRAKRFLEKREPKLN
HHHHHHHHHCCCHHC		47.5629967540
31UbiquitinationPKLNENIKNAMLIKG
CHHCHHHCHHEEEEC		50.6829967540
37UbiquitinationIKNAMLIKGGNANAT
HCHHEEEECCCCCCC		57.7229967540
47AcetylationNANATVTKVLKDVYA
CCCCCHHHHHHHHHH		41.0391019
502-HydroxyisobutyrylationATVTKVLKDVYALKK
CCHHHHHHHHHHHHC		48.40-
50MalonylationATVTKVLKDVYALKK
CCHHHHHHHHHHHHC		48.4032601280
50AcetylationATVTKVLKDVYALKK
CCHHHHHHHHHHHHC		48.4026051181
56AcetylationLKDVYALKKPYGVLY
HHHHHHHHCCCEEEE		43.4691023
57MalonylationKDVYALKKPYGVLYK
HHHHHHHCCCEEEEE		44.3026320211
57AcetylationKDVYALKKPYGVLYK
HHHHHHHCCCEEEEE		44.3026051181
59PhosphorylationVYALKKPYGVLYKKK
HHHHHCCCEEEEECC		28.84-
832-HydroxyisobutyrylationTSLEFFSKKSDCSLF
CCHHHHHCCCCCEEE		51.65-
83AcetylationTSLEFFSKKSDCSLF
CCHHHHHCCCCCEEE		51.6526051181
83UbiquitinationTSLEFFSKKSDCSLF
CCHHHHHCCCCCEEE		51.6529967540
84AcetylationSLEFFSKKSDCSLFM
CHHHHHCCCCCEEEE		50.7826051181
97AcetylationFMFGSHNKKRPNNLV
EEECCCCCCCCCCEE		44.7426051181
98UbiquitinationMFGSHNKKRPNNLVI
EECCCCCCCCCCEEE		77.67-
109PhosphorylationNLVIGRMYDYHVLDM
CEEEEECCCHHHHHH		16.40-
140AcetylationSKCPEGTKPMLIFAG
CCCCCCCCCEEEEEC		39.0126051181
156PhosphorylationDFDVTEDYRRLKSLL
CCCCCHHHHHHHHHH		7.44-
160UbiquitinationTEDYRRLKSLLIDFF
CHHHHHHHHHHHHHH		36.93-
189UbiquitinationYVLHFTALNGKIYFR
EEEEEEEECCEEEEE		8.6829967540
194PhosphorylationTALNGKIYFRSYKLL
EEECCEEEEEEEEHH		9.0920393185
209UbiquitinationLKKSGCRTPRIELEE
HHHCCCCCCCEEHHH		22.4624816145
212UbiquitinationSGCRTPRIELEEMGP
CCCCCCCEEHHHHCC		8.1429967540
220PhosphorylationELEEMGPSLDLVLRR
EHHHHCCCHHHHHHH		28.8720860994
236PhosphorylationHLASDDLYKLSMKMP
CCCCHHHHHHHHCCC		19.51-
236UbiquitinationHLASDDLYKLSMKMP
CCCCHHHHHHHHCCC		19.5124816145
239PhosphorylationSDDLYKLSMKMPKAL
CHHHHHHHHCCCHHC		16.5323090842
241UbiquitinationDLYKLSMKMPKALKP
HHHHHHHCCCHHCCC		48.99-
252MalonylationALKPKKKKNISHDTF
HCCCCCCCCCCCCCC		69.2826320211
252AcetylationALKPKKKKNISHDTF
HCCCCCCCCCCCCCC		69.2827452117
252UbiquitinationALKPKKKKNISHDTF
HCCCCCCCCCCCCCC		69.2829967540
255PhosphorylationPKKKKNISHDTFGTT
CCCCCCCCCCCCHHH		25.3825159151
258PhosphorylationKKNISHDTFGTTYGR
CCCCCCCCCHHHHHH		20.6729978859
261PhosphorylationISHDTFGTTYGRIHM
CCCCCCHHHHHHHHH		16.8028442448
262PhosphorylationSHDTFGTTYGRIHMQ
CCCCCHHHHHHHHHC		25.1028442448
263PhosphorylationHDTFGTTYGRIHMQK
CCCCHHHHHHHHHCH		12.3028152594
270UbiquitinationYGRIHMQKQDLSKLQ
HHHHHHCHHHHHHHH		37.90-
2752-HydroxyisobutyrylationMQKQDLSKLQTRKMK
HCHHHHHHHHHHHHC		52.49-
275UbiquitinationMQKQDLSKLQTRKMK
HCHHHHHHHHHHHHC		52.4929967540
278PhosphorylationQDLSKLQTRKMKGLK
HHHHHHHHHHHCCCC		42.5720860994
299UbiquitinationITEDHEKKSKRIKKN
CCCHHHHHHHHHCCC		59.2224816145
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 RPF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPF2_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 RPF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PUM3_HUMANKIAA0020physical
26344197
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPF2_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 MET-1, AND MASS SPECTROMETRY.

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