RRP1B_MOUSE - dbPTM
RRP1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP1B_MOUSE
UniProt AC Q91YK2
Protein Name Ribosomal RNA processing protein 1 homolog B
Gene Name Rrp1b
Organism Mus musculus (Mouse).
Sequence Length 724
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm . Chromosome . Predominantly located in the nucleolus with a small amount found in the nucleoplasm. Associates with the perichromatin region during metaphase and with cytoplasmic foci during telophase before
Protein Description Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (By similarity). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (By similarity). Involved in regulation of mRNA splicing. [PubMed: 23604122 Inhibits SIPA1 GTPase activity]
Protein Sequence MALAMQSSEFQFAQRLASSEKGVRDRAVRKLRQYLSARTQSDTGSFSQEELLKIWKGLFYCMWVQDEPLLQEELANIISQLIHVVNSLEAQYLFIQTFWQTMNREWQGIDKLQLDKYYMLIRLVLRQSFEVLKRNAWEESQITLFLDILMKEILSPESQSPNGVRTHLIDVYLEELTTVGGAELLADQNLKLIDPFCRIAAKTKDHTLVQTVARGVFEVIVDQSACVPQESVEERKTKEDGSGFPTKALACRKAVSGKKAALDECLRDGVIGSRERDICAALKDSGSPLQFDYKAVADRLLEIANSKSTPPFNRKRLCRLVRKFQDLCEGNGAPLSSAEDNGQRRHKRKRKKLLESEKGDTVSPAAEEDSGGHIHKKKRKKRKRSHFQPDTQNLDAVAVPKVPDSESEPDTAQRQAPCGQACVTEPTAEAVSSIGENSSKPTPVMPIHNKRKRPRKKKLRAHKEICKSTTLPQEDMSKNDAVSGHSQSSAAHISSSEGVQAQKRKRKLGALPDSSSDLPVQKSGTPTSPVEGKDGQTTLPRCKRSQKKTASSTLDPCDPSSQKPAISKKKKKTMKLMSNGVLESNPGQIQALGSNRTLKKPLKTEDDFVKFDTRFLPKPLFFRKAKNSSATRPQGPAGQLNKTPSSSKKVTFGLNRNMTAEFKKTDKSILVSPTGLSRVAFNPEQRPLHGVLKTATSSPASTPLSPMRLPATTPKRRPRAADFF
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
128PhosphorylationIRLVLRQSFEVLKRN
HHHHHHHHHHHHHHC		19.5524719451
259AcetylationRKAVSGKKAALDECL
HHHHCCCHHHHHHHH		42.2819858677
285PhosphorylationICAALKDSGSPLQFD
HHHHHHCCCCCCCCC		39.3125619855
287PhosphorylationAALKDSGSPLQFDYK
HHHHCCCCCCCCCHH		26.7925619855
306PhosphorylationRLLEIANSKSTPPFN
HHHHHHCCCCCCCCC		20.9729514104
309PhosphorylationEIANSKSTPPFNRKR
HHHCCCCCCCCCHHH		38.42-
336PhosphorylationEGNGAPLSSAEDNGQ
CCCCCCCCCCCHHHC		26.8323984901
337PhosphorylationGNGAPLSSAEDNGQR
CCCCCCCCCCHHHCH		43.2823984901
363PhosphorylationSEKGDTVSPAAEEDS
CCCCCCCCCCHHCCC		15.7727841257
370PhosphorylationSPAAEEDSGGHIHKK
CCCHHCCCCCCCCHH		50.37-
385PhosphorylationKRKKRKRSHFQPDTQ
HCHHCCHHCCCCCCC		31.5228066266
405PhosphorylationAVPKVPDSESEPDTA
ECCCCCCCCCCCCHH		36.6326824392
407PhosphorylationPKVPDSESEPDTAQR
CCCCCCCCCCCHHHH		59.3822802335
411PhosphorylationDSESEPDTAQRQAPC
CCCCCCCHHHHCCCC		35.0925619855
432PhosphorylationEPTAEAVSSIGENSS
CCCHHHHHHHCCCCC		24.24-
438PhosphorylationVSSIGENSSKPTPVM
HHHHCCCCCCCCCCC		35.12-
494PhosphorylationQSSAAHISSSEGVQA
CCCCHHHCCCCCHHH		20.25-
523PhosphorylationSDLPVQKSGTPTSPV
CCCCCCCCCCCCCCC		30.7025777480
525PhosphorylationLPVQKSGTPTSPVEG
CCCCCCCCCCCCCCC		30.4025777480
