SYNJ2BP
Synaptojanin-2-binding protein is a protein that in humans is encoded by the SYNJ2BP gene.[4][5]
Interactions
SYNJ2BP has been shown to interact with:
References
- GRCh38: Ensembl release 89: ENSG00000213463 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (May 2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway". The Journal of Biological Chemistry. 277 (21): 19008–18. doi:10.1074/jbc.M112472200. PMID 11882656.
- "Entrez Gene: SYNJ2BP synaptojanin 2 binding protein".
- Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H (Oct 2004). "Novel factors in regulation of activin signaling". Molecular and Cellular Endocrinology. 225 (1–2): 1–8. doi:10.1016/j.mce.2004.02.006. PMID 15451561.
- Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (Aug 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". The Journal of Biological Chemistry. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
Further reading
- Nemoto Y, De Camilli P (Jun 1999). "Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein". The EMBO Journal. 18 (11): 2991–3006. doi:10.1093/emboj/18.11.2991. PMC 1171381. PMID 10357812.
- Gotthardt M, Trommsdorff M, Nevitt MF, Shelton J, Richardson JA, Stockinger W, Nimpf J, Herz J (Aug 2000). "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction". The Journal of Biological Chemistry. 275 (33): 25616–24. doi:10.1074/jbc.M000955200. PMID 10827173.
- Weins A, Schwarz K, Faul C, Barisoni L, Linke WA, Mundel P (Oct 2001). "Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein". The Journal of Cell Biology. 155 (3): 393–404. doi:10.1083/jcb.200012039. PMC 2150840. PMID 11673475.
- Lin F, Yu YP, Woods J, Cieply K, Gooding B, Finkelstein P, Dhir R, Krill D, Becich MJ, Michalopoulos G, Finkelstein S, Luo JH (Nov 2001). "Myopodin, a synaptopodin homologue, is frequently deleted in invasive prostate cancers". The American Journal of Pathology. 159 (5): 1603–12. doi:10.1016/S0002-9440(10)63006-4. PMC 3277320. PMID 11696420.
- Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
- Tsuchida K, Nakatani M, Matsuzaki T, Yamakawa N, Liu Z, Bao Y, Arai KY, Murakami T, Takehara Y, Kurisaki A, Sugino H (Oct 2004). "Novel factors in regulation of activin signaling". Molecular and Cellular Endocrinology. 225 (1–2): 1–8. doi:10.1016/j.mce.2004.02.006. PMID 15451561.
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