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P26368

- U2AF2_HUMAN

UniProt

P26368 - U2AF2_HUMAN

Protein

Splicing factor U2AF 65 kDa subunit

Gene

U2AF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 4 (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 10.3 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. nucleotide binding Source: InterPro
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA export from nucleus Source: Reactome
    4. mRNA processing Source: ProtInc
    5. mRNA splicing, via spliceosome Source: HGNC
    6. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    7. RNA splicing Source: Reactome
    8. termination of RNA polymerase II transcription Source: Reactome
    9. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor U2AF 65 kDa subunit
    Alternative name(s):
    U2 auxiliary factor 65 kDa subunit
    Short name:
    hU2AF(65)
    Short name:
    hU2AF65
    U2 snRNP auxiliary factor large subunit
    Gene namesi
    Name:U2AF2
    Synonyms:U2AF65
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:23156. U2AF2.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear speck Source: MGI
    2. nucleoplasm Source: Reactome
    3. nucleus Source: HPA
    4. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921W → A: Decreases affinity for UAF1 by 3 orders of magnitude. 1 Publication
    Mutagenesisi96 – 961P → G: Decreases affinity for UAF1 by 2 orders of magnitude. 1 Publication
    Mutagenesisi104 – 1041P → G: Decreases affinity for UAF1 by 2 orders of magnitude. 1 Publication
    Mutagenesisi387 – 3882EE → RR: Reduces interaction with SF1.
    Mutagenesisi391 – 3944DDEE → AAAA: Reduces interaction with SF1.
    Mutagenesisi391 – 3944DDEE → RRKK: Reduces interaction with SF1.
    Mutagenesisi396 – 3972EE → AA: No effect.
    Mutagenesisi396 – 3972EE → GA: Reduces interaction with SF1.
    Mutagenesisi396 – 3972EE → KK: Reduces interaction with SF1.
    Mutagenesisi454 – 4541F → A: Reduces interaction with SF1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134908683.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 475474Splicing factor U2AF 65 kDa subunitPRO_0000081988Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine5 Publications
    Modified residuei2 – 21Phosphoserine3 Publications
    Modified residuei15 – 1515-hydroxylysine; by JMJD61 Publication
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei276 – 27615-hydroxylysine; by JMJD61 Publication

    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.1 Publication

    Keywords - PTMi

    Acetylation, Hydroxylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26368.
    PaxDbiP26368.
    PRIDEiP26368.

    PTM databases

    PhosphoSiteiP26368.

    Miscellaneous databases

    PMAP-CutDBP26368.

    Expressioni

    Gene expression databases

    ArrayExpressiP26368.
    BgeeiP26368.
    CleanExiHS_U2AF2.
    GenevestigatoriP26368.

    Organism-specific databases

    HPAiCAB010910.
    HPA041943.
    HPA043562.

    Interactioni

    Subunit structurei

    Interacts with U2AF1L4 By similarity. Heterodimer with U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1. Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542534EBI-742339,EBI-930964
    CHERPQ8IWX82EBI-742339,EBI-2555370
    CPSF7Q8N6842EBI-742339,EBI-746909
    MUC1P159412EBI-742339,EBI-2804728
    PRPF3O433952EBI-742339,EBI-744322
    RBM10P981752EBI-742339,EBI-721525
    RBM5P527562EBI-742339,EBI-714003
    SNRPAP090122EBI-742339,EBI-607085
    SNW1Q135735EBI-742339,EBI-632715
    SRPK2P783624EBI-742339,EBI-593303
    SUGP1Q8IWZ83EBI-742339,EBI-2691671
    U2AF1Q010818EBI-742339,EBI-632461

    Protein-protein interaction databases

    BioGridi116466. 129 interactions.
    DIPiDIP-2154N.
    IntActiP26368. 49 interactions.
    MINTiMINT-1192370.
    STRINGi9606.ENSP00000307863.

    Structurei

    Secondary structure

    1
    475
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi104 – 1096
    Beta strandi150 – 1556
    Helixi162 – 17514
    Beta strandi180 – 1834
    Beta strandi185 – 1917
    Beta strandi193 – 20412
    Helixi205 – 2117
    Helixi212 – 2143
    Beta strandi219 – 2224
    Beta strandi225 – 2273
    Beta strandi238 – 2403
    Beta strandi244 – 2463
    Beta strandi261 – 2644
    Helixi272 – 2809
    Beta strandi281 – 2833
    Beta strandi285 – 2928
    Turni294 – 2963
    Beta strandi299 – 30911
    Helixi312 – 3209
    Beta strandi326 – 3283
    Beta strandi331 – 3344
    Beta strandi376 – 3838
    Helixi386 – 3894
    Helixi392 – 40615
    Turni407 – 4093
    Beta strandi414 – 4163
    Turni422 – 4243
    Turni427 – 4304
    Beta strandi431 – 4355
    Helixi439 – 44911
    Beta strandi454 – 4574
    Beta strandi460 – 4634
    Helixi466 – 4705

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JMTX-ray2.20B85-112[»]
    1O0PNMR-A372-475[»]
    1OPINMR-A372-475[»]
    1U2FNMR-A148-237[»]
    2G4BX-ray2.50A148-336[»]
    2HZCX-ray1.47A148-229[»]
    2M0GNMR-B372-475[»]
    2U2FNMR-A258-342[»]
    2YH0NMR-A148-342[»]
    2YH1NMR-A148-342[»]
    3VAFX-ray2.49A/B148-336[»]
    3VAGX-ray2.19A/B148-336[»]
    3VAHX-ray2.50A/B148-336[»]
    3VAIX-ray2.20A/B148-336[»]
    3VAJX-ray1.90A/B148-336[»]
    3VAKX-ray2.17A/B148-336[»]
    3VALX-ray2.50A/B/D/I148-336[»]
    3VAMX-ray2.40A/B148-336[»]
    4FXWX-ray2.29A/C375-475[»]
    ProteinModelPortaliP26368.
    SMRiP26368. Positions 148-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26368.

    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.
    HOGENOMiHOG000180745.
    HOVERGENiHBG062169.
    InParanoidiP26368.
    KOiK12837.
    OMAiYARRETR.
    OrthoDBiEOG7CNZFZ.
    PhylomeDBiP26368.
    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]

    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: P26368-1) [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

    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 NATLVSPPST 350
    INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE 400
    DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT 450
    GRKFANRVVV TKYCDPDSYH RRDFW 475
    Length:475
    Mass (Da):53,501
    Last modified:January 23, 2007 - v4
    Checksum:i26AD271CD8FC6211
    GO
    Isoform 2 (identifier: P26368-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         345-348: Missing.

    Show »
    Length:471
    Mass (Da):53,121
    Checksum:i3F59A02CD2B03F46
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei345 – 3484Missing in isoform 2. 1 PublicationVSP_035414

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64044 mRNA. Translation: CAA45409.1.
    CH471135 Genomic DNA. Translation: EAW72404.1.
    BC008740 mRNA. Translation: AAH08740.1.
    BC030574 mRNA. Translation: AAH30574.1.
    CCDSiCCDS12933.1. [P26368-1]
    CCDS46197.1. [P26368-2]
    PIRiS20250.
    RefSeqiNP_001012496.1. NM_001012478.1. [P26368-2]
    NP_009210.1. NM_007279.2. [P26368-1]
    UniGeneiHs.528007.

    Genome annotation databases

    EnsembliENST00000308924; ENSP00000307863; ENSG00000063244. [P26368-1]
    ENST00000450554; ENSP00000388475; ENSG00000063244. [P26368-2]
    GeneIDi11338.
    KEGGihsa:11338.
    UCSCiuc002qlt.3. human. [P26368-2]
    uc002qlu.3. human. [P26368-1]

    Polymorphism databases

    DMDMi267188.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64044 mRNA. Translation: CAA45409.1 .
    CH471135 Genomic DNA. Translation: EAW72404.1 .
    BC008740 mRNA. Translation: AAH08740.1 .
    BC030574 mRNA. Translation: AAH30574.1 .
    CCDSi CCDS12933.1. [P26368-1 ]
    CCDS46197.1. [P26368-2 ]
    PIRi S20250.
    RefSeqi NP_001012496.1. NM_001012478.1. [P26368-2 ]
    NP_009210.1. NM_007279.2. [P26368-1 ]
    UniGenei Hs.528007.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JMT X-ray 2.20 B 85-112 [» ]
    1O0P NMR - A 372-475 [» ]
    1OPI NMR - A 372-475 [» ]
    1U2F NMR - A 148-237 [» ]
    2G4B X-ray 2.50 A 148-336 [» ]
    2HZC X-ray 1.47 A 148-229 [» ]
    2M0G NMR - B 372-475 [» ]
    2U2F NMR - A 258-342 [» ]
    2YH0 NMR - A 148-342 [» ]
    2YH1 NMR - A 148-342 [» ]
    3VAF X-ray 2.49 A/B 148-336 [» ]
    3VAG X-ray 2.19 A/B 148-336 [» ]
    3VAH X-ray 2.50 A/B 148-336 [» ]
    3VAI X-ray 2.20 A/B 148-336 [» ]
    3VAJ X-ray 1.90 A/B 148-336 [» ]
    3VAK X-ray 2.17 A/B 148-336 [» ]
    3VAL X-ray 2.50 A/B/D/I 148-336 [» ]
    3VAM X-ray 2.40 A/B 148-336 [» ]
    4FXW X-ray 2.29 A/C 375-475 [» ]
    ProteinModelPortali P26368.
    SMRi P26368. Positions 148-475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116466. 129 interactions.
    DIPi DIP-2154N.
    IntActi P26368. 49 interactions.
    MINTi MINT-1192370.
    STRINGi 9606.ENSP00000307863.

