ARHGAP5: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Rho GTPase-activating protein 5''' is an [[enzyme]] that in humans is encoded by the ''ARHGAP5'' [[gene]].<ref name="pmid8537347">{{cite journal | vauthors = Burbelo PD, Miyamoto S, Utani A, Brill S, Yamada KM, Hall A, Yamada Y | title = p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking | journal = J. Biol. Chem. | volume = 270 | issue = 52 | pages = 30919–26 | year = 1995 | date = Feb 1996 | pmid = 8537347 | pmc =  | doi = 10.1074/jbc.270.52.30919 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARHGAP5 Rho GTPase activating protein 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=394| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Rho GTPase activating protein 5
| HGNCid = 675
| Symbol = ARHGAP5
| AltSymbols =; RhoGAP5; p190-B
| OMIM = 602680
| ECnumber = 
| Homologene = 907
| MGIid = 1332637
| GeneAtlas_image1 = PBB_GE_ARHGAP5_217936_at_tn.png
| Function = {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0005100 |text = Rho GTPase activator activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 394
    | Hs_Ensembl = ENSG00000100852
    | Hs_RefseqProtein = NP_001025226
    | Hs_RefseqmRNA = NM_001030055
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 31616246
    | Hs_GenLoc_end = 31698685
    | Hs_Uniprot = Q13017
    | Mm_EntrezGene = 11855
    | Mm_Ensembl = ENSMUSG00000035133
    | Mm_RefseqmRNA = NM_009706
    | Mm_RefseqProtein = NP_033836
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 53437868
    | Mm_GenLoc_end = 53490452
    | Mm_Uniprot = Q3TQ76
  }}
}}
'''Rho GTPase activating protein 5''', also known as '''ARHGAP5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARHGAP5 Rho GTPase activating protein 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=394| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family which may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ARHGAP5 Rho GTPase activating protein 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=394| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
ARHGAP5 has been shown to [[Protein-protein interaction|interact]] with [[Rnd1]],<ref name=pmid12842009>{{cite journal | vauthors = Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH | title = Rnd proteins function as RhoA antagonists by activating p190 RhoGAP | journal = Curr. Biol. | volume = 13 | issue = 13 | pages = 1106–15  | date = Jul 2003 | pmid = 12842009 | doi = 10.1016/S0960-9822(03)00418-4 }}</ref> [[Rnd2]],<ref name=pmid12842009/> [[Rnd3]]<ref name=pmid12842009/> and [[RHOA]].<ref name=pmid12842009/>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|ARHGAP5}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Ellis C, Moran M, McCormick F, Pawson T | title = Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases | journal = Nature | volume = 343 | issue = 6256 | pages = 377–81 | year = 1990 | pmid = 1689011 | doi = 10.1038/343377a0 }}
| citations =
* {{cite journal | vauthors = Foster R, Hu KQ, Shaywitz DA, Settleman J | title = p190 RhoGAP, the major RasGAP-associated protein, binds GTP directly | journal = Mol. Cell. Biol. | volume = 14 | issue = 11 | pages = 7173–81 | year = 1994 | pmid = 7935432 | pmc = 359251 | doi =  }}
*{{cite journal | author=Ellis C, Moran M, McCormick F, Pawson T |title=Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. |journal=Nature |volume=343 |issue= 6256 |pages= 377-81 |year= 1990 |pmid= 1689011 |doi= 10.1038/343377a0 }}
* {{cite journal | vauthors = McGlade J, Brunkhorst B, Anderson D, Mbamalu G, Settleman J, Dedhar S, Rozakis-Adcock M, Chen LB, Pawson T | title = The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion | journal = EMBO J. | volume = 12 | issue = 8 | pages = 3073–81 | year = 1993 | pmid = 8344248 | pmc = 413572 | doi =  }}
