Reviewed, UniProtKB/Swiss-Prot Q92900 (RENT1_HUMAN)

Names and origin

Protein names

Recommended name:
    Regulator of nonsense transcripts 1
    EC=3.6.1.-
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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1129 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Part of a post-splicing multiprotein complex. Involved in nonsense-mediated decay (NMD) as part of the SMG1C complex, a mRNA surveillance complex that recognizes and degrades mRNAs containing premature translation termination codons (PTCs). The complex probably acts by associating with ribosomes during tranlation termination on mRNPs. If an exon junction complex (EJC) is located 50-55 or more nucleotides downstream from the termination codon, RENT1 is phosphorylated by SMG1, triggering nonsense-mediated decay (NMD). Essential for embryonic viability. Ref.7
Subunit structure	Found in a complex with RENT1, RENT2, RENT3A and RENT3B. Found in a complex with PARN. Found in a post-splicing complex with SMG1, NXF1, RBM8A, RENT1, RENT2, RENT3A, RENT3B and RNPS1. Found in a mRNA decay complex with EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, DCP2, RENT1, RENT2 and RENT3B. Interacts with EST1A and RENT2. Component of the SMG1C complex, at least composed of SMG1, SMG8 and SMG9. The SMG1C complex is then recruited on premature translation termination codons (PTCs) to form the ribosome:SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Interacts (when hyperphosphorylated) with PNRC2. Ref.8 Ref.11 Ref.15
Subcellular location	Cytoplasm. Cytoplasm › P-body. Note: Hyperphosphorylated form is targeted to the P-body, while unphosphorylated protein is distributed throughout the cytoplasm. Ref.7 Ref.11
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.14 Ref.16 Ref.17 Ref.18
Sequence similarities	Belongs to the DNA2/NAM7 helicase family. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: HGNC DNA replication Inferred from mutant phenotype. Source: HGNC cell cycle Inferred from mutant phenotype. Source: HGNC mRNA export from nucleus Traceable author statement. Source: HGNC nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Ref.1 Inferred from direct assay. Source: UniProtKB regulation of translational termination Inferred from mutant phenotype. Source: UniProtKB
Cellular component	chromatin Inferred from direct assay. Source: HGNC cytoplasm Ref.2 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Ref.15 Inferred from direct assay. Source: HGNC DNA binding Inferred from electronic annotation. Source: InterPro RNA binding Non-traceable author statement. Source: UniProtKB chromatin binding Inferred from direct assay. Source: HGNC protein binding Ref.9 Ref.14 Ref.21 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q9UI30	1	EBI-373471,EBI-373326
ACSS2	Q9NR19	1	EBI-373471,EBI-372879
BAT5	O95870	1	EBI-373471,EBI-348517
DCP1A	Q9NPI6	2	EBI-373471,EBI-374238
DCP2	Q8IU60	2	EBI-373471,EBI-521577
DOM3Z	O77932	1	EBI-373471,EBI-372173
EIF3A	Q14152	3	EBI-373492,EBI-366617
GNPTG	Q9UJJ9	1	EBI-373471,EBI-372067
HIRA	P54198	1	EBI-373471,EBI-372342
LSM8	O95777	1	EBI-373471,EBI-347779
NADSYN1	Q6IA69	1	EBI-373471,EBI-748610
NDRG1	Q92597	1	EBI-373471,EBI-716486
PLEKHB2	Q96CS7	1	EBI-373471,EBI-373552
RHOXF2	Q9BQY4	1	EBI-373471,EBI-372094
RPRD2	Q5VT52	1	EBI-373471,EBI-372367
SKI7	Q08491	1	EBI-373471,EBI-1389	From a different organism.
STAU1	O95793	2	EBI-373471,EBI-358174

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.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1129

1129

Regulator of nonsense transcripts 1

PRO_0000080716

Regions

Zinc finger

131 – 159

29

C2H2-type; atypical

Zinc finger

183 – 213

31

C4-type

Nucleotide binding

503 – 510

8

ATP Potential

Region

1 – 415

415

Sufficient for interaction with RENT2

Motif

1089 – 1090

2

[ST]-Q motif 1

Motif

1107 – 1108

2

[ST]-Q motif 2

Compositional bias

47 – 80

34

Ala/Gly/Pro-rich

Compositional bias

1042 – 1129

88

Gln/Ser-rich

Amino acid modifications

Modified residue

1089

1

Phosphoserine Probable

Modified residue

1107

1

Phosphoserine Ref.9 Ref.16 Ref.18

Modified residue

1127

1

Phosphoserine Ref.16

Modified residue

1129

1

Phosphotyrosine Ref.17

Natural variations

Alternative sequence

353 – 363

11

Missing in isoform 2.

VSP_003393

Natural variant

69

1

A → S: dbSNP rs17339451.

