RENT1_HUMAN - dbPTM
RENT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RENT1_HUMAN
UniProt AC Q92900
Protein Name Regulator of nonsense transcripts 1
Gene Name UPF1
Organism Homo sapiens (Human).
Sequence Length 1129
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 and allowing the recycling of NMD factors. 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. Essential for embryonic viability..
Protein Sequence MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPGPSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY
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
6Phosphorylation--MSVEAYGPSSQTL
--CCCEEECCCCCEE		18.9626074081
9PhosphorylationSVEAYGPSSQTLTFL
CCEEECCCCCEEEEE		30.6226074081
10PhosphorylationVEAYGPSSQTLTFLD
CEEECCCCCEEEEEE		30.2526074081
12PhosphorylationAYGPSSQTLTFLDTE
EECCCCCEEEEEEHH		29.7026074081
14PhosphorylationGPSSQTLTFLDTEEA
CCCCCEEEEEEHHHH		26.0726074081
28PhosphorylationAELLGADTQGSEFEF
HHHHCCCCCCCEEEE		34.0026074081
31PhosphorylationLGADTQGSEFEFTDF
HCCCCCCCEEEECCC		29.3326074081
39PhosphorylationEFEFTDFTLPSQTQT
EEEECCCCCCCCCCC		40.3426074081
42PhosphorylationFTDFTLPSQTQTPPG
ECCCCCCCCCCCCCC		49.3126074081
44PhosphorylationDFTLPSQTQTPPGGP
CCCCCCCCCCCCCCC		38.4526074081
46PhosphorylationTLPSQTQTPPGGPGG
CCCCCCCCCCCCCCC		34.5326074081
112PhosphorylationFEEDEEDTYYTKDLP
CCCCCCCCCCCCCCC		23.0029978859
113PhosphorylationEEDEEDTYYTKDLPI
CCCCCCCCCCCCCCC		22.8129978859
114PhosphorylationEDEEDTYYTKDLPIH
CCCCCCCCCCCCCCE		14.9229978859
115PhosphorylationDEEDTYYTKDLPIHA
CCCCCCCCCCCCCEE		13.9927642862
124PhosphorylationDLPIHACSYCGIHDP
CCCCEECCCCCCCCC		25.0027080861
125PhosphorylationLPIHACSYCGIHDPA
CCCEECCCCCCCCCC		8.4527080861
136PhosphorylationHDPACVVYCNTSKKW
CCCCEEEEECCCCCE		1.9928152594
139PhosphorylationACVVYCNTSKKWFCN
CEEEEECCCCCEEEC		38.0628152594
140PhosphorylationCVVYCNTSKKWFCNG
EEEEECCCCCEEECC		20.4627080861
141AcetylationVVYCNTSKKWFCNGR
EEEECCCCCEEECCC		52.5726051181
151PhosphorylationFCNGRGNTSGSHIVN
EECCCCCCCCHHHHH		36.9724719451
151 (in isoform 2)Phosphorylation-36.9724719451
152PhosphorylationCNGRGNTSGSHIVNH
ECCCCCCCCHHHHHH		42.1528348404
154PhosphorylationGRGNTSGSHIVNHLV
CCCCCCCHHHHHHHH		15.1428348404
200UbiquitinationLLGFIPAKADSVVVL
EEEECCCCCCEEEEE		47.58-
203PhosphorylationFIPAKADSVVVLLCR
ECCCCCCEEEEEEEC		22.9824245541
215PhosphorylationLCRQPCASQSSLKDI
EECCCCCCCHHCCCC		36.9920068231
215 (in isoform 2)Phosphorylation-36.99-
217PhosphorylationRQPCASQSSLKDINW
CCCCCCCHHCCCCCC		34.8320068231
218PhosphorylationQPCASQSSLKDINWD
CCCCCCHHCCCCCCC		31.6220068231
220UbiquitinationCASQSSLKDINWDSS
CCCCHHCCCCCCCCH		59.52-
247PhosphorylationSWLVKIPSEQEQLRA
HHHHCCCCHHHHHHH		56.2220860994
264UbiquitinationITAQQINKLEELWKE
HHHHHHHHHHHHHHH		59.9321890473
264 (in isoform 1)Ubiquitination-59.9321890473
