PDCD6

Protein-coding gene in the species Homo sapiens
PDCD6
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2ZN8, 2ZN9, 2ZND, 2ZNE, 2ZRS, 2ZRT, 3AAJ, 3AAK, 3WXA

Identifiers
AliasesPDCD6, ALG-2, PEF1B, ALG2, programmed cell death 6
External IDsOMIM: 601057; MGI: 109283; HomoloGene: 7880; GeneCards: PDCD6; OMA:PDCD6 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for PDCD6
Genomic location for PDCD6
Band5p15.33Start271,621 bp[1]
End314,974 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for PDCD6
Genomic location for PDCD6
Band13|13 C1Start74,451,628 bp[2]
End74,465,699 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 13: 74.45 – 74.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Programmed cell death protein 6 is a protein that in humans is encoded by the PDCD6 gene.[5]

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.[6]

Interactions

PDCD6 has been shown to interact with ASK1,[7] PDCD6IP,[8][9] Fas receptor,[10] ANXA11[9] and PEF1.[11]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000249915 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021576 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Vito P, Lacana E, D'Adamio L (February 1996). "Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3". Science. 271 (5248): 521–5. Bibcode:1996Sci...271..521V. doi:10.1126/science.271.5248.521. PMID 8560270. S2CID 22286752.
  6. ^ "Entrez Gene: PDCD6 programmed cell death 6".
  7. ^ Hwang, In-Sik; Jung Yong-Sam; Kim Eunhee (October 2002). "Interaction of ALG-2 with ASK1 influences ASK1 localization and subsequent JNK activation". FEBS Lett. 529 (2–3). Netherlands: 183–7. Bibcode:2002FEBSL.529..183H. doi:10.1016/S0014-5793(02)03329-X. ISSN 0014-5793. PMID 12372597. S2CID 9264865.
  8. ^ Vito, P; Pellegrini L; Guiet C; D'Adamio L (January 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). UNITED STATES: 1533–40. doi:10.1074/jbc.274.3.1533. ISSN 0021-9258. PMID 9880530.
  9. ^ a b Satoh, Hirokazu; Shibata Hideki; Nakano Yoshimi; Kitaura Yasuyuki; Maki Masatoshi (March 2002). "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner". Biochem. Biophys. Res. Commun. 291 (5). United States: 1166–72. doi:10.1006/bbrc.2002.6600. ISSN 0006-291X. PMID 11883939.
  10. ^ Jung, Y S; Kim K S; Kim K D; Lim J S; Kim J W; Kim E (October 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). United States: 420–6. doi:10.1006/bbrc.2001.5769. ISSN 0006-291X. PMID 11606059.
  11. ^ Kitaura, Y; Matsumoto S; Satoh H; Hitomi K; Maki M (April 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). United States: 14053–8. doi:10.1074/jbc.M008649200. ISSN 0021-9258. PMID 11278427.

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. Bibcode:2002FEBSL.529..183H. doi:10.1016/S0014-5793(02)03329-X. PMID 12372597. S2CID 9264865.
  • 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. Bibcode:2003FEBSL.545..151H. doi:10.1016/S0014-5793(03)00518-0. PMID 12804766. S2CID 42572647.
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  • 1hqv: STRUCTURE OF APOPTOSIS-LINKED PROTEIN ALG-2
    1hqv: STRUCTURE OF APOPTOSIS-LINKED PROTEIN ALG-2


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