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Identification
HMDB Protein ID HMDBP01959
Secondary Accession Numbers
  • 7384
Name Transforming protein RhoA
Synonyms
  1. Rho cDNA clone 12
  2. h12
Gene Name RHOA
Protein Type Unknown
Biological Properties
General Function Involved in GTP binding
Specific Function Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
purine nucleotide binding
binding
nucleotide binding
guanyl nucleotide binding
guanyl ribonucleotide binding
gtp binding
Process
biological regulation
regulation of biological process
regulation of cellular process
signal transduction
intracellular signal transduction
small gtpase mediated signal transduction
Cellular Location
  1. Cell membrane
  2. Lipid-anchor
  3. Cytoplasm
  4. Cytoplasmic side
  5. cytoskeleton
Gene Properties
Chromosome Location Chromosome:3
Locus 3p21.3
SNPs RHOA
Gene Sequence
>582 bp
ATGGCTGCCATCCGGAAGAAACTGGTGATTGTTGGTGATGGAGCCTGTGGAAAGACATGC
TTGCTCATAGTCTTCAGCAAGGACCAGTTCCCAGAGGTGTATGTGCCCACAGTGTTTGAG
AACTATGTGGCAGATATCGAGGTGGATGGAAAGCAGGTAGAGTTGGCTTTGTGGGACACA
GCTGGGCAGGAAGATTATGATCGCCTGAGGCCCCTCTCCTACCCAGATACCGATGTTATA
CTGATGTGTTTTTCCATCGACAGCCCTGATAGTTTAGAAAACATCCCAGAAAAGTGGACC
CCAGAAGTCAAGCATTTCTGTCCCAACGTGCCCATCATCCTGGTTGGGAATAAGAAGGAT
CTTCGGAATGATGAGCACACAAGGCGGGAGCTAGCCAAGATGAAGCAGGAGCCGGTGAAA
CCTGAAGAAGGCAGAGATATGGCAAACAGGATTGGCGCTTTTGGGTACATGGAGTGTTCA
GCAAAGACCAAAGATGGAGTGAGAGAGGTTTTTGAAATGGCTACGAGAGCTGCTCTGCAA
GCTAGACGTGGGAAGAAAAAATCTGGTTGCCTTGTCTTGTGA
Protein Properties
Number of Residues 193
Molecular Weight 21767.9
Theoretical pI 5.89
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Transforming protein RhoA
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
GenBank ID Protein 36030
UniProtKB/Swiss-Prot ID P61586
UniProtKB/Swiss-Prot Entry Name RHOA_HUMAN
PDB IDs
GenBank Gene ID X05026
GeneCard ID RHOA
GenAtlas ID RHOA
HGNC ID HGNC:667
References
General References
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  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  3. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  4. Houssa B, de Widt J, Kranenburg O, Moolenaar WH, van Blitterswijk WJ: Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA. J Biol Chem. 1999 Mar 12;274(11):6820-2. [PubMed:10066731 ]
  5. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed:1556108 ]
  6. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S: The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996 Apr 15;15(8):1885-93. [PubMed:8617235 ]
  7. Maesaki R, Shimizu T, Ihara K, Kuroda S, Kaibuchi K, Hakoshima T: Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA. J Struct Biol. 1999 Jun 15;126(2):166-70. [PubMed:10388627 ]
  8. Ren Y, Li R, Zheng Y, Busch H: Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J Biol Chem. 1998 Dec 25;273(52):34954-60. [PubMed:9857026 ]
  9. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. doi: 10.1016/j.molcel.2009.03.008. [PubMed:19362538 ]
  10. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. doi: 10.1126/science.1166382. Epub 2008 Nov 27. [PubMed:19039103 ]
  11. Yeramian P, Chardin P, Madaule P, Tavitian A: Nucleotide sequence of human rho cDNA clone 12. Nucleic Acids Res. 1987 Feb 25;15(4):1869. [PubMed:3822842 ]
  12. Fagan KP, Oliveira L, Pittler SJ: Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts. Exp Eye Res. 1994 Aug;59(2):235-7. [PubMed:7835413 ]
  13. Moscow JA, He R, Gudas JM, Cowan KH: Utilization of multiple polyadenylation signals in the human RHOA protooncogene. Gene. 1994 Jul 8;144(2):229-36. [PubMed:8039707 ]
  14. Nemoto Y, Namba T, Teru-uchi T, Ushikubi F, Morii N, Narumiya S: A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein. J Biol Chem. 1992 Oct 15;267(29):20916-20. [PubMed:1328215 ]
  15. Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K: Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 1996 May 1;15(9):2208-16. [PubMed:8641286 ]
  16. Pastey MK, Crowe JE Jr, Graham BS: RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation. J Virol. 1999 Sep;73(9):7262-70. [PubMed:10438814 ]
  17. Reynaud C, Fabre S, Jalinot P: The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element. J Biol Chem. 2000 Oct 27;275(43):33962-8. [PubMed:10940294 ]
  18. Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 2001 Nov 2;507(3):264-8. [PubMed:11696353 ]
  19. Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K: XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. J Biol Chem. 2002 Nov 8;277(45):42964-72. Epub 2002 Sep 6. [PubMed:12221096 ]
  20. Shao F, Merritt PM, Bao Z, Innes RW, Dixon JE: A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 2002 May 31;109(5):575-88. [PubMed:12062101 ]
  21. Wing MR, Snyder JT, Sondek J, Harden TK: Direct activation of phospholipase C-epsilon by Rho. J Biol Chem. 2003 Oct 17;278(42):41253-8. Epub 2003 Aug 4. [PubMed:12900402 ]
  22. Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE: Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):904-9. Epub 2003 Jan 21. [PubMed:12538863 ]
  23. Chen Y, Yang Z, Meng M, Zhao Y, Dong N, Yan H, Liu L, Ding M, Peng HB, Shao F: Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Mol Cell. 2009 Sep 24;35(6):841-55. doi: 10.1016/j.molcel.2009.09.004. [PubMed:19782033 ]
  24. Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS: Crystal structure of RhoA-GDP and its functional implications. Nat Struct Biol. 1997 Sep;4(9):699-703. [PubMed:9302995 ]
  25. Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T: Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J Biol Chem. 1998 Apr 17;273(16):9656-66. [PubMed:9545299 ]
  26. Shimizu T, Ihara K, Maesaki R, Kuroda S, Kaibuchi K, Hakoshima T: An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism. J Biol Chem. 2000 Jun 16;275(24):18311-7. [PubMed:10748207 ]
  27. Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF: MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81. [PubMed:11927263 ]
  28. Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J: Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat Struct Biol. 2002 Jun;9(6):468-75. [PubMed:12006984 ]
  29. Longenecker K, Read P, Lin SK, Somlyo AP, Nakamoto RK, Derewenda ZS: Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):876-80. Epub 2003 Apr 25. [PubMed:12777804 ]