Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8BWY3 (ERF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic peptide chain release factor subunit 1

Short name=Eukaryotic release factor 1
Short name=eRF1
Gene names
Name:Etf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA By similarity. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons By similarity.

Subunit structure

Heterodimer of two subunits, one of which binds GTP. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex By similarity. Interacts with Moloney murine leukemia virus (MoLV) reverse transcriptase/Ribonuclease H p80 (via RT and RNase domains); this interaction is essential for translational readthrough of amber codon between viral gag and pol genes. Interacts with MoLV Gag-Pol precursor. Ref.3

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the eukaryotic release factor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 437436Eukaryotic peptide chain release factor subunit 1
PRO_0000143140

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict401P → Q in AAH13717. Ref.2
Sequence conflict2071E → K in BAC33839. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BWY3 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: CECC50D100E59D19

FASTA43749,031
        10         20         30         40         50         60 
MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS 

        70         80         90        100        110        120 
NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI 

       130        140        150        160        170        180 
NTSLYLCDNK FHTEALTALL SDDSKFGFIV IDGSGALFGT LQGNTREVLH KFTVDLPKKH 

       190        200        210        220        230        240 
GRGGQSALRF ARLRMEKRHN YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD 

       250        260        270        280        290        300 
MFDQRLQSKV LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK 

       310        320        330        340        350        360 
YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ EKDKSHFTDK 

       370        380        390        400        410        420 
ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ 

       430 
GMEYQGGDDE FFDLDDY 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Spinal cord.
[2]"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].
Tissue: Mammary tumor.
[3]"Reverse transcriptase of Moloney murine leukemia virus binds to eukaryotic release factor 1 to modulate suppression of translational termination."
Orlova M., Yueh A., Leung J., Goff S.P.
Cell 115:319-331(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MOLONEY MURINE LEUKEMIA VIRUS REVERSE TRANSCRIPTASE/RIBONUCLEASE H P80 AND GAG-POL POLYPROTEIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK049607 mRNA. Translation: BAC33839.1.
AK164020 mRNA. Translation: BAE37589.1.
BC013717 mRNA. Translation: AAH13717.1.
CCDSCCDS29137.1.
RefSeqNP_659115.3. NM_144866.3.
UniGeneMm.329353.

3D structure databases

ProteinModelPortalQ8BWY3.
SMRQ8BWY3. Positions 7-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230388. 2 interactions.
IntActQ8BWY3. 1 interaction.
MINTMINT-1857670.

PTM databases

PhosphoSiteQ8BWY3.

Proteomic databases

MaxQBQ8BWY3.
PaxDbQ8BWY3.
PRIDEQ8BWY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025218; ENSMUSP00000025218; ENSMUSG00000024360.
GeneID225363.
KEGGmmu:225363.
UCSCuc008elu.1. mouse.

Organism-specific databases

CTD2107.
MGIMGI:2385071. Etf1.

Phylogenomic databases

eggNOGCOG1503.
GeneTreeENSGT00390000009004.
HOGENOMHOG000224681.
HOVERGENHBG005602.
InParanoidQ8BWY3.
KOK03265.
OMAWENLDIQ.
OrthoDBEOG7JT6XG.
PhylomeDBQ8BWY3.
TreeFamTF105672.

Gene expression databases

ArrayExpressQ8BWY3.
BgeeQ8BWY3.
CleanExMM_ETF1.
GenevestigatorQ8BWY3.

Family and domain databases

Gene3D3.30.1330.30. 1 hit.
3.30.960.10. 1 hit.
InterProIPR005140. eRF1_1_Pelota.
IPR005141. eRF1_2.
IPR005142. eRF1_3.
IPR029064. L30e-like.
IPR004403. Peptide_chain-rel_eRF1/aRF1.
IPR024049. Release_factor_eRF1/aRF1_N.
[Graphical view]
PANTHERPTHR10113. PTHR10113. 1 hit.
PfamPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SUPFAMSSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsTIGR03676. aRF1/eRF1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSETF1. mouse.
NextBio377641.
PROQ8BWY3.
SOURCESearch...

Entry information

Entry nameERF1_MOUSE
AccessionPrimary (citable) accession number: Q8BWY3
Secondary accession number(s): Q3TPZ6, Q91VH9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 98 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot