RENT1_MOUSE - dbPTM
RENT1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RENT1_MOUSE
UniProt AC Q9EPU0
Protein Name Regulator of nonsense transcripts 1
Gene Name Upf1
Organism Mus musculus (Mouse).
Sequence Length 1124
Subcellular Localization Cytoplasm. Cytoplasm, P-body. Nucleus. Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm..
Protein Description RNA-dependent helicase and ATPase required for nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD. Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation. UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways. Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2. For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (By similarity). Essential for embryonic viability..
Protein Sequence MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGAGGPGGAGAGGAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPVHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAFFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVVIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLSYYKEQKALVEGPLNNLRESLMQFSKPRKLVNTVNPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSNMYFQTHDQISMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKTKTGRGGRQKNRFGLPGPSQTTLPNSQASQDVASQPFSQGALTQGYVSMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY
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
10PhosphorylationVEAYGPSSQTLTFLD
CEEECCCCCEEEEEE		30.25-
31PhosphorylationLGADTQGSEFEFTDF
HCCCCCCCEEEECCC		29.33-
108PhosphorylationEEDEEDTYYTKDLPV
CCCCCCCCCCCCCCC		22.8122817900
146PhosphorylationFCNGRGNTSGSHIVN
EECCCCCCCCHHHHH		36.97-
195UbiquitinationLLGFIPAKADSVVVL
EEEECCCCCCEEEEE		47.58-
210PhosphorylationLCRQPCASQSSLKDI
EECCCCCCCHHCCCC		36.9928059163
213PhosphorylationQPCASQSSLKDINWD
CCCCCCHHCCCCCCC		31.6228059163
215UbiquitinationCASQSSLKDINWDSS
CCCCHHCCCCCCCCH		59.52-
259UbiquitinationITAQQINKLEELWKE
HHHHHHHHHHHHHHH		59.9322790023
277UbiquitinationATLEDLEKPGVDEEP
CCHHHHHCCCCCCCC		55.1322790023
362UbiquitinationIWLRDMRLMQGDEIC
EEEEECCCCCCCEEE		2.1127667366
369GlutathionylationLMQGDEICLRYKGDL
CCCCCEEEHHCCCCC		1.3424333276
369S-palmitoylationLMQGDEICLRYKGDL
CCCCCEEEHHCCCCC		1.3428526873
373UbiquitinationDEICLRYKGDLAPLW
CEEEHHCCCCCHHHH		39.2422790023
381UbiquitinationGDLAPLWKGIGHVIK
CCCHHHHCCCCEEEE		48.6222790023
425PhosphorylationDFVWKSTSFDRMQSA
EEEEECCCHHHHHHH		32.0423737553
434UbiquitinationDRMQSALKTFAVDET
HHHHHHHHHHCCCCC		41.1122790023
462UbiquitinationEVEDVVIKCQLPKRF
CEEEEEEEECCCCCC		12.3422790023
480PhosphorylationGLPDLNHSQVYAVKT
CCCCCCHHHHHHHHH		21.9225367039
483PhosphorylationDLNHSQVYAVKTVLQ
CCCHHHHHHHHHHHH		9.6822817900
560PhosphorylationKSREAIDSPVSFLAL
CCHHHCCCCHHHHHH		22.53-
571UbiquitinationFLALHNQIRNMDSMP
HHHHHHHHHCCCCCH		4.1127667366
582UbiquitinationDSMPELQKLQQLKDE
CCCHHHHHHHHHHHC		61.9722790023
587AcetylationLQKLQQLKDETGELS
HHHHHHHHHCCCCCC		49.5323954790
588UbiquitinationQKLQQLKDETGELSS
HHHHHHHHCCCCCCH		68.2527667366
594PhosphorylationKDETGELSSADEKRY
HHCCCCCCHHHHHHH		21.1228285833
599UbiquitinationELSSADEKRYRALKR
CCCHHHHHHHHHHHH		56.1027667366
622UbiquitinationNADVICCTCVGAGDP
CCCEEEEECCCCCCH		13.0527667366
633UbiquitinationAGDPRLAKMQFRSIL
CCCHHHHHHHHHEEE		37.5122790023
678GlutathionylationQLGPVVMCKKAAKAG
CCCCCHHHHHHHHCC		2.5024333276
683UbiquitinationVMCKKAAKAGLSQSL
HHHHHHHHCCCCHHH		48.0922790023
774UbiquitinationGTSYLNRTEAANVEK
CCCCCCHHHHCCHHH		28.9827667366
777UbiquitinationYLNRTEAANVEKITT
CCCHHHHCCHHHHHH		17.8627667366
781UbiquitinationTEAANVEKITTKLLK
HHHCCHHHHHHHHHH		40.86-
781MalonylationTEAANVEKITTKLLK
HHHCCHHHHHHHHHH		40.8626320211
785UbiquitinationNVEKITTKLLKAGAK
CHHHHHHHHHHCCCC		43.0822790023
788UbiquitinationKITTKLLKAGAKPDQ
HHHHHHHHCCCCCCC		56.0322790023
924UbiquitinationMQFSKPRKLVNTVNP
HHHCCCCHHHCCCCC		66.37-
924AcetylationMQFSKPRKLVNTVNP
HHHCCCCHHHCCCCC		66.3723806337
924MalonylationMQFSKPRKLVNTVNP
HHHCCCCHHHCCCCC		66.3726320211
941PhosphorylationRFMTTAMYDAREAII
CHHHHHCHHHHHHHC		12.1822817900
951PhosphorylationREAIIPGSVYDRSSQ
HHHHCCCCCCCCCCC		16.4929176673
953PhosphorylationAIIPGSVYDRSSQGR
HHCCCCCCCCCCCCC		13.8225367039
1014MethylationANGPAAGRGTPKTKT
CCCCCCCCCCCCCCC		40.88-
1084PhosphorylationGLSQPELSQDSYLGD
CCCCCCCCCCCCCCH		30.2222503102
1095PhosphorylationYLGDEFKSQIDVALS
CCCHHHHHHHCEECC		37.3825619855
1102PhosphorylationSQIDVALSQDSTYQG
HHHCEECCCCCCCCC		23.3925521595
1105PhosphorylationDVALSQDSTYQGERA
CEECCCCCCCCCCHH		22.7525521595
1106PhosphorylationVALSQDSTYQGERAY
EECCCCCCCCCCHHH		28.3127087446
1107PhosphorylationALSQDSTYQGERAYQ
ECCCCCCCCCCHHHH		20.6225521595
1113PhosphorylationTYQGERAYQHGGVTG
CCCCCHHHHCCCCCC		13.7825619855
1119PhosphorylationAYQHGGVTGLSQY--
HHHCCCCCCCCCC--		35.3625619855
1122PhosphorylationHGGVTGLSQY-----
CCCCCCCCCC-----		28.8617525332
1124PhosphorylationGVTGLSQY-------
CCCCCCCC-------		19.6925521595
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
28TPhosphorylationKinaseSMG1Q96Q15
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RENT1_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 RENT1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RENT1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RENT1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1102 AND SER-1122, ANDMASS SPECTROMETRY.

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