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Protein Page:
RENT1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RENT1 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. Found in a post-splicing messenger ribonucleoprotein (mRNP) complex. Associates with the exon junction complex (EJC). Associates with the SGM1C complex; is phosphorylated by the complex kinase component SGM1. Interacts with UPF2, UPF3A and UPF3B. Interacts with EST1A and SLBP. Interacts (when hyperphosphorylated) with PNRC2. Interacts with EIF2C1, EIF2C2 and GSPT2. Ubiquitous. Belongs to the DNA2/NAM7 helicase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Hydrolase; EC 3.6.4.-; C2H2-type zinc finger protein; EC 3.6.1.-
Chromosomal Location of Human Ortholog: 19p13.2-p13.11
Cellular Component: cytoplasm; nucleolus; chromatin; cytosol; nucleus
Molecular Function: protein binding; DNA binding; zinc ion binding; RNA binding; chromatin binding; helicase activity; ATP-dependent RNA helicase activity; ATP binding
Biological Process: ATP catabolic process; mRNA export from nucleus; RNA metabolic process; dosage compensation, by inactivation of X chromosome; mRNA catabolic process, nonsense-mediated decay; gene expression; DNA replication; DNA repair; regulation of translational termination; mRNA metabolic process
Reference #:  Q92900 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent helicase RENT1; delta helicase; FLJ43809; FLJ46894; hUpf1; KIAA0221; Nonsense mRNA reducing factor 1; NORF1; pNORF1; Regulator of nonsense transcripts 1; RENT1; UP Frameshift 1; up-frameshift mutation 1 homolog; Up-frameshift suppressor 1 homolog; UPF1; UPF1 regulator of nonsense transcripts homolog (yeast); yeast Upf1p homolog
Gene Symbols: UPF1
Molecular weight: 124,345 Da
Basal Isoelectric point: 6.18  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RENT1

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S1107‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S10-p VEAYGPSsQTLTFLD
2 0 T28-p AELLGADtQGsEFEF
0 1 S31-p LGADtQGsEFEFTDF
0 29 Y113-p EEDEEDTyyTKDLPI
0 8 Y114-p EDEEDTyyTKDLPIH
0 2 Y136-p HDPACVVyCNTSKKW
0 9 K200-ub LLGFIPAkADSVVVL
0 3 K220 CASQSSLKDINWDSS
0 2 K264-ub ITAQQINkLEELWKE
0 2 K282-ub ATLEDLEkPGVDEEP
0 1 K321-ub ADYDKKLkESQTQDN
0 1 Y344 LNKKRIAYFTLPKTD
0 1 T346 KKRIAYFTLPKTDSG
