M-RIP

Myosin phosphatase Rho-interacting protein is an enzyme that in humans is encoded by the MPRIP gene.[5][6]

MPRIP
Identifiers
Aliases	MPRIP, M-RIP, MRIP, RHOIP3, RIP3, p116Rip, myosin phosphatase Rho interacting protein
External IDs	OMIM: 612935 MGI: 1349438 HomoloGene: 9034 GeneCards: MPRIP
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p11.2 Start 17,042,545 bp[1] End 17,217,679 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B1.3 Start 59,661,305 bp[2] End 59,780,860 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin binding • GO:0001948 protein binding • cadherin binding Cellular component • cytoskeleton • focal adhesion • actin cytoskeleton • cytoplasm • cytosol Biological process • cell-cell adhesion Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	23164	26936
Ensembl	ENSG00000133030	ENSMUSG00000005417
UniProt	Q6WCQ1	P97434
RefSeq (mRNA)	NM_015134 NM_201274 NM_001364716	NM_012027 NM_201245 NM_001368931
RefSeq (protein)	NP_055949 NP_958431 NP_001351645	NP_036157 NP_957697 NP_001355860
Location (UCSC)	Chr 17: 17.04 – 17.22 Mb	Chr 11: 59.66 – 59.78 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

M-RIP has been shown to interact with RHOA.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000133030 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000005417 - 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 (May 1999). "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 Res. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
6. "Entrez Gene: M-RIP myosin phosphatase-Rho interacting protein".
7. Gebbink MF, Kranenburg O, Poland M, van Horck FP, Houssa B, Moolenaar WH (Jun 1997). "Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology". J. Cell Biol. 137 (7): 1603–13. doi:10.1083/jcb.137.7.1603. PMC 2137826. PMID 9199174.

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Gebbink MF, Kranenburg O, Poland M, van Horck FP, Houssa B, Moolenaar WH (1997). "Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology". J. Cell Biol. 137 (7): 1603–13. doi:10.1083/jcb.137.7.1603. PMC 2137826. PMID 9199174.
• Surks HK, Richards CT, Mendelsohn ME (2004). "Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA". J. Biol. Chem. 278 (51): 51484–93. doi:10.1074/jbc.M305622200. PMID 14506264.
• Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Mulder J, Ariaens A, van den Boomen D, Moolenaar WH (2005). "p116Rip targets myosin phosphatase to the actin cytoskeleton and is essential for RhoA/ROCK-regulated neuritogenesis". Mol. Biol. Cell. 15 (12): 5516–27. doi:10.1091/mbc.E04-04-0275. PMC 532030. PMID 15469989.
• Koga Y, Ikebe M (2005). "p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA". J. Biol. Chem. 280 (6): 4983–91. doi:10.1074/jbc.M410909200. PMID 15545284.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
• Surks HK, Riddick N, Ohtani K (2006). "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells". J. Biol. Chem. 280 (52): 42543–51. doi:10.1074/jbc.M506863200. PMID 16257966.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• 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.