Details for: RBM22

Gene ID: 55696

Symbol: RBM22

Ensembl ID: ENSG00000086589

Description: RNA binding motif protein 22

Associated with

Other Information

Genular Protein ID: 3167170830

Symbol: RBM22_HUMAN

Name: Pre-mRNA-splicing factor RBM22

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11230166

Title: Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.

PubMed ID: 11230166

DOI: 10.1101/gr.gr1547r

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

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: 8681136

Title: Transcriptional map of the Treacher Collins candidate gene region.

PubMed ID: 8681136

DOI: 10.1101/gr.6.1.26

PubMed ID: 11991638

Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.

PubMed ID: 11991638

DOI: 10.1017/s1355838202021088

PubMed ID: 17045351

Title: Nuclear translocation of the calcium-binding protein ALG-2 induced by the RNA-binding protein RBM22.

PubMed ID: 17045351

DOI: 10.1016/j.bbamcr.2006.09.003

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: 19133299

Title: The influence of calcium signaling on the regulation of alternative splicing.

PubMed ID: 19133299

DOI: 10.1016/j.bbamcr.2008.12.006

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: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21122810

Title: Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7.

PubMed ID: 21122810

DOI: 10.1016/j.bbamcr.2010.11.010

PubMed ID: 22246180

Title: Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre.

PubMed ID: 22246180

DOI: 10.1038/emboj.2011.502

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

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: 33220177

Title: Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative Pontocerebellar Hypoplasia with Microcephaly.

PubMed ID: 33220177

DOI: 10.1016/j.neuron.2020.10.035

PubMed ID: 28502770

Title: An Atomic Structure of the Human Spliceosome.

PubMed ID: 28502770

DOI: 10.1016/j.cell.2017.04.033

PubMed ID: 28076346

Title: Cryo-EM structure of a human spliceosome activated for step 2 of splicing.

PubMed ID: 28076346

DOI: 10.1038/nature21079

PubMed ID: 29361316

Title: Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex.

PubMed ID: 29361316

DOI: 10.1016/j.cell.2018.01.010

PubMed ID: 29360106

Title: Structure of the human activated spliceosome in three conformational states.

PubMed ID: 29360106

DOI: 10.1038/cr.2018.14

PubMed ID: 29301961

Title: Structure of a human catalytic step I spliceosome.

PubMed ID: 29301961

DOI: 10.1126/science.aar6401

PubMed ID: 30705154

Title: A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.

PubMed ID: 30705154

DOI: 10.1126/science.aaw5569

Sequence Information:

  • Length: 420
  • Mass: 46896
  • Checksum: A82549D8CC88C7D0
  • Sequence:
  • MATSLGSNTY NRQNWEDADF PILCQTCLGE NPYIRMTKEK YGKECKICAR PFTVFRWCPG 
    VRMRFKKTEV CQTCSKLKNV CQTCLLDLEY GLPIQVRDAG LSFKDDMPKS DVNKEYYTQN 
    MEREISNSDG TRPVGMLGKA TSTSDMLLKL ARTTPYYKRN RPHICSFWVK GECKRGEECP 
    YRHEKPTDPD DPLADQNIKD RYYGINDPVA DKLLKRASTM PRLDPPEDKT ITTLYVGGLG 
    DTITETDLRN HFYQFGEIRT ITVVQRQQCA FIQFATRQAA EVAAEKSFNK LIVNGRRLNV 
    KWGRSQAARG KEKEKDGTTD SGIKLEPVPG LPGALPPPPA AEEEASANYF NLPPSGPPAV 
    VNIALPPPPG IAPPPPPGFG PHMFHPMGPP PPFMRAPGPI HYPSQDPQRM GAHAGKHSSP

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.