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P62495

- ERF1_HUMAN

UniProt

P62495 - ERF1_HUMAN

Protein

Eukaryotic peptide chain release factor subunit 1

Gene

ETF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. 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.1 Publication

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. ribosome binding Source: UniProtKB
    4. RNA binding Source: ProtInc
    5. translation release factor activity Source: UniProtKB
    6. translation release factor activity, codon specific Source: InterPro
    7. translation termination factor activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. protein methylation Source: MGI
    6. regulation of translational termination Source: ProtInc
    7. RNA metabolic process Source: Reactome
    8. translation Source: Reactome
    9. translational termination Source: Reactome

    Keywords - Biological processi

    Nonsense-mediated mRNA decay, Protein biosynthesis

    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 subunit 1
    Short name:
    Eukaryotic release factor 1
    Short name:
    eRF1
    Alternative name(s):
    Protein Cl1
    TB3-1
    Gene namesi
    Name:ETF1
    Synonyms:ERF1, RF1, SUP45L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3477. ETF1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27893.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 437436Eukaryotic peptide chain release factor subunit 1PRO_0000143138Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62495.
    PaxDbiP62495.
    PeptideAtlasiP62495.
    PRIDEiP62495.

    PTM databases

    PhosphoSiteiP62495.

    Expressioni

    Gene expression databases

    ArrayExpressiP62495.
    BgeeiP62495.
    CleanExiHS_ETF1.
    GenevestigatoriP62495.

    Organism-specific databases

    HPAiCAB011686.

    Interactioni

    Subunit structurei

    Heterodimer of two subunits, one of which binds GTP. Component of the transient SURF (SMG1-UPF1-eRF1-eRF3) complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GSPT1P151702EBI-1047744,EBI-948993

    Protein-protein interaction databases

    BioGridi108408. 18 interactions.
    IntActiP62495. 11 interactions.
    MINTiMINT-5004401.
    STRINGi9606.ENSP00000353741.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Turni7 – 93
    Helixi10 – 2516
    Beta strandi30 – 323
    Beta strandi34 – 396
    Beta strandi41 – 433
    Helixi45 – 5915
    Helixi66 – 8217
    Beta strandi93 – 1019
    Helixi103 – 1053
    Beta strandi107 – 1148
    Beta strandi124 – 1307
    Helixi134 – 1396
    Beta strandi145 – 1506
    Beta strandi158 – 1625
    Beta strandi165 – 1706
    Beta strandi180 – 1856
    Helixi188 – 19710
    Turni198 – 2036
    Helixi204 – 2085
    Turni209 – 2124
    Beta strandi216 – 2183
    Beta strandi220 – 2223
    Beta strandi225 – 2295
    Turni230 – 2334
    Helixi234 – 2374
    Beta strandi240 – 2423
    Turni244 – 2496
    Beta strandi253 – 2553
    Helixi262 – 27110
    Turni274 – 2763
    Helixi278 – 29518
    Beta strandi296 – 2983
    Beta strandi301 – 3044
    Helixi305 – 3139
    Beta strandi318 – 3247
    Beta strandi329 – 3335
    Beta strandi336 – 3394
    Beta strandi342 – 3465
    Helixi348 – 3525
    Turni354 – 3563
    Turni360 – 3623
    Beta strandi368 – 3725
    Helixi374 – 3807
    Turni383 – 3864
    Beta strandi389 – 3924
    Beta strandi394 – 3963
    Helixi397 – 4048
    Turni405 – 4084
    Beta strandi409 – 4124
    Beta strandi420 – 4223
    Turni423 – 4253
    Beta strandi426 – 4283
    Helixi434 – 4374

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DT9X-ray2.70A1-437[»]
    2HSTNMR-A140-275[»]
    2KTUNMR-A276-437[»]
    2KTVNMR-A276-437[»]
    2LGTNMR-A1-142[»]
    2LLXNMR-A1-142[»]
    3E1YX-ray3.80A/B/C/D1-437[»]
    3J5Yelectron microscopy9.70A7-420[»]
    DisProtiDP00310.
    ProteinModelPortaliP62495.
    SMRiP62495. Positions 7-420.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62495.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eukaryotic release factor 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG1503.
    HOGENOMiHOG000224681.
    HOVERGENiHBG005602.
    InParanoidiP62495.
    KOiK03265.
    OMAiWENLDIQ.
    PhylomeDBiP62495.
    TreeFamiTF105672.

