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Q8IYD1

- ERF3B_HUMAN

UniProt

Q8IYD1 - ERF3B_HUMAN

Protein

Eukaryotic peptide chain release factor GTP-binding subunit ERF3B

Gene

GSPT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (08 Apr 2008)
      Previous versions | rss
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    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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei216 – 2161Interacts with GTP/GDPBy similarity
    Sitei350 – 3501Interacts with GTP/GDPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi210 – 2178GTPBy similarity
    Nucleotide bindingi287 – 2915GTPBy similarity
    Nucleotide bindingi349 – 3524GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cellular protein metabolic process Source: Reactome
    3. gene expression Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. translation Source: Reactome
    8. translational termination Source: Reactome

    Keywords - Biological processi

    Cell cycle, Nonsense-mediated mRNA decay, Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    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 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4622. GSPT2.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521L → K: Impairs interaction with UPF1 and PABPC1; when associated with A-55, K-56 and A-59. 1 Publication
    Mutagenesisi55 – 551N → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, K-56 and A-59. 1 Publication
    Mutagenesisi56 – 561A → K: Impairs interaction with UPF1 and PABPC1; when associated with K52, A-55, and A-59. 1 Publication
    Mutagenesisi59 – 591F → A: Impairs interaction with UPF1 and PABPC1; when associated with K-52, A-55 and K-56. 1 Publication

    Organism-specific databases

    PharmGKBiPA29013.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 628628Eukaryotic peptide chain release factor GTP-binding subunit ERF3BPRO_0000327256Add
    BLAST

    Proteomic databases

    MaxQBiQ8IYD1.
    PaxDbiQ8IYD1.
    PeptideAtlasiQ8IYD1.
    PRIDEiQ8IYD1.

    PTM databases

    PhosphoSiteiQ8IYD1.

    Expressioni

    Tissue specificityi

    Highly expressed in IUCC stage II colorectal cancer (CRC).1 Publication

    Gene expression databases

    BgeeiQ8IYD1.
    CleanExiHS_GSPT2.
    GenevestigatoriQ8IYD1.

    Organism-specific databases

    HPAiHPA044769.

    Interactioni

    Subunit structurei

    Interacts with ETF1 By similarity. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with UPF1 and PABPC1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PABPC1P119407EBI-3869637,EBI-81531
    UPF1Q929003EBI-3869637,EBI-373471

    Protein-protein interaction databases

    BioGridi117221. 20 interactions.
    IntActiQ8IYD1. 6 interactions.
    MINTiMINT-4994700.
    STRINGi9606.ENSP00000341247.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KUJX-ray1.40B59-73[»]
    ProteinModelPortaliQ8IYD1.
    SMRiQ8IYD1. Positions 198-625.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IYD1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini201 – 425225tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni210 – 2178G1PROSITE-ProRule annotation
    Regioni266 – 2705G2PROSITE-ProRule annotation
    Regioni287 – 2904G3PROSITE-ProRule annotation
    Regioni349 – 3524G4PROSITE-ProRule annotation
    Regioni391 – 3933G5PROSITE-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

    eggNOGiCOG5256.
    HOGENOMiHOG000229291.
    HOVERGENiHBG000179.
    InParanoidiQ8IYD1.
    KOiK03267.
    OMAiQVDMETP.
    OrthoDBiEOG76X5ZT.
    PhylomeDBiQ8IYD1.
    TreeFamiTF300566.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR009818. 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]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. 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.

    Q8IYD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSGSSSSDS APDCWDQVDM ESPGSAPSGD GVSSAVAEAQ REPLSSAFSR    50
    KLNVNAKPFV PNVHAAEFVP SFLRGPTQPP TLPAGSGSND ETCTGAGYPQ 100
    GKRMGRGAPV EPSREEPLVS LEGSNSAVTM ELSEPVVENG EVEMALEESW 150
    EHSKEVSEAE PGGGSSGDSG PPEESGQEMM EEKEEIRKSK SVIVPSGAPK 200
    KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER EAKEKNRETW 250
    YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG 300
    GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK 350
    MDDPTVNWSI ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANIKE 400
    QSDFCPWYTG LPFIPYLDNL PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL 450
    ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT ETDFVAPGEN LKIRLKGIEE 500
    EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN AVLHIHTCIE 550
    EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF 600
    PQMGRFTLRD EGKTIAIGKV LKLVPEKD 628
    Length:628
    Mass (Da):68,883
    Last modified:April 8, 2008 - v2
    Checksum:i909FCDEF04EC89C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251S → L in BAA91612. (PubMed:14702039)Curated
    Sequence conflicti119 – 1191V → A in BAA91612. (PubMed:14702039)Curated
    Sequence conflicti293 – 2931S → G in BAA91612. (PubMed:14702039)Curated
    Sequence conflicti354 – 3541P → H in AAH36077. (PubMed:15489334)Curated
    Sequence conflicti625 – 6251P → Q in AAH36077. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231P → T.1 Publication
    Corresponds to variant rs17855593 [ dbSNP | Ensembl ].
    VAR_042431

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS14336.1.
    RefSeqiNP_060564.2. NM_018094.4.
    UniGeneiHs.59523.

    Genome annotation databases

    EnsembliENST00000340438; ENSP00000341247; ENSG00000189369.
    GeneIDi23708.
    KEGGihsa:23708.
    UCSCiuc004dpl.3. human.

    Polymorphism databases

    DMDMi182647413.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS14336.1.
    RefSeqi NP_060564.2. NM_018094.4.
    UniGenei Hs.59523.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KUJ X-ray 1.40 B 59-73 [» ]
    ProteinModelPortali Q8IYD1.
    SMRi Q8IYD1. Positions 198-625.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117221. 20 interactions.
    IntActi Q8IYD1. 6 interactions.
    MINTi MINT-4994700.
    STRINGi 9606.ENSP00000341247.

    PTM databases

    PhosphoSitei Q8IYD1.

    Polymorphism databases

    DMDMi 182647413.

    Proteomic databases

    MaxQBi Q8IYD1.
    PaxDbi Q8IYD1.
    PeptideAtlasi Q8IYD1.
    PRIDEi Q8IYD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340438 ; ENSP00000341247 ; ENSG00000189369 .
    GeneIDi 23708.
    KEGGi hsa:23708.
    UCSCi uc004dpl.3. human.

    Organism-specific databases

    CTDi 23708.
    GeneCardsi GC0XP051503.
    H-InvDB HIX0023147.
    HGNCi HGNC:4622. GSPT2.
    HPAi HPA044769.
    MIMi 300418. gene.
    neXtProti NX_Q8IYD1.
    PharmGKBi PA29013.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5256.
    HOGENOMi HOG000229291.
    HOVERGENi HBG000179.
    InParanoidi Q8IYD1.
    KOi K03267.
    OMAi QVDMETP.
    OrthoDBi EOG76X5ZT.
    PhylomeDBi Q8IYD1.
    TreeFami TF300566.

    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 GSPT2. human.
    EvolutionaryTracei Q8IYD1.
    GeneWikii GSPT2.
    GenomeRNAii 23708.
    NextBioi 46605.
    PROi Q8IYD1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8IYD1.
    CleanExi HS_GSPT2.
    Genevestigatori Q8IYD1.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR009818. 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 ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    PF07145. PAM2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiERF3B_HUMAN
    AccessioniPrimary (citable) accession number: Q8IYD1
    Secondary accession number(s): Q9H909, Q9NVY0, Q9NY44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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, Reference proteome

    Documents

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

    External Data

    Dasty 3