264 (in isoform 2)Ubiquitination-59.9321890473
270UbiquitinationNKLEELWKENPSATL
HHHHHHHHHCCCCCH		61.30-
282UbiquitinationATLEDLEKPGVDEEP
CCHHHHHCCCCCCCC		55.1321906983
282 (in isoform 1)Ubiquitination-55.1321890473
282 (in isoform 2)Ubiquitination-55.1321890473
300PhosphorylationLLRYEDAYQYQNIFG
EEEHHHHHHHCCCCC		21.7827642862
302PhosphorylationRYEDAYQYQNIFGPL
EHHHHHHHCCCCCCC		7.2827642862
311AcetylationNIFGPLVKLEADYDK
CCCCCCEEECCHHHH		48.5726051181
318AcetylationKLEADYDKKLKESQT
EECCHHHHHHCHHCC		54.5025953088
3212-HydroxyisobutyrylationADYDKKLKESQTQDN
CHHHHHHCHHCCCCC		65.29-
321UbiquitinationADYDKKLKESQTQDN
CHHHHHHCHHCCCCC		65.2921906983
321 (in isoform 1)Ubiquitination-65.2921890473
321 (in isoform 2)Ubiquitination-65.2921890473
339UbiquitinationRWDLGLNKKRIAYFT
EEECCCCCCEEEEEE		48.7721890473
339 (in isoform 1)Ubiquitination-48.7721890473
339 (in isoform 2)Ubiquitination-48.7721890473
340UbiquitinationWDLGLNKKRIAYFTL
EECCCCCCEEEEEEE		48.22-
344PhosphorylationLNKKRIAYFTLPKTD
CCCCEEEEEEECCCC		8.50-
344 (in isoform 2)Phosphorylation-8.5020860994
346PhosphorylationKKRIAYFTLPKTDSG
CCEEEEEEECCCCCC		29.49-
346 (in isoform 2)Phosphorylation-29.4920860994
350PhosphorylationAYFTLPKTDSGNEDL
EEEEECCCCCCCCCE		33.20-
350 (in isoform 2)Phosphorylation-33.2020860994
352 (in isoform 2)Phosphorylation-49.0720860994
355 (in isoform 2)Methylation-57.13-
367 (in isoform 2)Ubiquitination-2.1121890473
368SulfoxidationWLRDMRLMQGDEICL
EEEECCCCCCCEEEH		2.7121406390
374GlutathionylationLMQGDEICLRYKGDL
CCCCCEEEHHCCCCC		1.3422555962
375 (in isoform 2)Ubiquitination-9.1221890473
378AcetylationDEICLRYKGDLAPLW
CEEEHHCCCCCHHHH		39.2425953088
378UbiquitinationDEICLRYKGDLAPLW
CEEEHHCCCCCHHHH		39.2421890473
378 (in isoform 1)Ubiquitination-39.2421890473
386AcetylationGDLAPLWKGIGHVIK
CCCHHHHCCCCEEEE		48.6225953088
386UbiquitinationGDLAPLWKGIGHVIK
CCCHHHHCCCCEEEE		48.6221890473
386 (in isoform 1)Ubiquitination-48.6221890473
428PhosphorylationQVDFVWKSTSFDRMQ
EEEEEEECCCHHHHH		17.3628509920
428 (in isoform 2)Ubiquitination-17.3621890473
429PhosphorylationVDFVWKSTSFDRMQS
EEEEEECCCHHHHHH		29.6828509920
430PhosphorylationDFVWKSTSFDRMQSA
EEEEECCCHHHHHHH		32.0421902226
433MethylationWKSTSFDRMQSALKT
EECCCHHHHHHHHHH		24.03115491039
439UbiquitinationDRMQSALKTFAVDET
HHHHHHHHHHCCCCC		41.1122053931
439 (in isoform 1)Ubiquitination-41.1121890473
451PhosphorylationDETSVSGYIYHKLLG
CCCCCCHHHHHHHHC		7.27-
455UbiquitinationVSGYIYHKLLGHEVE
CCHHHHHHHHCCCEE		28.56-
464 (in isoform 2)Phosphorylation-2.85-
467AcetylationEVEDVIIKCQLPKRF
CEEEEEEECCCCCCC		12.5726051181
467UbiquitinationEVEDVIIKCQLPKRF
CEEEEEEECCCCCCC		12.57-
474 (in isoform 2)Phosphorylation-9.18-
475PhosphorylationCQLPKRFTAQGLPDL
CCCCCCCCCCCCCCC		23.3120068231
481 (in isoform 2)Phosphorylation-66.2124719451
485PhosphorylationGLPDLNHSQVYAVKT
