Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q05D44

- IF2P_MOUSE

UniProt

Q05D44 - IF2P_MOUSE

Protein

Eukaryotic translation initiation factor 5B

Gene

Eif5b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Function in general translation initiation by promoting the binding of the formylmethionine-tRNA to ribosomes. Seems to function along with eIF-2 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi634 – 6418GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. translation initiation factor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 5B
    Short name:
    eIF-5B
    Alternative name(s):
    Translation initiation factor IF-2
    Gene namesi
    Name:Eif5b
    Synonyms:If2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2441772. Eif5b.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12161216Eukaryotic translation initiation factor 5BPRO_0000354071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei108 – 1081PhosphoserineBy similarity
    Modified residuei114 – 1141Phosphoserine2 Publications
    Modified residuei137 – 1371Phosphoserine3 Publications
    Modified residuei139 – 1391Phosphoserine3 Publications
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei172 – 1721PhosphoserineBy similarity
    Modified residuei183 – 1831PhosphoserineBy similarity
    Modified residuei184 – 1841PhosphoserineBy similarity
    Modified residuei187 – 1871Phosphoserine2 Publications
    Modified residuei191 – 1911Phosphoserine2 Publications
    Modified residuei215 – 2151Phosphoserine4 Publications
    Modified residuei300 – 3001PhosphothreonineBy similarity
    Modified residuei497 – 4971PhosphothreonineBy similarity
    Modified residuei556 – 5561PhosphoserineBy similarity
    Modified residuei584 – 5841PhosphoserineBy similarity
    Modified residuei585 – 5851PhosphoserineBy similarity
    Modified residuei587 – 5871PhosphoserineBy similarity
    Modified residuei591 – 5911PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05D44.
    PaxDbiQ05D44.
    PRIDEiQ05D44.

    PTM databases

    PhosphoSiteiQ05D44.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05D44.
    BgeeiQ05D44.
    GenevestigatoriQ05D44.

    Interactioni

    Subunit structurei

    Interacts with ANXA5 in a calcium and phospholipid-dependent manner.By similarity

    Protein-protein interaction databases

    BioGridi230580. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05D44.
    SMRiQ05D44. Positions 583-1195.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini625 – 842218tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni634 – 6418G1PROSITE-ProRule annotation
    Regioni659 – 6635G2PROSITE-ProRule annotation
    Regioni698 – 7014G3PROSITE-ProRule annotation
    Regioni752 – 7554G4PROSITE-ProRule annotation
    Regioni820 – 8223G5PROSITE-ProRule annotation

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 452414Lys-richAdd
    BLAST
    Compositional biasi235 – 561327Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0532.
    GeneTreeiENSGT00730000111064.
    HOVERGENiHBG019036.
    InParanoidiQ8CFF4.
    KOiK03243.
    OMAiGSLRMHT.
    OrthoDBiEOG7034GC.
    PhylomeDBiQ05D44.
    TreeFamiTF101535.

    Family and domain databases

    Gene3Di3.40.50.10050. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR029459. EFTU-type.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR023115. TIF_IF2_dom3.
    IPR009000. Transl_B-barrel.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF14578. GTP_EFTU_D4. 1 hit.
    PF11987. IF-2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52156. SSF52156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q05D44-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK     50
    QDFDENDILR ELEELSLEAQ GIRADRDAAA VKPTENNEEE SASKQDKKKK 100
    GQKGKKTSFD ENDSEELEDK DSKSKKTARP NSEAPLSGSE DADDSNKLSK 150
    KGKKAQKSTK KRDGSEEDED NSKRSKERSR VNSSGESGGE SDEFLQSRKG 200
    QKKNQKNKSV PTVDSGNEDD DSSFKIKTVA QKKAEKKERE KKKRDEEKAK 250
    LRKMKEKEEL EKGKKEQSKQ REPQKRPEEE VLTLRGTPDT GAASEEKGDT 300
    AAALEDDNEG DKKKKDKKKK KTEKDEKEKE KKKGPSKSTV KAIQEALAKL 350
    KEEEERQKRE EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL 400
    KKEGKLLTKS QREARARAEV TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK 450
    KKTPQQLESK EVSETLEISA PVEAVDQGGP EKEETPPSVE PEEEEDTEDA 500
    GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEEEE EEESEDEEEE 550
    GDSEGSDGDE EDCKLSDEKD SGKAGDTKPS KDASSDSEYD SDDDRTKEER 600
    AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT 650
    HVQDGEAGGI TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP 700
    GHESFSNLRN RGSSLCDIAI LVVDIMHGLE PQTIESINIL KSKKCPFIVA 750
    LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK DEFEERAKAI IVEFAQQGLN 800
    AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT MLSKRLAHCE 850
    ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL 900
    LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD 950
    EIPVLKDELI HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP 1000
    YAGINIGPVH KKDVMKASVM LEHDPQYAVI LAFDVRIERD AQEMADSLGV 1050
    RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF KHIAVFPCKM KILPQYIFNS 1100
    RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN HKQVDVAKKG 1150
    QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK 1200
    SDWQLIVELK KVFEII 1216
    Length:1,216
    Mass (Da):137,616
    Last modified:November 25, 2008 - v2
    Checksum:i38D1C21648E4EAEC
    GO

