PDCD6

PDCD6
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2ZN8, 2ZN9, 2ZND, 2ZNE, 2ZRS, 2ZRT, 3AAJ, 3AAK, 3WXA
Identifiers
Aliases	PDCD6, ALG-2, PEF1B, ALG2, programmed cell death 6
External IDs	OMIM: 601057; MGI: 109283; HomoloGene: 7880; GeneCards: PDCD6; OMA:PDCD6 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5p15.33 Start 271,621 bp End 314,974 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 C1 Start 74,451,628 bp End 74,465,699 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium mucosa of transverse colon right adrenal cortex prefrontal cortex left adrenal gland left adrenal cortex rectum Brodmann area 9 gonad anterior pituitary Top expressed in jejunum duodenum ileum epithelium of small intestine right kidney endothelial cell of lymphatic vessel Epithelium of choroid plexus vestibular sensory epithelium endocardial cushion fetal liver hematopoietic progenitor cell More reference expression data BioGPS n/a
Gene ontology Molecular function protein dimerization activity protein-membrane adaptor activity calcium-dependent protein binding metal ion binding calcium-dependent cysteine-type endopeptidase activity protein binding identical protein binding molecular adaptor activity magnesium ion binding calcium ion binding protein homodimerization activity protein-macromolecule adaptor activity Cellular component cytoplasm endosome endoplasmic reticulum membrane membrane endoplasmic reticulum extracellular exosome nucleus Golgi membrane COPII vesicle coat Cul3-RING ubiquitin ligase complex endoplasmic reticulum exit site ER to Golgi transport vesicle membrane cytoplasmic vesicle Biological process negative regulation of protein kinase B signaling cellular response to heat vascular endothelial growth factor receptor-2 signaling pathway positive regulation of endothelial cell proliferation negative regulation of vascular endothelial growth factor receptor signaling pathway positive regulation of angiogenesis positive regulation of endothelial cell migration response to calcium ion negative regulation of TOR signaling positive regulation of cysteine-type endopeptidase activity involved in apoptotic process angiogenesis apoptotic signaling pathway intracellular protein transport activation of cysteine-type endopeptidase activity involved in apoptotic process apoptotic process proteolysis endoplasmic reticulum to Golgi vesicle-mediated transport neural crest formation neural crest cell development COPII vesicle coating positive regulation of protein monoubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10016 18570 Ensembl ENSG00000249915 ENSMUSG00000021576 UniProt O75340 P12815 RefSeq (mRNA) NM_001267556 NM_001267557 NM_001267558 NM_001267559 NM_013232 NM_011051 NM_001359996 RefSeq (protein) NP_001254485 NP_001254486 NP_001254487 NP_001254488 NP_037364 NP_035181 NP_001346925 Location (UCSC) Chr 5: 0.27 – 0.31 Mb Chr 13: 74.45 – 74.47 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Programmed cell death protein 6 is a protein that in humans is encoded by the PDCD6 gene.

This gene encodes a calcium-binding protein belonging to the penta-EF-hand protein family. Calcium binding is important for homodimerization and for conformational changes required for binding to other protein partners. This gene product participates in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death. In mice deficient for this gene product, however, apoptosis was not blocked suggesting this gene product is functionally redundant.

Interactions

PDCD6 has been shown to interact with ASK1, PDCD6IP, Fas receptor, ANXA11 and PEF1.

Further reading

• Krebs J, Klemenz R (2001). "The ALG-2/AIP-complex, a modulator at the interface between cell proliferation and cell death? A hypothesis". Biochim. Biophys. Acta. 1498 (2–3): 153–61. doi:10.1016/S0167-4889(00)00091-4. PMID 11108958.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Vito P, Pellegrini L, Guiet C, D'Adamio L (1999). "Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction". J. Biol. Chem. 274 (3): 1533–40. doi:10.1074/jbc.274.3.1533. PMID 9880530.
• Tarabykina S, Møller AL, Durussel I, et al. (2000). "Two forms of the apoptosis-linked protein ALG-2 with different Ca(2+) affinities and target recognition". J. Biol. Chem. 275 (14): 10514–8. doi:10.1074/jbc.275.14.10514. PMID 10744743.
• Chen B, Borinstein SC, Gillis J, et al. (2000). "The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and modulates apoptosis in astrocytes". J. Biol. Chem. 275 (25): 19275–81. doi:10.1074/jbc.M908994199. PMID 10858458.
• Kitaura Y, Matsumoto S, Satoh H, et al. (2001). "Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner". J. Biol. Chem. 276 (17): 14053–8. doi:10.1074/jbc.M008649200. PMID 11278427.
• Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein–Protein Interaction Panel Using Mouse Full-Length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
• Jung YS, Kim KS, Kim KD, et al. (2001). "Apoptosis-linked gene 2 binds to the death domain of Fas and dissociates from Fas during Fas-mediated apoptosis in Jurkat cells". Biochem. Biophys. Res. Commun. 288 (2): 420–6. doi:10.1006/bbrc.2001.5769. PMID 11606059.
• Kitaura Y, Satoh H, Takahashi H, et al. (2002). "Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized by dimerization through their fifth EF-hand regions". Arch. Biochem. Biophys. 399 (1): 12–8. doi:10.1006/abbi.2001.2736. PMID 11883899.
• Satoh H, Shibata H, Nakano Y, et al. (2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochem. Biophys. Res. Commun. 291 (5): 1166–72. doi:10.1006/bbrc.2002.6600. PMID 11883939.
• Chatellard-Causse C, Blot B, Cristina N, et al. (2002). "Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization". J. Biol. Chem. 277 (32): 29108–15. doi:10.1074/jbc.M204019200. PMID 12034747.
• Hwang IS, Jung YS, Kim E (2002). "Interaction of ALG-2 with ASK1 influences ASK1 localization and subsequent JNK activation". FEBS Lett. 529 (2–3): 183–7. doi:10.1016/S0014-5793(02)03329-X. PMID 12372597.
• Satoh H, Nakano Y, Shibata H, Maki M (2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochim. Biophys. Acta. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
• Krebs J, Saremaslani P, Caduff R (2002). "ALG-2: a Ca2+ -binding modulator protein involved in cell proliferation and in cell death". Biochim. Biophys. Acta. 1600 (1–2): 68–73. doi:10.1016/S1570-9639(02)00446-6. PMID 12445461.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tomsig JL, Snyder SL, Creutz CE (2003). "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif". J. Biol. Chem. 278 (12): 10048–54. doi:10.1074/jbc.M212632200. PMID 12522145.
• Hansen C, Tarabykina S, la Cour JM, et al. (2003). "The PEF family proteins sorcin and grancalcin interact in vivo and in vitro". FEBS Lett. 545 (2–3): 151–4. doi:10.1016/S0014-5793(03)00518-0. PMID 12804766.

}}

External links

• PDCD6 human gene location in the UCSC Genome Browser.
• PDCD6 human gene details in the UCSC Genome Browser.