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Protein

Eukaryotic peptide chain release factor GTP-binding subunit ERF3B

Gene

Gspt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in translation termination in response to the termination codons UAA, UAG and UGA. May play a role as a potent stimulator of the release factor activity of ETF1. Exhibits GTPase activity, which is ribosome- and ETF1-dependent. May play a role in cell cycle progression. 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).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei220 – 2201Interacts with GTP/GDPBy similarity
Sitei354 – 3541Interacts with GTP/GDPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2218GTPBy similarity
Nucleotide bindingi291 – 2955GTPBy similarity
Nucleotide bindingi353 – 3564GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Nonsense-mediated mRNA decay, Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
Short name:
Eukaryotic peptide chain release factor subunit 3b
Short name:
eRF3b
Alternative name(s):
G1 to S phase transition protein 2 homolog
Gene namesi
Name:Gspt2
Synonyms:Erf3b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1316727. Gspt2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Eukaryotic peptide chain release factor GTP-binding subunit ERF3BPRO_0000327257Add
BLAST

Proteomic databases

EPDiQ149F3.
MaxQBiQ149F3.
PaxDbiQ149F3.
PeptideAtlasiQ149F3.
PRIDEiQ149F3.

PTM databases

iPTMnetiQ149F3.
PhosphoSiteiQ149F3.
SwissPalmiQ149F3.

Expressioni

Tissue specificityi

Highly expressed in brain. Moderately expressed in spleen and lung. Weakly expressed in heart, liver and kidney. Expression during the cell-cycle progession is constant.1 Publication

Developmental stagei

Barely detectable at E15, increased after birth to reach a maximum at P15.1 Publication

Gene expression databases

BgeeiQ149F3.
ExpressionAtlasiQ149F3. baseline and differential.
GenevisibleiQ149F3. MM.

Interactioni

Subunit structurei

Interacts with ETF1. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with UPF1 and PABPC1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ149F3. 2 interactions.
MINTiMINT-4125907.
STRINGi10090.ENSMUSP00000109523.

Structurei

3D structure databases

ProteinModelPortaliQ149F3.
SMRiQ149F3. Positions 202-629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini205 – 429225tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni214 – 2218G1PROSITE-ProRule annotation
Regioni270 – 2745G2PROSITE-ProRule annotation
Regioni291 – 2944G3PROSITE-ProRule annotation
Regioni353 – 3564G4PROSITE-ProRule annotation
Regioni395 – 3973G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0459. Eukaryota.
COG5256. LUCA.
GeneTreeiENSGT00620000087924.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiQ149F3.
KOiK03267.
OMAiDECEIME.
OrthoDBiEOG76X5ZT.
TreeFamiTF300566.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR009818. Ataxin-2_C.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q149F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLGSSSDSA PDCWDQVDME APGSAPSGDG IAPAAMAAAE AAEAEAQRKH
60 70 80 90 100
LSLAFSSQLN IHAKPFVPSV SAAEFVPSFL PGSAQPPAPT ASSCDETCIG
110 120 130 140 150
GAGEPEGKRM EWGAPVEPSK DGPLVSWEGS SSVVTMELSE PVVENGEVEM
160 170 180 190 200
ALEESWELKE VSEAKPEASL GDAGPPEESV KEVMEEKEEV RKSKSVSIPS
210 220 230 240 250
GAPKKEHVNV VFIGHVDAGK STIGGQIMFL TGMVDRRTLE KYEREAKEKN
260 270 280 290 300
RETWYLSWAL DTNQEERDKG KTVEVGRAYF ETEKKHFTIL DAPGHKSFVP
310 320 330 340 350
NMIGGASQAD LAVLVISARK GEFETGFEKG GQTREHAMLA KTAGVKYLIV
360 370 380 390 400
LINKMDDPTV DWSSERYEEC KEKLVPFLKK VGFSPKKDIH FMPCSGLTGA
410 420 430 440 450
NIKEQSDFCP WYTGLPFIPY LDSLPNFNRS IDGPIRLPIV DKYKDMGTVV
460 470 480 490 500
LGKLESGSIF KGQQLVMMPN KHSVEVLGIV SDDAETDFVA PGENLKIRLK
510 520 530 540 550
GIEEEEILPG FILCEPSNLC HSGRTFDVQI VIIEHKSIIC PGYNAVLHIH
560 570 580 590 600
TCIEEVEITA LISLVDKKSG EKSKTRPRFV KQDQVCIARL RTAGTICLET
610 620 630
FKDFPQMGRF TLRDEGKTIA IGKVLKLVPE KD
Length:632
Mass (Da):69,147
Last modified:August 22, 2006 - v1
Checksum:i9783F5C867D8EB13
GO