CCCCCCHHHHHHHHH		21.9228152594
488PhosphorylationDLNHSQVYAVKTVLQ
CCCHHHHHHHHHHHH		9.6828152594
491AcetylationHSQVYAVKTVLQRPL
HHHHHHHHHHHHCCH		25.4126051181
492PhosphorylationSQVYAVKTVLQRPLS
HHHHHHHHHHHCCHH		21.6124719451
499 (in isoform 2)Phosphorylation-26.5524719451
507 (in isoform 2)Phosphorylation-41.0824719451
510PhosphorylationGPPGTGKTVTSATIV
CCCCCCCCCCHHHHH		30.2924719451
512PhosphorylationPGTGKTVTSATIVYH
CCCCCCCCHHHHHHH		20.2028152594
513PhosphorylationGTGKTVTSATIVYHL
CCCCCCCHHHHHHHH		21.0528152594
515PhosphorylationGKTVTSATIVYHLAR
CCCCCHHHHHHHHHH		15.6728152594
518PhosphorylationVTSATIVYHLARQGN
CCHHHHHHHHHHCCC		6.3024719451
544UbiquitinationAVDQLTEKIHQTGLK
CHHHHHHHHHHHCHH		40.01-
551UbiquitinationKIHQTGLKVVRLCAK
HHHHHCHHHHHHHHC		39.77-
554 (in isoform 2)Phosphorylation-27.3424719451
557 (in isoform 2)Phosphorylation-19.90-
565PhosphorylationKSREAIDSPVSFLAL
CCHHHCCCCHHHHHH		22.5320068231
568PhosphorylationEAIDSPVSFLALHNQ
HHCCCCHHHHHHHHH		20.2320068231
576 (in isoform 2)Ubiquitination-4.1121890473
579SulfoxidationLHNQIRNMDSMPELQ
HHHHHHCCCCCHHHH		2.6421406390
587UbiquitinationDSMPELQKLQQLKDE
CCCHHHHHHHHHHHC		61.9721890473
587 (in isoform 1)Ubiquitination-61.9721890473
592AcetylationLQKLQQLKDETGELS
HHHHHHHHHCCCCCC		49.5323749302
592UbiquitinationLQKLQQLKDETGELS
HHHHHHHHHCCCCCC		49.53-
593 (in isoform 2)Ubiquitination-68.2521890473
595PhosphorylationLQQLKDETGELSSAD
HHHHHHCCCCCCHHH		46.20-
599PhosphorylationKDETGELSSADEKRY
HHCCCCCCHHHHHHH		21.1223312004
600PhosphorylationDETGELSSADEKRYR
HCCCCCCHHHHHHHH		52.9823312004
604AcetylationELSSADEKRYRALKR
CCCHHHHHHHHHHHH		56.1025953088
604UbiquitinationELSSADEKRYRALKR
CCCHHHHHHHHHHHH		56.1021906983
604 (in isoform 1)Ubiquitination-56.1021890473
627 (in isoform 2)Ubiquitination-13.0521890473
638AcetylationAGDPRLAKMQFRSIL
CCCHHHHHHHHHEEE		37.5125953088
638UbiquitinationAGDPRLAKMQFRSIL
CCCHHHHHHHHHEEE		37.5122053931
638 (in isoform 1)Ubiquitination-37.5121890473
657GlutathionylationTQATEPECMVPVVLG
CCCCCCCHHHEEEEC		4.9522555962
677 (in isoform 2)Ubiquitination-11.5821890473
688UbiquitinationVMCKKAAKAGLSQSL
HHHHHHHHCCCCHHH		48.0921890473
688 (in isoform 1)Ubiquitination-48.0921890473
692PhosphorylationKAAKAGLSQSLFERL
HHHHCCCCHHHHHHH		19.4621712546
779 (in isoform 2)Ubiquitination-28.9821890473
782 (in isoform 2)Ubiquitination-17.86-
786AcetylationTEAANVEKITTKLLK
HHHCCHHHHHHHHHH		40.8623749302
786MalonylationTEAANVEKITTKLLK
HHHCCHHHHHHHHHH		40.8626320211
786UbiquitinationTEAANVEKITTKLLK
HHHCCHHHHHHHHHH		40.86-
786 (in isoform 2)Ubiquitination-40.8621890473
790AcetylationNVEKITTKLLKAGAK
CHHHHHHHHHHCCCC		43.0825953088
790MalonylationNVEKITTKLLKAGAK
CHHHHHHHHHHCCCC		43.0826320211
790UbiquitinationNVEKITTKLLKAGAK
CHHHHHHHHHHCCCC		43.0821890473
790 (in isoform 1)Ubiquitination-43.0821890473
