STAMBP
From Wikipedia, the free encyclopedia
Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox STAM-binding protein is a protein that in humans is encoded by the STAMBP gene.[1][2]
Function
Cytokine-mediated signal transduction in the JAK-STAT cascade requires the involvement of adaptor molecules. One such signal-transducing adaptor molecule contains an SH3 domain that is required for induction of MYC and cell growth. The protein encoded by this gene binds to the SH3 domain of the signal-transducing adaptor molecule, and plays a critical role in cytokine-mediated signaling for MYC induction and cell cycle progression. Multiple alternatively spliced transcript variants encoding the same protein isoform have been found for this gene.[2]
Clinical significance
Mutations in this gene have been associated with a unique congenital progressive encephalopathy known as MIC-CAP.[3]
Interactions
STAMBP has been shown to interact with RNF11,[4] Signal transducing adaptor molecule[1][5] and GRAP2.[6][7]
References
Page Template:Reflist/styles.css has no content.
- ^ a b Page Module:Citation/CS1/styles.css has no content.Tanaka N, Kaneko K, Asao H, Kasai H, Endo Y, Fujita T, et al. (July 1999). "Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines". The Journal of Biological Chemistry. 274 (27): 19129–19135. doi:10.1074/jbc.274.27.19129. PMID 10383417.
- ^ a b Page Module:Citation/CS1/styles.css has no content."Entrez Gene: STAMBP STAM binding protein".
- ^ Page Module:Citation/CS1/styles.css has no content.McDonell LM, Mirzaa GM, Alcantara D, Schwartzentruber J, Carter MT, Lee LJ, et al. (FORGE Canada Consortium) (2013). "Mutations in STAMBP, encoding a deubiquitinating enzyme, cause microcephaly–capillary malformation syndrome". Nature Genetics. 45 (5): 556–562. doi:10.1038/ng.2602. ISSN 1061-4036. PMC 4000253. PMID 23542699.
- ^ Page Module:Citation/CS1/styles.css has no content.Li H, Seth A (March 2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–1808. doi:10.1038/sj.onc.1207319. PMID 14755250. S2CID 37253372.
- ^ Page Module:Citation/CS1/styles.css has no content.Kato M, Miyazawa K, Kitamura N (December 2000). "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP". The Journal of Biological Chemistry. 275 (48): 37481–37487. doi:10.1074/jbc.M007251200. PMID 10982817.
- ^ Page Module:Citation/CS1/styles.css has no content.Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- ^ Page Module:Citation/CS1/styles.css has no content.Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, et al. (May 1999). "Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT". The Journal of Experimental Medicine. 189 (9): 1383–1390. doi:10.1084/jem.189.9.1383. PMC 2193052. PMID 10224278.
Further reading
Page Template:Refbegin/styles.css has no content.
- Page Module:Citation/CS1/styles.css has no content.Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–113. doi:10.1006/abio.1996.0138. PMID 8619474.
- Page Module:Citation/CS1/styles.css has no content.Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–358. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Page Module:Citation/CS1/styles.css has no content.Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, et al. (May 1999). "Grf40, A novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT". The Journal of Experimental Medicine. 189 (9): 1383–1390. doi:10.1084/jem.189.9.1383. PMC 2193052. PMID 10224278.
- Page Module:Citation/CS1/styles.css has no content.Endo K, Takeshita T, Kasai H, Sasaki Y, Tanaka N, Asao H, et al. (July 2000). "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Letters. 477 (1–2): 55–61. Bibcode:2000FEBSL.477...55E. doi:10.1016/S0014-5793(00)01760-9. PMID 10899310. S2CID 31811757.
- Page Module:Citation/CS1/styles.css has no content.Itoh F, Asao H, Sugamura K, Heldin CH, ten Dijke P, Itoh S (August 2001). "Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads". The EMBO Journal. 20 (15): 4132–4142. doi:10.1093/emboj/20.15.4132. PMC 149146. PMID 11483516.
- Page Module:Citation/CS1/styles.css has no content.Ishii N, Owada Y, Yamada M, Miura S, Murata K, Asao H, et al. (December 2001). "Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice". Molecular and Cellular Biology. 21 (24): 8626–8637. doi:10.1128/MCB.21.24.8626-8637.2001. PMC 100023. PMID 11713295.
- Page Module:Citation/CS1/styles.css has no content.Maytal-Kivity V, Reis N, Hofmann K, Glickman MH (Sep 2002). "MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function". BMC Biochemistry. 3 28. doi:10.1186/1471-2091-3-28. PMC 129983. PMID 12370088.
- Page Module:Citation/CS1/styles.css has no content.Ibarrola N, Kratchmarova I, Nakajima D, Schiemann WP, Moustakas A, Pandey A, et al. (January 2004). "Cloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor beta signaling". BMC Cell Biology. 5 2. doi:10.1186/1471-2121-5-2. PMC 385422. PMID 14728725.
- Page Module:Citation/CS1/styles.css has no content.Ambroggio XI, Rees DC, Deshaies RJ (January 2004). "JAMM: a metalloprotease-like zinc site in the proteasome and signalosome". PLOS Biology. 2 (1): E2. doi:10.1371/journal.pbio.0020002. PMC 300881. PMID 14737182.
- Page Module:Citation/CS1/styles.css has no content.Li H, Seth A (March 2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–1808. doi:10.1038/sj.onc.1207319. PMID 14755250. S2CID 37253372.
- Page Module:Citation/CS1/styles.css has no content.McCullough J, Clague MJ, Urbé S (August 2004). "AMSH is an endosome-associated ubiquitin isopeptidase". The Journal of Cell Biology. 166 (4): 487–492. doi:10.1083/jcb.200401141. PMC 2172215. PMID 15314065.
- Page Module:Citation/CS1/styles.css has no content.Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- Page Module:Citation/CS1/styles.css has no content.Row PE, Prior IA, McCullough J, Clague MJ, Urbé S (May 2006). "The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation". The Journal of Biological Chemistry. 281 (18): 12618–12624. doi:10.1074/jbc.M512615200. PMID 16520378.
- Page Module:Citation/CS1/styles.css has no content.Nakamura M, Tanaka N, Kitamura N, Komada M (June 2006). "Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes". Genes to Cells: Devoted to Molecular & Cellular Mechanisms. 11 (6): 593–606. doi:10.1111/j.1365-2443.2006.00963.x. PMID 16716190. S2CID 30077507.
- Page Module:Citation/CS1/styles.css has no content.Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (September 2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–346. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
