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Q92900 (RENT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of nonsense transcripts 1

EC=3.6.4.-
Alternative name(s):
ATP-dependent helicase RENT1
Nonsense mRNA reducing factor 1
Short name=NORF1
Up-frameshift suppressor 1 homolog
Short name=hUpf1
Gene names
Name:UPF1
Synonyms:KIAA0221, RENT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.17 Ref.22 Ref.30 Ref.36

Subunit structure

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 AGO1, AGO2 and GSPT2. Interacts with isoform 1 and isoform 5of ADAR/ADAR1. Ref.7 Ref.8 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.25 Ref.28

Subcellular location

Cytoplasm. CytoplasmP-body. Nucleus. Note: Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm. Ref.7 Ref.12 Ref.25 Ref.28

Tissue specificity

Ubiquitous.

Domain

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Post-translational modification

Phosphorylated by SMG1; required for formation of mRNA surveillance complexes. Ref.10 Ref.11 Ref.14 Ref.19 Ref.28

Sequence similarities

Belongs to the DNA2/NAM7 helicase family.

Contains 1 UPF1-type zinc finger.

Sequence caution

The sequence BAA19664.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.15Ref.36. Source: GOC

DNA repair

Inferred from direct assay PubMed 16488880. Source: HGNC

DNA replication

Inferred from mutant phenotype PubMed 16488880. Source: HGNC

RNA metabolic process

Traceable author statement. Source: Reactome

dosage compensation by inactivation of X chromosome

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

histone mRNA catabolic process

Inferred from mutant phenotype Ref.17. Source: UniProtKB

mRNA export from nucleus

Traceable author statement PubMed 16488880. Source: HGNC

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process

Inferred from mutant phenotype PubMed 23828042. Source: UniProt

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from direct assay PubMed 17468741. Source: UniProtKB

regulation of translational termination

Inferred from mutant phenotype PubMed 9620853. Source: UniProtKB

   Cellular_componentchromatin

Inferred from direct assay PubMed 16488880. Source: HGNC

cytoplasm

Non-traceable author statement Ref.2. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

exon-exon junction complex

Inferred from direct assay PubMed 16601204. Source: UniProtKB

nucleus

Inferred from direct assay Ref.25. Source: UniProtKB

supraspliceosomal complex

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Inferred from direct assay Ref.36. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: InterPro

RNA binding

Non-traceable author statement Ref.9. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 16488880. Source: HGNC

helicase activity

Non-traceable author statement Ref.2. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18423202Ref.30. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92900-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92900-2)

The sequence of this isoform differs from the canonical sequence as follows:
     353-363: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11291129Regulator of nonsense transcripts 1
PRO_0000080716

Regions

Zinc finger121 – 272152UPF1-type
Nucleotide binding506 – 5105ATP
Region1 – 415415Sufficient for interaction with RENT2
Motif1089 – 10902[ST]-Q motif 1
Motif1107 – 11082[ST]-Q motif 2
Compositional bias47 – 8034Ala/Gly/Pro-rich
Compositional bias1042 – 112988Gln/Ser-rich

Sites

Binding site4861ATP
Binding site6761ATP
Binding site7131ATP
Binding site8441ATP

Amino acid modifications

Modified residue10891Phosphoserine Ref.10 Ref.19
Modified residue11071Phosphoserine Ref.10 Ref.19 Ref.21 Ref.24 Ref.29 Ref.31 Ref.33
Modified residue11101Phosphoserine Ref.31 Ref.33
Modified residue11271Phosphoserine Ref.31

Natural variations

Alternative sequence353 – 36311Missing in isoform 2.
VSP_003393
Natural variant691A → S. Ref.3
Corresponds to variant rs17339451 [ dbSNP | Ensembl ].
VAR_056207

