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Q8IYD1

- ERF3B_HUMAN

UniProt

Q8IYD1 - ERF3B_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00620000087924.
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

        10         20         30         40         50
MDSGSSSSDS APDCWDQVDM ESPGSAPSGD GVSSAVAEAQ REPLSSAFSR
60 70 80 90 100
KLNVNAKPFV PNVHAAEFVP SFLRGPTQPP TLPAGSGSND ETCTGAGYPQ
110 120 130 140 150
GKRMGRGAPV EPSREEPLVS LEGSNSAVTM ELSEPVVENG EVEMALEESW
160 170 180 190 200
EHSKEVSEAE PGGGSSGDSG PPEESGQEMM EEKEEIRKSK SVIVPSGAPK
210 220 230 240 250
KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER EAKEKNRETW
260 270 280 290 300
YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG
310 320 330 340 350
GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK
360 370 380 390 400
MDDPTVNWSI ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANIKE
410 420 430 440 450
QSDFCPWYTG LPFIPYLDNL PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL
460 470 480 490 500
ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT ETDFVAPGEN LKIRLKGIEE
510 520 530 540 550
EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN AVLHIHTCIE
560 570 580 590 600
EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF
610 620
PQMGRFTLRD EGKTIAIGKV LKLVPEKD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00620000087924.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 114 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

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