Q8IYD1 (ERF3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GSPT2
Synonyms:	ERF3B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	628 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell cycle Nonsense-mediated mRNA decay Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC cell cycle Inferred from electronic annotation. Source: UniProtKB-KW nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PABPC1	P11940	3	EBI-3869637,EBI-81531
UPF1	Q92900	3	EBI-3869637,EBI-373471

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 628	628	Eukaryotic peptide chain release factor GTP-binding subunit ERF3B		PRO_0000327256
Regions
	Nucleotide binding	210 – 217	8	GTP By similarity
	Nucleotide binding	287 – 291	5	GTP By similarity
	Nucleotide binding	349 – 352	4	GTP By similarity
Sites
	Site	216	1	Interacts with GTP/GDP By similarity
	Site	350	1	Interacts with GTP/GDP By similarity
Natural variations
	Natural variant	23	1	P → T. Ref.5 Corresponds to variant rs17855593 [ dbSNP | Ensembl ].		VAR_042431
Experimental info
	Mutagenesis	52	1	L → K: Impairs interaction with UPF1 and PABPC1; when associated with A-55, K-56 and A-59. Ref.9
	Mutagenesis	55	1	N → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, K-56 and A-59. Ref.9
	Mutagenesis	56	1	A → K: Impairs interaction with UPF1 and PABPC1; when associated with K52, A-55, and A-59. Ref.9
	Mutagenesis	59	1	F → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, A-55 and K-56. Ref.9
	Sequence conflict	25	1	S → L in BAA91612. Ref.2
	Sequence conflict	119	1	V → A in BAA91612. Ref.2
	Sequence conflict	293	1	S → G in BAA91612. Ref.2
	Sequence conflict	354	1	P → H in AAH36077. Ref.5
	Sequence conflict	625	1	P → Q in AAH36077. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8IYD1 [UniParc]. Last modified April 8, 2008. Version 2. Checksum: 909FCDEF04EC89C9	FASTA	628	68,883
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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.

IPI

IPI00642097.

RefSeq

NP_060564.2. NM_018094.4.

UniGene

Hs.59523.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KUJ	X-ray	1.40	B	59-73	[»]

ProteinModelPortal

Q8IYD1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IYD1. 4 interactions.

STRING

9606.ENSP00000341247.

PTM databases

PhosphoSite

Q8IYD1.

Polymorphism databases

DMDM

182647413.

Proteomic databases

PaxDb

Q8IYD1.

PeptideAtlas

Q8IYD1.

PRIDE

Q8IYD1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000340438; ENSP00000341247; ENSG00000189369.
ENST00000594695; ENSP00000470900; ENSG00000268273.

GeneID

23708.

KEGG

hsa:23708.

UCSC

uc004dpl.3. human.

Organism-specific databases

CTD

23708.

GeneCards

GC0XP051503.

H-InvDB

HIX0023147.

HGNC

HGNC:4622. GSPT2.

HPA

HPA044769.

MIM

300418. gene.

neXtProt

NX_Q8IYD1.

PharmGKB

PA29013.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5256.

HOGENOM

HOG000229291.

HOVERGEN

HBG000179.

InParanoid

Q8IYD1.

KO

K03267.

OMA

ETDYVAP.

OrthoDB

EOG43TZVF.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q8IYD1.

CleanEx

HS_GSPT2.

Genevestigator

Q8IYD1.

Family and domain databases

InterPro

IPR009818. Ataxin-2_C.
IPR000795. EF_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
PF07145. PAM2. 1 hit.
[Graphical view]

PRINTS

PR00315. ELONGATNFCT.

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.

PROSITE

PS00301. EFACTOR_GTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GSPT2. human.

EvolutionaryTrace

Q8IYD1.

GenomeRNAi

23708.

NextBio

46605.

SOURCE

Search...

Entry information

Entry name

ERF3B_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.