STRN3

Protein-coding gene in the species Homo sapiens
STRN3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4N6J

Identifiers
AliasesSTRN3, SG2NA, PPP2R6B, striatin 3, S/G2NA
External IDsOMIM: 614766; MGI: 2151064; HomoloGene: 82078; GeneCards: STRN3; OMA:STRN3 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for STRN3
Genomic location for STRN3
Band14q12Start30,893,799 bp[1]
End31,026,401 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for STRN3
Genomic location for STRN3
Band12|12 B3Start51,656,415 bp[2]
End51,738,680 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • epithelium of colon

  • biceps brachii

  • sural nerve

  • Skeletal muscle tissue of biceps brachii

  • testicle

  • tail of epididymis

  • Skeletal muscle tissue of rectus abdominis

  • gastrocnemius muscle

  • muscle of thigh
Top expressed in
  • interventricular septum

  • triceps brachii muscle

  • temporal muscle

  • ankle

  • muscle of thigh

  • medial head of gastrocnemius muscle

  • intercostal muscle

  • sternocleidomastoid muscle

  • digastric muscle

  • soleus muscle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • DNA-binding transcription factor activity
  • protein phosphatase 2A binding
  • protein binding
  • calmodulin binding
  • armadillo repeat domain binding
  • protein-containing complex binding
Cellular component
  • cytoplasm
  • neuronal cell body
  • plasma membrane
  • Golgi apparatus
  • dendrite
  • protein phosphatase type 2A complex
  • membrane
  • nucleus
  • nucleoplasm
  • protein-containing complex
  • FAR/SIN/STRIPAK complex
Biological process
  • response to estradiol
  • negative regulation of intracellular estrogen receptor signaling pathway
  • negative regulation of transcription by RNA polymerase II
  • negative regulation of transcription, DNA-templated
  • positive regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

29966

94186

Ensembl

ENSG00000196792

ENSMUSG00000020954

UniProt

Q13033

Q9ERG2

RefSeq (mRNA)

NM_001083893
NM_014574

NM_001172098
NM_052973
NM_001364437

RefSeq (protein)

NP_001077362
NP_055389

NP_001165569
NP_443205
NP_001351366

Location (UCSC)Chr 14: 30.89 – 31.03 MbChr 12: 51.66 – 51.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Striatin-3 is a protein that in humans is encoded by the STRN3 gene.[5][6][7]

Interactions

STRN3 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196792 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020954 – 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. ^ Muro Y, Chan EK, Landberg G, Tan EM (Mar 1995). "A cell-cycle nuclear autoantigen containing WD-40 motifs expressed mainly in S and G2 phase cells". Biochem. Biophys. Res. Commun. 207 (3): 1029–37. doi:10.1006/bbrc.1995.1288. PMID 7864889.
  6. ^ Moreno CS, Park S, Nelson K, Ashby D, Hubalek F, Lane WS, Pallas DC (Mar 2000). "WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A". J. Biol. Chem. 275 (8): 5257–63. doi:10.1074/jbc.275.8.5257. PMC 3505218. PMID 10681496.
  7. ^ "Entrez Gene: STRN3 striatin, calmodulin binding protein 3".
  8. ^ a b c d e f g h i j Goudreault M, D'Ambrosio LM, Kean MJ, Mullin MJ, Larsen BG, Sanchez A, Chaudhry S, Chen GI, Sicheri F, Nesvizhskii AI, Aebersold R, Raught B, Gingras AC (Jan 2009). "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein". Mol. Cell. Proteomics. 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.
  9. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

  • Landberg G, Tan EM (1994). "Characterization of a DNA-binding nuclear autoantigen mainly associated with S phase and G2 cells". Exp. Cell Res. 212 (2): 255–61. doi:10.1006/excr.1994.1141. PMID 7910562.
  • Castets F, Rakitina T, Gaillard S, Moqrich A, Mattei MG, Monneron A (2000). "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain". J. Biol. Chem. 275 (26): 19970–7. doi:10.1074/jbc.M909782199. PMID 10748158.
  • Moreno CS, Lane WS, Pallas DC (2001). "A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes". J. Biol. Chem. 276 (26): 24253–60. doi:10.1074/jbc.M102398200. PMC 3503316. PMID 11319234.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Foster LJ, Rudich A, Talior I, Patel N, Huang X, Furtado LM, Bilan PJ, Mann M, Klip A (2006). "Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC)". J. Proteome Res. 5 (1): 64–75. doi:10.1021/pr0502626. PMID 16396496.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.


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