Details for: PDCD6

Gene ID: 10016

Symbol: PDCD6

Ensembl ID: ENSG00000249915

Description: programmed cell death 6

Associated with

Other Information

Genular Protein ID: 506862438

Symbol: PDCD6_HUMAN

Name: Programmed cell death protein 6

UniProtKB Accession Codes:

Database IDs:

Citations:

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: 11278427

Title: Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner.

PubMed ID: 11278427

DOI: 10.1074/jbc.m008649200

PubMed ID: 11883899

Title: Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by dimerization through their fifth EF-hand regions.

PubMed ID: 11883899

DOI: 10.1006/abbi.2001.2736

PubMed ID: 11883939

Title: ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner.

PubMed ID: 11883939

DOI: 10.1006/bbrc.2002.6600

PubMed ID: 16132846

Title: Programmed cell death 6 (PDCD6) protein interacts with death-associated protein kinase 1 (DAPk1): additive effect on apoptosis via caspase-3 dependent pathway.

PubMed ID: 16132846

DOI: 10.1007/s10529-005-7869-x

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: 16957052

Title: The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A.

PubMed ID: 16957052

DOI: 10.1091/mbc.e06-05-0444

PubMed ID: 17889823

Title: The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-inducible gene product localized at the endoplasmic reticulum membrane.

PubMed ID: 17889823

DOI: 10.1016/j.abb.2007.07.028

PubMed ID: 18256029

Title: Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants.

PubMed ID: 18256029

DOI: 10.1074/jbc.m800717200

PubMed ID: 19520058

Title: Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101.

PubMed ID: 19520058

DOI: 10.1016/j.bbrc.2009.06.015

PubMed ID: 19864416

Title: Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent interactor of mucolipin-1.

PubMed ID: 19864416

DOI: 10.1074/jbc.m109.047241

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: 21893193

Title: Programmed cell death 6 (PDCD6) inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2.

PubMed ID: 21893193

DOI: 10.1016/j.cellsig.2011.08.013

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: 25944712

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

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27716508

Title: Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-adaptor.

PubMed ID: 27716508

DOI: 10.1016/j.cell.2016.09.026

PubMed ID: 27813252

Title: The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein.

PubMed ID: 27813252

DOI: 10.1111/febs.13949

PubMed ID: 18997320

Title: Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2.

PubMed ID: 18997320

DOI: 10.1107/s1744309108030297

PubMed ID: 18940611

Title: Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism.

PubMed ID: 18940611

DOI: 10.1016/j.str.2008.07.012

PubMed ID: 20691033

Title: Molecular basis for defect in Alix-binding by alternatively spliced isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in target recognition.

PubMed ID: 20691033

DOI: 10.1186/1472-6807-10-25

PubMed ID: 25667979

Title: Structural analysis of the complex between penta-EF-hand ALG-2 protein and Sec31A peptide reveals a novel target recognition mechanism of ALG-2.

PubMed ID: 25667979

DOI: 10.3390/ijms16023677

PubMed ID: 27784779

Title: Structural and functional study of apoptosis-linked gene-2.Heme-binding protein 2 interactions in HIV-1 production.

PubMed ID: 27784779

DOI: 10.1074/jbc.m116.752444

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 191
  • Mass: 21868
  • Checksum: D0B5944CF3C696AD
  • Sequence:
  • MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF 
    NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS 
    GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY 
    EQYLSMVFSI V

Genular Protein ID: 2958232421

Symbol: Q53FC3_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: 191
  • Mass: 21896
  • Checksum: F7459453D1FB898F
  • Sequence:
  • MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF 
    NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELRQALS 
    GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY 
    EQYLSMVFSI V

Genular Protein ID: 2482884710

Symbol: A0A087WZ38_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15372022

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

PubMed ID: 15372022

DOI: 10.1038/nature02919

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

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: 25944712

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

PubMed ID: 25944712

Sequence Information:

  • Length: 123
  • Mass: 13959
  • Checksum: 40F29F4E7345041B
  • Sequence:
  • MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGYRLSD 
    QFHDILIRKF DRQGRGQIAF DDFIQGCIVL QRLTDIFRRY DTDQDGWIQV SYEQYLSMVF 
    SIV

Genular Protein ID: 3322098855

Symbol: A0A024QZ42_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: 15372022

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

PubMed ID: 15372022

DOI: 10.1038/nature02919

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 25944712

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

PubMed ID: 25944712

Sequence Information:

  • Length: 121
  • Mass: 14450
  • Checksum: E0396F5D7C53A23F
  • Sequence:
  • MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS GFGYRLSDQF 
    HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI 
    V

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.