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Q9HAU5

- RENT2_HUMAN

UniProt

Q9HAU5 - RENT2_HUMAN

Protein

Regulator of nonsense transcripts 2

Gene

UPF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. gene expression Source: Reactome
    2. liver development Source: Ensembl
    3. mRNA export from nucleus Source: HGNC
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    6. organ regeneration Source: Ensembl
    7. RNA metabolic process Source: Reactome

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of nonsense transcripts 2
    Alternative name(s):
    Nonsense mRNA reducing factor 2
    Up-frameshift suppressor 2 homolog
    Short name:
    hUpf2
    Gene namesi
    Name:UPF2
    Synonyms:KIAA1408, RENT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17854. UPF2.

    Subcellular locationi

    Cytoplasmperinuclear region 3 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. cytosol Source: Reactome
    3. exon-exon junction complex Source: UniProtKB
    4. nucleus Source: HGNC
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi796 – 7972RK → EE: Strongly impairs RNA-binding.
    Mutagenesisi847 – 8471D → K: Does not abolish interaction with UPF3B. 1 Publication
    Mutagenesisi851 – 8522ED → KR: Does not abolish interaction with UPF3B. Does not abolish interaction with UPF3B; when associated with D-854.
    Mutagenesisi854 – 8541R → D: Does not abolish interaction with UPF3B; when associated with K-851 and R-852. 1 Publication
    Mutagenesisi858 – 8581E → R: Abolishes interaction with UPF3B and association with SMG1 and RBM8A; reduces phosphorylation of UPF1. 2 Publications
    Mutagenesisi894 – 8941Y → A: Does not impair RNA-binding; when associated with A-932. 1 Publication
    Mutagenesisi932 – 9321Y → A: Does not impair RNA-binding; when associated with A-894. 1 Publication
    Mutagenesisi1113 – 11131F → E: Abolishes interaction with UPF1.
    Mutagenesisi1120 – 11201M → E: Decreases interaction with UPF1; does not reduce NMD efficiency. 1 Publication
    Mutagenesisi1121 – 11211M → E: Decreases interaction with UPF1; does not reduce NMD efficiency. 1 Publication
    Mutagenesisi1123 – 11231E → R: Decreases interaction with UPF1. 1 Publication
    Mutagenesisi1169 – 11691M → E: Decreases interaction with UPF1. 1 Publication
    Mutagenesisi1171 – 11711F → E: Abolishes interaction with UPF1; reduces NMD efficiency. 1 Publication
    Mutagenesisi1171 – 11711F → E: Greatly reduces NMD efficiency; when associated with E-1173 and E-1174. 1 Publication
    Mutagenesisi1173 – 11731M → E: Abolishes interaction with UPF1. 1 Publication
    Mutagenesisi1173 – 11731M → E: Greatly reduces NMD efficiency; when associated with E-1171 and E-1174. 1 Publication
    Mutagenesisi1174 – 11741L → E: Abolishes interaction with UPF1; reduces NMD efficiency. 1 Publication
    Mutagenesisi1174 – 11741L → E: Greatly reduces NMD efficiency; when associated with E-1171 and E-1173. 1 Publication
    Mutagenesisi1176 – 11761R → E: Decreases interaction with UPF1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134945630.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12721272Regulator of nonsense transcripts 2PRO_0000097248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1088 – 10881Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HAU5.
    PaxDbiQ9HAU5.
    PRIDEiQ9HAU5.

    PTM databases

    PhosphoSiteiQ9HAU5.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9HAU5.
    BgeeiQ9HAU5.
    GenevestigatoriQ9HAU5.

    Interactioni

    Subunit structurei

    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 EIF1.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SMG1Q96Q157EBI-372073,EBI-1049832
    UPF1Q9290025EBI-372073,EBI-373471
    UPF3BQ9BZI76EBI-372073,EBI-372780

    Protein-protein interaction databases

    BioGridi117490. 87 interactions.
    DIPiDIP-31148N.
    IntActiQ9HAU5. 35 interactions.
    MINTiMINT-265195.

