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NMD2_YEAST
ID   NMD2_YEAST              Reviewed;        1089 AA.
AC   P38798; D3DL27;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=Nonsense-mediated mRNA decay protein 2;
DE   AltName: Full=Up-frameshift suppressor 2;
GN   Name=NMD2; Synonyms=IFS1, SUA1, UPF2; OrderedLocusNames=YHR077C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7883168; DOI=10.1101/gad.9.4.437;
RA   He F., Jacobson A.;
RT   "Identification of a novel component of the nonsense-mediated mRNA decay
RT   pathway by use of an interacting protein screen.";
RL   Genes Dev. 9:437-454(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PLY136;
RX   PubMed=7883167; DOI=10.1101/gad.9.4.423;
RA   Cui Y., Hagan K.W., Zhang S., Peltz S.W.;
RT   "Identification and characterization of genes that are required for the
RT   accelerated degradation of mRNAs containing a premature translational
RT   termination codon.";
RL   Genes Dev. 9:423-436(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7604038; DOI=10.1073/pnas.92.14.6587;
RA   Lee S.I., Umen J.G., Varmus H.E.;
RT   "A genetic screen identifies cellular factors involved in retroviral -1
RT   frameshifting.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6587-6591(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Involved in nonsense-mediated decay of mRNAs containing
CC       premature stop codons. It interacts, via its C-terminus, with
CC       NAM7/UPF1. Could be involved in determining the efficiency of
CC       translational termination or reinitiation or factors involved in the
CC       initial assembly of an initiation- and termination-competent mRNP.
CC   -!- INTERACTION:
CC       P38798; P48412: UPF3; NbExp=3; IntAct=EBI-12071, EBI-20117;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1280 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U14974; AAA67724.1; -; Genomic_DNA.
DR   EMBL; U12137; AAA66521.1; -; Genomic_DNA.
DR   EMBL; U28158; AAA74948.1; -; Genomic_DNA.
DR   EMBL; U10556; AAB68893.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06771.1; -; Genomic_DNA.
DR   PIR; S48244; S48244.
DR   RefSeq; NP_011944.2; NM_001179207.1.
DR   PDB; 4LUN; X-ray; 1.64 A; U=1-310.
DR   PDBsum; 4LUN; -.
DR   AlphaFoldDB; P38798; -.
DR   SMR; P38798; -.
DR   BioGRID; 36511; 349.
DR   ComplexPortal; CPX-1315; Nonsense-mediated decay complex.
DR   DIP; DIP-2295N; -.
DR   IntAct; P38798; 6.
DR   MINT; P38798; -.
DR   STRING; 4932.YHR077C; -.
DR   iPTMnet; P38798; -.
DR   MaxQB; P38798; -.
DR   PaxDb; P38798; -.
DR   PRIDE; P38798; -.
DR   EnsemblFungi; YHR077C_mRNA; YHR077C; YHR077C.
DR   GeneID; 856476; -.
DR   KEGG; sce:YHR077C; -.
DR   SGD; S000001119; NMD2.
DR   VEuPathDB; FungiDB:YHR077C; -.
DR   eggNOG; KOG2051; Eukaryota.
DR   GeneTree; ENSGT00530000064318; -.
DR   HOGENOM; CLU_002633_1_0_1; -.
DR   InParanoid; P38798; -.
DR   OMA; DFQHHQI; -.
DR   BioCyc; YEAST:G3O-31124-MON; -.
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P38798; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38798; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR   GO; GO:0005844; C:polysome; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0071026; P:cytoplasmic RNA surveillance; IC:ComplexPortal.
DR   GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR   GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IGI:SGD.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:SGD.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   InterPro; IPR039762; Nmd2/UPF2.
DR   InterPro; IPR007193; Upf2/Nmd2_C.
DR   PANTHER; PTHR12839; PTHR12839; 2.
DR   Pfam; PF02854; MIF4G; 3.
DR   Pfam; PF04050; Upf2; 1.
DR   SMART; SM00543; MIF4G; 3.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome.
FT   CHAIN           1..1089
FT                   /note="Nonsense-mediated mRNA decay protein 2"
FT                   /id="PRO_0000096873"
FT   REGION          819..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..868
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..939
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2
FT                   /note="D -> YQQ (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..17
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           34..44
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           52..60
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           69..81
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           87..104
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           106..116
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           130..152
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           170..172
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           182..190
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           201..210
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           212..214
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           231..271
FT                   /evidence="ECO:0007829|PDB:4LUN"
FT   HELIX           277..303
FT                   /evidence="ECO:0007829|PDB:4LUN"
SQ   SEQUENCE   1089 AA;  126747 MW;  13BBE725675CBF52 CRC64;
     MDDGRKKELH DLNTRAWNGE EVFPLKSKKL DSSIKRNTGF IKKLKKGFVK GSESSLLKDL
     SEASLEKYLS EIIVTVTECL LNVLNKNDDV IAAVEIISGL HQRFNGRFTS PLLGAFLQAF
     ENPSVDIESE RDELQRITRV KGNLRVFTEL YLVGVFRTLD DIESKDAIPN FLQKKTGRKD
     PLLFSILREI LNYKFKLGFT TTIATAFIKK FAPLFRDDDN SWDDLIYDSK LKGALQSLFK
     NFIDATFARA TELHKKVNKL QREHQKCQIR TGKLRDEYVE EYDKLLPIFI RFKTSAITLG
     EFFKLEIPEL EGASNDDLKE TASPMITNQI LPPNQRLWEN EDTRKFYEIL PDISKTVEES
     QSSKTEKDSN VNSKNINLFF TDLEMADCKD IIDDLSNRYW SSYLDNKATR NRILKFFMET
     QDWSKLPVYS RFIATNSKYM PEIVSEFINY LDNGFRSQLH SNKINVKNII FFSEMIKFQL
     IPSFMIFHKI RTLIMYMQVP NNVEILTVLL EHSGKFLLNK PEYKELMEKM VQLIKDKKND
     RQLNMNMKSA LENIITLLYP PSVKSLNVTV KTITPEQQFY RILIRSELSS LDFKHIVKLV
     RKAHWDDVAI QKVLFSLFSK PHKISYQNIP LLTKVLGGLY SYRRDFVIRC IDQVLENIER
     GLEINDYGQN MHRISNVRYL TEIFNFEMIK SDVLLDTIYH IIRFGHINNQ PNPFYLNYSD
     PPDNYFRIQL VTTILLNINR TPAAFTKKCK LLLRFFEYYT FIKEQPLPKE TEFRVSSTFK
     KYENIFGNTK FERSENLVES ASRLESLLKS LNAIKSKDDR VKGSSASIHN GKESAVPIES
     ITEDDEDEDD ENDDGVDLLG EDEDAEISTP NTESAPGKHQ AKQDESEDED DEDDDEDDDD
     DDDDDDDDGE EGDEDDDEDD DDEDDDDEEE EDSDSDLEYG GDLDADRDIE MKRMYEEYER
     KLKDEEERKA EEELERQFQK MMQESIDARK SEKVVASKIP VISKPVSVQK PLLLKKSEEP
     SSSKETYEEL SKPKKIAFTF LTKSGKKTQS RILQLPTDVK FVSDVLEEEE KLKTERNKIK
     KIVLKRSFD
 
 
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