RRP1_HUMAN - dbPTM
RRP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP1_HUMAN
UniProt AC P56182
Protein Name Ribosomal RNA processing protein 1 homolog A
Gene Name RRP1
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization Nucleus, nucleolus .
Protein Description Plays a critical role in the generation of 28S rRNA..
Protein Sequence MVSRVQLPPEIQLAQRLAGNEQVTRDRAVRKLRKYIVARTQRAAGGFTHDELLKVWKGLFYCMWMQDKPLLQEELGRTISQLVHAFQTTEAQHLFLQAFWQTMNREWTGIDRLRLDKFYMLMRMVLNESLKVLKMQGWEERQIEELLELLMTEILHPSSQAPNGVKSHFIEIFLEELTKVGAEELTADQNLKFIDPFCRIAARTKDSLVLNNITRGIFETIVEQAPLAIEDLLNELDTQDEEVASDSDESSEGGERGDALSQKRSEKPPAGSICRAEPEAGEEQAGDDRDSGGPVLQFDYEAVANRLFEMASRQSTPSQNRKRLYKVIRKLQDLAGGIFPEDEIPEKACRRLLEGRRQKKTKKQKRLLRLQQERGKGEKEPPSPGMERKRSRRRGVGADPEARAEAGEQPGTAERALLRDQPRGRGQRGARQRRRTPRPLTSARAKAANVQEPEKKKKRRE
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
3Phosphorylation-----MVSRVQLPPE
-----CCCCCCCCHH		25.9923312004
24PhosphorylationLAGNEQVTRDRAVRK
HCCCCCCCHHHHHHH		26.9229255136
42UbiquitinationYIVARTQRAAGGFTH
HHHHHHHHHCCCCCH		26.2821963094
54AcetylationFTHDELLKVWKGLFY
CCHHHHHHHHHHHHH		59.6926822725
55UbiquitinationTHDELLKVWKGLFYC
CHHHHHHHHHHHHHH		6.8724816145
192AcetylationLTADQNLKFIDPFCR
CCCCCCCCCCCHHHH		48.0726051181
192UbiquitinationLTADQNLKFIDPFCR
CCCCCCCCCCCHHHH		48.0721906983
204PhosphorylationFCRIAARTKDSLVLN
HHHHHHHCCCCHHHC		34.1820068231
205UbiquitinationCRIAARTKDSLVLNN
HHHHHHCCCCHHHCC		39.5024816145
207PhosphorylationIAARTKDSLVLNNIT
HHHHCCCCHHHCCCC		23.1821406692
209UbiquitinationARTKDSLVLNNITRG
HHCCCCHHHCCCCHH		6.6024816145
220PhosphorylationITRGIFETIVEQAPL
CCHHHHHHHHHHCCH		21.4121406692
238PhosphorylationDLLNELDTQDEEVAS
HHHHHCCCCCHHHHC		51.0121406692
245PhosphorylationTQDEEVASDSDESSE
CCCHHHHCCCCCCCC		42.7121406692
247PhosphorylationDEEVASDSDESSEGG
CHHHHCCCCCCCCCC		40.5621406692
250PhosphorylationVASDSDESSEGGERG
HHCCCCCCCCCCCHH		38.3821406692
251PhosphorylationASDSDESSEGGERGD
HCCCCCCCCCCCHHC		37.9121406692
261PhosphorylationGERGDALSQKRSEKP
CCHHCHHHHHCCCCC		35.0621406692
267UbiquitinationLSQKRSEKPPAGSIC
HHHHCCCCCCCCCCC		58.51-
272PhosphorylationSEKPPAGSICRAEPE
CCCCCCCCCCCCCCC		22.1828674419
291PhosphorylationQAGDDRDSGGPVLQF
CCCCCCCCCCCEEEE		46.6825849741
300PhosphorylationGPVLQFDYEAVANRL
CCEEEECHHHHHHHH		13.6930108239
306UbiquitinationDYEAVANRLFEMASR
CHHHHHHHHHHHHHC		30.8924816145
330AcetylationRLYKVIRKLQDLAGG
HHHHHHHHHHHHHCC		39.1026051181
330UbiquitinationRLYKVIRKLQDLAGG
HHHHHHHHHHHHHCC		39.1029967540
347AcetylationPEDEIPEKACRRLLE
CCHHCCHHHHHHHHH		47.6426051181
347UbiquitinationPEDEIPEKACRRLLE
CCHHCCHHHHHHHHH		47.6429967540
359UbiquitinationLLEGRRQKKTKKQKR
HHHHHHHHCCHHHHH		61.6724816145
379AcetylationQERGKGEKEPPSPGM
HHCCCCCCCCCCCCC		81.7126051181
383PhosphorylationKGEKEPPSPGMERKR
CCCCCCCCCCCHHHH		44.8123401153
391PhosphorylationPGMERKRSRRRGVGA
CCCHHHHHHHCCCCC		32.92-
412PhosphorylationEAGEQPGTAERALLR
HHCCCCCHHHHHHHH		31.8426055452
423MethylationALLRDQPRGRGQRGA
HHHHCCCCCCCHHHH		41.6397770605
427MethylationDQPRGRGQRGARQRR
CCCCCCCHHHHHHHC		38.9926797129
436PhosphorylationGARQRRRTPRPLTSA
HHHHHCCCCCCCHHH		23.1030576142
444MethylationPRPLTSARAKAANVQ
CCCCHHHHHHHHCCC		36.0783448203
455AcetylationANVQEPEKKKKRRE-
HCCCCHHHHHHHCC-		79.2820167786
456UbiquitinationNVQEPEKKKKRRE--
CCCCHHHHHHHCC--		62.9624816145
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 RRP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
427QMethylation

26797129
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 RRP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RRP1_HUMAN !!
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 RRP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-383 AND THR-412, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory