Details for: SERBP1

Gene ID: 26135

Symbol: SERBP1

Ensembl ID: ENSG00000142864

Description: SERPINE1 mRNA binding protein 1

Associated with

Other Information

Genular Protein ID: 946910371

Symbol: SERB1_HUMAN

Name: SERPINE1 mRNA-binding protein 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10810093

Title: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics.

PubMed ID: 10810093

DOI: 10.1101/gr.10.5.703

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: 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: 12505151

Title: Characterization of a new family of proteins that interact with the C-terminal region of the chromatin-remodeling factor CHD-3.

PubMed ID: 12505151

DOI: 10.1016/s0014-5793(02)03737-7

PubMed ID: 11001948

Title: Identification and cDNA cloning of a novel RNA-binding protein that interacts with the cyclic nucleotide-responsive sequence in the type-1 plasminogen activator inhibitor mRNA.

PubMed ID: 11001948

DOI: 10.1074/jbc.m006538200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

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: 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: 18632687

Title: TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules.

PubMed ID: 18632687

DOI: 10.1093/hmg/ddn203

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: 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: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

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: 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: 28882895

Title: Peptide array based screening reveals a large number of proteins interacting with the ankyrin repeat domain of the zDHHC17 S-acyltransferase.

PubMed ID: 28882895

DOI: 10.1074/jbc.m117.799650

PubMed ID: 28695742

Title: Human Regulatory Protein Ki-1/57 Is a Target of SUMOylation and Affects PML Nuclear Body Formation.

PubMed ID: 28695742

DOI: 10.1021/acs.jproteome.7b00001

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: 36691768

Title: TORC1 phosphorylates and inhibits the ribosome preservation factor Stm1 to activate dormant ribosomes.

PubMed ID: 36691768

DOI: 10.15252/embj.2022112344

PubMed ID: 23636399

Title: Structures of the human and Drosophila 80S ribosome.

PubMed ID: 23636399

DOI: 10.1038/nature12104

PubMed ID: 32687489

Title: Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.

PubMed ID: 32687489

DOI: 10.1371/journal.pbio.3000780

Sequence Information:

  • Length: 408
  • Mass: 44965
  • Checksum: 2289992374FA6A96
  • Sequence:
  • MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ 
    TNSNAAGKQL RKESQKDRKN PLPPSVGVVD KKEETQPPVA LKKEGIRRVG RRPDQQLQGE 
    GKIIDRRPER RPPRERRFEK PLEEKGEGGE FSVDRPIIDR PIRGRGGLGR GRGGRGRGMG 
    RGDGFDSRGK REFDRHSGSD RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK 
    QISYNYSDLD QSNVTEETPE GEEHHPVADT ENKENEVEEV KEEGPKEMTL DEWKAIQNKD 
    RAKVEFNIRK PNEGADGQWK KGFVLHKSKS EEAHAEDSVM DHHFRKPAND ITSQLEINFG 
    DLGRPGRGGR GGRGGRGRGG RPNRGSRTDK SSASAPDVDD PEAFPALA

Genular Protein ID: 29091373

Symbol: Q63HR1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 387
  • Mass: 42441
  • Checksum: 01D41E04F651C92E
  • Sequence:
  • MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ 
    TNSNAAGKQL RKESQKDRKN PLPPSVGVVD KKEETQPPVA LKKEGIRRIG RRPDQQLQGE 
    GKIIDRRPER RPPRERRFEK PLEEKGEGGE FSVDRPIIDR PIRGRGGLGR GRGGRGRGMG 
    RGDGFDSRGK REFDRHSGSD RSGLKHEDKR GGSGSHNWGT VKDELTDLDQ SNVTEETPEG 
    EEHHPVADTE NKENEVEEVK EEGPKEMTLD EWKAIQNKDR AKVEFNIRKP NEGADGQWKK 
    GFVLHKSKSE EAHAEDSVMD HHFRKPANDI TSQLEINFGD LGRPGRGGRG GRGGRGRGGR 
    PNRGSRTDKS SASAPDVDDP EAFPALA

Genular Protein ID: 2389805125

Symbol: Q5VU21_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8125298

Title: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.

PubMed ID: 8125298

DOI: 10.1016/0378-1119(94)90802-8

PubMed ID: 9373149

Title: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.

PubMed ID: 9373149

DOI: 10.1016/S0378-1119(97)00411-3

Sequence Information:

  • Length: 387
  • Mass: 42427
  • Checksum: 8C47134D22C1CCFA
  • Sequence:
  • MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ 
    TNSNAAGKQL RKESQKDRKN PLPPSVGVVD KKEETQPPVA LKKEGIRRVG RRPDQQLQGE 
    GKIIDRRPER RPPRERRFEK PLEEKGEGGE FSVDRPIIDR PIRGRGGLGR GRGGRGRGMG 
    RGDGFDSRGK REFDRHSGSD RSGLKHEDKR GGSGSHNWGT VKDELTDLDQ SNVTEETPEG 
    EEHHPVADTE NKENEVEEVK EEGPKEMTLD EWKAIQNKDR AKVEFNIRKP NEGADGQWKK 
    GFVLHKSKSE EAHAEDSVMD HHFRKPANDI TSQLEINFGD LGRPGRGGRG GRGGRGRGGR 
    PNRGSRTDKS SASAPDVDDP EAFPALA

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.