RRP1B_HUMAN - dbPTM
RRP1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP1B_HUMAN
UniProt AC Q14684
Protein Name Ribosomal RNA processing protein 1 homolog B
Gene Name RRP1B
Organism Homo sapiens (Human).
Sequence Length 758
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Chromosome . Predominantly located in the nucleolus with a small amount found in the nucleoplasm (PubMed:20926688). Associates with the perichromatin region during metaphase and with cytoplasmic foci during
Protein Description Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1. [PubMed: 20040599 Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus]
Protein Sequence MAPAMQPAEIQFAQRLASSEKGIRDRAVKKLRQYISVKTQRETGGFSQEELLKIWKGLFYCMWVQDEPLLQEELANTIAQLVHAVNNSAAQHLFIQTFWQTMNREWKGIDRLRLDKYYMLIRLVLRQSFEVLKRNGWEESRIKVFLDVLMKEVLCPESQSPNGVRFHFIDIYLDELSKVGGKELLADQNLKFIDPFCKIAAKTKDHTLVQTIARGVFEAIVDQSPFVPEETMEEQKTKVGDGDLSAEEIPENEVSLRRAVSKKKTALGKNHSRKDGLSDERGRDDCGTFEDTGPLLQFDYKAVADRLLEMTSRKNTPHFNRKRLSKLIKKFQDLSEGSSISQLSFAEDISADEDDQILSQGKHKKKGNKLLEKTNLEKEKGSRVFCVEEEDSESSLQKRRRKKKKKHHLQPENPGPGGAAPSLEQNRGREPEASGLKALKARVAEPGAEATSSTGEESGSEHPPAVPMHNKRKRPRKKSPRAHREMLESAVLPPEDMSQSGPSGSHPQGPRGSPTGGAQLLKRKRKLGVVPVNGSGLSTPAWPPLQQEGPPTGPAEGANSHTTLPQRRRLQKKKAGPGSLELCGLPSQKTASLKKRKKMRVMSNLVEHNGVLESEAGQPQALGSSGTCSSLKKQKLRAESDFVKFDTPFLPKPLFFRRAKSSTATHPPGPAVQLNKTPSSSKKVTFGLNRNMTAEFKKTDKSILVSPTGPSRVAFDPEQKPLHGVLKTPTSSPASSPLVAKKPLTTTPRRRPRAMDFF
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
5Sulfoxidation---MAPAMQPAEIQF
---CCCCCCHHHHHH		4.8321406390
212-HydroxyisobutyrylationQRLASSEKGIRDRAV
HHHHHCCCCHHHHHH		62.68-
21AcetylationQRLASSEKGIRDRAV
HHHHHCCCCHHHHHH		62.6825953088
21UbiquitinationQRLASSEKGIRDRAV
HHHHHCCCCHHHHHH		62.6824816145
38AcetylationLRQYISVKTQRETGG
HHHHHCCCCCHHCCC		31.9525953088
47PhosphorylationQRETGGFSQEELLKI
CHHCCCCCHHHHHHH		39.7030266825
116AcetylationIDRLRLDKYYMLIRL
CCHHHHHHHHHHHHH		42.7626051181
128PhosphorylationIRLVLRQSFEVLKRN
HHHHHHHHHHHHHHC		19.5524719451
151AcetylationVFLDVLMKEVLCPES
HHHHHHHHHHHCCCC		40.2726051181
160PhosphorylationVLCPESQSPNGVRFH
HHCCCCCCCCCCEEE		29.6121815630
164 (in isoform 2)Ubiquitination-8.2021890473
178AcetylationIYLDELSKVGGKELL
EEHHHHHHCCCCHHH		58.4826051181
182AcetylationELSKVGGKELLADQN
HHHHCCCCHHHCCCC		38.9827452117
182UbiquitinationELSKVGGKELLADQN
HHHHCCCCHHHCCCC		38.9821906983
182 (in isoform 1)Ubiquitination-38.9821890473
191AcetylationLLADQNLKFIDPFCK
HHCCCCCCCCCCCHH		48.0726051181
191UbiquitinationLLADQNLKFIDPFCK
HHCCCCCCCCCCCHH		48.0729967540
197S-nitrosocysteineLKFIDPFCKIAAKTK
CCCCCCCHHHHHCCC		3.66-
197S-nitrosylationLKFIDPFCKIAAKTK
CCCCCCCHHHHHCCC		3.6619483679
198AcetylationKFIDPFCKIAAKTKD
CCCCCCHHHHHCCCC		35.4426051181
198UbiquitinationKFIDPFCKIAAKTKD
CCCCCCHHHHHCCCC		35.4429967540
2042-HydroxyisobutyrylationCKIAAKTKDHTLVQT
HHHHHCCCCCHHHHH		46.97-
204UbiquitinationCKIAAKTKDHTLVQT
HHHHHCCCCCHHHHH		46.9729967540
224PhosphorylationFEAIVDQSPFVPEET