    Family and domain databases

    Gene3Di3.30.1330.30. 1 hit.
    3.30.960.10. 1 hit.
    InterProiIPR005140. eRF1_1_Pelota.
    IPR005141. eRF1_2.
    IPR005142. eRF1_3.
    IPR029064. L30e-like.
    IPR004403. Peptide_chain-rel_eRF1/aRF1.
    IPR024049. Release_factor_eRF1/aRF1_N.
    [Graphical view]
    PANTHERiPTHR10113. PTHR10113. 1 hit.
    PfamiPF03463. eRF1_1. 1 hit.
    PF03464. eRF1_2. 1 hit.
    PF03465. eRF1_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF55315. SSF55315. 1 hit.
    SSF55481. SSF55481. 1 hit.
    TIGRFAMsiTIGR03676. aRF1/eRF1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62495-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK    50
    MLADEFGTAS NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI 100
    VTEEGKEKKV NIDFEPFKPI NTSLYLCDNK FHTEALTALL SDDSKFGFIV 150
    IDGSGALFGT LQGNTREVLH KFTVDLPKKH GRGGQSALRF ARLRMEKRHN 200
    YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD MFDQRLQSKV 250
    LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK 300
    YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ 350
    EKDKSHFTDK ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS 400
    QFVKGFGGIG GILRYRVDFQ GMEYQGGDDE FFDLDDY 437
    Length:437
    Mass (Da):49,031
    Last modified:January 23, 2007 - v3
    Checksum:iCECC50D100E59D19
    GO
    Isoform 2 (identifier: P62495-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.

    Show »
    Length:404
    Mass (Da):45,463
    Checksum:iF70FB4B7D81FD5C1
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3333Missing in isoform 2. 2 PublicationsVSP_056189Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75715 mRNA. Translation: AAA36665.1. Sequence problems.
    X81625 mRNA. Translation: CAA57281.1.
    U90176 mRNA. Translation: AAB49726.1.
    AF095901 Genomic DNA. Translation: AAD43966.1.
    BT007374 mRNA. Translation: AAP36038.1.
    AK312510 mRNA. Translation: BAG35411.1.
    AC011385 Genomic DNA. No translation available.
    AC113403 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62130.1.
    CH471062 Genomic DNA. Translation: EAW62131.1.
    CH471062 Genomic DNA. Translation: EAW62132.1.
    BC088358 mRNA. Translation: AAH88358.1.
    BC014269 mRNA. Translation: AAH14269.1.
    CCDSiCCDS4207.1.
    PIRiS50853.
    RefSeqiNP_001243231.1. NM_001256302.1.
    NP_004721.1. NM_004730.3.
    UniGeneiHs.483494.

    Genome annotation databases

    EnsembliENST00000360541; ENSP00000353741; ENSG00000120705.
    ENST00000499810; ENSP00000421288; ENSG00000120705.
    GeneIDi2107.
    KEGGihsa:2107.
    UCSCiuc003ldc.5. human.

    Polymorphism databases

    DMDMi50402099.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75715 mRNA. Translation: AAA36665.1 . Sequence problems.
    X81625 mRNA. Translation: CAA57281.1 .
    U90176 mRNA. Translation: AAB49726.1 .
    AF095901 Genomic DNA. Translation: AAD43966.1 .
    BT007374 mRNA. Translation: AAP36038.1 .
    AK312510 mRNA. Translation: BAG35411.1 .
    AC011385 Genomic DNA. No translation available.
    AC113403 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62130.1 .
    CH471062 Genomic DNA. Translation: EAW62131.1 .
    CH471062 Genomic DNA. Translation: EAW62132.1 .
    BC088358 mRNA. Translation: AAH88358.1 .
    BC014269 mRNA. Translation: AAH14269.1 .
    CCDSi CCDS4207.1.
    PIRi S50853.
    RefSeqi NP_001243231.1. NM_001256302.1.
    NP_004721.1. NM_004730.3.
    UniGenei Hs.483494.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DT9 X-ray 2.70 A 1-437 [» ]
    2HST NMR - A 140-275 [» ]
    2KTU NMR - A 276-437 [» ]
    2KTV NMR - A 276-437 [» ]
    2LGT NMR - A 1-142 [» ]
    2LLX NMR - A 1-142 [» ]
    3E1Y X-ray 3.80 A/B/C/D 1-437 [» ]
    3J5Y electron microscopy 9.70 A 7-420 [» ]
    DisProti DP00310.
    ProteinModelPortali P62495.
    SMRi P62495. Positions 7-420.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108408. 18 interactions.
    IntActi P62495. 11 interactions.
    MINTi MINT-5004401.
    STRINGi 9606.ENSP00000353741.