793AcetylationKITTKLLKAGAKPDQ
HHHHHHHHCCCCCCC		56.0325953088
793MalonylationKITTKLLKAGAKPDQ
HHHHHHHHCCCCCCC		56.0326320211
793UbiquitinationKITTKLLKAGAKPDQ
HHHHHHHHCCCCCCC		56.03-
797UbiquitinationKLLKAGAKPDQIGII
HHHHCCCCCCCEEEE		48.4821906983
797 (in isoform 1)Ubiquitination-48.4821890473
811MethylationITPYEGQRSYLVQYM
EECCCCCCHHHHHHE		37.82115491023
845UbiquitinationDAFQGREKDFIILSC
CCCCCCCCCEEEEEE		57.49-
879PhosphorylationVALTRARYGVIIVGN
HCHHCCEEEEEEECC		18.1128152594
888UbiquitinationVIIVGNPKALSKQPL
EEEECCHHHHCCCCH		66.99-
892AcetylationGNPKALSKQPLWNHL
CCHHHHCCCCHHHHH		57.7025953088
892UbiquitinationGNPKALSKQPLWNHL
CCHHHHCCCCHHHHH		57.70-
907UbiquitinationLNYYKEQKVLVEGPL
HHHHHHCCEEEECCC		38.33-
915 (in isoform 2)Ubiquitination-48.9321890473
926AcetylationESLMQFSKPRKLVNT
HHHHHHCCCHHHHHC		50.5625953088
926UbiquitinationESLMQFSKPRKLVNT
HHHHHHCCCHHHHHC		50.5621890473
926 (in isoform 1)Ubiquitination-50.5621890473
929MalonylationMQFSKPRKLVNTINP
HHHCCCHHHHHCCCC		66.3726320211
929UbiquitinationMQFSKPRKLVNTINP
HHHCCCHHHHHCCCC		66.37-
933PhosphorylationKPRKLVNTINPGARF
CCHHHHHCCCCCCCC		18.0428857561
939MethylationNTINPGARFMTTAMY
HCCCCCCCCHHHHCH		27.99115491031
942PhosphorylationNPGARFMTTAMYDAR
CCCCCCHHHHCHHHH		14.5321945579
943PhosphorylationPGARFMTTAMYDARE
CCCCCHHHHCHHHHH		9.5321945579
945 (in isoform 2)Phosphorylation-2.6724719451
946NitrationRFMTTAMYDAREAII
CCHHHHCHHHHHHHC		12.18-
946PhosphorylationRFMTTAMYDAREAII
CCHHHHCHHHHHHHC		12.1821945579
956O-linked_GlycosylationREAIIPGSVYDRSSQ
HHHHCCCCCCCCCCC		16.4930059200
956PhosphorylationREAIIPGSVYDRSSQ
HHHHCCCCCCCCCCC		16.4929978859
958PhosphorylationAIIPGSVYDRSSQGR
HHCCCCCCCCCCCCC		13.8228796482
970PhosphorylationQGRPSSMYFQTHDQI
CCCCCCEEEECCCCC		8.42-
1019MethylationANGPAAGRGTPKGKT
CCCCCCCCCCCCCCC		40.8824129315
1084PhosphorylationQMSQPGLSQPELSQD
CCCCCCCCCCCCCCC		49.9911544179
1089PhosphorylationGLSQPELSQDSYLGD
CCCCCCCCCCCCCCH		30.2226657352
1092PhosphorylationQPELSQDSYLGDEFK
CCCCCCCCCCCHHHH		18.0226074081
1093PhosphorylationPELSQDSYLGDEFKS
CCCCCCCCCCHHHHH		24.0026074081
1096 (in isoform 2)Phosphorylation-56.4124719451
1099 (in isoform 2)Phosphorylation-39.1324719451
1100PhosphorylationYLGDEFKSQIDVALS
CCCHHHHHHHCEECC		37.3825159151
1100 (in isoform 2)Phosphorylation-37.38-
1101 (in isoform 2)Phosphorylation-36.17-
1107PhosphorylationSQIDVALSQDSTYQG
HHHCEECCCCCCCCC		23.3919664994
1110PhosphorylationDVALSQDSTYQGERA
CEECCCCCCCCCCHH		22.7525159151
1111PhosphorylationVALSQDSTYQGERAY
EECCCCCCCCCCHHH		28.3125159151
1112PhosphorylationALSQDSTYQGERAYQ
ECCCCCCCCCCHHHH		20.6228176443
1113 (in isoform 2)Phosphorylation-47.57-
1116 (in isoform 2)Phosphorylation-45.4827251275
1118PhosphorylationTYQGERAYQHGGVTG
CCCCCHHHHCCCCCC		13.7825159151
1118 (in isoform 2)Phosphorylation-13.7824719451
1124PhosphorylationAYQHGGVTGLSQY--
HHHCCCCCCCCCC--		35.3622167270
1127PhosphorylationHGGVTGLSQY-----
CCCCCCCCCC-----		28.8619664994
1129PhosphorylationGVTGLSQY-------
CCCCCCCC-------		19.6922167270
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
1084SPhosphorylationKinaseSMG1Q96Q15
PSP
1089SPhosphorylationKinaseSMG1Q96Q15
PSP
1107SPhosphorylationKinaseSMG1Q96Q15
PSP
1127SPhosphorylationKinaseSMG1Q96Q15
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RENT1_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 RENT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIRA_HUMANHIRAphysical
15231747
RENT2_HUMANUPF2physical
14527413
REN3B_HUMANUPF3Bphysical
14527413
DCP2_HUMANDCP2physical
14527413
XRN1_HUMANXRN1physical
14527413
EXOS2_HUMANEXOSC2physical
14527413
EXOS4_HUMANEXOSC4physical
14527413
PARN_HUMANPARNphysical
14527413
EXOSX_HUMANEXOSC10physical
14527413
RENT2_HUMANUPF2physical
12723973
PABP1_HUMANPABPC1physical
12723973
REN3A_HUMANUPF3Aphysical
12723973
REN3B_HUMANUPF3Bphysical
12723973
RENT2_HUMANUPF2physical
11073994
SMG1_HUMANSMG1physical
11544179
DCP1A_HUMANDCP1Aphysical
12417715
DCP2_HUMANDCP2physical
12417715
REN3A_HUMANUPF3Aphysical
11163187
REN3B_HUMANUPF3Bphysical
11163187
RENT2_HUMANUPF2physical
11163187
RENT2_HUMANUPF2physical
16488880
DPOD1_HUMANPOLD1physical
16488880
RENT2_HUMANUPF2physical
16086026
SLBP_HUMANSLBPphysical
16086026
VIGLN_HUMANHDLBPphysical
22939629
VPS35_HUMANVPS35physical
22939629
TMX1_HUMANTMX1physical
22939629
SMG1_HUMANSMG1physical
19417104
SMG8_HUMANSMG8physical
19417104
SMG9_HUMANSMG9physical
19417104
RENT2_HUMANUPF2physical
19417104
RBM8A_HUMANRBM8Aphysical
19417104
RL11_HUMANRPL11physical
19417104
RS6_HUMANRPS6physical
19417104
EF2_HUMANEEF2physical
19417104
ERF3A_HUMANGSPT1physical
19417104
RL7A_HUMANRPL7Aphysical
19417104
RS3_HUMANRPS3physical
19417104
PABP1_HUMANPABPC1physical
19417104
NCBP1_HUMANNCBP1physical
19417104
NCBP2_HUMANNCBP2physical
19417104
REN3B_HUMANUPF3Bphysical
19417104
IF4A3_HUMANEIF4A3physical
19417104
MGN_HUMANMAGOHphysical
19417104
HBB_HUMANHBBphysical
21145460
SMG5_HUMANSMG5physical
21145460
SMG7_HUMANSMG7physical
21145460
EST1A_HUMANSMG6physical
21145460
RENT2_HUMANUPF2physical
21145460
REN3B_HUMANUPF3Bphysical
21145460
IF4A3_HUMANEIF4A3physical
21145460
PABP1_HUMANPABPC1physical
21145460
XRN1_HUMANXRN1physical
21145460
ERF3A_HUMANGSPT1physical
18256688
RENT2_HUMANUPF2physical
18256688
DCP2_HUMANDCP2physical
16364915
EDC4_HUMANEDC4physical
16364915
DCP1A_HUMANDCP1Aphysical
16364915
EDC3_HUMANEDC3physical
16364915
DSRAD_HUMANADARphysical
18362360
SMG1_HUMANSMG1physical
18423202
ERF3A_HUMANGSPT1physical
18423202
DCP1A_HUMANDCP1Aphysical
18423202
XRN1_HUMANXRN1physical
18423202
EXOS2_HUMANEXOSC2physical
18423202
EIF3A_HUMANEIF3Aphysical
18423202
EIF3B_HUMANEIF3Bphysical