HHHHHCCCCCCCHHH		18.8226074081
231PhosphorylationSPFVPEETMEEQKTK
CCCCCHHHHHHHCCC		28.3723532336
237PhosphorylationETMEEQKTKVGDGDL
HHHHHHCCCCCCCCC		30.5622617229
238UbiquitinationTMEEQKTKVGDGDLS
HHHHHCCCCCCCCCC		51.7829967540
245PhosphorylationKVGDGDLSAEEIPEN
CCCCCCCCHHHCCCC		38.0719664994
255PhosphorylationEIPENEVSLRRAVSK
HCCCCHHHHHHHHHH		15.2422167270
261PhosphorylationVSLRRAVSKKKTALG
HHHHHHHHHHHCCCC		37.4626074081
262UbiquitinationSLRRAVSKKKTALGK
HHHHHHHHHHCCCCC		52.2524816145
265PhosphorylationRAVSKKKTALGKNHS
HHHHHHHCCCCCCCC		35.67-
278PhosphorylationHSRKDGLSDERGRDD
CCCCCCCCCCCCCCC		42.8521815630
286GlutathionylationDERGRDDCGTFEDTG
CCCCCCCCCCCCCCC		6.9222555962
292PhosphorylationDCGTFEDTGPLLQFD
CCCCCCCCCCHHHHC		33.2429214152
306MethylationDYKAVADRLLEMTSR
CHHHHHHHHHHHHHC		31.28115492929
314UbiquitinationLLEMTSRKNTPHFNR
HHHHHHCCCCCCCCH		66.0129967540
316PhosphorylationEMTSRKNTPHFNRKR
HHHHCCCCCCCCHHH		22.6028555341
335PhosphorylationIKKFQDLSEGSSISQ
HHHHHHHCCCCCHHH		48.4720873877
338PhosphorylationFQDLSEGSSISQLSF
HHHHCCCCCHHHHHH		22.0520873877
339PhosphorylationQDLSEGSSISQLSFA
HHHCCCCCHHHHHHC		36.8020873877
341PhosphorylationLSEGSSISQLSFAED
HCCCCCHHHHHHCCC		27.3229632367
344PhosphorylationGSSISQLSFAEDISA
CCCHHHHHHCCCCCC		18.1230266825
350PhosphorylationLSFAEDISADEDDQI
HHHCCCCCCCCCHHH		41.8230266825
359PhosphorylationDEDDQILSQGKHKKK
CCCHHHHHCCCCHHH		38.2230266825
369AcetylationKHKKKGNKLLEKTNL
CCHHHHCHHHHHCCC		64.2212440423
3732-HydroxyisobutyrylationKGNKLLEKTNLEKEK
HHCHHHHHCCCCCCC		42.56-
3782-HydroxyisobutyrylationLEKTNLEKEKGSRVF
HHHCCCCCCCCCCEE		68.82-
386CarbamidationEKGSRVFCVEEEDSE
CCCCCEEEECCCCCH		3.2617322306
386GlutathionylationEKGSRVFCVEEEDSE
CCCCCEEEECCCCCH		3.2622555962
392PhosphorylationFCVEEEDSESSLQKR
EEECCCCCHHHHHHH		42.5329255136
394PhosphorylationVEEEDSESSLQKRRR
ECCCCCHHHHHHHHH		40.0630266825
395PhosphorylationEEEDSESSLQKRRRK
CCCCCHHHHHHHHHH		30.6723401153
398AcetylationDSESSLQKRRRKKKK
CCHHHHHHHHHHHHH		53.8426051181
422PhosphorylationGPGGAAPSLEQNRGR
CCCCCCCHHHHHCCC		39.5525159151
434PhosphorylationRGREPEASGLKALKA
CCCCCCHHHHHHHHH		42.8918669648
437UbiquitinationEPEASGLKALKARVA
CCCHHHHHHHHHHHC		56.0224816145
451PhosphorylationAEPGAEATSSTGEES
CCCCCCCCCCCCCCC		18.0823401153
452PhosphorylationEPGAEATSSTGEESG
CCCCCCCCCCCCCCC		32.7123401153
453PhosphorylationPGAEATSSTGEESGS
CCCCCCCCCCCCCCC		35.7629255136
454PhosphorylationGAEATSSTGEESGSE
CCCCCCCCCCCCCCC		48.6729255136
458PhosphorylationTSSTGEESGSEHPPA
CCCCCCCCCCCCCCC		43.2329255136
460PhosphorylationSTGEESGSEHPPAVP
CCCCCCCCCCCCCCC		41.8529255136
471AcetylationPAVPMHNKRKRPRKK
CCCCCCCCCCCCCCC		44.6226051181
479PhosphorylationRKRPRKKSPRAHREM
CCCCCCCCHHHHHHH		23.7426074081
489PhosphorylationAHREMLESAVLPPED
HHHHHHHHHCCCHHH		21.5126074081
498PhosphorylationVLPPEDMSQSGPSGS
CCCHHHHHCCCCCCC		33.2522199227
500PhosphorylationPPEDMSQSGPSGSHP
CHHHHHCCCCCCCCC		45.4226074081
