Details for: RBM15

Gene ID: 64783

Symbol: RBM15

Ensembl ID: ENSG00000162775

Description: RNA binding motif protein 15

Associated with

Other Information

Genular Protein ID: 735681789

Symbol: RBM15_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11431691

Title: Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of acute megakaryoblastic leukemia.

PubMed ID: 11431691

DOI: 10.1038/90054

PubMed ID: 11344311

Title: Involvement of a human gene related to the Drosophila spen gene in the recurrent t(1;22) translocation of acute megakaryocytic leukemia.

PubMed ID: 11344311

DOI: 10.1073/pnas.101001498

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

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: 16129689

Title: Interaction of the Epstein-Barr virus mRNA export factor EB2 with human Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links Spen proteins with splicing regulation and mRNA export.

PubMed ID: 16129689

DOI: 10.1074/jbc.m501725200

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17001072

Title: RNA-binding motif protein 15 binds to the RNA transport element RTE and provides a direct link to the NXF1 export pathway.

PubMed ID: 17001072

DOI: 10.1074/jbc.m608745200

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

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: 19786495

Title: Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA.

PubMed ID: 19786495

DOI: 10.1093/nar/gkp782

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 19586903

Title: The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1.

PubMed ID: 19586903

DOI: 10.1074/jbc.m109.040113

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22927943

Title: Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via a SPOC domain that is required for cytokine-independent proliferation.

PubMed ID: 22927943

DOI: 10.1371/journal.pone.0042965

PubMed ID: 24100041

Title: Identification of Wilms' tumor 1-associating protein complex and its role in alternative splicing and the cell cycle.

PubMed ID: 24100041

DOI: 10.1074/jbc.m113.500397

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

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26575292

Title: Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing.

PubMed ID: 26575292

DOI: 10.7554/elife.07938

PubMed ID: 27602518

Title: m(6)A RNA methylation promotes XIST-mediated transcriptional repression.

PubMed ID: 27602518

DOI: 10.1038/nature19342

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

Sequence Information:

  • Length: 977
  • Mass: 107189
  • Checksum: FB26AFE246E40282
  • Sequence:
  • MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER SPVKAKRSRG 
    GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL DKSSSRGGSR EYDTGGGSSS 
    SRLHSYSSPS TKNSSGGGES RSSSRGGGGE SRSSGAASSA PGGGDGAEYK TLKISELGSQ 
    LSDEAVEDGL FHEFKRFGDV SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL 
    YDRPLKIEAV YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL 
    GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG AGAGAAPFRE 
    VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI TEVDIKRPSR GQTSTYGFLK 
    FENLDMSHRA KLAMSGKIII RNPIKIGYGK ATPTTRLWVG GLGPWVPLAA LAREFDRFGT 
    IRTIDYRKGD SWAYIQYESL DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP 
    LPLTHYELVT DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT 
    AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG RHLDRSPESD 
    RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS PIRDRRGSLE KSQGDKRDRK 
    NSASAERDRK HRTTAPTEGK SPLKKEDRSD GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA 
    SPKLCLAWQG MLLLKNSNFP SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP 
    KLDEVTRRIK VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA 
    AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM IIVRGFGFQI 
    GVRYENKKRE NLALTLL

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.