*{{cite journal | author=Foster R, Hu KQ, Shaywitz DA, Settleman J |title=p190 RhoGAP, the major RasGAP-associated protein, binds GTP directly. |journal=Mol. Cell. Biol. |volume=14 |issue= 11 |pages= 7173-81 |year= 1994 |pmid= 7935432 |doi=  }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=McGlade J, Brunkhorst B, Anderson D, ''et al.'' |title=The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. |journal=EMBO J. |volume=12 |issue= 8 |pages= 3073-81 |year= 1993 |pmid= 8344248 |doi=  }}
* {{cite journal | vauthors = Zrihan-Licht S, Fu Y, Settleman J, Schinkmann K, Shaw L, Keydar I, Avraham S, Avraham H | title = RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion | journal = Oncogene | volume = 19 | issue = 10 | pages = 1318–28 | year = 2000 | pmid = 10713673 | doi = 10.1038/sj.onc.1203422 }}
*{{cite journal  | author=Burbelo PD, Miyamoto S, Utani A, ''et al.'' |title=p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking. |journal=J. Biol. Chem. |volume=270 |issue= 52 |pages= 30919-26 |year= 1996 |pmid= 8537347 |doi=  }}
* {{cite journal | vauthors = Kulkarni SV, Gish G, van der Geer P, Henkemeyer M, Pawson T | title = Role of p120 Ras-GAP in directed cell movement | journal = J. Cell Biol. | volume = 149 | issue = 2 | pages = 457–70 | year = 2000 | pmid = 10769036 | pmc = 2175152 | doi = 10.1083/jcb.149.2.457 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Chakravarty G, Roy D, Gonzales M, Gay J, Contreras A, Rosen JM | title = P190-B, a Rho-GTPase-activating protein, is differentially expressed in terminal end buds and breast cancer | journal = Cell Growth Differ. | volume = 11 | issue = 7 | pages = 343–54 | year = 2000 | pmid = 10939588 | doi =  }}
*{{cite journal | author=Zrihan-Licht S, Fu Y, Settleman J, ''et al.'' |title=RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion. |journal=Oncogene |volume=19 |issue= 10 |pages= 1318-28 |year= 2000 |pmid= 10713673 |doi= 10.1038/sj.onc.1203422 }}
* {{cite journal | vauthors = Shiota M, Tanihiro T, Nakagawa Y, Aoki N, Ishida N, Miyazaki K, Ullrich A, Miyazaki H | title = Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone | journal = Mol. Endocrinol. | volume = 17 | issue = 4 | pages = 534–49 | year = 2003 | pmid = 12554790 | doi = 10.1210/me.2002-0187 }}
*{{cite journal | author=Kulkarni SV, Gish G, van der Geer P, ''et al.'' |title=Role of p120 Ras-GAP in directed cell movement. |journal=J. Cell Biol. |volume=149 |issue= 2 |pages= 457-70 |year= 2000 |pmid= 10769036 |doi= }}
* {{cite journal | vauthors = Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH | title = Rnd proteins function as RhoA antagonists by activating p190 RhoGAP | journal = Curr. Biol. | volume = 13 | issue = 13 | pages = 1106–15 | year = 2003 | pmid = 12842009 | doi = 10.1016/S0960-9822(03)00418-4 }}
*{{cite journal | author=Chakravarty G, Roy D, Gonzales M, ''et al.'' |title=P190-B, a Rho-GTPase-activating protein, is differentially expressed in terminal end buds and breast cancer. |journal=Cell Growth Differ. |volume=11 |issue= 7 |pages= 343-54 |year= 2000 |pmid= 10939588 |doi=  }}
* {{cite journal | vauthors = Su L, Agati JM, Parsons SJ | title = p190RhoGAP is cell cycle regulated and affects cytokinesis | journal = J. Cell Biol. | volume = 163 | issue = 3 | pages = 571–82 | year = 2003 | pmid = 14610059 | pmc = 2173658 | doi = 10.1083/jcb.200308007 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Res. | volume = 14 | issue = 7 | pages = 1324–32 | year = 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
