Q9HAU5 (RENT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of nonsense transcripts 2

Alternative name(s):
Nonsense mRNA reducing factor 2
Up-frameshift suppressor 2 homolog
Short name=hUpf2

Gene names

Name:	UPF2
Synonyms:	KIAA1408, RENT2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1272 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA. Ref.2 Ref.13 Ref.15
Subunit structure	Found in a post-splicing messenger ribonucleoprotein (mRNP) complex. Associates with the exon junction complex (EJC). Interacts with SMG1, EST1A, UPF1, UPF3A, UPF3B, EIF4A1 and EIF1. Ref.1 Ref.2 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Cytoplasm › perinuclear region Ref.1 Ref.2 Ref.3.
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Contains 3 MIF4G domains.
Sequence caution	The sequence BAA92646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gene expression Traceable author statement. Source: Reactome liver development Inferred from electronic annotation. Source: Compara mRNA export from nucleus Traceable author statement PubMed 16488880. Source: HGNC nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype PubMed 18369367. Source: UniProtKB organ regeneration Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome exon-exon junction complex Inferred from direct assay PubMed 16601204. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMG1	Q96Q15	6	EBI-372073,EBI-1049832
UPF1	Q92900	8	EBI-372073,EBI-373471
UPF3B	Q9BZI7	6	EBI-372073,EBI-372780

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HAU5-1)

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: Q9HAU5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-83: Missing.
     588-609: AMDFCMNMNTKANRKKLVRALF → EKAFCNGNLARVNLLLRMAVKK
     610-1272: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1272

1272

Regulator of nonsense transcripts 2

PRO_0000097248

Regions

Domain

168 – 431

264

MIF4G 1

Domain

569 – 758

190

MIF4G 2

Domain

773 – 986

214

MIF4G 3

Region

94 – 133

40

Sufficient for interaction with UPF1

Region

711 – 928

218

Sufficient for interaction with UPF3A and UPF3B

Region

757 – 1272

516

Sufficient for interaction with EIF4A1 and EIF1

Region

839 – 859

21

Binds to UPF3B

Region

1084 – 1272

189

Sufficient for interaction with UPF1 C-terminus

Region

1105 – 1198

94

Necessary for interaction with UPF1

Region

1105 – 1129

25

Interaction with UPF1

Region

1167 – 1207

41

Interaction with UPF1

Coiled coil

54 – 134

81

Potential

Coiled coil

487 – 559

73

Potential

Compositional bias

6 – 136

131

Glu/Lys-rich

Compositional bias

1025 – 1094

70

Glu-rich

Amino acid modifications

Modified residue

1088

1

Phosphothreonine Ref.17

Natural variations

Alternative sequence

54 – 83

30

Missing in isoform 2.

VSP_012958

Alternative sequence

588 – 609

22

AMDFC…VRALF → EKAFCNGNLARVNLLLRMAV KK in isoform 2.

VSP_012959

Alternative sequence

610 – 1272

663

Missing in isoform 2.

VSP_012960

Natural variant

496

1

N → S.
Corresponds to variant rs7079388 [ dbSNP | Ensembl ].

VAR_024345

Experimental info

Mutagenesis

796 – 797

2

RK → EE: Strongly impairs RNA-binding.

Mutagenesis

847

1

D → K: Does not abolish interaction with UPF3B. Ref.18

Mutagenesis

851 – 852

2

ED → KR: Does not abolish interaction with UPF3B. Does not abolish interaction with UPF3B; when associated with D-854.

Mutagenesis

854

1

R → D: Does not abolish interaction with UPF3B; when associated with K-851 and R-852. Ref.18

Mutagenesis

858

1

E → R: Abolishes interaction with UPF3B and association with SMG1 and RBM8A; reduces phosphorylation of UPF1. Ref.14 Ref.18

Mutagenesis

894

1

Y → A: Does not impair RNA-binding; when associated with A-932. Ref.18

Mutagenesis

932

1

Y → A: Does not impair RNA-binding; when associated with A-894. Ref.18

Mutagenesis

1113

1

F → E: Abolishes interaction with UPF1.

Mutagenesis

1120

1

M → E: Decreases interaction with UPF1; does not reduce NMD efficiency. Ref.19

Mutagenesis

1121

1

M → E: Decreases interaction with UPF1; does not reduce NMD efficiency. Ref.19

Mutagenesis

1123

1

E → R: Decreases interaction with UPF1. Ref.19

Mutagenesis

1169

1

M → E: Decreases interaction with UPF1. Ref.19

Mutagenesis

1171

1

F → E: Abolishes interaction with UPF1; reduces NMD efficiency. Ref.19

Mutagenesis

1171

1

F → E: Greatly reduces NMD efficiency; when associated with E-1173 and E-1174. Ref.19

Mutagenesis

1173

1

M → E: Abolishes interaction with UPF1. Ref.19

Mutagenesis

1173

1

M → E: Greatly reduces NMD efficiency; when associated with E-1171 and E-1174. Ref.19

Mutagenesis

1174

1

L → E: Abolishes interaction with UPF1; reduces NMD efficiency. Ref.19

Mutagenesis

1174

1

L → E: Greatly reduces NMD efficiency; when associated with E-1171 and E-1173. Ref.19

Mutagenesis

1176

1

R → E: Decreases interaction with UPF1. Ref.19

Sequence conflict

119

1

A → T in BAC04721. Ref.5

Sequence conflict

338

1

F → L in BAC04721. Ref.5

Sequence conflict

844

1

H → Q in AAG48509. Ref.2

Sequence conflict

844

1

H → Q in BAA92646. Ref.4

Sequence conflict

969

1

P → S in BAA92646. Ref.4

Secondary structure

1

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1272

Helix Strand Turn

Details...

Helix

770 – 780

11

Helix

788 – 796

9

Helix

803 – 814

12

Helix

816 – 818

3

Helix

821 – 823

3

Helix

824 – 834

11

Turn

835 – 837

3

Helix

839 – 859

21

Helix

862 – 864

3

Helix

865 – 880

16

Helix

886 – 898

13

Beta strand

909 – 911

3

Helix

917 – 929

13

Helix

930 – 932

3

Helix

936 – 957

22

Beta strand

964 – 966

3

Helix

970 – 983

14

Helix

993 – 1011

19

Helix

1108 – 1126

19

Beta strand

1168 – 1174

7

Beta strand

1183 – 1192

10

Helix

1193 – 1197

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 95F3C57D2854BB44	FASTA	1,272	147,810
	10 20 30 40 50 60 MPAERKKPAS MEEKDSLPNN KEKDCSERRT VSSKERPKDD IKLTAKKEVS KAPEDKKKRL 70 80 90 100 110 120 EDDKRKKEDK ERKKKDEEKV KAEEESKKKE EEEKKKHQEE ERKKQEEQAK RQQEEEAAAQ 130 140 150 160 170 180 MKEKEESIQL HQEAWERHHL RKELRSKNQN APDSRPEENF FSRLDSSLKK NTAFVKKLKT 190 200 210 220 230 240 ITEQQRDSLS HDFNGLNLSK YIAEAVASIV EAKLKISDVN CAVHLCSLFH QRYADFAPSL 250 260 270 280 290 300 LQVWKKHFEA RKEEKTPNIT KLRTDLRFIA ELTIVGIFTD KEGLSLIYEQ LKNIINADRE 310 320 330 340 350 360 SHTHVSVVIS FCRHCGDDIA GLVPRKVKSA AEKFNLSFPP SEIISPEKQQ PFQNLLKEYF 370 380 390 400 410 420 TSLTKHLKRD HRELQNTERQ NRRILHSKGE LSEDRHKQYE EFAMSYQKLL ANSQSLADLL 430 440 450 460 470 480 DENMPDLPQD KPTPEEHGPG IDIFTPGKPG EYDLEGGIWE DEDARNFYEN LIDLKAFVPA 490 500 510 520 530 540 ILFKDNEKSC QNKESNKDDT KEAKESKENK EVSSPDDLEL ELENLEINDD TLELEGGDEA 550 560 570 580 590 600 EDLTKKLLDE QEQEDEEAST GSHLKLIVDA FLQQLPNCVN RDLIDKAAMD FCMNMNTKAN 610 620 630 640 650 660 RKKLVRALFI VPRQRLDLLP FYARLVATLH PCMSDVAEDL CSMLRGDFRF HVRKKDQINI 670 680 690 700 710 720 ETKNKTVRFI GELTKFKMFT KNDTLHCLKM LLSDFSHHHI EMACTLLETC GRFLFRSPES 730 740 750 760 770 780 HLRTSVLLEQ MMRKKQAMHL DARYVTMVEN AYYYCNPPPA EKTVKKKRPP LQEYVRKLLY 790 800 810 820 830 840 KDLSKVTTEK VLRQMRKLPW QDQEVKDYVI CCMINIWNVK YNSIHCVANL LAGLVLYQED 850 860 870 880 890 900 VGIHVVDGVL EDIRLGMEVN QPKFNQRRIS SAKFLGELYN YRMVESAVIF RTLYSFTSFG 910 920 930 940 950 960 VNPDGSPSSL DPPEHLFRIR LVCTILDTCG QYFDRGSSKR KLDCFLVYFQ RYVWWKKSLE 970 980 990 1000 1010 1020 VWTKDHPFPI DIDYMISDTL ELLRPKIKLC NSLEESIRQV QDLEREFLIK LGLVNDKDSK 1030 1040 1050 1060 1070 1080 DSMTEGENLE EDEEEEEGGA ETEEQSGNES EVNEPEEEEG SDNDDDEGEE EEEENTDYLT 1090 1100 1110 1120 1130 1140 DSNKENETDE ENTEVMIKGG GLKHVPCVED EDFIQALDKM MLENLQQRSG ESVKVHQLDV 1150 1160 1170 1180 1190 1200 AIPLHLKSQL RKGPPLGGGE GEAESADTMP FVMLTRKGNK QQFKILNVPM SSQLAANHWN 1210 1220 1230 1240 1250 1260 QQQAEQEERM RMKKLTLDIN ERQEQEDYQE MLQSLAQRPA PANTNRERRP RYQHPKGAPN 1270 ADLIFKTGGR RR
	Isoform 2 [UniParc]. Checksum: FA8367F0C864C24E	FASTA	579	66,842
	10 20 30 40 50 60 MPAERKKPAS MEEKDSLPNN KEKDCSERRT VSSKERPKDD IKLTAKKEVS KAPEESKKKE 70 80 90 100 110 120 EEEKKKHQEE ERKKQEEQAK RQQEEEAAAQ MKEKEESIQL HQEAWERHHL RKELRSKNQN 130 140 150 160 170 180 APDSRPEENF FSRLDSSLKK NTAFVKKLKT ITEQQRDSLS HDFNGLNLSK YIAEAVASIV 190 200 210 220 230 240 EAKLKISDVN CAVHLCSLFH QRYADFAPSL LQVWKKHFEA RKEEKTPNIT KLRTDLRFIA 250 260 270 280 290 300 ELTIVGIFTD KEGLSLIYEQ LKNIINADRE SHTHVSVVIS FCRHCGDDIA GLVPRKVKSA 310 320 330 340 350 360 AEKFNLSFPP SEIISPEKQQ PFQNLLKEYF TSLTKHLKRD HRELQNTERQ NRRILHSKGE 370 380 390 400 410 420 LSEDRHKQYE EFAMSYQKLL ANSQSLADLL DENMPDLPQD KPTPEEHGPG IDIFTPGKPG 430 440 450 460 470 480 EYDLEGGIWE DEDARNFYEN LIDLKAFVPA ILFKDNEKSC QNKESNKDDT KEAKESKENK 490 500 510 520 530 540 EVSSPDDLEL ELENLEINDD TLELEGGDEA EDLTKKLLDE QEQEDEEAST GSHLKLIVDA 550 560 570 FLQQLPNCVN RDLIDKAEKA FCNGNLARVN LLLRMAVKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UPF1; EIF4A1 AND EIF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Heart.
[2]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH UPF1; UPF3A AND UPF3B, SUBCELLULAR LOCATION.
[3]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UPF1; UPF3A AND UPF3B, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[4]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1023-1272.
[6]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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].
[9]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-1272. Tissue: Testis.
[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: INTERACTION WITH SMG1.
[11]	"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.
[12]	"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.
[13]	"Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements." Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E. Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A COMPLEX WITH UPF3B AND RNPS1.
[14]	"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: SUBUNIT, MUTAGENESIS OF GLU-858.
[15]	"NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity." Chamieh H., Ballut L., Bonneau F., Le Hir H. Nat. Struct. Mol. Biol. 15:85-93(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, RECONSTITUTION OF THE EJC CORE-UPF COMPLEX.
[16]	"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].
[17]	"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 THR-1088, MASS SPECTROMETRY.
[18]	"The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3." Kadlec J., Izaurralde E., Cusack S. Nat. Struct. Mol. Biol. 11:330-337(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 768-1015 IN COMPLEX WITH UPF3B RNP-LIKE DOMAIN, RNA-BINDING, MUTAGENESIS OF 796-ARG-ARG-797; ASP-847; 851-GLU-ASP-852; ARG-854; GLU-858; TYR-894 AND TYR-932.
[19]	"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 1105-1198 IN COMPLEX WITH UPF1, MUTAGENESIS OF MET-1120; MET-1121; GLU-1123; MET-1169; PHE-1171; MET-1173; LEU-1174 AND ARG-1176.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF301013 mRNA. Translation: AAG33225.1.
AY013249 mRNA. Translation: AAG48509.1.
AF318574 mRNA. Translation: AAG60689.1.
AB037829 mRNA. Translation: BAA92646.1. Different initiation.
AK000764 mRNA. Translation: BAA91369.1.
AK096191 mRNA. Translation: BAC04721.1.
AL138898, AC073160, AL645617 Genomic DNA. Translation: CAH73458.1.
AL138898, AC073160, AL645617 Genomic DNA. Translation: CAH73459.1.
AL645617, AC073160, AL138898 Genomic DNA. Translation: CAI16755.1.
AL645617, AC073160, AL138898 Genomic DNA. Translation: CAI16756.1.
CH471072 Genomic DNA. Translation: EAW86329.1.
CH471072 Genomic DNA. Translation: EAW86330.1.
CH471072 Genomic DNA. Translation: EAW86332.1.
CH471072 Genomic DNA. Translation: EAW86333.1.
BC114964 mRNA. Translation: AAI14965.1.
BC115737 mRNA. Translation: AAI15738.1.
AL080198 mRNA. Translation: CAB45771.1.

IPI

IPI00300504.
IPI00472081.

PIR

T12507.

RefSeq

NP_056357.1. NM_015542.3.
NP_542166.1. NM_080599.2.

UniGene

Hs.370689.
Hs.610110.
Hs.732383.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UW4	X-ray	1.95	B/D	768-1015	[»]
2WJV	X-ray	2.85	D/E	1105-1198	[»]

ProteinModelPortal

Q9HAU5.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31148N.

IntAct

Q9HAU5. 30 interactions.

MINT

MINT-265195.

PTM databases

PhosphoSite

Q9HAU5.

Polymorphism databases

DMDM

60390647.

Proteomic databases

PaxDb

Q9HAU5.

PRIDE

Q9HAU5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356352; ENSP00000348708; ENSG00000151461.
ENST00000357604; ENSP00000350221; ENSG00000151461.
ENST00000379172; ENSP00000368470; ENSG00000151461.
ENST00000397053; ENSP00000380244; ENSG00000151461.

GeneID

26019.

KEGG

hsa:26019.

UCSC

uc001ila.3. human.

Organism-specific databases

CTD

26019.

GeneCards

GC10M011962.

HGNC

HGNC:17854. UPF2.

MIM

605529. gene.

neXtProt

NX_Q9HAU5.

PharmGKB

PA134945630.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG321770.

HOVERGEN

HBG079124.

InParanoid

Q9HAU5.

KO

K14327.

OMA

YLEQMMR.

OrthoDB

EOG4W3SM5.

PhylomeDB

Q9HAU5.

Enzyme and pathway databases

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9HAU5.

Bgee

Q9HAU5.

Genevestigator

Q9HAU5.

GermOnline

ENSG00000151461. Homo sapiens.

Family and domain databases

Gene3D

1.25.40.180. 4 hits.

InterPro

IPR016024. ARM-type_fold.
IPR016021. MIF4-like_typ_1/2/3.
IPR003890. MIF4G-like_typ-3.
IPR007193. Up-fram_suppressor-2.
[Graphical view]

Pfam

PF02854. MIF4G. 3 hits.
PF04050. Upf2. 1 hit.
[Graphical view]

SMART

SM00543. MIF4G. 3 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 3 hits.

ProtoNet

Search...

Other

ChiTaRS

UPF2. human.

EvolutionaryTrace

Q9HAU5.

GenomeRNAi

26019.

NextBio

47788.

SOURCE

Search...

Entry information

Entry name

RENT2_HUMAN

Accession

Primary (citable) accession number: Q9HAU5
Secondary accession number(s): A6NLJ5 , D3DRS0, Q14BM1, Q5W0J4, Q8N8U1, Q9H1J2, Q9NWL1, Q9P2D9, Q9Y4M9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.