    PTM databases

    PhosphoSitei P26368.

    Polymorphism databases

    DMDMi 267188.

    Proteomic databases

    MaxQBi P26368.
    PaxDbi P26368.
    PRIDEi P26368.

    Protocols and materials databases

    DNASUi 11338.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000308924 ; ENSP00000307863 ; ENSG00000063244 . [P26368-1 ]
    ENST00000450554 ; ENSP00000388475 ; ENSG00000063244 . [P26368-2 ]
    GeneIDi 11338.
    KEGGi hsa:11338.
    UCSCi uc002qlt.3. human. [P26368-2 ]
    uc002qlu.3. human. [P26368-1 ]

    Organism-specific databases

    CTDi 11338.
    GeneCardsi GC19P056165.
    HGNCi HGNC:23156. U2AF2.
    HPAi CAB010910.
    HPA041943.
    HPA043562.
    MIMi 191318. gene.
    neXtProti NX_P26368.
    PharmGKBi PA134908683.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298004.
    HOGENOMi HOG000180745.
    HOVERGENi HBG062169.
    InParanoidi P26368.
    KOi K12837.
    OMAi YARRETR.
    OrthoDBi EOG7CNZFZ.
    PhylomeDBi P26368.
    TreeFami TF314111.

    Enzyme and pathway databases

    Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi U2AF2. human.
    EvolutionaryTracei P26368.
    GeneWikii U2AF2.
    GenomeRNAii 11338.
    NextBioi 43079.
    PMAP-CutDB P26368.
    PROi P26368.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26368.
    Bgeei P26368.
    CleanExi HS_U2AF2.
    Genevestigatori P26368.

    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 domain structure of the mammalian splicing factor U2AF."
      Zamore P.D., Patton J.G., Green M.R.
      Nature 355:609-614(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Tissue: Lymph and Skin.
    4. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
      Submitted (NOV-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 196-203; 277-286 AND 463-471, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    5. "Large-scale proteomic analysis of the human spliceosome."
      Rappsilber J., Ryder U., Lamond A.I., Mann M.
      Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 261-286, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
    6. "A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
      Tronchere H., Wang J., Fu X.D.
      Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZRSR2.
    7. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
      Zhang W.-J., Wu J.Y.
      Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAF11.
    8. "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly."
      Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J.
      EMBO J. 18:4549-4559(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SF1.
    9. "Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
      Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
      J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."
      Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., Sattler M.
      Nat. Struct. Mol. Biol. 14:620-629(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM17.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing."
      Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.
      Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: FUNCTION, HYDROXYLATION AT LYS-15 AND LYS-276.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing."
      Chen Y., Zhang L., Jones K.A.
      Genes Dev. 25:701-716(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNW1.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65))."
      Ito T., Muto Y., Green M.R., Yokoyama S.
      EMBO J. 18:4523-4534(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 148-237.
    25. "Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP."
      Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M.
      Mol. Cell 11:965-976(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 372-475 IN COMPLEX WITH SF1, MUTAGENESIS OF 387-GLU-GLU-388; 391-ASP--GLU-393; 396-GLU-GLU-397 AND PHE-454.
    26. "A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer."
      Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.
      Cell 106:595-605(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 90-112 IN COMPLEX WITH U2AF1, MUTAGENESIS OF TRP-92; PRO-96 AND PRO-104.

    Entry informationi

    Entry nameiU2AF2_HUMAN
    AccessioniPrimary (citable) accession number: P26368
    Secondary accession number(s): Q96HC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 168 of the entry and version 4 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 19
      Human chromosome 19: 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