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Protein Page:
RENT1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: EC 3.6.1.-; C2H2-type zinc finger protein; EC 3.6.4.-; Hydrolase
Cellular Component: cytoplasm; chromatin; nucleus; cytosol
Molecular Function: protein binding; DNA binding; zinc ion binding; RNA binding; chromatin binding; helicase activity; ATP binding; ATP-dependent RNA helicase activity
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 repair; DNA replication; 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

 
2 0 T28-p AELLGADtQGSEFEF
0 29 Y113-p EEDEEDTyyTKDLPI
0 6 Y114-p EDEEDTyyTKDLPIH
0 2 Y136-p HDPACVVyCNTSKKW
0 9 K200-u LLGFIPAkADSVVVL
0 3 K220 CASQSSLKDINWDSS
0 2 K264-u ITAQQINkLEELWKE
0 2 K282-u ATLEDLEkPGVDEEP
0 1 K321-u ADYDKKLkESQTQDN
0 2 K378-u DEICLRYkGDLAPLW
0 2 K386-a GDLAPLWkGIGHVIK
0 3 K386-u GDLAPLWkGIGHVIK
0 44 K439-u DRMQSALkTFAVDET
0 3 K467 EVEDVIIKCQLPKRF
0 1 T475-p CQLPKRFtAQGLPDL
0 76 Y488-p DLNHSQVyAVKTVLQ
0 1 S565-p KSREAIDsPVSFLAL
0 3 K587-u DSMPELQkLQQLKDE
0 3 K604-u ELSSADEkRYRALKR
0 14 K638-u AGDPRLAkMQFRSIL
0 2 K688-u VMCKKAAkAGLSQSL
0 1 K786 TEAANVEKITTkLLK
0 2 K790-u NVEKITTkLLKAGAk
0 1 K793 KITTkLLKAGAkPDQ
0 1 K797-u kLLKAGAkPDQIGII
0 2 K926-u ESLMQFSkPRkLVNT
0 2 K929-u MQFSkPRkLVNTINP
0 307 Y946-p RFMTTAMyDAREAII
0 1 S956-p REAIIPGsVyDRSSQ
0 82 Y958-p AIIPGsVyDRSSQGR
0 1 R1019-m1 ANGPAAGrGTPKGKT
1 4 S1084-p QMSQPGLsQPELsQD
4 0 S1089-p GLsQPELsQDSYLGD
6 44 S1107-p SQIDVALsQDstyQG
0 20 S1110-p DVALsQDstyQGERA
0 7 T1111-p VALsQDstyQGERAy
0 19 Y1112-p ALsQDstyQGERAyQ
0 11 Y1118-p tyQGERAyQHGGVTG
0 1 T1124 AyQHGGVTGLsQy__
2 54 S1127-p HGGVTGLsQy_____
0 108 Y1129-p GVTGLsQy_______
  mouse

 
T28 AELLGADTQGSEFEF
Y108-p EEDEEDTyYTKDLPV
Y109 EDEEDTyYTKDLPVH
Y131 HDPACVVYCNTSKKW
K195-u LLGFIPAkADSVVVL
K215-u CASQSSLkDINWDSS
K259-u ITAQQINkLEELWKE
K277-u ATLEDLEkPGVDEEP
K316 ADYDKKLKESQTQDN
K373-u DEICLRYkGDLAPLW
K381 GDLAPLWKGIGHVIK
K381-u GDLAPLWkGIGHVIK
K434-u DRMQSALkTFAVDET
K462-u EVEDVVIkCQLPKRF
T470 CQLPKRFTAQGLPDL
Y483-p DLNHSQVyAVKTVLQ
S560 KSREAIDSPVSFLAL
K582-u DSMPELQkLQQLKDE
K599-u ELSSADEkRYRALKR
K633-u AGDPRLAkMQFRSIL
K683-u VMCKKAAkAGLSQSL
K781-u TEAANVEkITTkLLk
K785-u NVEkITTkLLkAGAK
K788-u kITTkLLkAGAKPDQ
K792 kLLkAGAKPDQIGII
K921 ESLMQFSKPRkLVNT
K924-u MQFSKPRkLVNTVNP
Y941-p RFMTTAMyDAREAII
S951 REAIIPGSVyDRSSQ
Y953-p AIIPGSVyDRSSQGR
R1014 ANGPAAGRGTPKTKT
S1079 QMSQPGLSQPELsQD
S1084-p GLSQPELsQDSYLGD
S1102-p SQIDVALsQDstyQG
S1105-p DVALsQDstyQGERA
T1106-p VALsQDstyQGERAY
Y1107-p ALsQDstyQGERAYQ
Y1113 tyQGERAYQHGGVtG
T1119-p AYQHGGVtGLsQy__
S1122-p HGGVtGLsQy_____
Y1124-p GVtGLsQy_______
  rat

 
T28 AELLGADTQGSEFEF
Y108 EEDEEDTYYTKDLPV
Y109 EDEEDTYYTKDLPVH
Y131 HDPACVVYCNTSKKW
K195 LLGFIPAKADSVVVL
K215 CASQSSLKDINWDSS
K259 ITAQQINKLEELWKE
K277 ATLEDLEKPGVDEEP
K316 ADYDKKLKESQTQDN
K373 DEICLRYKGDLAPLW
K381 GDLAPLWKGIGHVIK
K381 GDLAPLWKGIGHVIK
K434 DRMQSALKTFAVDET
K462 EVEDVVIKCQLPKRF
T470 CQLPKRFTAQGLPDL
Y483 DLNHSQVYAVKTVLQ
S560 KSREAIDSPVSFLAL
K582 DSMPELQKLQQLKDE
K599 ELSSADEKRYRALKR
K633 AGDPRLAKMQFRSIL
K683 VMCKKAAKAGLSQSL
K781 TEAANVEKITTKLLK
K785 NVEKITTKLLKAGAK
K788 KITTKLLKAGAKPDQ
K792 KLLKAGAKPDQIGII
K921 ESLMQFSKPRKLVNT
K924 MQFSKPRKLVNTVNP
Y941 RFMTTAMYDAREAII
S951 REAIIPGSVYDRSSQ
Y953 AIIPGSVYDRSSQGR
R1014 ANGPAAGRGTPKSKT
S1079 QMSQPGLSQPELSQD
S1084 GLSQPELSQDSYLGD
S1102 SQIDVALSQDSTYQG
S1105 DVALSQDSTYQGERA
T1106 VALSQDSTYQGERAY
Y1107 ALSQDSTYQGERAYQ
Y1113 TYQGERAYQHGGVTG
T1119 AYQHGGVTGLSQY__
S1122 HGGVTGLSQY_____
Y1124 GVTGLSQY_______
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