    Sequence cautioni

    The sequence AAH18347.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH37150.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH40746.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH60288.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211D → N in BAE26259. (PubMed:16141072)Curated
    Sequence conflicti188 – 1881G → C in BAE26259. (PubMed:16141072)Curated
    Sequence conflicti254 – 2541M → L in BAE26259. (PubMed:16141072)Curated
    Sequence conflicti302 – 3021A → V in BAE26259. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC114583 Genomic DNA. No translation available.
    AK145146 mRNA. Translation: BAE26259.1.
    AK145732 mRNA. Translation: BAE26614.1.
    AK163527 mRNA. Translation: BAE37384.1.
    BC018347 mRNA. Translation: AAH18347.1. Sequence problems.
    BC037150 mRNA. Translation: AAH37150.1. Sequence problems.
    BC040746 mRNA. Translation: AAH40746.1. Sequence problems.
    BC060288 mRNA. Translation: AAH60288.1. Sequence problems.
    CCDSiCCDS35544.1.
    RefSeqiNP_938045.2. NM_198303.2.
    UniGeneiMm.260943.

    Genome annotation databases

    EnsembliENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
    GeneIDi226982.
    KEGGimmu:226982.
    UCSCiuc007aso.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC114583 Genomic DNA. No translation available.
    AK145146 mRNA. Translation: BAE26259.1 .
    AK145732 mRNA. Translation: BAE26614.1 .
    AK163527 mRNA. Translation: BAE37384.1 .
    BC018347 mRNA. Translation: AAH18347.1 . Sequence problems.
    BC037150 mRNA. Translation: AAH37150.1 . Sequence problems.
    BC040746 mRNA. Translation: AAH40746.1 . Sequence problems.
    BC060288 mRNA. Translation: AAH60288.1 . Sequence problems.
    CCDSi CCDS35544.1.
    RefSeqi NP_938045.2. NM_198303.2.
    UniGenei Mm.260943.

    3D structure databases

    ProteinModelPortali Q05D44.
    SMRi Q05D44. Positions 583-1195.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 230580. 1 interaction.

    PTM databases

    PhosphoSitei Q05D44.

    Proteomic databases

    MaxQBi Q05D44.
    PaxDbi Q05D44.
    PRIDEi Q05D44.

    Protocols and materials databases

    DNASUi 226982.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027252 ; ENSMUSP00000027252 ; ENSMUSG00000026083 .
    GeneIDi 226982.
    KEGGi mmu:226982.
    UCSCi uc007aso.1. mouse.

    Organism-specific databases

    CTDi 9669.
    MGIi MGI:2441772. Eif5b.

    Phylogenomic databases

    eggNOGi COG0532.
    GeneTreei ENSGT00730000111064.
    HOVERGENi HBG019036.
    InParanoidi Q8CFF4.
    KOi K03243.
    OMAi GSLRMHT.
    OrthoDBi EOG7034GC.
    PhylomeDBi Q05D44.
    TreeFami TF101535.

    Miscellaneous databases

    ChiTaRSi EIF5B. mouse.
    NextBioi 378430.
    PROi Q05D44.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05D44.
    Bgeei Q05D44.
    Genevestigatori Q05D44.

    Family and domain databases

    Gene3Di 3.40.50.10050. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR029459. EFTU-type.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR023115. TIF_IF2_dom3.
    IPR009000. Transl_B-barrel.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF14578. GTP_EFTU_D4. 1 hit.
    PF11987. IF-2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52156. SSF52156. 1 hit.
    SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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] OF 1-771.
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina and Mammary gland.
    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] OF 1-402.
      Strain: FVB/N.
      Tissue: Limb and Mammary tumor.
    4. "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
      Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
      EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    6. "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-187 AND SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Teratocarcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139; SER-187; SER-191 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "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-137 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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-165 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 SER-114; SER-137; SER-139 AND SER-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiIF2P_MOUSE
    AccessioniPrimary (citable) accession number: Q05D44
    Secondary accession number(s): Q3SYI4
    , Q3TQJ8, Q3UL37, Q3UM39, Q6PAI0, Q8CFF4, Q8CGD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2008
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 65 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3