0 1 T350 AYFTLPKTDSGNEDL
0 1 S352 FTLPKTDSGNEDLVI
0 2 K378-ub DEICLRYkGDLAPLW
0 2 K386-ac GDLAPLWkGIGHVIK
0 3 K386-ub GDLAPLWkGIGHVIK
0 44 K439-ub DRMQSALkTFAVDET
0 3 K467 EVEDVIIKCQLPKRF
0 1 T475-p CQLPKRFtAQGLPDL
0 76 Y488-p DLNHSQVyAVKTVLQ
0 1 S565-p KSREAIDsPVSFLAL
0 3 K587-ub DSMPELQkLQQLkDE
0 2 K592-ac LQkLQQLkDEtGELS
0 1 T595-p LQQLkDEtGELSSAD
0 3 K604-ub ELSSADEkRYRALKR
0 14 K638-ub AGDPRLAkMQFRSIL
0 2 K688-ub VMCKKAAkAGLsQSL
0 1 S692-p KAAkAGLsQSLFERL
0 1 K786 TEAANVEKITTkLLK
0 2 K790-ub NVEKITTkLLKAGAk
0 1 K793 KITTkLLKAGAkPDQ
0 1 K797-ub kLLKAGAkPDQIGII
0 1 Y879-p VALTRARyGVIIVGN
0 2 K926-ub ESLMQFSkPRkLVNT
0 2 K929-ub MQFSkPRkLVNTINP
0 274 Y946-p RFMTTAMyDAREAII
0 1 S956-p REAIIPGsVyDRSSQ
0 81 Y958-p AIIPGsVyDRSSQGR
0 1 Y970-p QGRPSSMyFQTHDQI
0 1 R1019-m1 ANGPAAGrGTPKGKT
1 4 S1084-p QMSQPGLsQPELsQD
4 0 S1089-p GLsQPELsQDSYLGD
0 1 S1100-p YLGDEFKsQIDVALs
6 55 S1107-p sQIDVALsQDstyQG
0 26 S1110-p DVALsQDstyQGERA
0 9 T1111-p VALsQDstyQGERAy
0 20 Y1112-p ALsQDstyQGERAyQ
0 16 Y1118-p tyQGERAyQHGGVTG
0 1 T1124 AyQHGGVTGLsQy__
3 63 S1127-p HGGVTGLsQy_____
0 100 Y1129-p GVTGLsQy_______
  RENT1 iso2  
S10 VEAYGPSSQTLTFLD
T28 AELLGADTQGSEFEF
S31 LGADTQGSEFEFTDF
Y113 EEDEEDTYYTKDLPI
Y114 EDEEDTYYTKDLPIH
Y136 HDPACVVYCNTSKKW
K200 LLGFIPAKADSVVVL
K220 CASQSSLKDINWDSS
K264 ITAQQINKLEELWKE
K282 ATLEDLEKPGVDEEP
K321 ADYDKKLKESQTQDN
Y344-p LNKKRIAyFtLPKtD
T346-p KKRIAyFtLPKtDsD
T350-p AyFtLPKtDsDMRLM
S352-p FtLPKtDsDMRLMQG
K367 DEICLRYKGDLAPLW
K375 GDLAPLWKGIGHVIK
K375 GDLAPLWKGIGHVIK
K428 DRMQSALKTFAVDET
K456 EVEDVIIKCQLPKRF
T464 CQLPKRFTAQGLPDL
Y477 DLNHSQVYAVKTVLQ
S554 KSREAIDSPVSFLAL
K576 DSMPELQKLQQLKDE
K581 LQKLQQLKDETGELS
T584 LQQLKDETGELSSAD
K593 ELSSADEKRYRALKR
K627 AGDPRLAKMQFRSIL
K677 VMCKKAAKAGLSQSL
S681 KAAKAGLSQSLFERL
K775 TEAANVEKITTKLLK
K779 NVEKITTKLLKAGAK
K782 KITTKLLKAGAKPDQ
K786 KLLKAGAKPDQIGII
Y868 VALTRARYGVIIVGN
K915 ESLMQFSKPRKLVNT
K918 MQFSKPRKLVNTINP
Y935 RFMTTAMYDAREAII
S945 REAIIPGSVYDRSSQ
Y947 AIIPGSVYDRSSQGR
Y959 QGRPSSMYFQTHDQI
R1008 ANGPAAGRGTPKGKT
S1073 QMSQPGLSQPELSQD
S1078 GLSQPELSQDSYLGD
S1089 YLGDEFKSQIDVALS
S1096 SQIDVALSQDSTYQG
S1099 DVALSQDSTYQGERA
T1100 VALSQDSTYQGERAY
Y1101 ALSQDSTYQGERAYQ
Y1107 TYQGERAYQHGGVTG
T1113 AYQHGGVTGLsQY__
S1116-p HGGVTGLsQY_____
Y1118 GVTGLsQY_______
  mouse

 
S10 VEAYGPSSQTLTFLD
T28 AELLGADTQGSEFEF
S31 LGADTQGSEFEFTDF
