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P62495

- ERF1_HUMAN

UniProt

P62495 - ERF1_HUMAN

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Protein

Eukaryotic peptide chain release factor subunit 1

Gene
ETF1, ERF1, RF1, SUP45L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. ribosome binding Source: UniProtKB
  4. RNA binding Source: ProtInc
  5. translation release factor activity Source: UniProtKB
  6. translation release factor activity, codon specific Source: InterPro
  7. translation termination factor activity Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. protein methylation Source: MGI
  6. regulation of translational termination Source: ProtInc
  7. RNA metabolic process Source: Reactome
  8. translation Source: Reactome
  9. translational termination Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Nonsense-mediated mRNA decay, Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_1986. Eukaryotic Translation Termination.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. 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
Alternative name(s):
Protein Cl1
TB3-1
Gene namesi
Name:ETF1
Synonyms:ERF1, RF1, SUP45L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:3477. ETF1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 437436Eukaryotic peptide chain release factor subunit 1PRO_0000143138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62495.
PaxDbiP62495.
PeptideAtlasiP62495.
PRIDEiP62495.

PTM databases

PhosphoSiteiP62495.

Expressioni

Gene expression databases

ArrayExpressiP62495.
BgeeiP62495.
CleanExiHS_ETF1.
GenevestigatoriP62495.

Organism-specific databases

HPAiCAB011686.

Interactioni

Subunit structurei

Heterodimer of two subunits, one of which binds GTP. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GSPT1P151702EBI-1047744,EBI-948993

Protein-protein interaction databases

BioGridi108408. 18 interactions.
IntActiP62495. 11 interactions.
MINTiMINT-5004401.
STRINGi9606.ENSP00000353741.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63
Turni7 – 93
Helixi10 – 2516
Beta strandi30 – 323
Beta strandi34 – 396
Beta strandi41 – 433
Helixi45 – 5915
Helixi66 – 8217
Beta strandi93 – 1019
Helixi103 – 1053
Beta strandi107 – 1148
Beta strandi124 – 1307
Helixi134 – 1396
Beta strandi145 – 1506
Beta strandi158 – 1625
Beta strandi165 – 1706
Beta strandi180 – 1856
Helixi188 – 19710
Turni198 – 2036
Helixi204 – 2085
Turni209 – 2124
Beta strandi216 – 2183
Beta strandi220 – 2223
Beta strandi225 – 2295
Turni230 – 2334
Helixi234 – 2374
Beta strandi240 – 2423
Turni244 – 2496
Beta strandi253 – 2553
Helixi262 – 27110
Turni274 – 2763
Helixi278 – 29518
Beta strandi296 – 2983
Beta strandi301 – 3044
Helixi305 – 3139
Beta strandi318 – 3247
Beta strandi329 – 3335
Beta strandi336 – 3394
Beta strandi342 – 3465
Helixi348 – 3525
Turni354 – 3563
Turni360 – 3623
Beta strandi368 – 3725
Helixi374 – 3807
Turni383 – 3864
Beta strandi389 – 3924
Beta strandi394 – 3963
Helixi397 – 4048
Turni405 – 4084
Beta strandi409 – 4124
Beta strandi420 – 4223
Turni423 – 4253
Beta strandi426 – 4283
Helixi434 – 4374

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00310.
ProteinModelPortaliP62495.
SMRiP62495. Positions 7-420.

Miscellaneous databases

EvolutionaryTraceiP62495.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1503.
HOGENOMiHOG000224681.
HOVERGENiHBG005602.
InParanoidiP62495.
KOiK03265.
OMAiWENLDIQ.
PhylomeDBiP62495.
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.

P62495-1 [UniParc]FASTAAdd to Basket

« Hide

MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK    50
MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI 100
VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SDDSKFGFIV 150
IDGSGALFGT LQGNTREVLH KFTVDLPKKH GRGGQSALRF ARLRMEKRHN 200
YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD MFDQRLQSKV 250
LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK 300
YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ 350
EKDKSHFTDK ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS 400
QFVKGFGGIG GILRYRVDFQ GMEYQGGDDE FFDLDDY 437
Length:437
Mass (Da):49,031
Last modified:January 23, 2007 - v3
Checksum:iCECC50D100E59D19
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4207.1.
PIRiS50853.
RefSeqiNP_004721.1. NM_004730.3.
UniGeneiHs.483494.

Genome annotation databases

EnsembliENST00000360541; ENSP00000353741; ENSG00000120705.
GeneIDi2107.
KEGGihsa:2107.
UCSCiuc003ldc.5. human.

Polymorphism databases

DMDMi50402099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4207.1.
PIRi S50853.
RefSeqi NP_004721.1. NM_004730.3.
UniGenei Hs.483494.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DT9 X-ray 2.70 A 1-437 [» ]
2HST NMR - A 140-275 [» ]
2KTU NMR - A 276-437 [» ]
2KTV NMR - A 276-437 [» ]
2LGT NMR - A 1-142 [» ]
2LLX NMR - A 1-142 [» ]
3E1Y X-ray 3.80 A/B/C/D 1-437 [» ]
3J5Y electron microscopy 9.70 A 7-420 [» ]
DisProti DP00310.
ProteinModelPortali P62495.
SMRi P62495. Positions 7-420.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108408. 18 interactions.
IntActi P62495. 11 interactions.
MINTi MINT-5004401.
STRINGi 9606.ENSP00000353741.

PTM databases

PhosphoSitei P62495.

Polymorphism databases

DMDMi 50402099.

Proteomic databases

MaxQBi P62495.
PaxDbi P62495.
PeptideAtlasi P62495.
PRIDEi P62495.

Protocols and materials databases

DNASUi 2107.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360541 ; ENSP00000353741 ; ENSG00000120705 .
GeneIDi 2107.
KEGGi hsa:2107.
UCSCi uc003ldc.5. human.

Organism-specific databases

CTDi 2107.
GeneCardsi GC05M137843.
HGNCi HGNC:3477. ETF1.
HPAi CAB011686.
MIMi 600285. gene.
neXtProti NX_P62495.
PharmGKBi PA27893.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1503.
HOGENOMi HOG000224681.
HOVERGENi HBG005602.
InParanoidi P62495.
KOi K03265.
OMAi WENLDIQ.
PhylomeDBi P62495.
TreeFami TF105672.

Enzyme and pathway databases

Reactomei REACT_1986. Eukaryotic Translation Termination.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSi ETF1. human.
EvolutionaryTracei P62495.
GeneWikii Eukaryotic_release_factors.
GenomeRNAii 2107.
NextBioi 8519.
PROi P62495.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62495.
Bgeei P62495.
CleanExi HS_ETF1.
Genevestigatori P62495.

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. "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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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.

Entry informationi

Entry nameiERF1_HUMAN
AccessioniPrimary (citable) accession number: P62495
Secondary accession number(s): B2R6B4
, D3DQC1, P46055, Q5M7Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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