18423202
IF2A_HUMANEIF2S1physical
18423202
IF2B_HUMANEIF2S2physical
18423202
ERF3B_HUMANGSPT2physical
16452507
ERF3A_HUMANGSPT1physical
16452507
SMG1_HUMANSMG1physical
16452507
RUVB1_HUMANRUVBL1physical
20371770
RUVB2_HUMANRUVBL2physical
20371770
SMG5_HUMANSMG5physical
20371770
SMG7_HUMANSMG7physical
20371770
RENT2_HUMANUPF2physical
20371770
REN3B_HUMANUPF3Bphysical
20371770
IF4A3_HUMANEIF4A3physical
20371770
RBM8A_HUMANRBM8Aphysical
20371770
PKHB2_HUMANPLEKHB2physical
15231747
NADE_HUMANNADSYN1physical
15231747
ACSA_HUMANACSS2physical
15231747
ABHGA_HUMANABHD16Aphysical
15231747
RHXF2_HUMANRHOXF2physical
15231747
RPRD2_HUMANRPRD2physical
15231747
GNPTG_HUMANGNPTGphysical
15231747
NDUBA_HUMANNDUFB10physical
15231747
DXO_HUMANDXOphysical
15231747
PKHA5_HUMANPLEKHA5physical
15231747
STAU2_HUMANSTAU2physical
24778252
MOV10_HUMANMOV10physical
24778252
STAU1_HUMANSTAU1physical
24778252
RENT2_HUMANUPF2physical
24778252
DNA2_HUMANDNA2physical
24778252
REN3B_HUMANUPF3Bphysical
24778252
ABCF3_HUMANABCF3physical
26344197
DIAP1_HUMANDIAPH1physical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
SMCA4_HUMANSMARCA4physical
26344197
HNRPQ_HUMANSYNCRIPphysical
26344197
TTC4_HUMANTTC4physical
26344197
UBL7_HUMANUBL7physical
26344197
VPS35_HUMANVPS35physical
26344197
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 RENT1_HUMAN

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Related Literatures of Post-Translational Modification
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-1107 AND SER-1127, ANDMASS 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-1107, AND MASSSPECTROMETRY.
"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-1107, AND MASSSPECTROMETRY.
"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-1107 AND SER-1127, ANDMASS SPECTROMETRY.
"Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exonjunction complex triggers Upf1 phosphorylation and nonsense-mediatedmRNA decay.";
Kashima I., Yamashita A., Izumi N., Kataoka N., Morishita R.,Hoshino S., Ohno M., Dreyfuss G., Ohno S.;
Genes Dev. 20:355-367(2006).
Cited for: IDENTIFICATION IN THE SURF COMPLEX, PHOSPHORYLATION AT SER-1089 ANDSER-1107, AND MUTAGENESIS OF CYS-126; LYS-509; SER-1084; SER-1089;SER-1107 AND SER-1127.
"Human SMG-1, a novel phosphatidylinositol 3-kinase-related proteinkinase, associates with components of the mRNA surveillance complexand is involved in the regulation of nonsense-mediated mRNA decay.";
Yamashita A., Ohnishi T., Kashima I., Taya Y., Ohno S.;
Genes Dev. 15:2215-2228(2001).
Cited for: PHOSPHORYLATION AT SER-1089 AND SER-1107, AND MUTAGENESIS OF SER-1089;SER-1107 AND GLN-1108.
"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 TYR-1129, AND MASSSPECTROMETRY.

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