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P62495 (ERF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Alternative name(s):
Protein Cl1
TB3-1
Gene names
Name:ETF1
Synonyms:ERF1, RF1, SUP45L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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. Ref.2

Subunit structure

Heterodimer of two subunits, one of which binds GTP. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Ref.10

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the eukaryotic release factor 1 family.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
Protein biosynthesis
   Cellular componentCytoplasm
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

protein methylation

Inferred from direct assay PubMed 18539146. Source: MGI

regulation of translational termination

Traceable author statement Ref.2. Source: ProtInc

translation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement Ref.2. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionRNA binding

Traceable author statement Ref.2. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9620853PubMed 9712840. Source: UniProtKB

ribosome binding

Traceable author statement PubMed 12867083. Source: UniProtKB

translation release factor activity

Traceable author statement PubMed 15326224. Source: UniProtKB

translation release factor activity, codon specific

Inferred from electronic annotation. Source: InterPro

translation termination factor activity

Traceable author statement Ref.4. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GSPT1P151702EBI-1047744,EBI-948993

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 437436Eukaryotic peptide chain release factor subunit 1
PRO_0000143138

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.9 Ref.12

Secondary structure

.............................................................................................. 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62495 [UniParc].

Last modified January 23, 2007. Version 3.
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]"Identification of a human cDNA with high homology to yeast omnipotent suppressor 45."
Grenett H.E., Fuller G.M., Bounelis P.
Gene 110:239-243(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor."
Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G., Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L.
Nature 372:701-703(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION, FUNCTION.
[3]"The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1."
Andjelkovic N., Zolnierowicz S., van Hoof C., Goris J., Hemmings B.A.
EMBO J. 15:7156-7167(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"Human release factor eRF1: structural organisation of the unique functional gene on chromosome 5 and of the three processed pseudogenes."
Guenet L., Toutain B., Guilleret I., Chauvel B., Deaven L.L., Longmire J.L., Le Gall L.Y., David V., Le Treut A.
FEBS Lett. 454:131-136(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. expand/collapse author list , 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].
Tissue: Thalamus.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Testis.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
Tissue: Platelet.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SURF COMPLEX.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The crystal structure of human eukaryotic release factor eRF1 --mechanism of stop codon recognition and peptidyl-tRNA hydrolysis."
Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D.
Cell 100:311-321(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[14]"Eukaryotic class 1 translation termination factor eRF1 -- the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis."
Ivanova E.V., Kolosov P.M., Birdsall B., Kelly G., Pastore A., Kisselev L.L., Polshakov V.I.
FEBS J. 274:4223-4237(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 140-277.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M75715 mRNA. Translation: AAA36665.1. Sequence problems.
X81625 mRNA. Translation: CAA57281.1.
U90176 mRNA. Translation: AAB49726.1.
AF095901 Genomic DNA. Translation: AAD43966.1.
AK312510 mRNA. Translation: BAG35411.1.
CH471062 Genomic DNA. Translation: EAW62130.1.
CH471062 Genomic DNA. Translation: EAW62131.1.
BC088358 mRNA. Translation: AAH88358.1.
CCDSCCDS4207.1.
PIRS50853.
RefSeqNP_004721.1. NM_004730.3.
UniGeneHs.483494.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DT9X-ray2.70A1-437[»]
2HSTNMR-A140-275[»]
2KTUNMR-A276-437[»]
2KTVNMR-A276-437[»]
2LGTNMR-A1-142[»]
2LLXNMR-A1-142[»]
3E1YX-ray3.80A/B/C/D1-437[»]
3J5Yelectron microscopy9.70A7-420[»]
DisProtDP00310.
ProteinModelPortalP62495.
SMRP62495. Positions 7-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108408. 18 interactions.
IntActP62495. 11 interactions.
MINTMINT-5004401.
STRING9606.ENSP00000353741.

PTM databases

PhosphoSiteP62495.

Polymorphism databases

DMDM50402099.

Proteomic databases

MaxQBP62495.
PaxDbP62495.
PeptideAtlasP62495.
PRIDEP62495.

Protocols and materials databases

DNASU2107.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360541; ENSP00000353741; ENSG00000120705.
GeneID2107.
KEGGhsa:2107.
UCSCuc003ldc.5. human.

Organism-specific databases

CTD2107.
GeneCardsGC05M137843.
HGNCHGNC:3477. ETF1.
HPACAB011686.
MIM600285. gene.
neXtProtNX_P62495.
PharmGKBPA27893.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1503.
HOGENOMHOG000224681.
HOVERGENHBG005602.
InParanoidP62495.
KOK03265.
OMAWENLDIQ.
PhylomeDBP62495.
TreeFamTF105672.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP62495.
BgeeP62495.
CleanExHS_ETF1.
GenevestigatorP62495.

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. human.
EvolutionaryTraceP62495.
GeneWikiEukaryotic_release_factors.
GenomeRNAi2107.
NextBio8519.
PROP62495.
SOURCESearch...

Entry information

Entry nameERF1_HUMAN
AccessionPrimary (citable) accession number: P62495
Secondary accession number(s): B2R6B4 expand/collapse secondary AC list , D3DQC1, P46055, Q5M7Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM