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Q5F2E7

- NUFP2_MOUSE

UniProt

Q5F2E7 - NUFP2_MOUSE

Protein

Nuclear fragile X mental retardation-interacting protein 2

Gene

Nufip2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    Binds RNA.By similarity

    GO - Molecular functioni

    1. RNA binding Source: HGNC

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear fragile X mental retardation-interacting protein 2
    Alternative name(s):
    82 kDa FMRP-interacting protein
    Short name:
    82-FIP
    FMRP-interacting protein 2
    Gene namesi
    Name:Nufip2
    Synonyms:Kiaa1321
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1915814. Nufip2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Localized in both nucleus and cytoplasm in most neurons. In the cortex, distributed in a diffuse way in the nucleus and in the cytoplasm. Localized in the cytoplasm in neurons of the dentate gyrus in the olfactive bulb, in the ependymal epithelium and in the granular layer of the cerebellum. In Purkinje cells, distributed in both cell compartments and in nuclear dots adjacent to the nucleolus.

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nucleus Source: HGNC
    3. polysomal ribosome Source: HGNC

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 692692Nuclear fragile X mental retardation-interacting protein 2PRO_0000245522Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei88 – 881PhosphothreonineBy similarity
    Modified residuei113 – 1131PhosphoserineBy similarity
    Modified residuei114 – 1141PhosphoserineBy similarity
    Modified residuei213 – 2131Phosphoserine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei219 – 2191PhosphotyrosineBy similarity
    Modified residuei220 – 2201PhosphothreonineBy similarity
    Modified residuei221 – 2211PhosphothreonineBy similarity
    Modified residuei376 – 3761PhosphoserineBy similarity
    Modified residuei569 – 5691PhosphothreonineBy similarity
    Modified residuei570 – 5701PhosphoserineBy similarity
    Modified residuei626 – 6261PhosphoserineBy similarity
    Modified residuei630 – 6301PhosphothreonineBy similarity
    Modified residuei634 – 6341PhosphoserineBy similarity
    Modified residuei649 – 6491Phosphoserine3 Publications
    Modified residuei652 – 6521PhosphoserineBy similarity
    Modified residuei689 – 6891PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5F2E7.
    PaxDbiQ5F2E7.
    PRIDEiQ5F2E7.

    PTM databases

    PhosphoSiteiQ5F2E7.

    Expressioni

    Gene expression databases

    BgeeiQ5F2E7.
    GenevestigatoriQ5F2E7.

    Interactioni

    Subunit structurei

    Interacts with FMRP.By similarity

    Protein-protein interaction databases

    BioGridi212929. 1 interaction.
    STRINGi10090.ENSMUSP00000049412.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5F2E7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 6150His-richAdd
    BLAST
    Compositional biasi373 – 41442Ser-richAdd
    BLAST

    Phylogenomic databases

    eggNOGiopiNOG06224.
    GeneTreeiENSGT00440000038328.
    HOGENOMiHOG000220869.
    HOVERGENiHBG065794.
    OMAiKEMESVW.
    OrthoDBiEOG71RXJ4.
    PhylomeDBiQ5F2E7.
    TreeFamiTF332832.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5F2E7-1) [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

    MEEKPGQPQP QHHHSHHHPH HHPQQQQQQQ SHHHHHYYFY NHSHNHHHHH    50
    HHQQPHQYLQ HGAEGSPKAQ PKPLKHEQKH TLQQHQETPK KKTGYGEING 100
    NAGEREISLK SLSSDEATNP ISRVLNGNQQ VVETSLKQTV KTSTFGKAGI 150
    KTKNFIQKNS MDKKNGKSYE NKSGETQAVD KTDTIAIPNG VITSSSGYIT 200
    NGYMSKGADN DGSGSESGYT TPKKRKARRN SAKGCENLNL VQDKIMQETS 250
    VPALKQGLET LKPDYSEQKG MRVDGSKPIW KYETGPGGTS RGKPAMGDVL 300
    RKSSDIKPGL SSKKFDDRPK GKHASAAASK EDSWTLFKPP PVFPVDNSSA 350
    KIVPKISYAS KVKENLNKTV QNSSVSPSSS SSSSSTGETQ TQSSSRLSQV 400
    PMSALKSVTS ASFSNGPVLA GTDGSVYPSG GQPLLTTAAN TLTPISTGTD 450
    SVLQDMSLAS AAVEQIKSSL FIYPSNMQTV LLSAQVDLPS QTDQQNLGDI 500
    FQNQWGLSFI NEPSAGPETV IGKSSDHKVM EVTFQGEYPA TLVSQGAEII 550
    PSGTEHPVFP KAYELEKRTS PQVLGHILKP GTTESGALSL DPSHIGDLQK 600
    ADTSSQGALV FLSKDYEIEN QNPLASPTNT LLGSAKEQRY QRGLERNDSW 650
    GSFDLRAAIV YHTKEMESIW NLQKQDPKRI ITYNEAMDSP DQ 692
    Length:692
    Mass (Da):75,657
    Last modified:March 15, 2005 - v1
    Checksum:i3E295AC111814564
    GO
    Isoform 2 (identifier: Q5F2E7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         676-692: DPKRIITYNEAMDSPDQ → VFCLCVYMYTYVHHVMSLHGRERTLDPLELALHWS

    Note: No experimental confirmation available.

