Details for: KHDRBS1

Gene ID: 10657

Symbol: KHDRBS1

Ensembl ID: ENSG00000121774

Description: KH RNA binding domain containing, signal transduction associated 1

Associated with

Other Information

Genular Protein ID: 568621641

Symbol: KHDR1_HUMAN

Name: KH domain-containing, RNA-binding, signal transduction-associated protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 1374686

Title: Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62.

PubMed ID: 1374686

DOI: 10.1016/0092-8674(92)90455-l

PubMed ID: 9013542

Title: A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain.

PubMed ID: 9013542

DOI: 10.1074/jbc.272.6.3129

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: 9045636

Title: Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling.

PubMed ID: 9045636

DOI: 10.1074/jbc.272.10.6214

PubMed ID: 10332027

Title: T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis.

PubMed ID: 10332027

DOI: 10.1093/hmg/8.6.959

PubMed ID: 10913193

Title: Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding ability.

PubMed ID: 10913193

DOI: 10.1128/mcb.20.16.6114-6126.2000

PubMed ID: 11585385

Title: Human leptin signaling in human peripheral blood mononuclear cells: activation of the JAK-STAT pathway.

PubMed ID: 11585385

DOI: 10.1006/cimm.2001.1815

PubMed ID: 12529443

Title: Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1.

PubMed ID: 12529443

DOI: 10.1091/mbc.e02-08-0484

PubMed ID: 15782174

Title: Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.

PubMed ID: 15782174

DOI: 10.1038/nmeth715

PubMed ID: 15021911

Title: The RNA binding protein Sam68 is acetylated in tumor cell lines, and its acetylation correlates with enhanced RNA binding activity.

PubMed ID: 15021911

DOI: 10.1038/sj.onc.1207484

PubMed ID: 16179349

Title: Tyrosine phosphorylation of sam68 by breast tumor kinase regulates intranuclear localization and cell cycle progression.

PubMed ID: 16179349

DOI: 10.1074/jbc.m505802200

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: 17890166

Title: The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.

PubMed ID: 17890166

DOI: 10.1016/j.bbapap.2007.07.015

PubMed ID: 17371836

Title: The RNA-binding protein Sam68 modulates the alternative splicing of Bcl-x.

PubMed ID: 17371836

DOI: 10.1083/jcb.200701005

PubMed ID: 17924679

Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

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: 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: 20186123

Title: The splicing regulator Sam68 binds to a novel exonic splicing silencer and functions in SMN2 alternative splicing in spinal muscular atrophy.

PubMed ID: 20186123

DOI: 10.1038/emboj.2010.19

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: 21613532

Title: The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway.

PubMed ID: 21613532

DOI: 10.1261/rna.2616111

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: 22253824

Title: Localization of nucleoporin Tpr to the nuclear pore complex is essential for Tpr mediated regulation of the export of unspliced RNA.

PubMed ID: 22253824

DOI: 10.1371/journal.pone.0029921

PubMed ID: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24514149

Title: The transcription factor FBI-1 inhibits SAM68-mediated BCL-X alternative splicing and apoptosis.

PubMed ID: 24514149

DOI: 10.1002/embr.201338241

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: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

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

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 26758068

Title: Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.

PubMed ID: 26758068

DOI: 10.1038/ncomms10355

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: 29496907

Title: Phosphoproteomics analysis identifies novel candidate substrates of the non-receptor tyrosine kinase, SRMS.

PubMed ID: 29496907

DOI: 10.1074/mcp.ra118.000643

PubMed ID: 20610388

Title: Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain.

PubMed ID: 20610388

DOI: 10.1074/jbc.m110.126185

PubMed ID: 22000517

Title: Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68.

PubMed ID: 22000517

DOI: 10.1016/j.str.2011.07.013

Sequence Information:

  • Length: 443
  • Mass: 48227
  • Checksum: 59FB4DB6FB4DBE98
  • Sequence:
  • MQRRDDPAAR MSRSSGRSGS MDPSGAHPSV RQTPSRQPPL PHRSRGGGGG SRGGARASPA 
    TQPPPLLPPS ATGPDATVGG PAPTPLLPPS ATASVKMEPE NKYLPELMAE KDSLDPSFTH 
    AMQLLTAEIE KIQKGDSKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ 
    GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA 
    YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVPVRG RGAAPPPPPV 
    PRGRGVGPPR GALVRGTPVR GAITRGATVT RGVPPPPTVR GAPAPRARTA GIQRIPLPPP 
    PAPETYEEYG YDDTYAEQSY EGYEGYYSQS QGDSEYYDYG HGEVQDSYEA YGQDDWNGTR 
    PSLKAPPARP VKGAYREHPY GRY

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.