    PTM databases

    PhosphoSitei P62495.

    Polymorphism databases

    DMDMi 50402099.

    Proteomic databases

    MaxQBi P62495.
    PaxDbi P62495.
    PeptideAtlasi P62495.
    PRIDEi P62495.

    Protocols and materials databases

    DNASUi 2107.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360541 ; ENSP00000353741 ; ENSG00000120705 .
    ENST00000499810 ; ENSP00000421288 ; ENSG00000120705 .
    GeneIDi 2107.
    KEGGi hsa:2107.
    UCSCi uc003ldc.5. human.

    Organism-specific databases

    CTDi 2107.
    GeneCardsi GC05M137843.
    HGNCi HGNC:3477. ETF1.
    HPAi CAB011686.
    MIMi 600285. gene.
    neXtProti NX_P62495.
    PharmGKBi PA27893.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1503.
    HOGENOMi HOG000224681.
    HOVERGENi HBG005602.
    InParanoidi P62495.
    KOi K03265.
    OMAi WENLDIQ.
    PhylomeDBi P62495.
    TreeFami TF105672.

    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 ETF1. human.
    EvolutionaryTracei P62495.
    GeneWikii Eukaryotic_release_factors.
    GenomeRNAii 2107.
    NextBioi 8519.
    PROi P62495.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62495.
    Bgeei P62495.
    CleanExi HS_ETF1.
    Genevestigatori P62495.

    Family and domain databases

    Gene3Di 3.30.1330.30. 1 hit.
    3.30.960.10. 1 hit.
    InterProi IPR005140. eRF1_1_Pelota.
    IPR005141. eRF1_2.
    IPR005142. eRF1_3.
    IPR029064. L30e-like.
    IPR004403. Peptide_chain-rel_eRF1/aRF1.
    IPR024049. Release_factor_eRF1/aRF1_N.
    [Graphical view ]
    PANTHERi PTHR10113. PTHR10113. 1 hit.
    Pfami PF03463. eRF1_1. 1 hit.
    PF03464. eRF1_2. 1 hit.
    PF03465. eRF1_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55315. SSF55315. 1 hit.
    SSF55481. SSF55481. 1 hit.
    TIGRFAMsi TIGR03676. aRF1/eRF1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a human cDNA with high homology to yeast omnipotent suppressor 45."
      Grenett H.E., Fuller G.M., Bounelis P.
      Gene 110:239-243(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor."
      Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G., Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L.
      Nature 372:701-703(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION, FUNCTION.
    3. "The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1."
      Andjelkovic N., Zolnierowicz S., van Hoof C., Goris J., Hemmings B.A.
      EMBO J. 15:7156-7167(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "Human release factor eRF1: structural organisation of the unique functional gene on chromosome 5 and of the three processed pseudogenes."
      Guenet L., Toutain B., Guilleret I., Chauvel B., Deaven L.L., Longmire J.L., Le Gall L.Y., David V., Le Treut A.
      FEBS Lett. 454:131-136(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "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] (ISOFORM 1).
      Tissue: Thalamus.
    7. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORMS 1 AND 2).
      Tissue: Lymph and Testis.
    10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The crystal structure of human eukaryotic release factor eRF1 --mechanism of stop codon recognition and peptidyl-tRNA hydrolysis."
      Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D.
      Cell 100:311-321(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    16. "Eukaryotic class 1 translation termination factor eRF1 -- the NMR structure and dynamics of the middle domain involved in triggering ribosome-dependent peptidyl-tRNA hydrolysis."
      Ivanova E.V., Kolosov P.M., Birdsall B., Kelly G., Pastore A., Kisselev L.L., Polshakov V.I.
      FEBS J. 274:4223-4237(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 140-277.

    Entry informationi

    Entry nameiERF1_HUMAN
    AccessioniPrimary (citable) accession number: P62495
    Secondary accession number(s): B2R6B4
    , D3DQC1, P46055, Q5M7Z7, Q96CG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 110 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3