    Show »
    Length:710
    Mass (Da):77,885
    Checksum:i3123F4711F98E38B
    GO

    Sequence cautioni

    The sequence BAC65776.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521Missing in BAE42015. (PubMed:16141072)Curated
    Sequence conflicti57 – 571Q → R in BAE42015. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei676 – 69217DPKRI…DSPDQ → VFCLCVYMYTYVHHVMSLHG RERTLDPLELALHWS in isoform 2. 1 PublicationVSP_019729Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122494 mRNA. Translation: BAC65776.1. Different initiation.
    AK132603 mRNA. Translation: BAE21256.1.
    AK152336 mRNA. Translation: BAE31134.1.
    AK160601 mRNA. Translation: BAE35905.1.
    AK170764 mRNA. Translation: BAE42015.1.
    AL591136 Genomic DNA. Translation: CAI51880.1.
    CCDSiCCDS25083.1. [Q5F2E7-1]
    RefSeqiNP_001019376.1. NM_001024205.2. [Q5F2E7-1]
    XP_006534125.1. XM_006534062.1. [Q5F2E7-1]
    UniGeneiMm.428996.

    Genome annotation databases

    EnsembliENSMUST00000100802; ENSMUSP00000098365; ENSMUSG00000037857. [Q5F2E7-1]
    ENSMUST00000181023; ENSMUSP00000137922; ENSMUSG00000037857. [Q5F2E7-2]
    GeneIDi68564.
    KEGGimmu:68564.
    UCSCiuc007khd.2. mouse. [Q5F2E7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122494 mRNA. Translation: BAC65776.1 . Different initiation.
    AK132603 mRNA. Translation: BAE21256.1 .
    AK152336 mRNA. Translation: BAE31134.1 .
    AK160601 mRNA. Translation: BAE35905.1 .
    AK170764 mRNA. Translation: BAE42015.1 .
    AL591136 Genomic DNA. Translation: CAI51880.1 .
    CCDSi CCDS25083.1. [Q5F2E7-1 ]
    RefSeqi NP_001019376.1. NM_001024205.2. [Q5F2E7-1 ]
    XP_006534125.1. XM_006534062.1. [Q5F2E7-1 ]
    UniGenei Mm.428996.

    3D structure databases

    ProteinModelPortali Q5F2E7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212929. 1 interaction.
    STRINGi 10090.ENSMUSP00000049412.

    PTM databases

    PhosphoSitei Q5F2E7.

    Proteomic databases

    MaxQBi Q5F2E7.
    PaxDbi Q5F2E7.
    PRIDEi Q5F2E7.

    Protocols and materials databases

    DNASUi 68564.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100802 ; ENSMUSP00000098365 ; ENSMUSG00000037857 . [Q5F2E7-1 ]
    ENSMUST00000181023 ; ENSMUSP00000137922 ; ENSMUSG00000037857 . [Q5F2E7-2 ]
    GeneIDi 68564.
    KEGGi mmu:68564.
    UCSCi uc007khd.2. mouse. [Q5F2E7-1 ]

    Organism-specific databases

    CTDi 57532.
    MGIi MGI:1915814. Nufip2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi opiNOG06224.
    GeneTreei ENSGT00440000038328.
    HOGENOMi HOG000220869.
    HOVERGENi HBG065794.
    OMAi KEMESVW.
    OrthoDBi EOG71RXJ4.
    PhylomeDBi Q5F2E7.
    TreeFami TF332832.

    Miscellaneous databases

    NextBioi 327462.
    PROi Q5F2E7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5F2E7.
    Genevestigatori Q5F2E7.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Dendritic cell, Embryo and Head.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "82-FIP, a novel FMRP (fragile X mental retardation protein) interacting protein, shows a cell cycle-dependent intracellular localization."
      Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S., Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.
      Hum. Mol. Genet. 12:1689-1698(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    6. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-215 AND SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "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-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiNUFP2_MOUSE
    AccessioniPrimary (citable) accession number: Q5F2E7
    Secondary accession number(s): Q3TCE2, Q3V195, Q80TF1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 74 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3