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Q8BWY3

- ERF1_MOUSE

UniProt

Q8BWY3 - ERF1_MOUSE

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Protein

Eukaryotic peptide chain release factor subunit 1

Gene

Etf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. 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

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. translation release factor activity, codon specific Source: InterPro

GO - Biological processi

  1. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
  2. protein methylation Source: MGI
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Nonsense-mediated mRNA decay, Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic peptide chain release factor subunit 1
Short name:
Eukaryotic release factor 1
Short name:
eRF1
Gene namesi
Name:Etf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:2385071. Etf1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 437436Eukaryotic peptide chain release factor subunit 1PRO_0000143140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BWY3.
PaxDbiQ8BWY3.
PRIDEiQ8BWY3.

PTM databases

PhosphoSiteiQ8BWY3.

Expressioni

Gene expression databases

BgeeiQ8BWY3.
CleanExiMM_ETF1.
ExpressionAtlasiQ8BWY3. baseline and differential.
GenevestigatoriQ8BWY3.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi230388. 2 interactions.
IntActiQ8BWY3. 1 interaction.
MINTiMINT-1857670.

Structurei

3D structure databases

ProteinModelPortaliQ8BWY3.
SMRiQ8BWY3. Positions 5-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic release factor 1 family.Curated

Phylogenomic databases

eggNOGiCOG1503.
GeneTreeiENSGT00390000009004.
HOGENOMiHOG000224681.
HOVERGENiHBG005602.
InParanoidiQ8BWY3.
KOiK03265.
OMAiWENLDIQ.
OrthoDBiEOG7JT6XG.
PhylomeDBiQ8BWY3.
TreeFamiTF105672.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
3.30.960.10. 1 hit.
InterProiIPR005140. 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]
PANTHERiPTHR10113. PTHR10113. 1 hit.
PfamiPF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsiTIGR03676. aRF1/eRF1. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BWY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK
60 70 80 90 100
MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI
110 120 130 140 150
VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SDDSKFGFIV
160 170 180 190 200
IDGSGALFGT LQGNTREVLH KFTVDLPKKH GRGGQSALRF ARLRMEKRHN
210 220 230 240 250
YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD MFDQRLQSKV
260 270 280 290 300
LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK
310 320 330 340 350
YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ
360 370 380 390 400
EKDKSHFTDK ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS
410 420 430
QFVKGFGGIG GILRYRVDFQ GMEYQGGDDE FFDLDDY
Length:437
Mass (Da):49,031
Last modified:January 23, 2007 - v4
Checksum:iCECC50D100E59D19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401P → Q in AAH13717. (PubMed:15489334)Curated
Sequence conflicti207 – 2071E → K in BAC33839. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049607 mRNA. Translation: BAC33839.1.
AK164020 mRNA. Translation: BAE37589.1.
BC013717 mRNA. Translation: AAH13717.1.
CCDSiCCDS29137.1.
RefSeqiNP_659115.3. NM_144866.3.
UniGeneiMm.329353.

Genome annotation databases

EnsembliENSMUST00000025218; ENSMUSP00000025218; ENSMUSG00000024360.
GeneIDi225363.
KEGGimmu:225363.
UCSCiuc008elu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK049607 mRNA. Translation: BAC33839.1 .
AK164020 mRNA. Translation: BAE37589.1 .
BC013717 mRNA. Translation: AAH13717.1 .
CCDSi CCDS29137.1.
RefSeqi NP_659115.3. NM_144866.3.
UniGenei Mm.329353.

3D structure databases

ProteinModelPortali Q8BWY3.
SMRi Q8BWY3. Positions 5-437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230388. 2 interactions.
IntActi Q8BWY3. 1 interaction.
MINTi MINT-1857670.

PTM databases

PhosphoSitei Q8BWY3.

Proteomic databases

MaxQBi Q8BWY3.
PaxDbi Q8BWY3.
PRIDEi Q8BWY3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025218 ; ENSMUSP00000025218 ; ENSMUSG00000024360 .
GeneIDi 225363.
KEGGi mmu:225363.
UCSCi uc008elu.1. mouse.

Organism-specific databases

CTDi 2107.
MGIi MGI:2385071. Etf1.

Phylogenomic databases

eggNOGi COG1503.
GeneTreei ENSGT00390000009004.
HOGENOMi HOG000224681.
HOVERGENi HBG005602.
InParanoidi Q8BWY3.
KOi K03265.
OMAi WENLDIQ.
OrthoDBi EOG7JT6XG.
PhylomeDBi Q8BWY3.
TreeFami TF105672.

Enzyme and pathway databases

Reactomei REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSi ETF1. mouse.
NextBioi 377641.
PROi Q8BWY3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BWY3.
CleanExi MM_ETF1.
ExpressionAtlasi Q8BWY3. baseline and differential.
Genevestigatori Q8BWY3.

Family and domain databases

Gene3Di 3.30.1330.30. 1 hit.
3.30.960.10. 1 hit.
InterProi IPR005140. 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 ]
PANTHERi PTHR10113. PTHR10113. 1 hit.
Pfami PF03463. eRF1_1. 1 hit.
PF03464. eRF1_2. 1 hit.
PF03465. eRF1_3. 1 hit.
[Graphical view ]
SUPFAMi SSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsi TIGR03676. aRF1/eRF1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiERF1_MOUSE
AccessioniPrimary (citable) accession number: Q8BWY3
Secondary accession number(s): Q3TPZ6, Q91VH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 101 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3