    Structurei

    Secondary structure

    1
    1272
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi122 – 14928
    Helixi152 – 1543
    Helixi158 – 1625
    Helixi168 – 17710
    Helixi178 – 1803
    Helixi183 – 1853
    Helixi186 – 19510
    Helixi202 – 21110
    Helixi216 – 2183
    Helixi219 – 23214
    Helixi236 – 25318
    Helixi259 – 27416
    Helixi280 – 29718
    Beta strandi299 – 3013
    Helixi305 – 32016
    Helixi325 – 33410
    Helixi346 – 37530
    Turni376 – 3827
    Helixi383 – 3864
    Turni387 – 3893
    Turni395 – 3984
    Helixi399 – 41921
    Beta strandi460 – 4623
    Helixi463 – 4697
    Helixi474 – 4763
    Helixi539 – 54911
    Helixi560 – 57415
    Helixi575 – 5773
    Helixi581 – 59414
    Helixi598 – 60912
    Helixi613 – 6186
    Helixi619 – 62911
    Turni630 – 6323
    Helixi635 – 65319
    Helixi660 – 67516
    Helixi681 – 69313
    Helixi697 – 71620
    Helixi718 – 73720
    Helixi742 – 75514
    Helixi770 – 78011
    Helixi788 – 7969
    Helixi803 – 81412
    Helixi816 – 8183
    Helixi821 – 8233
    Helixi824 – 83411
    Turni835 – 8373
    Helixi839 – 85921
    Helixi862 – 8643
    Helixi865 – 88016
    Helixi886 – 89813
    Beta strandi909 – 9113
    Helixi917 – 92913
    Helixi930 – 9323
    Helixi936 – 95722
    Beta strandi964 – 9663
    Helixi970 – 98314
    Helixi993 – 101119
    Helixi1108 – 112619
    Beta strandi1168 – 11747
    Beta strandi1183 – 119210
    Helixi1193 – 11975

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UW4X-ray1.95B/D768-1015[»]
    2WJVX-ray2.85D/E1105-1198[»]
    4CEKX-ray2.35A455-757[»]
    4CEMX-ray2.60A/B121-486[»]
    ProteinModelPortaliQ9HAU5.
    SMRiQ9HAU5. Positions 121-429, 457-757, 768-1014, 1105-1198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HAU5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 431264MIF4G 1Add
    BLAST
    Domaini569 – 758190MIF4G 2Add
    BLAST
    Domaini773 – 986214MIF4G 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 13340Sufficient for interaction with UPF1Add
    BLAST
    Regioni711 – 928218Sufficient for interaction with UPF3A and UPF3BAdd
    BLAST
    Regioni757 – 1272516Sufficient for interaction with EIF4A1 and EIF1Add
    BLAST
    Regioni839 – 85921Binds to UPF3BAdd
    BLAST
    Regioni1084 – 1272189Sufficient for interaction with UPF1 C-terminusAdd
    BLAST
    Regioni1105 – 119894Necessary for interaction with UPF1Add
    BLAST
    Regioni1105 – 112925Interaction with UPF1Add
    BLAST
    Regioni1167 – 120741Interaction with UPF1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili54 – 13481Sequence AnalysisAdd
    BLAST
    Coiled coili487 – 55973Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 136131Glu/Lys-richAdd
    BLAST
    Compositional biasi1025 – 109470Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 MIF4G domains.Curated

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG321770.
    HOVERGENiHBG079124.
    InParanoidiQ9HAU5.
    KOiK14327.
    OMAiIRKLHWE.
    OrthoDBiEOG70GMDS.
    PhylomeDBiQ9HAU5.
    TreeFamiTF300543.

    Family and domain databases

    Gene3Di1.25.40.180. 4 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    IPR007193. Up-fram_suppressor-2.
    [Graphical view]
    PfamiPF02854. MIF4G. 3 hits.
    PF04050. Upf2. 1 hit.
    [Graphical view]
    SMARTiSM00543. MIF4G. 3 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HAU5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPAERKKPAS MEEKDSLPNN KEKDCSERRT VSSKERPKDD IKLTAKKEVS     50
    KAPEDKKKRL EDDKRKKEDK ERKKKDEEKV KAEEESKKKE EEEKKKHQEE 100
    ERKKQEEQAK RQQEEEAAAQ MKEKEESIQL HQEAWERHHL RKELRSKNQN 150
    APDSRPEENF FSRLDSSLKK NTAFVKKLKT ITEQQRDSLS HDFNGLNLSK 200
    YIAEAVASIV EAKLKISDVN CAVHLCSLFH QRYADFAPSL LQVWKKHFEA 250
    RKEEKTPNIT KLRTDLRFIA ELTIVGIFTD KEGLSLIYEQ LKNIINADRE 300
    SHTHVSVVIS FCRHCGDDIA GLVPRKVKSA AEKFNLSFPP SEIISPEKQQ 350
    PFQNLLKEYF TSLTKHLKRD HRELQNTERQ NRRILHSKGE LSEDRHKQYE 400
    EFAMSYQKLL ANSQSLADLL DENMPDLPQD KPTPEEHGPG IDIFTPGKPG 450
    EYDLEGGIWE DEDARNFYEN LIDLKAFVPA ILFKDNEKSC QNKESNKDDT 500
    KEAKESKENK EVSSPDDLEL ELENLEINDD TLELEGGDEA EDLTKKLLDE 550
    QEQEDEEAST GSHLKLIVDA FLQQLPNCVN RDLIDKAAMD FCMNMNTKAN 600
    RKKLVRALFI VPRQRLDLLP FYARLVATLH PCMSDVAEDL CSMLRGDFRF 650
    HVRKKDQINI ETKNKTVRFI GELTKFKMFT KNDTLHCLKM LLSDFSHHHI 700
    EMACTLLETC GRFLFRSPES HLRTSVLLEQ MMRKKQAMHL DARYVTMVEN 750
    AYYYCNPPPA EKTVKKKRPP LQEYVRKLLY KDLSKVTTEK VLRQMRKLPW 800
    QDQEVKDYVI CCMINIWNVK YNSIHCVANL LAGLVLYQED VGIHVVDGVL 850
    EDIRLGMEVN QPKFNQRRIS SAKFLGELYN YRMVESAVIF RTLYSFTSFG 900
    VNPDGSPSSL DPPEHLFRIR LVCTILDTCG QYFDRGSSKR KLDCFLVYFQ 950
    RYVWWKKSLE VWTKDHPFPI DIDYMISDTL ELLRPKIKLC NSLEESIRQV 1000
    QDLEREFLIK LGLVNDKDSK DSMTEGENLE EDEEEEEGGA ETEEQSGNES 1050
    EVNEPEEEEG SDNDDDEGEE EEEENTDYLT DSNKENETDE ENTEVMIKGG 1100
    GLKHVPCVED EDFIQALDKM MLENLQQRSG ESVKVHQLDV AIPLHLKSQL 1150
    RKGPPLGGGE GEAESADTMP FVMLTRKGNK QQFKILNVPM SSQLAANHWN 1200
    QQQAEQEERM RMKKLTLDIN ERQEQEDYQE MLQSLAQRPA PANTNRERRP 1250
    RYQHPKGAPN ADLIFKTGGR RR 1272
    Length:1,272
    Mass (Da):147,810
    Last modified:March 1, 2001 - v1
    Checksum:i95F3C57D2854BB44
    GO
    Isoform 2 (identifier: Q9HAU5-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:579
    Mass (Da):66,842
    Checksum:iFA8367F0C864C24E
    GO

    Sequence cautioni

    The sequence BAA92646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191A → T in BAC04721. (PubMed:14702039)Curated
    Sequence conflicti338 – 3381F → L in BAC04721. (PubMed:14702039)Curated
    Sequence conflicti844 – 8441H → Q in AAG48509. (PubMed:11163187)Curated
    Sequence conflicti844 – 8441H → Q in BAA92646. (PubMed:10718198)Curated
    Sequence conflicti969 – 9691P → S in BAA92646. (PubMed:10718198)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti496 – 4961N → S.
    Corresponds to variant rs7079388 [ dbSNP | Ensembl ].
    VAR_024345

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei54 – 8330Missing in isoform 2. 1 PublicationVSP_012958Add
    BLAST
    Alternative sequencei588 – 60922AMDFC…VRALF → EKAFCNGNLARVNLLLRMAV KK in isoform 2. 1 PublicationVSP_012959Add
    BLAST
    Alternative sequencei610 – 1272663Missing in isoform 2. 1 PublicationVSP_012960Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS7086.1. [Q9HAU5-1]
    PIRiT12507.
    RefSeqiNP_056357.1. NM_015542.3. [Q9HAU5-1]
    NP_542166.1. NM_080599.2. [Q9HAU5-1]
    UniGeneiHs.370689.
    Hs.610110.
    Hs.732383.

    Genome annotation databases

    EnsembliENST00000356352; ENSP00000348708; ENSG00000151461. [Q9HAU5-1]
    ENST00000357604; ENSP00000350221; ENSG00000151461. [Q9HAU5-1]
    ENST00000397053; ENSP00000380244; ENSG00000151461. [Q9HAU5-1]
    GeneIDi26019.
    KEGGihsa:26019.
    UCSCiuc001ila.3. human. [Q9HAU5-1]

    Polymorphism databases

    DMDMi60390647.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS7086.1. [Q9HAU5-1 ]
    PIRi T12507.
    RefSeqi NP_056357.1. NM_015542.3. [Q9HAU5-1 ]
    NP_542166.1. NM_080599.2. [Q9HAU5-1 ]
    UniGenei Hs.370689.
    Hs.610110.
    Hs.732383.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    4CEK X-ray 2.35 A 455-757 [» ]
    4CEM X-ray 2.60 A/B 121-486 [» ]
    ProteinModelPortali Q9HAU5.
    SMRi Q9HAU5. Positions 121-429, 457-757, 768-1014, 1105-1198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117490. 87 interactions.
    DIPi DIP-31148N.
    IntActi Q9HAU5. 35 interactions.
    MINTi MINT-265195.

    PTM databases

    PhosphoSitei Q9HAU5.

    Polymorphism databases

    DMDMi 60390647.

    Proteomic databases

    MaxQBi Q9HAU5.
    PaxDbi Q9HAU5.
    PRIDEi Q9HAU5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356352 ; ENSP00000348708 ; ENSG00000151461 . [Q9HAU5-1 ]
    ENST00000357604 ; ENSP00000350221 ; ENSG00000151461 . [Q9HAU5-1 ]
    ENST00000397053 ; ENSP00000380244 ; ENSG00000151461 . [Q9HAU5-1 ]
    GeneIDi 26019.
    KEGGi hsa:26019.
    UCSCi uc001ila.3. human. [Q9HAU5-1 ]

    Organism-specific databases

    CTDi 26019.
    GeneCardsi GC10M011962.
    HGNCi HGNC:17854. UPF2.
    MIMi 605529. gene.
    neXtProti NX_Q9HAU5.
    PharmGKBi PA134945630.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG321770.
    HOVERGENi HBG079124.
    InParanoidi Q9HAU5.
    KOi K14327.
    OMAi IRKLHWE.
    OrthoDBi EOG70GMDS.
    PhylomeDBi Q9HAU5.
    TreeFami TF300543.

    Enzyme and pathway databases

    Reactomei REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi UPF2. human.
    EvolutionaryTracei Q9HAU5.
    GeneWikii UPF2.
    GenomeRNAii 26019.
    NextBioi 47788.
    PROi Q9HAU5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAU5.
    Bgeei Q9HAU5.
    Genevestigatori Q9HAU5.

    Family and domain databases

    Gene3Di 1.25.40.180. 4 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    IPR007193. Up-fram_suppressor-2.
    [Graphical view ]
    Pfami PF02854. MIF4G. 3 hits.
    PF04050. Upf2. 1 hit.
    [Graphical view ]
    SMARTi SM00543. MIF4G. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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.
    20. "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.

    Entry informationi

    Entry nameiRENT2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAU5
    Secondary accession number(s): A6NLJ5
    , D3DRS0, Q14BM1, Q5W0J4, Q8N8U1, Q9H1J2, Q9NWL1, Q9P2D9, Q9Y4M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3