Experimental info

Mutagenesis1261C → S: Abolishes ability to interact with UPF2/RENT2 and copurifies with greater amounts of SMG1, SMG8 and SMG9. Ref.9 Ref.19 Ref.27
Mutagenesis506 – 5083GTG → RTE: Prevents dephosphorylation and targets the protein to the P-body. Ref.9 Ref.28
Mutagenesis5091K → A: Inhibits histone mRNA degradation, ATPase activity and ATP binding. Ref.9 Ref.17 Ref.19 Ref.34
Mutagenesis610 – 6112KR → AA: Impairs RNA binding. Ref.9
Mutagenesis6151R → A: Impairs RNA binding. Ref.9 Ref.34
Mutagenesis647 – 6482DE → AA: Loss of ATPase activity and helicase activity. Ref.9
Mutagenesis6761Q → A: Impairs ATPase activity, no effect on ATP binding. Ref.9 Ref.34
Mutagenesis7141R → A: Impairs ATPase activity and ATP binding. Ref.9 Ref.34
Mutagenesis8431R → A: Inhibits histone mRNA degradation. Ref.7 Ref.9 Ref.17
Mutagenesis8431R → C: Abolishes NMD. Ref.7 Ref.9 Ref.17
Mutagenesis8761R → A: Impairs ATPase activity and ATP binding. Ref.9 Ref.34
Mutagenesis10841S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1089, A-1107 and A-1127. Ref.9 Ref.19
Mutagenesis10891S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1107 and A-1127. Ref.9 Ref.10 Ref.19
Mutagenesis10891S → A: Still phosphorylated but with less efficiency. Ref.9 Ref.10 Ref.19
Mutagenesis11071S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1127. Ref.9 Ref.10 Ref.19
Mutagenesis11071S → A: Impairs phosphorylation. Ref.9 Ref.10 Ref.19
Mutagenesis11081Q → N: Impairs phosphorylation. Ref.9 Ref.10
Mutagenesis11271S → A: Impairs association with UPF2, SMG1 and SMG7 and impairs phosphorylation; when associated with A-1084, A-1089 and A-1107. Ref.9 Ref.19
Sequence conflict611G → S in AAC51140. Ref.2
Sequence conflict4661I → T in AAC51140. Ref.2
Sequence conflict4781G → A in AAC50771. Ref.1
Sequence conflict5241G → D in AAC50771. Ref.1
Sequence conflict5571A → P in AAC50771. Ref.1
Sequence conflict901 – 9022NY → IF in AAC50771. Ref.1

Secondary structure

................................................................................................................................................................ 1129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: 6CCA6FE42B15BA28

FASTA1,129124,345
        10         20         30         40         50         60 
MSVEAYGPSS QTLTFLDTEE AELLGADTQG SEFEFTDFTL PSQTQTPPGG PGGPGGGGAG 

        70         80         90        100        110        120 
GPGGAGAGAA AGQLDAQVGP EGILQNGAVD DSVAKTSQLL AELNFEEDEE DTYYTKDLPI 

       130        140        150        160        170        180 
HACSYCGIHD PACVVYCNTS KKWFCNGRGN TSGSHIVNHL VRAKCKEVTL HKDGPLGETV 

       190        200        210        220        230        240 
LECYNCGCRN VFLLGFIPAK ADSVVVLLCR QPCASQSSLK DINWDSSQWQ PLIQDRCFLS 

       250        260        270        280        290        300 
WLVKIPSEQE QLRARQITAQ QINKLEELWK ENPSATLEDL EKPGVDEEPQ HVLLRYEDAY 

       310        320        330        340        350        360 
QYQNIFGPLV KLEADYDKKL KESQTQDNIT VRWDLGLNKK RIAYFTLPKT DSGNEDLVII 

       370        380        390        400        410        420 
WLRDMRLMQG DEICLRYKGD LAPLWKGIGH VIKVPDNYGD EIAIELRSSV GAPVEVTHNF 

       430        440        450        460        470        480 
QVDFVWKSTS FDRMQSALKT FAVDETSVSG YIYHKLLGHE VEDVIIKCQL PKRFTAQGLP 

       490        500        510        520        530        540 
DLNHSQVYAV KTVLQRPLSL IQGPPGTGKT VTSATIVYHL ARQGNGPVLV CAPSNIAVDQ 

       550        560        570        580        590        600 
LTEKIHQTGL KVVRLCAKSR EAIDSPVSFL ALHNQIRNMD SMPELQKLQQ LKDETGELSS 

       610        620        630        640        650        660 
ADEKRYRALK RTAERELLMN ADVICCTCVG AGDPRLAKMQ FRSILIDEST QATEPECMVP 

       670        680        690        700        710        720 
VVLGAKQLIL VGDHCQLGPV VMCKKAAKAG LSQSLFERLV VLGIRPIRLQ VQYRMHPALS 

       730        740        750        760        770        780 
AFPSNIFYEG SLQNGVTAAD RVKKGFDFQW PQPDKPMFFY VTQGQEEIAS SGTSYLNRTE 

       790        800        810        820        830        840 
AANVEKITTK LLKAGAKPDQ IGIITPYEGQ RSYLVQYMQF SGSLHTKLYQ EVEIASVDAF 

       850        860        870        880        890        900 
QGREKDFIIL SCVRANEHQG IGFLNDPRRL NVALTRARYG VIIVGNPKAL SKQPLWNHLL 

