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Q8JZQ9

- EIF3B_MOUSE

UniProt

Q8JZQ9 - EIF3B_MOUSE

Protein

Eukaryotic translation initiation factor 3 subunit B

Gene

Eif3b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.1 Publication

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: IntAct
    3. translation initiation factor activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    2. regulation of translational initiation Source: UniProtKB-HAMAP
    3. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit BUniRule annotation
    Short name:
    eIF3bUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 subunit 9UniRule annotation
    eIF-3-etaUniRule annotation
    eIF3 p116
    Gene namesi
    Name:Eif3b
    Synonyms:Eif3s9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:106478. Eif3b.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    2. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    3. eukaryotic translation initiation factor 3 complex Source: UniProtKB
    4. eukaryotic translation initiation factor 3 complex, eIF3m Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic death.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 803803Eukaryotic translation initiation factor 3 subunit BPRO_0000223479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineUniRule annotation
    Modified residuei31 – 311Phosphothreonine1 Publication
    Modified residuei68 – 681Phosphoserine1 PublicationUniRule annotation
    Modified residuei74 – 741Phosphothreonine2 Publications
    Modified residuei75 – 751Phosphoserine3 PublicationsUniRule annotation
    Modified residuei79 – 791Phosphoserine4 PublicationsUniRule annotation
    Modified residuei90 – 901Phosphoserine1 PublicationUniRule annotation
    Modified residuei120 – 1201Phosphoserine5 PublicationsUniRule annotation
    Modified residuei123 – 1231Phosphoserine4 PublicationsUniRule annotation
    Modified residuei141 – 1411PhosphoserineUniRule annotation
    Modified residuei143 – 1431PhosphoserineUniRule annotation
    Modified residuei153 – 1531PhosphoserineUniRule annotation
    Modified residuei198 – 1981N6-acetyllysineBy similarity
    Modified residuei228 – 2281PhosphoserineUniRule annotation
    Modified residuei277 – 2771N6-acetyllysineBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8JZQ9.
    PaxDbiQ8JZQ9.
    PRIDEiQ8JZQ9.

    PTM databases

    PhosphoSiteiQ8JZQ9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ8JZQ9.
    GenevestigatoriQ8JZQ9.

    Interactioni

    Subunit structurei

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may also interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Also interacts with UPF2 and HNRPD.2 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eif4g1Q6NZJ62EBI-4286513,EBI-8175606

    Protein-protein interaction databases

    BioGridi205699. 3 interactions.
    IntActiQ8JZQ9. 11 interactions.
    MINTiMINT-1899500.
    STRINGi10090.ENSMUSP00000075175.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8JZQ9.
    SMRiQ8JZQ9. Positions 159-263, 331-697.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini174 – 25784RRMUniRule annotationAdd
    BLAST
    Repeati321 – 35939WD 1Add
    BLAST
    Repeati361 – 40646WD 2Add
    BLAST
    Repeati410 – 44839WD 3Add
    BLAST
    Repeati549 – 59042WD 4Add
    BLAST
    Repeati638 – 68346WD 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni113 – 402290Sufficient for interaction with EIF3EUniRule annotationAdd
    BLAST
    Regioni159 – 263105Sufficient for interaction with EIF3JUniRule annotationAdd
    BLAST

    Domaini

    The RRM domain mediates interaction with EIF3J.UniRule annotation

    Sequence similaritiesi

    Belongs to the eIF-3 subunit B family.UniRule annotation
    Contains 1 RRM (RNA recognition motif) domain.UniRule annotation
    Contains 5 WD repeats.UniRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG5354.
    GeneTreeiENSGT00550000074913.
    HOGENOMiHOG000265546.
    HOVERGENiHBG006127.
    KOiK03253.
    OMAiHTLRVNK.
    OrthoDBiEOG7KM5S6.
    PhylomeDBiQ8JZQ9.
    TreeFamiTF101521.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    2.130.10.10. 1 hit.
    3.30.70.330. 1 hit.
    HAMAPiMF_03001. eIF3b.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR011400. EIF3B.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR013979. TIF_beta_prop-like.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view]
    PANTHERiPTHR14068. PTHR14068. 1 hit.
    PfamiPF08662. eIF2A. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036424. eIF3b. 1 hit.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8JZQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE    50
    DAEAGPEPEV RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE 100
    AVGEQARGHP SAGAEEEGGS DGSAAEAEPR ALENGEADEP SFSDPEDFVD 150
    DVSEEELLGD VLKDRPQEAD GIDSVIVVDN VPQVGPDRLE KLKNVIHKIF 200
    SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD GYKLDKQHTF 250
    RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE 300
    SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG 350
    GDKFKQIQRF SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT 400
    GHKKRGFHCE SSAHWPIFKW SHDGKFFARM TLDTLSIYET PSMGLLDKKS 450
    LKISGIKDFS WSPGGNIIAF WVPEDKDIPA RVTLMQLPTR QEIRVRNLFN 500
    VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE KQVPVDVVEM 550
    KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA 600
    NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP 650
    TGRYVVTSVS WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL 700
    LSQDQIKQIK KDLKKYSKIF EQKDRLSQSK ASKELVERRR TMMEDFRQYR 750
    KMAQELYMKQ KNERLELRGG VDTDELDSNV DDWEEETIEF FVTEEVIPLG 800
    SQE 803
    Length:803
    Mass (Da):91,370
    Last modified:October 1, 2002 - v1
    Checksum:iD770AC70BFE9832F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033722 mRNA. Translation: BAC28445.1.
    AK167618 mRNA. Translation: BAE39671.1.
    AK170938 mRNA. Translation: BAE42128.1.
    BC007175 mRNA. Translation: AAH07175.1.
    BC031704 mRNA. Translation: AAH31704.1.
    CCDSiCCDS19819.1.
    PIRiJC7862.
    RefSeqiNP_598677.1. NM_133916.2.
    UniGeneiMm.21671.

    Genome annotation databases

    EnsembliENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
    GeneIDi27979.
    KEGGimmu:27979.
    UCSCiuc009ahr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK033722 mRNA. Translation: BAC28445.1 .
    AK167618 mRNA. Translation: BAE39671.1 .
    AK170938 mRNA. Translation: BAE42128.1 .
    BC007175 mRNA. Translation: AAH07175.1 .
    BC031704 mRNA. Translation: AAH31704.1 .
    CCDSi CCDS19819.1.
    PIRi JC7862.
    RefSeqi NP_598677.1. NM_133916.2.
    UniGenei Mm.21671.

    3D structure databases

    ProteinModelPortali Q8JZQ9.
    SMRi Q8JZQ9. Positions 159-263, 331-697.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205699. 3 interactions.
    IntActi Q8JZQ9. 11 interactions.
    MINTi MINT-1899500.
    STRINGi 10090.ENSMUSP00000075175.

    PTM databases

    PhosphoSitei Q8JZQ9.

    Proteomic databases

    MaxQBi Q8JZQ9.
    PaxDbi Q8JZQ9.
    PRIDEi Q8JZQ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100507 ; ENSMUSP00000098076 ; ENSMUSG00000056076 .
    GeneIDi 27979.
    KEGGi mmu:27979.
    UCSCi uc009ahr.1. mouse.

    Organism-specific databases

    CTDi 8662.
    MGIi MGI:106478. Eif3b.

    Phylogenomic databases

    eggNOGi COG5354.
    GeneTreei ENSGT00550000074913.
    HOGENOMi HOG000265546.
    HOVERGENi HBG006127.
    KOi K03253.
    OMAi HTLRVNK.
    OrthoDBi EOG7KM5S6.
    PhylomeDBi Q8JZQ9.
    TreeFami TF101521.

    Miscellaneous databases

    ChiTaRSi EIF3B. mouse.
    NextBioi 306472.
    PROi Q8JZQ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8JZQ9.
    Genevestigatori Q8JZQ9.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    2.130.10.10. 1 hit.
    3.30.70.330. 1 hit.
    HAMAPi MF_03001. eIF3b.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR011400. EIF3B.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR013979. TIF_beta_prop-like.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [Graphical view ]
    PANTHERi PTHR14068. PTHR14068. 1 hit.
    Pfami PF08662. eIF2A. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036424. eIF3b. 1 hit.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
      Tissue: Embryonic stem cell.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Cecum and Placenta.
    3. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    5. "mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin."
      Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr.
      EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND RPS6.
    6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Reconstitution reveals the functional core of mammalian eIF3."
      Masutani M., Sonenberg N., Yokoyama S., Imataka H.
      EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
      Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
      J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Teratocarcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75; SER-79; SER-90; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79; SER-120 AND SER-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiEIF3B_MOUSE
    AccessioniPrimary (citable) accession number: Q8JZQ9
    Secondary accession number(s): Q922K2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Translation initiation factors
      List of translation initiation factor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3