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Protein

Eukaryotic peptide chain release factor subunit 1-2

Gene

ERF1-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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 (PubMed:15474304). Modulates plant growth and development (PubMed:16113224).1 Publication1 Publication

GO - Molecular functioni

  • translation release factor activity Source: TAIR
  • translation release factor activity, codon specific Source: InterPro

GO - Biological processi

  • regulation of growth Source: UniProtKB-KW
  • translational termination Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Growth regulation, Protein biosynthesis

Enzyme and pathway databases

ReactomeiR-ATH-72764. Eukaryotic Translation Termination.
R-ATH-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-ATH-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic peptide chain release factor subunit 1-2
Short name:
Eukaryotic release factor 1-2
Short name:
eRF1-2
Alternative name(s):
Omnipotent suppressor protein 1 homolog 2
Short name:
SUP1 homolog 2
Gene namesi
Name:ERF1-2
Ordered Locus Names:At1g12920
ORF Names:F13K23.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G12920.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801G → A: Loss of peptidyl-tRNA hydrolytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 434433Eukaryotic peptide chain release factor subunit 1-2PRO_0000143163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9LPV8.
PRIDEiQ9LPV8.

PTM databases

iPTMnetiQ9LPV8.

Expressioni

Gene expression databases

GenevisibleiQ9LPV8. AT.

Interactioni

Subunit structurei

Heterodimer of two subunits, one of which binds GTP.

Protein-protein interaction databases

BioGridi23090. 3 interactions.
IntActiQ9LPV8. 2 interactions.
STRINGi3702.AT1G12920.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LPV8.
SMRiQ9LPV8. Positions 5-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic release factor 1 family.Curated

Phylogenomic databases

eggNOGiKOG0688. Eukaryota.
COG1503. LUCA.
HOGENOMiHOG000224681.
InParanoidiQ9LPV8.
KOiK03265.
OMAiKTTRTHV.
PhylomeDBiQ9LPV8.

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]
SMARTiSM01194. eRF1_1. 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.

Q9LPV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEADTNIE IWKIKKLIKG LESARGNGTS MISLIMPPRD QVSRVTKMLG
60 70 80 90 100
DEYGTASNIK SRVNRQSVLS AITSAQQRLK LYNKVPTNGL VLYTGTIVND
110 120 130 140 150
DGKEKKVTFD FEPFRPINAS LYLCDNKFHT EALNELLESD DKFGFIVMDG
160 170 180 190 200
NGTLFGTLSG NTREVLHKFT VDLPKKHGRG GQSALRFARL RMEKRHNYVR
210 220 230 240 250
KTAELATQFY INPATSQPNV SGLILAGSAD FKTELSQSEL FDPRLQAKIL
260 270 280 290 300
NVVDVSYGGE NGFNQAIELS AEILSNVKFI QEKKLIGKYF EEISQDTGKY
310 320 330 340 350
VFGVEDTLKA LEMGAIETLI VWENLDINRY ELKNSTTGEM VVKHFGKDQE
360 370 380 390 400
SDTSNFHDSE TNAELEVQEK MPLLEWFANE YKRFGCTLEF VTNKSQEGSQ
410 420 430
FCRGFGGIGG MLRYQLDMRT FDELSDTEVY EDSD
Length:434
Mass (Da):48,941
Last modified:October 1, 2000 - v1
Checksum:i63454371B158D851
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012187 Genomic DNA. Translation: AAF78496.1.
CP002684 Genomic DNA. Translation: AEE28949.1.
AY034963 mRNA. Translation: AAK59469.1.
BT026125 mRNA. Translation: ABG48481.1.
AY086623 mRNA. Translation: AAM63682.1.
X69374 mRNA. Translation: CAA49171.1.
U40218 mRNA. Translation: AAA91170.1.
Z18188 mRNA. Translation: CAA79125.1.
PIRiH86262.
S31445.
RefSeqiNP_172752.1. NM_101163.2.
UniGeneiAt.23958.

Genome annotation databases

EnsemblPlantsiAT1G12920.1; AT1G12920.1; AT1G12920.
GeneIDi837850.
GrameneiAT1G12920.1; AT1G12920.1; AT1G12920.
KEGGiath:AT1G12920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012187 Genomic DNA. Translation: AAF78496.1.
CP002684 Genomic DNA. Translation: AEE28949.1.
AY034963 mRNA. Translation: AAK59469.1.
BT026125 mRNA. Translation: ABG48481.1.
AY086623 mRNA. Translation: AAM63682.1.
X69374 mRNA. Translation: CAA49171.1.
U40218 mRNA. Translation: AAA91170.1.
Z18188 mRNA. Translation: CAA79125.1.
PIRiH86262.
S31445.
RefSeqiNP_172752.1. NM_101163.2.
UniGeneiAt.23958.

3D structure databases

ProteinModelPortaliQ9LPV8.
SMRiQ9LPV8. Positions 5-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23090. 3 interactions.
IntActiQ9LPV8. 2 interactions.
STRINGi3702.AT1G12920.1.

PTM databases

iPTMnetiQ9LPV8.

Proteomic databases

PaxDbiQ9LPV8.
PRIDEiQ9LPV8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G12920.1; AT1G12920.1; AT1G12920.
GeneIDi837850.
GrameneiAT1G12920.1; AT1G12920.1; AT1G12920.
KEGGiath:AT1G12920.

Organism-specific databases

TAIRiAT1G12920.

Phylogenomic databases

eggNOGiKOG0688. Eukaryota.
COG1503. LUCA.
HOGENOMiHOG000224681.
InParanoidiQ9LPV8.
KOiK03265.
OMAiKTTRTHV.
PhylomeDBiQ9LPV8.

Enzyme and pathway databases

ReactomeiR-ATH-72764. Eukaryotic Translation Termination.
R-ATH-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-ATH-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiQ9LPV8.

Gene expression databases

GenevisibleiQ9LPV8. AT.

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]
SMARTiSM01194. eRF1_1. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
SSF55481. SSF55481. 1 hit.
TIGRFAMsiTIGR03676. aRF1/eRF1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Three eukaryotic release factor one (eRF1) homologs from Arabidopsis thaliana Columbia."
    Brown C.M., Quigley F.R., Miller W.A.
    Plant Gene Register PGR95-123
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 131-434.
    Strain: cv. C24.
    Tissue: Flower.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-201.
    Strain: cv. Columbia.
    Tissue: Flower bud.
  8. "Translation termination in Arabidopsis thaliana: characterisation of three versions of release factor 1."
    Chapman B., Brown C.
    Gene 341:219-225(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-180.
  9. "Cosuppression of eukaryotic release factor 1-1 in Arabidopsis affects cell elongation and radial cell division."
    Petsch K.A., Mylne J., Botella J.R.
    Plant Physiol. 139:115-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERF1Y_ARATH
AccessioniPrimary (citable) accession number: Q9LPV8
Secondary accession number(s): Q147G8
, Q39098, Q39223, Q41987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.