VAR_056207

Experimental info

Mutagenesis

126

1

C → S: Abolishes ability to interact with RENT2/UPF2 and copurifies with greater amounts of SMG1, SMG8 and SMG9.

Mutagenesis

506 – 508

3

GTG → RTE: Prevents dephosphorylation and targets the protein to the P-body.

Mutagenesis

843

1

R → C: Abolishes NMD. Ref.7

Mutagenesis

1089

1

S → A: Still phosphorylated but with less efficiency. Ref.9

Mutagenesis

1107

1

S → A: Impairs phosphorylation. Ref.9

Mutagenesis

1108

1

Q → N: Impairs phosphorylation. Ref.9

Sequence conflict

61

1

G → S in AAC51140. Ref.2

Sequence conflict

466

1

I → T in AAC51140. Ref.2

Sequence conflict

478

1

G → A in AAC50771. Ref.1

Sequence conflict

524

1

G → D in AAC50771. Ref.1

Sequence conflict

557

1

A → P in AAC50771. Ref.1

Sequence conflict

901 – 902

2

NY → IF in AAC50771. Ref.1

Secondary structure

1

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1129

Helix Strand Turn

Details...

Turn

124 – 126

3

Turn

131 – 133

3

Beta strand

134 – 137

4

Turn

138 – 141

4

Beta strand

142 – 146

5

Beta strand

151 – 153

3

Helix

155 – 162

8

Beta strand

168 – 170

3

Turn

184 – 186

3

Turn

191 – 193

3

Beta strand

194 – 197

4

Beta strand

206 – 209

4

Turn

210 – 214

5

Helix

216 – 219

4

Turn

220 – 222

3

Helix

226 – 228

3

Beta strand

230 – 234

5

Turn

240 – 242

3

Helix

248 – 253

6

Helix

259 – 270

12

Helix

299 – 323

25

Beta strand

326 – 329

4

Beta strand

331 – 335

5

Beta strand

341 – 346

6

Beta strand

372 – 377

6

Beta strand

379 – 382

4

Beta strand

386 – 393

8

Beta strand

400 – 407

8

Beta strand

418 – 424

7

Helix

429 – 443

15

Helix

451 – 456

6

Helix

484 – 494

11

Beta strand

497 – 502

6

Helix

509 – 521

13

Beta strand

523 – 525

3

Beta strand

528 – 534

7

Helix

535 – 546

12

Turn

547 – 549

3

Beta strand

552 – 554

3

Helix

559 – 561

3

Turn

566 – 570

5

Helix

572 – 576

5

Helix

583 – 589

7

Helix

600 – 619

20

Beta strand

622 – 627

6

Helix

629 – 632

4

Helix

634 – 636

3

Beta strand

642 – 646

5

Helix

649 – 651

3

Helix

654 – 661

8

Turn

662 – 664

3

Beta strand

665 – 672

8

Helix

684 – 689

6

Turn

690 – 692

3

Helix

695 – 701

7

Helix

717 – 727

11

Beta strand

733 – 736

4

Helix

739 – 741

3

Beta strand

757 – 761

5

Helix

778 – 792

15

Turn

793 – 795

3

Helix

798 – 800

3

Beta strand

801 – 804

4

Helix

808 – 820

13

Helix

826 – 831

6

Beta strand

832 – 835

4

Helix

837 – 840

4

Beta strand

845 – 852

8

Turn

863 – 865

3

Helix

867 – 873

7

Beta strand

876 – 885

10

Helix

887 – 890

4

Helix

894 – 905

12

Helix

914 – 916

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 18, 2001. Version 2. Checksum: 6CCA6FE42B15BA28	FASTA	1,129	124,345
	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
	Isoform 2. Checksum: A485D3ED52C39D06	FASTA	1,118	123,036
	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 DSDMRLMQGD 370 380 390 400 410 420 EICLRYKGDL APLWKGIGHV IKVPDNYGDE IAIELRSSVG APVEVTHNFQ VDFVWKSTSF 430 440 450 460 470 480 DRMQSALKTF AVDETSVSGY IYHKLLGHEV EDVIIKCQLP KRFTAQGLPD LNHSQVYAVK 490 500 510 520 530 540 TVLQRPLSLI QGPPGTGKTV TSATIVYHLA RQGNGPVLVC APSNIAVDQL TEKIHQTGLK 550 560 570 580 590 600 VVRLCAKSRE AIDSPVSFLA LHNQIRNMDS MPELQKLQQL KDETGELSSA DEKRYRALKR 610 620 630 640 650 660 TAERELLMNA DVICCTCVGA GDPRLAKMQF RSILIDESTQ ATEPECMVPV VLGAKQLILV 670 680 690 700 710 720 GDHCQLGPVV MCKKAAKAGL SQSLFERLVV LGIRPIRLQV QYRMHPALSA FPSNIFYEGS 730 740 750 760 770 780 LQNGVTAADR VKKGFDFQWP QPDKPMFFYV TQGQEEIASS GTSYLNRTEA ANVEKITTKL 790 800 810 820 830 840 LKAGAKPDQI GIITPYEGQR SYLVQYMQFS GSLHTKLYQE VEIASVDAFQ GREKDFIILS 850 860 870 880 890 900 CVRANEHQGI GFLNDPRRLN VALTRARYGV IIVGNPKALS KQPLWNHLLN YYKEQKVLVE 910 920 930 940 950 960 GPLNNLRESL MQFSKPRKLV NTINPGARFM TTAMYDAREA IIPGSVYDRS SQGRPSSMYF 970 980 990 1000 1010 1020 QTHDQIGMIS AGPSHVAAMN IPIPFNLVMP PMPPPGYFGQ ANGPAAGRGT PKGKTGRGGR 1030 1040 1050 1060 1070 1080 QKNRFGLPGP SQTNLPNSQA SQDVASQPFS QGALTQGYIS MSQPSQMSQP GLSQPELSQD 1090 1100 1110 SYLGDEFKSQ IDVALSQDST YQGERAYQHG GVTGLSQY