*{{cite journal  | author=Shiota M, Tanihiro T, Nakagawa Y, ''et al.'' |title=Protein tyrosine phosphatase PTP20 induces actin cytoskeleton reorganization by dephosphorylating p190 RhoGAP in rat ovarian granulosa cells stimulated with follicle-stimulating hormone. |journal=Mol. Endocrinol. |volume=17 |issue= 4 |pages= 534-49 |year= 2004 |pmid= 12554790 |doi= 10.1210/me.2002-0187 }}
* {{cite journal | vauthors = Blanchetot C, Chagnon M, Dubé N, Hallé M, Tremblay ML | title = Substrate-trapping techniques in the identification of cellular PTP targets | journal = Methods | volume = 35 | issue = 1 | pages = 44–53 | year = 2005 | pmid = 15588985 | doi = 10.1016/j.ymeth.2004.07.007 }}
*{{cite journal | author=Wennerberg K, Forget MA, Ellerbroek SM, ''et al.'' |title=Rnd proteins function as RhoA antagonists by activating p190 RhoGAP. |journal=Curr. Biol. |volume=13 |issue= 13 |pages= 1106-15 |year= 2004 |pmid= 12842009 |doi= }}
* {{cite journal | vauthors = Vargo-Gogola T, Heckman BM, Gunther EJ, Chodosh LA, Rosen JM | title = P190-B Rho GTPase-activating protein overexpression disrupts ductal morphogenesis and induces hyperplastic lesions in the developing mammary gland | journal = Mol. Endocrinol. | volume = 20 | issue = 6 | pages = 1391–405 | year = 2006 | pmid = 16469769 | doi = 10.1210/me.2005-0426 }}
*{{cite journal | author=Su L, Agati JM, Parsons SJ |title=p190RhoGAP is cell cycle regulated and affects cytokinesis. |journal=J. Cell Biol. |volume=163 |issue= 3 |pages= 571-82 |year= 2004 |pmid= 14610059 |doi= 10.1083/jcb.200308007 }}
* {{cite journal | vauthors = Zhan X, Desiderio DM | title = Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry | journal = Anal. Biochem. | volume = 354 | issue = 2 | pages = 279–89 | year = 2006 | pmid = 16777052 | doi = 10.1016/j.ab.2006.05.024 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
*{{cite journal | author=Blanchetot C, Chagnon M, Dubé N, ''et al.'' |title=Substrate-trapping techniques in the identification of cellular PTP targets. |journal=Methods |volume=35 |issue= 1 |pages= 44-53 |year= 2005 |pmid= 15588985 |doi= 10.1016/j.ymeth.2004.07.007 }}
*{{cite journal | author=Vargo-Gogola T, Heckman BM, Gunther EJ, ''et al.'' |title=P190-B Rho GTPase-activating protein overexpression disrupts ductal morphogenesis and induces hyperplastic lesions in the developing mammary gland. |journal=Mol. Endocrinol. |volume=20 |issue= 6 |pages= 1391-405 |year= 2006 |pmid= 16469769 |doi= 10.1210/me.2005-0426 }}
*{{cite journal | author=Zhan X, Desiderio DM |title=Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry. |journal=Anal. Biochem. |volume=354 |issue= 2 |pages= 279-89 |year= 2006 |pmid= 16777052 |doi= 10.1016/j.ab.2006.05.024 }}
}}
{{refend}}
{{refend}}


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Revision as of 02:16, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Rho GTPase-activating protein 5 is an enzyme that in humans is encoded by the ARHGAP5 gene.[1][2]

Function

Rho GTPase activating protein 5 negatively regulates RHO GTPases, a family that may mediate cytoskeleton changes by stimulating the hydrolysis of bound GTP. Two transcript variants encoding different isoforms have been found for this gene.[2]

Interactions

ARHGAP5 has been shown to interact with Rnd1,[3] Rnd2,[3] Rnd3[3] and RHOA.[3]

References

  1. ↑ Burbelo PD, Miyamoto S, Utani A, Brill S, Yamada KM, Hall A, Yamada Y (Feb 1996). "p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking". J. Biol. Chem. 270 (52): 30919–26. doi:10.1074/jbc.270.52.30919. PMID 8537347. Check date values in: |year= / |date= mismatch (help)
  2. ↑ 2.0 2.1 "Entrez Gene: ARHGAP5 Rho GTPase activating protein 5".
  3. ↑ 3.0 3.1 3.2 3.3 Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Curr. Biol. 13 (13): 1106–15. doi:10.1016/S0960-9822(03)00418-4. PMID 12842009.

External links

Further reading


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