CLSTN1

Protein-coding gene in humans
CLSTN1
Identifiers
AliasesCLSTN1, ALC-ALPHA, CDHR12, CSTN1, PIK3CD, XB31alpha, alcalpha1, alcalpha2, CST-1, calsyntenin 1
External IDsOMIM: 611321; MGI: 1929895; HomoloGene: 8814; GeneCards: CLSTN1; OMA:CLSTN1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for CLSTN1
Genomic location for CLSTN1
Band1p36.22Start9,728,926 bp[1]
End9,823,984 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for CLSTN1
Genomic location for CLSTN1
Band4|4 E2Start149,670,925 bp[2]
End149,733,356 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • frontal pole

  • postcentral gyrus

  • Brodmann area 10

  • paraflocculus of cerebellum

  • middle temporal gyrus

  • orbitofrontal cortex

  • superior frontal gyrus

  • Brodmann area 46

  • cerebellar vermis

  • right hemisphere of cerebellum
Top expressed in
  • primary motor cortex

  • cingulate gyrus

  • neural layer of retina

  • prefrontal cortex

  • habenula

  • primary visual cortex

  • superior frontal gyrus

  • medial dorsal nucleus

  • piriform cortex

  • medial geniculate nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • X11-like protein binding
  • calcium ion binding
  • amyloid-beta binding
  • protein binding
  • kinesin binding
Cellular component
  • integral component of membrane
  • postsynaptic membrane
  • Golgi apparatus
  • cell projection
  • endoplasmic reticulum membrane
  • membrane
  • Golgi membrane
  • plasma membrane
  • synapse
  • extracellular region
  • cell surface
  • cell junction
  • endoplasmic reticulum
  • nucleus
  • postsynaptic density
  • postsynaptic endosome
  • glutamatergic synapse
  • GABA-ergic synapse
  • integral component of postsynaptic density membrane
  • integral component of spine apparatus membrane
Biological process
  • cell adhesion
  • positive regulation of synaptic transmission
  • regulation of cell growth
  • homophilic cell adhesion via plasma membrane adhesion molecules
  • positive regulation of synapse assembly
  • regulation of synapse maturation
  • neurotransmitter receptor transport to postsynaptic membrane
  • vesicle-mediated transport in synapse
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

22883

65945

Ensembl

ENSG00000171603

ENSMUSG00000039953

UniProt

O94985

Q9EPL2

RefSeq (mRNA)

NM_014944
NM_001009566
NM_001302883

NM_001290989
NM_023051

RefSeq (protein)

NP_001009566
NP_001289812
NP_055759

NP_001277918
NP_075538

Location (UCSC)Chr 1: 9.73 – 9.82 MbChr 4: 149.67 – 149.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Calsyntenin-1 is a protein that in humans is encoded by the CLSTN1 gene.[5][6]

Clinical relevance

Mutations in this gene have been shown associated to pathogenic mechanisms of Alzheimer's disease.[7]

Interactions

CLSTN1 has been shown to interact with APBA2[8][9] and Amyloid precursor protein.[8][9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171603 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000039953 – 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. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Dec 1998). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
  6. ^ "Entrez Gene: CLSTN1 calsyntenin 1".
  7. ^ Vagnoni A, Perkinton MS, Gray EH, Francis PT, Noble W, Miller CC (Jul 2012). "Calsyntenin-1 mediates axonal transport of the amyloid precursor protein and regulates Aβ production". Human Molecular Genetics. 21 (13): 2845–54. doi:10.1093/hmg/dds109. PMC 3373235. PMID 22434822.
  8. ^ a b Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (Dec 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". The Journal of Biological Chemistry. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.
  9. ^ a b Araki Y, Miyagi N, Kato N, Yoshida T, Wada S, Nishimura M, Komano H, Yamamoto T, De Strooper B, Yamamoto K, Suzuki T (Jun 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". The Journal of Biological Chemistry. 279 (23): 24343–54. doi:10.1074/jbc.M401925200. PMID 15037614.

Further reading

  • Konecna A, Frischknecht R, Kinter J, Ludwig A, Steuble M, Meskenaite V, Indermühle M, Engel M, Cen C, Mateos JM, Streit P, Sonderegger P (Aug 2006). "Calsyntenin-1 docks vesicular cargo to kinesin-1" (PDF). Molecular Biology of the Cell. 17 (8): 3651–63. doi:10.1091/mbc.E06-02-0112. PMC 1525238. PMID 16760430.[permanent dead link]
  • Schmitt-Ulms G, Hansen K, Liu J, Cowdrey C, Yang J, DeArmond SJ, Cohen FE, Prusiner SB, Baldwin MA (Jun 2004). "Time-controlled transcardiac perfusion cross-linking for the study of protein interactions in complex tissues". Nature Biotechnology. 22 (6): 724–31. doi:10.1038/nbt969. PMID 15146195. S2CID 36630738.
  • Araki Y, Miyagi N, Kato N, Yoshida T, Wada S, Nishimura M, Komano H, Yamamoto T, De Strooper B, Yamamoto K, Suzuki T (Jun 2004). "Coordinated metabolism of Alcadein and amyloid beta-protein precursor regulates FE65-dependent gene transactivation". The Journal of Biological Chemistry. 279 (23): 24343–54. doi:10.1074/jbc.M401925200. PMID 15037614.
  • Araki Y, Tomita S, Yamaguchi H, Miyagi N, Sumioka A, Kirino Y, Suzuki T (Dec 2003). "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like protein-mediated stabilization of amyloid beta-protein precursor metabolism". The Journal of Biological Chemistry. 278 (49): 49448–58. doi:10.1074/jbc.M306024200. PMID 12972431.
  • Nakayama M, Kikuno R, Ohara O (Nov 2002). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Research. 12 (11): 1773–84. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.
  • Vogt L, Schrimpf SP, Meskenaite V, Frischknecht R, Kinter J, Leone DP, Ziegler U, Sonderegger P (Jan 2001). "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein with a cytoplasmic calcium-binding domain". Molecular and Cellular Neurosciences. 17 (1): 151–66. doi:10.1006/mcne.2000.0937. PMID 11161476. S2CID 30856590.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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.
  • Maruyama K, Sugano S (Jan 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.


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