Details for: U2AF2
Associated with
Other Information
Genular Protein ID: 2084893903
Symbol: U2AF2_HUMAN
Name: Splicing factor U2AF 65 kDa subunit
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 1538748
Title: Cloning and domain structure of the mammalian splicing factor U2AF.
PubMed ID: 1538748
DOI: 10.1038/355609a0
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 12176931
Title: Large-scale proteomic analysis of the human spliceosome.
PubMed ID: 12176931
DOI: 10.1101/gr.473902
PubMed ID: 9237760
Title: A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA.
PubMed ID: 9237760
DOI: 10.1038/41137
PubMed ID: 9447963
Title: Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing.
PubMed ID: 9447963
DOI: 10.1128/mcb.18.2.676
PubMed ID: 10449420
Title: Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly.
PubMed ID: 10449420
PubMed ID: 14654843
Title: Proteomic characterization of the human centrosome by protein correlation profiling.
PubMed ID: 14654843
DOI: 10.1038/nature02166
PubMed ID: 15009664
Title: Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors.
PubMed ID: 15009664
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 17024186
Title: An interaction between U2AF 65 and CF I(m) links the splicing and 3' end processing machineries.
PubMed ID: 17024186
PubMed ID: 17589525
Title: U2AF-homology motif interactions are required for alternative splicing regulation by SPF45.
PubMed ID: 17589525
DOI: 10.1038/nsmb1260
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19641227
Title: Blom7alpha is a novel heterogeneous nuclear ribonucleoprotein K homology domain protein involved in pre-mRNA splicing that interacts with SNEVPrp19-Pso4.
PubMed ID: 19641227
PubMed ID: 19470458
Title: The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing.
PubMed ID: 19470458
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 19574390
Title: Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing.
PubMed ID: 19574390
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21460037
Title: SKIP counteracts p53-mediated apoptosis via selective regulation of p21Cip1 mRNA splicing.
PubMed ID: 21460037
DOI: 10.1101/gad.2002611
PubMed ID: 21536736
Title: The RNA polymerase II C-terminal domain promotes splicing activation through recruitment of a U2AF65-Prp19 complex.
PubMed ID: 21536736
DOI: 10.1101/gad.2038011
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22223895
Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
PubMed ID: 22223895
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 27720643
Title: Molecular architecture of SF3b and structural consequences of its cancer-related mutations.
PubMed ID: 27720643
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 10449418
Title: Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65)).
PubMed ID: 10449418
PubMed ID: 12718882
Title: Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP.
PubMed ID: 12718882
PubMed ID: 11551507
Title: A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.
PubMed ID: 11551507
Sequence Information:
- Length: 475
- Mass: 53501
- Checksum: 26AD271CD8FC6211
- Sequence:
MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSPPST INQTPVTLQV PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.