Y108-p EEDEEDTyYTKDLPV
Y109 EDEEDTyYTKDLPVH
Y131 HDPACVVYCNTSKKW
K195-ub LLGFIPAkADSVVVL
K215-ub CASQSSLkDINWDSS
K259-ub ITAQQINkLEELWKE
K277-ub ATLEDLEkPGVDEEP
K316 ADYDKKLKESQTQDN
F339 LNKKRIAFFTLPKTD
T341 KKRIAFFTLPKTDSG
T345 AFFTLPKTDSGNEDL
S347 FTLPKTDSGNEDLVI
K373-ub DEICLRYkGDLAPLW
K381 GDLAPLWKGIGHVIK
K381-ub GDLAPLWkGIGHVIK
K434-ub DRMQSALkTFAVDET
K462-ub EVEDVVIkCQLPKRF
T470 CQLPKRFTAQGLPDL
Y483-p DLNHSQVyAVKTVLQ
S560 KSREAIDSPVSFLAL
K582-ub DSMPELQkLQQLkDE
K587-ac LQkLQQLkDETGELS
T590 LQQLkDETGELSSAD
K599-ub ELSSADEkRYRALKR
K633-ub AGDPRLAkMQFRSIL
K683-ub VMCKKAAkAGLSQSL
S687 KAAkAGLSQSLFERL
K781-ub TEAANVEkITTkLLk
K785-ub NVEkITTkLLkAGAK
K788-ub kITTkLLkAGAKPDQ
K792 kLLkAGAKPDQIGII
Y874 VALTRARYGVIIVGN
K921 ESLMQFSKPRkLVNT
K924-ub MQFSKPRkLVNTVNP
Y941-p RFMTTAMyDAREAII
S951 REAIIPGSVyDRSSQ
Y953-p AIIPGSVyDRSSQGR
Y965 QGRPSNMYFQTHDQI
R1014 ANGPAAGRGTPKTKT
S1079 QMSQPGLSQPELsQD
S1084-p GLSQPELsQDSYLGD
S1095 YLGDEFKSQIDVALs
S1102-p SQIDVALsQDstyQG
S1105-p DVALsQDstyQGERA
T1106-p VALsQDstyQGERAY
Y1107-p ALsQDstyQGERAYQ
Y1113 tyQGERAYQHGGVtG
T1119-p AYQHGGVtGLsQy__
S1122-p HGGVtGLsQy_____
Y1124-p GVtGLsQy_______
  rat

 
S10 VEAYGPSSQTLTFLD
T28 AELLGADTQGSEFEF
S31 LGADTQGSEFEFTDF
Y108 EEDEEDTYYTKDLPV
Y109 EDEEDTYYTKDLPVH
Y131 HDPACVVYCNTSKKW
K195 LLGFIPAKADSVVVL
K215 CASQSSLKDINWDSS
K259 ITAQQINKLEELWKE
K277 ATLEDLEKPGVDEEP
K316 ADYDKKLKESQTQDN
F339 LNKKRIAFFTLPKTD
T341 KKRIAFFTLPKTDSG
T345 AFFTLPKTDSGNEDL
S347 FTLPKTDSGNEDLVI
K373 DEICLRYKGDLAPLW
K381-ac GDLAPLWkGIGHVIK
K381 GDLAPLWKGIGHVIK
K434 DRMQSALKTFAVDET
K462 EVEDVVIKCQLPKRF
T470 CQLPKRFTAQGLPDL
Y483 DLNHSQVYAVKTVLQ
S560 KSREAIDSPVSFLAL
K582 DSMPELQKLQQLkDE
K587-ac LQKLQQLkDETGELS
T590 LQQLkDETGELSSAD
K599 ELSSADEKRYRALKR
K633 AGDPRLAKMQFRSIL
K683 VMCKKAAKAGLSQSL
S687 KAAKAGLSQSLFERL
K781 TEAANVEKITTKLLK
K785 NVEKITTKLLKAGAK
K788 KITTKLLKAGAKPDQ
K792 KLLKAGAKPDQIGII
Y874 VALTRARYGVIIVGN
K921 ESLMQFSKPRKLVNT
K924 MQFSKPRKLVNTVNP
Y941 RFMTTAMYDAREAII
S951 REAIIPGSVYDRSSQ
Y953 AIIPGSVYDRSSQGR
Y965 QGRPSNMYFQTHDQI
R1014 ANGPAAGRGTPKSKT
S1079 QMSQPGLSQPELSQD
S1084 GLSQPELSQDSYLGD
S1095 YLGDEFKSQIDVALs
S1102-p SQIDVALsQDsTYQG
S1105-p DVALsQDsTYQGERA
T1106 VALsQDsTYQGERAY
Y1107 ALsQDsTYQGERAYQ
Y1113 TYQGERAYQHGGVTG
T1119 AYQHGGVTGLSQY__
S1122 HGGVTGLSQY_____
Y1124 GVTGLSQY_______
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