503PhosphorylationDMSQSGPSGSHPQGP
HHHCCCCCCCCCCCC		57.3527174698
505PhosphorylationSQSGPSGSHPQGPRG
HCCCCCCCCCCCCCC		36.0126074081
513PhosphorylationHPQGPRGSPTGGAQL
CCCCCCCCCCCHHHH		22.1429255136
515PhosphorylationQGPRGSPTGGAQLLK
CCCCCCCCCHHHHHH		50.3630266825
522AcetylationTGGAQLLKRKRKLGV
CCHHHHHHCCCCCCC		65.5525953088
522MethylationTGGAQLLKRKRKLGV
CCHHHHHHCCCCCCC		65.55115977411
522UbiquitinationTGGAQLLKRKRKLGV
CCHHHHHHCCCCCCC		65.5524816145
535PhosphorylationGVVPVNGSGLSTPAW
CCEECCCCCCCCCCC		31.2122210691
538PhosphorylationPVNGSGLSTPAWPPL
ECCCCCCCCCCCCCC		35.5522210691
539PhosphorylationVNGSGLSTPAWPPLQ
CCCCCCCCCCCCCCC		23.28-
579PhosphorylationKKKAGPGSLELCGLP
HCCCCCCCCHHCCCC		23.0825159151
583GlutathionylationGPGSLELCGLPSQKT
CCCCCHHCCCCCCCC		3.7222555962
587PhosphorylationLELCGLPSQKTASLK
CHHCCCCCCCCCCCH		49.7224667141
592PhosphorylationLPSQKTASLKKRKKM
CCCCCCCCCHHHHHH		46.0526074081
624PhosphorylationGQPQALGSSGTCSSL
CCCCHHCCCCCCHHH		26.8425159151
625PhosphorylationQPQALGSSGTCSSLK
CCCHHCCCCCCHHHH		36.0025159151
627PhosphorylationQALGSSGTCSSLKKQ
CHHCCCCCCHHHHHH		15.9125159151
629PhosphorylationLGSSGTCSSLKKQKL
HCCCCCCHHHHHHHH		38.2425159151
630PhosphorylationGSSGTCSSLKKQKLR
CCCCCCHHHHHHHHH		46.4825159151
632AcetylationSGTCSSLKKQKLRAE
CCCCHHHHHHHHHHC		55.9225953088
634 (in isoform 2)Ubiquitination-48.7221890473
640PhosphorylationKQKLRAESDFVKFDT
HHHHHHCCCCCCCCC		35.0525159151
647PhosphorylationSDFVKFDTPFLPKPL
CCCCCCCCCCCCCCC		21.0522199227
652AcetylationFDTPFLPKPLFFRRA
CCCCCCCCCCCEEEC		57.4019608861
652UbiquitinationFDTPFLPKPLFFRRA
CCCCCCCCCCCEEEC		57.4022817900
652 (in isoform 1)Ubiquitination-57.4021890473
661PhosphorylationLFFRRAKSSTATHPP
CCEEECCCCCCCCCC		31.7528450419
662PhosphorylationFFRRAKSSTATHPPG
CEEECCCCCCCCCCC		22.7330576142
663PhosphorylationFRRAKSSTATHPPGP
EEECCCCCCCCCCCC		42.5428450419
665PhosphorylationRAKSSTATHPPGPAV
ECCCCCCCCCCCCCE		34.7028450419
676AcetylationGPAVQLNKTPSSSKK
CCCEECCCCCCCCCC		71.1026051181
677PhosphorylationPAVQLNKTPSSSKKV
CCEECCCCCCCCCCE		27.5923927012
679PhosphorylationVQLNKTPSSSKKVTF
EECCCCCCCCCCEEE		53.1023927012
680PhosphorylationQLNKTPSSSKKVTFG
ECCCCCCCCCCEEEE		47.5925159151
681PhosphorylationLNKTPSSSKKVTFGL
CCCCCCCCCCEEEEE		40.6123927012
693PhosphorylationFGLNRNMTAEFKKTD
EEECCCCCEEEECCC		26.9528555341
699PhosphorylationMTAEFKKTDKSILVS
CCEEEECCCCCEEEC		49.6124732914
701UbiquitinationAEFKKTDKSILVSPT
EEEECCCCCEEECCC		44.6324816145
702PhosphorylationEFKKTDKSILVSPTG
EEECCCCCEEECCCC		24.7830266825
706PhosphorylationTDKSILVSPTGPSRV
CCCCEEECCCCCCCC		17.1919664994
708PhosphorylationKSILVSPTGPSRVAF
CCEEECCCCCCCCEE		54.9730266825
711PhosphorylationLVSPTGPSRVAFDPE
EECCCCCCCCEECCC		40.5130183078
712CitrullinationVSPTGPSRVAFDPEQ
ECCCCCCCCEECCCC		27.24-
712CitrullinationVSPTGPSRVAFDPEQ
ECCCCCCCCEECCCC		27.24-
720AcetylationVAFDPEQKPLHGVLK
CEECCCCCCCCCCCC		48.1323749302
727MethylationKPLHGVLKTPTSSPA
CCCCCCCCCCCCCCC		50.48115977419
