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P26369

- U2AF2_MOUSE

UniProt

P26369 - U2AF2_MOUSE

Protein

Splicing factor U2AF 65 kDa subunit

Gene

U2af2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Necessary for the splicing of pre-mRNA. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10 By similarity.By similarity

    GO - Molecular functioni

    1. C2H2 zinc finger domain binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    3. RNA splicing Source: UniProtKB

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor U2AF 65 kDa subunit
    Alternative name(s):
    U2 auxiliary factor 65 kDa subunit
    U2 snRNP auxiliary factor large subunit
    Gene namesi
    Name:U2af2
    Synonyms:U2af65
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98886. U2af2.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. spliceosomal complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 475474Splicing factor U2AF 65 kDa subunitPRO_0000081989Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei15 – 1515-hydroxylysine; by JMJD6By similarity
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei276 – 27615-hydroxylysine; by JMJD6By similarity

    Post-translational modificationi

    Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.By similarity

    Keywords - PTMi

    Acetylation, Hydroxylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26369.
    PaxDbiP26369.
    PRIDEiP26369.

    PTM databases

    PhosphoSiteiP26369.

    Miscellaneous databases

    PMAP-CutDBP26369.

    Expressioni

    Gene expression databases

    ArrayExpressiP26369.
    BgeeiP26369.
    GenevestigatoriP26369.

    Interactioni

    Subunit structurei

    Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17 By similarity. Interacts with U2AF1L4.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi204400. 1 interaction.
    IntActiP26369. 3 interactions.
    MINTiMINT-4139054.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi376 – 3838
    Helixi386 – 3883
    Beta strandi389 – 3913
    Helixi392 – 40716
    Beta strandi412 – 4165
    Turni427 – 4304
    Beta strandi431 – 4388
    Helixi439 – 44911
    Beta strandi454 – 4574
    Beta strandi460 – 4645
    Helixi466 – 4705

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2M52NMR-A371-475[»]
    3V4MX-ray1.80A/B372-475[»]
    ProteinModelPortaliP26369.
    SMRiP26369. Positions 148-342, 371-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 23183RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini259 – 33779RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini385 – 46682RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi27 – 6236Arg/Ser-rich (RS domain)Add
    BLAST

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated
    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG298004.
    GeneTreeiENSGT00750000117711.
    HOGENOMiHOG000180745.
    HOVERGENiHBG062169.
    InParanoidiP26369.
    KOiK12837.
    OMAiYARRETR.
    OrthoDBiEOG7CNZFZ.
    PhylomeDBiP26369.
    TreeFamiTF314111.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR006529. U2AF_lg.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    TIGRFAMsiTIGR01642. U2AF_lg. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P26369-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD    50
    QRSASRDRRR RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE 100
    HITPMQYKAM QAAGQIPATA LLPTMTPDGL AVTPTPVPVV GSQMTRQARR 150
    LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ APGNPVLAVQ INQDKNFAFL 200
    EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV 250
    STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK 300
    GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSLPST 350
    INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE 400
    DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT 450
    GRKFANRVVV TKYCDPDSYH RRDFW 475
    Length:475
    Mass (Da):53,517
    Last modified:January 23, 2007 - v3
    Checksum:i2D81375CD8FC7251
    GO

    Sequence cautioni

    The sequence CAA45875.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64587 mRNA. Translation: CAA45874.1.
    X64587 mRNA. Translation: CAA45875.1. Different initiation.
    AK078496 mRNA. Translation: BAC37309.1.
    CCDSiCCDS57476.1.
    PIRiS22646.
    RefSeqiNP_001192160.1. NM_001205231.1.
    UniGeneiMm.360389.

    Genome annotation databases

    EnsembliENSMUST00000005041; ENSMUSP00000005041; ENSMUSG00000030435.
    GeneIDi22185.
    KEGGimmu:22185.
    UCSCiuc009ezu.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64587 mRNA. Translation: CAA45874.1 .
    X64587 mRNA. Translation: CAA45875.1 . Different initiation.
    AK078496 mRNA. Translation: BAC37309.1 .
    CCDSi CCDS57476.1.
    PIRi S22646.
    RefSeqi NP_001192160.1. NM_001205231.1.
    UniGenei Mm.360389.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2M52 NMR - A 371-475 [» ]
    3V4M X-ray 1.80 A/B 372-475 [» ]
    ProteinModelPortali P26369.
    SMRi P26369. Positions 148-342, 371-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204400. 1 interaction.
    IntActi P26369. 3 interactions.
    MINTi MINT-4139054.

    PTM databases

    PhosphoSitei P26369.

    Proteomic databases

    MaxQBi P26369.
    PaxDbi P26369.
    PRIDEi P26369.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005041 ; ENSMUSP00000005041 ; ENSMUSG00000030435 .
    GeneIDi 22185.
    KEGGi mmu:22185.
    UCSCi uc009ezu.3. mouse.

    Organism-specific databases

    CTDi 11338.
    MGIi MGI:98886. U2af2.

    Phylogenomic databases

    eggNOGi NOG298004.
    GeneTreei ENSGT00750000117711.
    HOGENOMi HOG000180745.
    HOVERGENi HBG062169.
    InParanoidi P26369.
    KOi K12837.
    OMAi YARRETR.
    OrthoDBi EOG7CNZFZ.
    PhylomeDBi P26369.
    TreeFami TF314111.

    Miscellaneous databases

    NextBioi 302149.
    PMAP-CutDB P26369.
    PROi P26369.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26369.
    Bgeei P26369.
    Genevestigatori P26369.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR006529. U2AF_lg.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    TIGRFAMsi TIGR01642. U2AF_lg. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of the murine homologue of the human splicing factor U2AF65."
      Sailer A., Macdonald N.J., Weissmann C.
      Nucleic Acids Res. 20:2374-2374(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SL/AM.
    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.
    3. "Auxiliary splice factor U2AF26 and transcription factor Gfi1 cooperate directly in regulating CD45 alternative splicing."
      Heyd F., ten Dam G., Moeroey T.
      Nat. Immunol. 7:859-867(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH U2AF1L4.
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiU2AF2_MOUSE
    AccessioniPrimary (citable) accession number: P26369
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3