Details for: HNRNPDL

Gene ID: 9987

Symbol: HNRNPDL

Ensembl ID: ENSG00000152795

Description: heterogeneous nuclear ribonucleoprotein D like

Associated with

Other Information

Genular Protein ID: 3322387566

Symbol: HNRDL_HUMAN

Name: Heterogeneous nuclear ribonucleoprotein D-like

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9538234

Title: Cloning and characterization of a cDNA encoding a novel heterogeneous nuclear ribonucleoprotein-like protein and its expression in myeloid leukemia cells.

PubMed ID: 9538234

DOI: 10.1093/oxfordjournals.jbchem.a021964

PubMed ID: 10072754

Title: Two forms of expression and genomic structure of the human heterogeneous nuclear ribonucleoprotein D-like JKTBP gene (HNRPDL).

PubMed ID: 10072754

DOI: 10.1016/s0378-1119(99)00020-7

PubMed ID: 11705999

Title: Identification of the nucleocytoplasmic shuttling sequence of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its interaction with mRNA.

PubMed ID: 11705999

DOI: 10.1074/jbc.m108477200

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

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: 15190078

Title: Regulation of murine cytochrome c oxidase Vb gene expression during myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like protein (JKTBP1) reciprocally regulate transcription activity by physical interaction with the BERF-1/ZBP-89 factor.

PubMed ID: 15190078

DOI: 10.1074/jbc.m403160200

PubMed ID: 9524220

Title: Molecular cloning of the cDNA encoding A + U-rich element RNA binding factor.

PubMed ID: 9524220

DOI: 10.1016/s0167-4781(97)00223-6

PubMed ID: 12406575

Title: Interactions of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its domains with high-affinity binding sites.

PubMed ID: 12406575

DOI: 10.1016/s0378-1119(02)00926-5

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: 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: 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: 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: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24647604

Title: A defect in the RNA-processing protein HNRPDL causes limb-girdle muscular dystrophy 1G (LGMD1G).

PubMed ID: 24647604

DOI: 10.1093/hmg/ddu127

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: 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: 420
  • Mass: 46438
  • Checksum: 00F631863859D0CA
  • Sequence:
  • MEVPPRLSHV PPPLFPSAPA TLASRSLSHW RPRPPRQLAP LLPSLAPSSA RQGARRAQRH 
    VTAQQPSRLA GGAAIKGGRR RRPDLFRRHF KSSSIQRSAA AAAATRTARQ HPPADSSVTM 
    EDMNEYSNIE EFAEGSKINA SKNQQDDGKM FIGGLSWDTS KKDLTEYLSR FGEVVDCTIK 
    TDPVTGRSRG FGFVLFKDAA SVDKVLELKE HKLDGKLIDP KRAKALKGKE PPKKVFVGGL 
    SPDTSEEQIK EYFGAFGEIE NIELPMDTKT NERRGFCFIT YTDEEPVKKL LESRYHQIGS 
    GKCEIKVAQP KEVYRQQQQQ QKGGRGAAAG GRGGTRGRGR GQGQNWNQGF NNYYDQGYGN 
    YNSAYGGDQN YSGYGGYDYT GYNYGNYGYG QGYADYSGQQ STYGKASRGG GNHQNNYQPY

Genular Protein ID: 1366536481

Symbol: A0A087WUK2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

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: 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: 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: 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: 23186163

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

PubMed ID: 23186163

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

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 363
  • Mass: 40040
  • Checksum: F59C1E61EAB22BC2
  • Sequence:
  • MEVPPRLSHV PPPLFPSAPA TLASRSLSHW RPRPPRQLAP LLPSLAPSSA RQGARRAQRH 
    VTAQQPSRLA GGAAIKGGRR RRPDLFRRHF KSSSIQRSAA AAAATRTARQ HPPADSSVTM 
    EDMNEYSNIE EFAEGSKINA SKNQQDDGKM FIGGLSWDTS KKDLTEYLSR FGEVVDCTIK 
    TDPVTGRSRG FGFVLFKDAA SVDKVLELKE HKLDGKLIDP KRAKALKGKE PPKKVFVGGL 
    SPDTSEEQIK EYFGAFGEIE NIELPMDTKT NERRGFCFIT YTDEEPVKKL LESRYHQIGS 
    GKCEIKVAQP KEVYRQQQQQ QKGGRGAAAG GRGGTRGRGR GQQSTYGKAS RGGGNHQNNY 
    QPY

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.