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Q8IYD1 (ERF3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 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 names
Name:GSPT2
Synonyms:ERF3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.8

Subunit structure

Interacts with ETF1 By similarity. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with UPF1 and PABPC1. Ref.9 Ref.10

Subcellular location

Cytoplasm Probable.

Tissue specificity

Highly expressed in IUCC stage II colorectal cancer (CRC). Ref.7

Sequence similarities

Belongs to the GTP-binding elongation factor family. ERF3 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PABPC1P119407EBI-3869637,EBI-81531
UPF1Q929003EBI-3869637,EBI-373471

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 628628Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
PRO_0000327256

Regions

Nucleotide binding210 – 2178GTP By similarity
Nucleotide binding287 – 2915GTP By similarity
Nucleotide binding349 – 3524GTP By similarity

Sites

Site2161Interacts with GTP/GDP By similarity
Site3501Interacts with GTP/GDP By similarity

Natural variations

Natural variant231P → T. Ref.5
Corresponds to variant rs17855593 [ dbSNP | Ensembl ].
VAR_042431

Experimental info

Mutagenesis521L → K: Impairs interaction with UPF1 and PABPC1; when associated with A-55, K-56 and A-59. Ref.9
Mutagenesis551N → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, K-56 and A-59. Ref.9
Mutagenesis561A → K: Impairs interaction with UPF1 and PABPC1; when associated with K52, A-55, and A-59. Ref.9
Mutagenesis591F → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, A-55 and K-56. Ref.9
Sequence conflict251S → L in BAA91612. Ref.2
Sequence conflict1191V → A in BAA91612. Ref.2
Sequence conflict2931S → G in BAA91612. Ref.2
Sequence conflict3541P → H in AAH36077. Ref.5
Sequence conflict6251P → Q in AAH36077. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8IYD1 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 909FCDEF04EC89C9

FASTA62868,883
        10         20         30         40         50         60 
MDSGSSSSDS APDCWDQVDM ESPGSAPSGD GVSSAVAEAQ REPLSSAFSR KLNVNAKPFV 

        70         80         90        100        110        120 
PNVHAAEFVP SFLRGPTQPP TLPAGSGSND ETCTGAGYPQ GKRMGRGAPV EPSREEPLVS 

       130        140        150        160        170        180 
LEGSNSAVTM ELSEPVVENG EVEMALEESW EHSKEVSEAE PGGGSSGDSG PPEESGQEMM 

       190        200        210        220        230        240 
EEKEEIRKSK SVIVPSGAPK KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER 

       250        260        270        280        290        300 
EAKEKNRETW YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG 

       310        320        330        340        350        360 
GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK MDDPTVNWSI 

       370        380        390        400        410        420 
ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANIKE QSDFCPWYTG LPFIPYLDNL 

       430        440        450        460        470        480 
PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT 

       490        500        510        520        530        540 
ETDFVAPGEN LKIRLKGIEE EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN 

       550        560        570        580        590        600 
AVLHIHTCIE EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF 

       610        620 
PQMGRFTLRD EGKTIAIGKV LKLVPEKD 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a novel termination release factor eRF3b expressing the eRF3 activity in vitro and in vivo."
Jakobsen C.G., Segaard T.M., Jean-Jean O., Frolova L., Justesen J.
Mol. Biol. (Mosk.) 35:672-681(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"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: Teratocarcinoma.
[3]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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], VARIANT THR-23.
Tissue: Brain.
[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: FUNCTION.
[7]"Transcriptional census of 36 microdissected colorectal cancers yields a gene signature to distinguish UICC II and III."
Groene J., Mansmann U., Meister R., Staub E., Roepcke S., Heinze M., Klaman I., Bruemmendorf T., Hermann K., Loddenkemper C., Pilarsky C., Mann B., Adams H.-P., Buhr H.J., Rosenthal A.
Int. J. Cancer 119:1829-1836(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Human eukaryotic release factor 3a depletion causes cell cycle arrest at G1 phase through inhibition of the mTOR pathway."
Chauvin C., Salhi S., Jean-Jean O.
Mol. Cell. Biol. 27:5619-5629(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay."
Singh G., Rebbapragada I., Lykke-Andersen J.
PLoS Biol. 6:E111-E111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UPF1 AND PABPC1, MUTAGENESIS OF LEU-52; ASN-55; ALA-56 AND PHE-59.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ251548 mRNA. Translation: CAB91089.1.
AK001303 mRNA. Translation: BAA91612.1.
AL929101 Genomic DNA. Translation: CAH71524.1.
CH471230 Genomic DNA. Translation: EAW62898.1.
BC036077 mRNA. Translation: AAH36077.1.
CCDSCCDS14336.1.
RefSeqNP_060564.2. NM_018094.4.
UniGeneHs.59523.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KUJX-ray1.40B59-73[»]
ProteinModelPortalQ8IYD1.
SMRQ8IYD1. Positions 198-625.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117221. 20 interactions.
IntActQ8IYD1. 6 interactions.
MINTMINT-4994700.
STRING9606.ENSP00000341247.

PTM databases

PhosphoSiteQ8IYD1.

Polymorphism databases

DMDM182647413.

Proteomic databases

MaxQBQ8IYD1.
PaxDbQ8IYD1.
PeptideAtlasQ8IYD1.
PRIDEQ8IYD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340438; ENSP00000341247; ENSG00000189369.
ENST00000594695; ENSP00000470900; ENSG00000268273.
GeneID23708.
KEGGhsa:23708.
UCSCuc004dpl.3. human.

Organism-specific databases

CTD23708.
GeneCardsGC0XP051503.
H-InvDBHIX0023147.
HGNCHGNC:4622. GSPT2.
HPAHPA044769.
MIM300418. gene.
neXtProtNX_Q8IYD1.
PharmGKBPA29013.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5256.
HOGENOMHOG000229291.
HOVERGENHBG000179.
InParanoidQ8IYD1.
KOK03267.
OMAQVDMETP.
OrthoDBEOG76X5ZT.
PhylomeDBQ8IYD1.
TreeFamTF300566.

Enzyme and pathway databases

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

Gene expression databases

BgeeQ8IYD1.
CleanExHS_GSPT2.
GenevestigatorQ8IYD1.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR009818. Ataxin-2_C.
IPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSPT2. human.
EvolutionaryTraceQ8IYD1.
GeneWikiGSPT2.
GenomeRNAi23708.
NextBio46605.
PROQ8IYD1.
SOURCESearch...

Entry information

Entry nameERF3B_HUMAN
AccessionPrimary (citable) accession number: Q8IYD1
Secondary accession number(s): Q9H909, Q9NVY0, Q9NY44
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: July 9, 2014
This is version 111 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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