NAM7/YMR080C Protein Information Help

Standard Name Nam7p
Systematic Name Ymr080cp
Alias Ifs2p , Mof4p , Upf1p 1 , Sup113p 2
ORF Classification Verified
Description ATP-dependent RNA helicase of the SFI superfamily; involved in nonsense mediated mRNA decay; required for efficient translation termination at nonsense codons and targeting of NMD substrates to P-bodies; involved in telomere maintenance; forms cytoplasmic foci upon DNA replication stress (3, 4, 5, 6, 7)
Name Description Nuclear Accommodation of Mitochondria
Experimental Data
Molecules/cell 6090 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 971
Molecular Weight (Da) 109,429
Isoelectric Point (pI) 6.45

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Nam7p (InterPro)
Physical Interactions There are 71 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000004EEDA | P30771
MIPS: YMR080C
NCBI: 173142 | 327200469 | 400350 | 4023 | 6323726 | 807962 | NP_013797.1
GenBank/EMBL/DDBJ: DAA09978.1 | M76659 | X62394 | Z49259
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
Amino Acid Sequence (or in FASTA format)
 
       1  MVGSGSHTPY DISNSPSDVN VQPATQLNST LVEDDDVDNQ LFEEAQVTET
      51  GFRSPSASDN SCAYCGIDSA KCVIKCNSCK KWFCNTKNGT SSSHIVNHLV
     101  LSHHNVVSLH PDSDLGDTVL ECYNCGRKNV FLLGFVSAKS EAVVVLLCRI
     151  PCAQTKNANW DTDQWQPLIE DRQLLSWVAE QPTEEEKLKA RLITPSQISK
     201  LEAKWRSNKD ATINDIDAPE EQEAIPPLLL RYQDAYEYQR SYGPLIKLEA
     251  DYDKQLKESQ ALEHISVSWS LALNNRHLAS FTLSTFESNE LKVAIGDEMI
     301  LWYSGMQHPD WEGRGYIVRL PNSFQDTFTL ELKPSKTPPP THLTTGFTAE
     351  FIWKGTSYDR MQDALKKFAI DKKSISGYLY YKILGHQVVD ISFDVPLPKE
     401  FSIPNFAQLN SSQSNAVSHV LQRPLSLIQG PPGTGKTVTS ATIVYHLSKI
     451  HKDRILVCAP SNVAVDHLAA KLRDLGLKVV RLTAKSREDV ESSVSNLALH
     501  NLVGRGAKGE LKNLLKLKDE VGELSASDTK RFVKLVRKTE AEILNKADVV
     551  CCTCVGAGDK RLDTKFRTVL IDESTQASEP ECLIPIVKGA KQVILVGDHQ
     601  QLGPVILERK AADAGLKQSL FERLISLGHV PIRLEVQYRM NPYLSEFPSN
     651  MFYEGSLQNG VTIEQRTVPN SKFPWPIRGI PMMFWANYGR EEISANGTSF
     701  LNRIEAMNCE RIITKLFRDG VKPEQIGVIT PYEGQRAYIL QYMQMNGSLD
     751  KDLYIKVEVA SVDAFQGREK DYIILSCVRA NEQQAIGFLR DPRRLNVGLT
     801  RAKYGLVILG NPRSLARNTL WNHLLIHFRE KGCLVEGTLD NLQLCTVQLV
     851  RPQPRKTERP MNAQFNVESE MGDFPKFQDF DAQSMVSFSG QIGDFGNAFV
     901  DNTELSSYIN NEYWNFENFK SAFSQKQNRN EIDDRNLYQE EASHLNSNFA
     951  RELQREEQKH ELSKDFSNLG I*

external links for Nam7p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Nam7p
1) Leeds P, et al.  (1991) The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev 5(12A):2303-14
2) Ono B, et al.  (2005) Suppression of termination mutations caused by defects of the NMD machinery in Saccharomyces cerevisiae. Genes Genet Syst 80(5):311-6
3) de la Cruz J, et al.  (1999) Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem Sci 24(5):192-8
4) Askree SH, et al.  (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63
5) Sheth U and Parker R  (2006) Targeting of aberrant mRNAs to cytoplasmic processing bodies. Cell 125(6):1095-109
6) Takahashi S, et al.  (2008) Upf1 potentially serves as a RING-related E3 ubiquitin ligase via its association with Upf3 in yeast. RNA 14(9):1950-8
7) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41