References

	« Hide 'large scale' referencesShow '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: 8855285] [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: 9064659] [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: 9039502] [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: 10454541] [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. , 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: 15057824] [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: 15489334] [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: 11163187] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A COMPLEX WITH RENT2; RENT3A AND RENT3B, 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: 11073994] [Abstract] Cited for: INTERACTION WITH RENT2.
[9]	"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: 11544179] [Abstract] Cited for: PHOSPHORYLATION AT SER-1089 ANS SER-1107, MUTAGENESIS OF SER-1089; SER-1107 AND GLN-1108.
[10]	"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: 11331269] [Abstract] Cited for: PHOSPHORYLATION.
[11]	"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: 11113196] [Abstract] Cited for: INTERACTION WITH RENT2, SUBCELLULAR LOCATION.
[12]	"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: 11546874] [Abstract] Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; RBM8A; RENT2; RENT3A; RENT3B AND RNPS1.
[13]	"Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities." Lejeune F., Li X., Maquat L.E. Mol. Cell 12:675-687(2003) [PubMed: 14527413] [Abstract] Cited for: IDENTIFICATION IN A MRNA DECAY COMPLEX WITH EXOSC2; EXOSC4; EXOSC10; PARN; XRN1; DCP2; RENT2 AND RENT3B.
[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: 14636577] [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: 12554878] [Abstract] Cited for: INTERACTION WITH EST1A.
[16]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1127, MASS SPECTROMETRY.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient 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) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1129, MASS SPECTROMETRY.
[18]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: 19417104] [Abstract] Cited for: IDENTIFICATION IN THE SMG1C COMPLEX, MUTAGENESIS OF CYS-126.
[21]	"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: 19150429] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH PNRC2, MUTAGENESIS OF 506-GLY--GLY-508.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00034049.
IPI00399170.

RefSeq

NP_002902.2.

UniGene

Hs.515266

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GJK	X-ray	2.60	A	295-914	[»]
2GK6	X-ray	2.40	A/B	295-914	[»]
2GK7	X-ray	2.80	A	295-914	[»]
2IYK	X-ray	2.95	A/B	115-272	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92900. 37 interactions.

PTM databases

PhosphoSite

Q92900.

Proteomic databases

PRIDE

Q92900.

Genome annotation databases

Ensembl

ENSG00000005007. Homo sapiens. [Contig view]

GeneID

5976.

KEGG

hsa:5976.

UCSC

uc002nkf.1. human.
uc002nkg.1. human.

Organism-specific databases

GeneCards

GC19P018804.

H-InvDB

HIX0014926.

HGNC

HGNC:9962. UPF1.

MIM

601430. gene.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q92900.

HOVERGEN

Q92900.

OMA

Q92900. SEFPSNM.

Gene expression databases

ArrayExpress

Q92900.

Bgee

Q92900.

CleanEx

HS_UPF1.

GermOnline

ENSG00000005007. Homo sapiens.

Family and domain databases

InterPro

IPR006935. Restrct_endonuc_I_R/III_Res.
IPR018999. RNA-helicase_UPF1_UPF2-interct.
[Graphical view]

Pfam

PF04851. ResIII. 1 hit.
PF09416. UPF1_Zn_bind. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

23259.

SOURCE

Search...

Entry information

Entry name

RENT1_HUMAN

Accession

Primary (citable) accession number: Q92900
Secondary accession number(s): O00239 , O43343, Q86Z25, Q92842

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	October 18, 2001
Last modified:	July 7, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)