STAMBP

STAMBP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSTAMBP, AMSH, MICCAP, STAM binding protein
External IDsMGI: 1917777 HomoloGene: 4719 GeneCards: STAMBP
Orthologs
SpeciesHumanMouse
Entrez

10617

70527

Ensembl

n/a

ENSMUSG00000006906

UniProt

O95630

Q9CQ26

RefSeq (mRNA)

NM_006463
NM_201647
NM_213622

NM_024239
NM_001362078
NM_001362079
NM_001362080

RefSeq (protein)

NP_077201
NP_001349007
NP_001349008
NP_001349009

Location (UCSC)n/aChr 6: 83.54 – 83.57 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

STAM-binding protein is a protein that in humans is encoded by the STAMBP gene.[4][5]

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.[5]

Mutations in this gene have been associated to cases of microcephaly (doi:10.1038/ng.2602)

Interactions

STAMBP has been shown to interact with RNF11,[6] Signal transducing adaptor molecule[4][7] and GRAP2.[8][9]

References

  1. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006906 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:".
  3. ↑ "Mouse PubMed Reference:".
  4. 1 2 Tanaka N, Kaneko K, Asao H, Kasai H, Endo Y, Fujita T, Takeshita T, Sugamura K (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): 19129–35. doi:10.1074/jbc.274.27.19129. PMID 10383417.
  5. 1 2 "Entrez Gene: STAMBP STAM binding protein".
  6. ↑ Li H, Seth A (March 2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–8. doi:10.1038/sj.onc.1207319. PMID 14755250.
  7. ↑ 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): 37481–7. doi:10.1074/jbc.M007251200. PMID 10982817.
  8. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  9. ↑ Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K (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): 1383–90. doi:10.1084/jem.189.9.1383. PMC 2193052. PMID 10224278.

Further reading

  • 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): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Asada H, Ishii N, Sasaki Y, Endo K, Kasai H, Tanaka N, Takeshita T, Tsuchiya S, Konno T, Sugamura K (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): 1383–90. doi:10.1084/jem.189.9.1383. PMC 2193052. PMID 10224278.
  • Endo K, Takeshita T, Kasai H, Sasaki Y, Tanaka N, Asao H, Kikuchi K, Yamada M, Chenb M, O'Shea JJ, Sugamura K (July 2000). "STAM2, a new member of the STAM family, binding to the Janus kinases". FEBS Letters. 477 (1–2): 55–61. doi:10.1016/S0014-5793(00)01760-9. PMID 10899310.
  • 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): 4132–42. doi:10.1093/emboj/20.15.4132. PMC 149146. PMID 11483516.
  • Ishii N, Owada Y, Yamada M, Miura S, Murata K, Asao H, Kondo H, Sugamura K (December 2001). "Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice". Molecular and Cellular Biology. 21 (24): 8626–37. doi:10.1128/MCB.21.24.8626-8637.2001. PMC 100023. PMID 11713295.
  • Maytal-Kivity V, Reis N, Hofmann K, Glickman MH (2006). "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.
  • Ibarrola N, Kratchmarova I, Nakajima D, Schiemann WP, Moustakas A, Pandey A, Mann M (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.
  • 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.
  • Li H, Seth A (March 2004). "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein". Oncogene. 23 (10): 1801–8. doi:10.1038/sj.onc.1207319. PMID 14755250.
  • McCullough J, Clague MJ, Urbé S (August 2004). "AMSH is an endosome-associated ubiquitin isopeptidase". The Journal of Cell Biology. 166 (4): 487–92. doi:10.1083/jcb.200401141. PMC 2172215. PMID 15314065.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • 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): 12618–24. doi:10.1074/jbc.M512615200. PMID 16520378.
  • 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. 11 (6): 593–606. doi:10.1111/j.1365-2443.2006.00963.x. PMID 16716190.
  • 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): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
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