728PhosphorylationPLHGVLKTPTSSPAS
CCCCCCCCCCCCCCC		27.8629255136
730PhosphorylationHGVLKTPTSSPASSP
CCCCCCCCCCCCCCC		47.2529255136
731O-linked_GlycosylationGVLKTPTSSPASSPL
CCCCCCCCCCCCCCC		35.2119664995
731O-linked_GlycosylationGVLKTPTSSPASSPL
CCCCCCCCCCCCCCC		35.2119664995
731PhosphorylationGVLKTPTSSPASSPL
CCCCCCCCCCCCCCC		35.2129255136
732PhosphorylationVLKTPTSSPASSPLV
CCCCCCCCCCCCCCC		27.2819664994
735PhosphorylationTPTSSPASSPLVAKK
CCCCCCCCCCCCCCC		35.5529255136
736PhosphorylationPTSSPASSPLVAKKP
CCCCCCCCCCCCCCC		25.1029255136
741AcetylationASSPLVAKKPLTTTP
CCCCCCCCCCCCCCC		47.6625953088
745PhosphorylationLVAKKPLTTTPRRRP
CCCCCCCCCCCCCCC		36.8320068231
746PhosphorylationVAKKPLTTTPRRRPR
CCCCCCCCCCCCCCC		42.3530576142
747PhosphorylationAKKPLTTTPRRRPRA
CCCCCCCCCCCCCCC		15.0126055452
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 RRP1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP1B_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 RRP1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LC7L3_HUMANLUC7L3physical
19710015
YBOX3_HUMANYBX3physical
19710015
CUBN_HUMANCUBNphysical
19710015
DDX21_HUMANDDX21physical
19710015
H1X_HUMANH1FXphysical
19710015
ROA1_HUMANHNRNPA1physical
19710015
ILF3_HUMANILF3physical
19710015
LARP1_HUMANLARP1physical
19710015
LC7L2_HUMANLUC7L2physical
19710015
NUCL_HUMANNCLphysical
19710015
NPM_HUMANNPM1physical
19710015
PARP1_HUMANPARP1physical
19710015
PP1A_HUMANPPP1CAphysical
19710015
PRP4B_HUMANPRPF4Bphysical
19710015
RL10A_HUMANRPL10Aphysical
19710015
RL4_HUMANRPL4physical
19710015
RL5_HUMANRPL5physical
19710015
RLA0_HUMANRPLP0physical
19710015
RL1D1_HUMANRSL1D1physical
19710015
SDF2L_HUMANSDF2L1physical
19710015
SRSF1_HUMANSRSF1physical
19710015
SRSF6_HUMANSRSF6physical
19710015
S22AB_HUMANSLC22A11physical
19710015
THOC4_HUMANALYREFphysical
19710015
TOP1_HUMANTOP1physical
19710015
PP1R7_HUMANPPP1R7physical
27173435
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 RRP1B_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-350; SER-732AND SER-735, AND MASS SPECTROMETRY.
"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-245; SER-392; THR-451;SER-453; THR-454; SER-458; SER-460; SER-513; SER-706; THR-728;SER-731; SER-732 AND SER-736, 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 SER-245; SER-350; SER-392;SER-394; SER-395; SER-452; SER-453; SER-458; SER-702; SER-706; SER-732AND SER-736, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-513, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, 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-245; SER-513; THR-515;SER-706; SER-711; SER-732 AND SER-736, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND THR-747, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-513 ANDSER-706, AND MASS SPECTROMETRY.
"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-245, AND MASSSPECTROMETRY.

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