527PhosphorylationVQKSGTPTSPVEGKD
CCCCCCCCCCCCCCC		45.5624453211
528PhosphorylationQKSGTPTSPVEGKDG
CCCCCCCCCCCCCCC		28.3125521595
618AcetylationFDTRFLPKPLFFRKA
CCCCCCCCCCCEEEC		57.40-
628PhosphorylationFFRKAKNSSATRPQG
CEEECCCCCCCCCCC		22.2026239621
629PhosphorylationFRKAKNSSATRPQGP
EEECCCCCCCCCCCC		42.9526239621
631PhosphorylationKAKNSSATRPQGPAG
ECCCCCCCCCCCCCC		44.8426239621
643PhosphorylationPAGQLNKTPSSSKKV
CCCCCCCCCCCCCEE		27.5929514104
646PhosphorylationQLNKTPSSSKKVTFG
CCCCCCCCCCEEEEE		47.5929514104
668PhosphorylationEFKKTDKSILVSPTG
ECCCCCCCEEECCCC		24.7829514104
672PhosphorylationTDKSILVSPTGLSRV
CCCCEEECCCCCCCE		17.1926824392
674PhosphorylationKSILVSPTGLSRVAF
CCEEECCCCCCCEEC		43.1624068923
677PhosphorylationLVSPTGLSRVAFNPE
EECCCCCCCEECCCC		26.5021149613
678CitrullinationVSPTGLSRVAFNPEQ
ECCCCCCCEECCCCC		28.9124463520
678CitrullinationVSPTGLSRVAFNPEQ
ECCCCCCCEECCCCC		28.91-
694PhosphorylationPLHGVLKTATSSPAS
CCCCCCCCCCCCCCC		30.8925159016
696PhosphorylationHGVLKTATSSPASTP
CCCCCCCCCCCCCCC		34.6625159016
697PhosphorylationGVLKTATSSPASTPL
CCCCCCCCCCCCCCC		31.6825159016
698PhosphorylationVLKTATSSPASTPLS
CCCCCCCCCCCCCCC		21.8222942356
701PhosphorylationTATSSPASTPLSPMR
CCCCCCCCCCCCCCC		33.6626239621
702PhosphorylationATSSPASTPLSPMRL
CCCCCCCCCCCCCCC		30.2925159016
705PhosphorylationSPASTPLSPMRLPAT
CCCCCCCCCCCCCCC		20.1828725479
712PhosphorylationSPMRLPATTPKRRPR
CCCCCCCCCCCCCCC		41.5125159016
713PhosphorylationPMRLPATTPKRRPRA
CCCCCCCCCCCCCCH		28.9926239621
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP1B_MOUSE !!
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_MOUSE !!
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
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
RRP1B_HUMANRRP1Bphysical
19710015
RL1D1_HUMANRSL1D1physical
19710015
SRSF1_HUMANSRSF1physical
19710015
SRSF6_HUMANSRSF6physical
19710015
THOC4_HUMANALYREFphysical
19710015
C1QBP_HUMANC1QBPphysical
19710015
BOREA_HUMANCDCA8physical
19710015
DDX47_HUMANDDX47physical
19710015
DNJC9_HUMANDNAJC9physical
19710015
ERH_HUMANERHphysical
19710015
RGPA1_HUMANRALGAPA1physical
19710015
HNRL1_HUMANHNRNPUL1physical
19710015
ITAD_HUMANITGADphysical
19710015
LRC59_HUMANLRRC59physical
19710015
LYAR_HUMANLYARphysical
19710015
TAB1_HUMANTAB1physical
19710015
KI67_HUMANMKI67physical
19710015
NEDD1_HUMANNEDD1physical
19710015
KAP0_HUMANPRKAR1Aphysical
19710015
RCN1_HUMANRCN1physical
19710015
SRP14_HUMANSRP14physical
19710015
STAU1_HUMANSTAU1physical
19710015
TIF1B_HUMANTRIM28physical
19710015
TYY2_HUMANYY2physical
19710015
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RRP1B_MOUSE

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Related Literatures of Post-Translational Modification

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