Sequence cautioni

The sequence BAA32527.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB31621.1 differs from that shown. Reason: Frameshift at position 591. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → G in BAA32527 (PubMed:9712840).Curated
Sequence conflicti84 – 841A → P in BAA32527 (PubMed:9712840).Curated
Sequence conflicti197 – 1971S → A in BAA32527 (PubMed:9712840).Curated
Sequence conflicti262 – 2621T → K in BAB31621 (PubMed:16141072).Curated
Sequence conflicti510 – 5101G → A in BAB31621 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019241 mRNA. Translation: BAB31621.1. Frameshift.
AL645466 Genomic DNA. Translation: CAM15955.1.
BC117825 mRNA. Translation: AAI17826.1.
BC117826 mRNA. Translation: AAI17827.1.
AB003503 mRNA. Translation: BAA32527.1. Different initiation.
CCDSiCCDS41064.1.
RefSeqiNP_032205.2. NM_008179.2.
UniGeneiMm.20826.

Genome annotation databases

EnsembliENSMUST00000096368; ENSMUSP00000109523; ENSMUSG00000071723.
GeneIDi14853.
KEGGimmu:14853.
UCSCiuc009tto.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019241 mRNA. Translation: BAB31621.1. Frameshift.
AL645466 Genomic DNA. Translation: CAM15955.1.
BC117825 mRNA. Translation: AAI17826.1.
BC117826 mRNA. Translation: AAI17827.1.
AB003503 mRNA. Translation: BAA32527.1. Different initiation.
CCDSiCCDS41064.1.
RefSeqiNP_032205.2. NM_008179.2.
UniGeneiMm.20826.

3D structure databases

ProteinModelPortaliQ149F3.
SMRiQ149F3. Positions 202-629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ149F3. 2 interactions.
MINTiMINT-4125907.
STRINGi10090.ENSMUSP00000109523.

PTM databases

iPTMnetiQ149F3.
PhosphoSiteiQ149F3.
SwissPalmiQ149F3.

Proteomic databases

EPDiQ149F3.
MaxQBiQ149F3.
PaxDbiQ149F3.
PeptideAtlasiQ149F3.
PRIDEiQ149F3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000096368; ENSMUSP00000109523; ENSMUSG00000071723.
GeneIDi14853.
KEGGimmu:14853.
UCSCiuc009tto.1. mouse.

Organism-specific databases

CTDi23708.
MGIiMGI:1316727. Gspt2.

Phylogenomic databases

eggNOGiKOG0459. Eukaryota.
COG5256. LUCA.
GeneTreeiENSGT00620000087924.
HOGENOMiHOG000229291.
HOVERGENiHBG000179.
InParanoidiQ149F3.
KOiK03267.
OMAiDECEIME.
OrthoDBiEOG76X5ZT.
TreeFamiTF300566.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ149F3.
SOURCEiSearch...

Gene expression databases

BgeeiQ149F3.
ExpressionAtlasiQ149F3. baseline and differential.
GenevisibleiQ149F3. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR009818. Ataxin-2_C.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamiPF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Embryo.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
  4. "Molecular cloning of a novel member of the eukaryotic polypeptide chain-releasing factors (eRF). Its identification as eRF3 interacting with eRF1."
    Hoshino S., Imai M., Mizutani M., Kikuchi Y., Hanaoka F., Ui M., Katada T.
    J. Biol. Chem. 273:22254-22259(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-632, INTERACTION WITH ETF1, TISSUE SPECIFICITY.
  5. Cited for: INTERACTION WITH ETF1, FUNCTION.
  6. "Involvement of human release factors eRF3a and eRF3b in translation termination and regulation of the termination complex formation."
    Chauvin C., Salhi S., Le Goff C., Viranaicken W., Diop D., Jean-Jean O.
    Mol. Cell. Biol. 25:5801-5811(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiERF3B_MOUSE
AccessioniPrimary (citable) accession number: Q149F3
Secondary accession number(s): O88180, Q9CY91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 87 of the entry and version 1 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

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.