       910        920        930        940        950        960 
NYYKEQKVLV EGPLNNLRES LMQFSKPRKL VNTINPGARF MTTAMYDARE AIIPGSVYDR 

       970        980        990       1000       1010       1020 
SSQGRPSSMY FQTHDQIGMI SAGPSHVAAM NIPIPFNLVM PPMPPPGYFG QANGPAAGRG 

      1030       1040       1050       1060       1070       1080 
TPKGKTGRGG RQKNRFGLPG PSQTNLPNSQ ASQDVASQPF SQGALTQGYI SMSQPSQMSQ 

      1090       1100       1110       1120 
PGLSQPELSQ DSYLGDEFKS QIDVALSQDS TYQGERAYQH GGVTGLSQY 

« Hide

Isoform 2 [UniParc].

Checksum: A485D3ED52C39D06
Show »

FASTA1,118123,036

References

« Hide 'large scale' references
[1]"Mammalian orthologues of a yeast regulator of nonsense transcript stability."
Perlick H.A., Medghalchi S.M., Spencer F.A., Kendzior R.J. Jr., Dietz H.C.
Proc. Natl. Acad. Sci. U.S.A. 93:10928-10932(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Heart.
[2]"Cloning and characterization of HUPF1, a human homolog of the Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein."
Applequist S.E., Selg M., Raman C., Jaeck H.-M.
Nucleic Acids Res. 25:814-821(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHARACTERIZATION.
[3]"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-69.
Tissue: Bone marrow.
[4]"SMG-2 is a phosphorylated protein required for mRNA surveillance in Caenorhabditis elegans and related to Upf1p of yeast."
Page M.F., Carr B., Anders K.R., Grimson A., Anderson P.
Mol. Cell. Biol. 19:5943-5951(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[7]"Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon."
Lykke-Andersen J., Shu M.-D., Steitz J.A.
Cell 103:1121-1131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH WITH UPF2; UPF3A AND UPF3B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-843.
[8]"Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes."
Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.
Mol. Cell. Biol. 20:8944-8957(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UPF2.
[9]"Characterization of the biochemical properties of the human Upf1 gene product that is involved in nonsense-mediated mRNA decay."
Bhattacharya A., Czaplinski K., Trifillis P., He F., Jacobson A., Peltz S.W.
RNA 6:1226-1235(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, RNA-BINDING, MUTAGENESIS OF 647-ASP-GLU-648.
[10]"Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1089 AND SER-1107, MUTAGENESIS OF SER-1089; SER-1107 AND GLN-1108.
[11]"Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein."
Denning G., Jamieson L., Maquat L.E., Thompson E.A., Fields A.P.
J. Biol. Chem. 276:22709-22714(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[12]"Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)."
Serin G., Gersappe A., Black J.D., Aronoff R., Maquat L.E.
Mol. Cell. Biol. 21:209-223(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UPF2, SUBCELLULAR LOCATION.
[13]"Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
Lykke-Andersen J., Shu M.-D., Steitz J.A.
Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, ASSOCIATION WITH THE EJC COMPLEX.
[14]"Phosphorylation of hUPF1 induces formation of mRNA surveillance complexes containing hSMG-5 and hSMG-7."
Ohnishi T., Yamashita A., Kashima I., Schell T., Anders K.R., Grimson A., Hachiya T., Hentze M.W., Anderson P., Ohno S.
Mol. Cell 12:1187-1200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[15]"Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1."
Chiu S.-Y., Serin G., Ohara O., Maquat L.E.
RNA 9:77-87(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EST1A.
[16]"SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway."
Fukuhara N., Ebert J., Unterholzner L., Lindner D., Izaurralde E., Conti E.
Mol. Cell 17:537-547(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMG7.
[17]"Regulated degradation of replication-dependent histone mRNAs requires both ATR and Upf1."
Kaygun H., Marzluff W.F.
Nat. Struct. Mol. Biol. 12:794-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLBP, MUTAGENESIS OF LYS-509 AND ARG-843.
[18]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Binding of a novel SMG-1-Upf1-eRF1-eRF3 complex (SURF) to the exon junction complex triggers Upf1 phosphorylation and nonsense-mediated mRNA 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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SURF COMPLEX, PHOSPHORYLATION AT SER-1089 AND SER-1107, MUTAGENESIS OF CYS-126; LYS-509; SER-1084; SER-1089; SER-1107 AND SER-1127.
[20]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[21]"ATM and ATR substrate analysis reveals extensive protein networks responsive 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[22]"Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
Mullen T.E., Marzluff W.F.
Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
[23]"A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay."
Singh G., Rebbapragada I., Lykke-Andersen J.
PLoS Biol. 6:E111-E111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSPT2.
[24]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact in the cell nucleus."
Agranat L., Raitskin O., Sperling J., Sperling R.
Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAR, SUBCELLULAR LOCATION.
[26]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE SMG1C COMPLEX, MUTAGENESIS OF CYS-126.
[28]"Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex."
Cho H., Kim K.M., Kim Y.K.
Mol. Cell 33:75-86(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PNRC2, MUTAGENESIS OF 506-GLY--GLY-508.
[29]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[30]"Upf1 ATPase-dependent mRNP disassembly is required for completion of nonsense- mediated mRNA decay."
Franks T.M., Singh G., Lykke-Andersen J.
Cell 143:938-950(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNP DISASSEMBLY.
[31]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; SER-1110 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[32]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"Structural and functional insights into the human Upf1 helicase core."
Cheng Z., Muhlrad D., Lim M.K., Parker R., Song H.
EMBO J. 26:253-264(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 295-914, MUTAGENESIS OF LYS-509; 610-LYS--ARG-612; ARG-615; 647-ASP-GLU-648; GLN-676; ARG-714 AND ARG-876.
[35]"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2."
Clerici M., Mourao A., Gutsche I., Gehring N.H., Hentze M.W., Kulozik A., Kadlec J., Sattler M., Cusack S.
EMBO J. 28:2293-2306(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 115-914 IN COMPLEX WITH UPF2.
[36]"Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2."
Chakrabarti S., Jayachandran U., Bonneau F., Fiorini F., Basquin C., Domcke S., Le Hir H., Conti E.
Mol. Cell 41:693-703(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 295-925 IN COMPLEX WITH ATP ANALOG AND RNA, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65533 mRNA. Translation: AAC50771.1.
U59323 mRNA. Translation: AAC51140.1.
D86988 mRNA. Translation: BAA19664.2. Different initiation.
AF074016 mRNA. Translation: AAC26788.1.
AC003972 Genomic DNA. Translation: AAB94785.1.
BC039817 mRNA. Translation: AAH39817.1.
CCDSCCDS12386.1. [Q92900-2]
RefSeqNP_002902.2. NM_002911.3. [Q92900-2]
XP_005260072.1. XM_005260015.1. [Q92900-1]
UniGeneHs.515266.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GJKX-ray2.60A295-925[»]
2GK6X-ray2.40A/B295-925[»]
2GK7X-ray2.80A295-925[»]
2IYKX-ray2.95A/B115-272[»]
2WJVX-ray2.85A/B115-925[»]
2WJYX-ray2.50A115-925[»]
2XZOX-ray2.40A295-925[»]
2XZPX-ray2.72A295-925[»]
ProteinModelPortalQ92900.
SMRQ92900. Positions 116-925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111908. 87 interactions.
DIPDIP-29875N.
IntActQ92900. 78 interactions.
MINTMINT-5005507.
STRING9606.ENSP00000262803.

PTM databases

PhosphoSiteQ92900.

Polymorphism databases

DMDM17380291.

Proteomic databases

MaxQBQ92900.
PaxDbQ92900.
PRIDEQ92900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262803; ENSP00000262803; ENSG00000005007. [Q92900-2]
ENST00000599848; ENSP00000470142; ENSG00000005007. [Q92900-1]
GeneID5976.
KEGGhsa:5976.
UCSCuc002nkf.3. human. [Q92900-2]
uc002nkg.3. human. [Q92900-1]

Organism-specific databases

CTD5976.
GeneCardsGC19P018942.
HGNCHGNC:9962. UPF1.
HPAHPA019587.
HPA020857.
MIM601430. gene.
neXtProtNX_Q92900.
PharmGKBPA34328.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1112.
HOGENOMHOG000205990.
HOVERGENHBG061556.
InParanoidQ92900.
KOK14326.
OMAFLALHEQ.
OrthoDBEOG76QFGF.
PhylomeDBQ92900.
TreeFamTF300554.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ92900.
BgeeQ92900.
CleanExHS_UPF1.
GenevestigatorQ92900.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR027417. P-loop_NTPase.
IPR018999. RNA-helicase_UPF1_UPF2-interct.
[Graphical view]
PfamPF09416. UPF1_Zn_bind. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUPF1. human.
EvolutionaryTraceQ92900.
GeneWikiUPF1.
GenomeRNAi5976.
NextBio23259.
PROQ92900.
SOURCESearch...

Entry information

Entry nameRENT1_HUMAN
AccessionPrimary (citable) accession number: Q92900
Secondary accession number(s): O00239 expand/collapse secondary AC list , O43343, Q86Z25, Q92842
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM