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Q9HAU5

- RENT2_HUMAN

UniProt

Q9HAU5 - RENT2_HUMAN

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi796 – 7972RK → EE: Strongly impairs RNA-binding. 1 Publication
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. 1 Publication
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

BgeeiQ9HAU5.
ExpressionAtlasiQ9HAU5. baseline and differential.
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.
GeneTreeiENSGT00530000064318.
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) [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

        10         20         30         40         50
MPAERKKPAS MEEKDSLPNN KEKDCSERRT VSSKERPKDD IKLTAKKEVS
60 70 80 90 100
KAPEDKKKRL EDDKRKKEDK ERKKKDEEKV KAEEESKKKE EEEKKKHQEE
110 120 130 140 150
ERKKQEEQAK RQQEEEAAAQ MKEKEESIQL HQEAWERHHL RKELRSKNQN
160 170 180 190 200
APDSRPEENF FSRLDSSLKK NTAFVKKLKT ITEQQRDSLS HDFNGLNLSK
210 220 230 240 250
YIAEAVASIV EAKLKISDVN CAVHLCSLFH QRYADFAPSL LQVWKKHFEA
260 270 280 290 300
RKEEKTPNIT KLRTDLRFIA ELTIVGIFTD KEGLSLIYEQ LKNIINADRE
310 320 330 340 350
SHTHVSVVIS FCRHCGDDIA GLVPRKVKSA AEKFNLSFPP SEIISPEKQQ
360 370 380 390 400
PFQNLLKEYF TSLTKHLKRD HRELQNTERQ NRRILHSKGE LSEDRHKQYE
410 420 430 440 450
EFAMSYQKLL ANSQSLADLL DENMPDLPQD KPTPEEHGPG IDIFTPGKPG
460 470 480 490 500
EYDLEGGIWE DEDARNFYEN LIDLKAFVPA ILFKDNEKSC QNKESNKDDT
510 520 530 540 550
KEAKESKENK EVSSPDDLEL ELENLEINDD TLELEGGDEA EDLTKKLLDE
560 570 580 590 600
QEQEDEEAST GSHLKLIVDA FLQQLPNCVN RDLIDKAAMD FCMNMNTKAN
610 620 630 640 650
RKKLVRALFI VPRQRLDLLP FYARLVATLH PCMSDVAEDL CSMLRGDFRF
660 670 680 690 700
HVRKKDQINI ETKNKTVRFI GELTKFKMFT KNDTLHCLKM LLSDFSHHHI
710 720 730 740 750
EMACTLLETC GRFLFRSPES HLRTSVLLEQ MMRKKQAMHL DARYVTMVEN
760 770 780 790 800
AYYYCNPPPA EKTVKKKRPP LQEYVRKLLY KDLSKVTTEK VLRQMRKLPW
810 820 830 840 850
QDQEVKDYVI CCMINIWNVK YNSIHCVANL LAGLVLYQED VGIHVVDGVL
860 870 880 890 900
EDIRLGMEVN QPKFNQRRIS SAKFLGELYN YRMVESAVIF RTLYSFTSFG
910 920 930 940 950
VNPDGSPSSL DPPEHLFRIR LVCTILDTCG QYFDRGSSKR KLDCFLVYFQ
960 970 980 990 1000
RYVWWKKSLE VWTKDHPFPI DIDYMISDTL ELLRPKIKLC NSLEESIRQV
1010 1020 1030 1040 1050
QDLEREFLIK LGLVNDKDSK DSMTEGENLE EDEEEEEGGA ETEEQSGNES
1060 1070 1080 1090 1100
EVNEPEEEEG SDNDDDEGEE EEEENTDYLT DSNKENETDE ENTEVMIKGG
1110 1120 1130 1140 1150
GLKHVPCVED EDFIQALDKM MLENLQQRSG ESVKVHQLDV AIPLHLKSQL
1160 1170 1180 1190 1200
RKGPPLGGGE GEAESADTMP FVMLTRKGNK QQFKILNVPM SSQLAANHWN
1210 1220 1230 1240 1250
QQQAEQEERM RMKKLTLDIN ERQEQEDYQE MLQSLAQRPA PANTNRERRP
1260 1270
RYQHPKGAPN ADLIFKTGGR RR
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.
GeneTreei ENSGT00530000064318.
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

Bgeei Q9HAU5.
ExpressionAtlasi Q9HAU5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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