UniProt Accession

 RHOA_HUMAN; P61586; P06749; Q53HM4; Q5U024; Q9UDJ0; Q9UEJ4 

Genbank Protein ID

 X05026; L25080; AF498970; BT019870; AK222556; BX647063; AC104452; AC121247; AC137114; BC001360; BC005976; L09159; M83094 

Genbank Nucleotide ID

 CAA28690.1; AAC33178.1; AAM21117.1; AAV38673.1; BAD96276.1; CAE46190.1; AAH01360.1; AAH05976.1; AAA50612.1; AAA67539.1 

Protein Name

 Transforming protein RhoA 

Protein Synonyms/Alias

 Rho cDNA clone 12; h12 

Gene Name

 RHOA 

Gene Synonyms/Alias

 ARH12; ARHA; RHO12 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MAAIRKKLVIVGD	ubiquitination	[1, 2]
7	*MAAIRKKLVIVGDG	ubiquitination	[1, 2]
104	EKWTPEVKHFCPNVP	ubiquitination	[3, 4]
118	PIILVGNKKDLRNDE	ubiquitination	[2]
119	IILVGNKKDLRNDEH	ubiquitination	[2]
133	HTRRELAKMKQEPVK	ubiquitination	[5, 6]
135	RRELAKMKQEPVKPE	ubiquitination	[2, 4, 5, 6, 7, 8, 9]
140	KMKQEPVKPEEGRDM	ubiquitination	[5]
162	GYMECSAKTKDGVRE	ubiquitination	[1, 2, 6, 9]
164	MECSAKTKDGVREVF	ubiquitination	[2, 6]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA- DIAPH1 signaling pathway plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. 

Sequence Annotation

 NP_BIND 12 19 GTP.
 NP_BIND 59 63 GTP (By similarity).
 NP_BIND 117 120 GTP.
 MOTIF 34 42 Effector region (Potential).
 MOD_RES 34 34 O-AMP-tyrosine; by Haemophilus IbpA.
 MOD_RES 37 37 O-AMP-threonine; by Vibrio VopS.
 MOD_RES 41 41 ADP-ribosylasparagine; by botulinum toxin
 MOD_RES 188 188 Phosphoserine; by PKG/PRKG1.
 MOD_RES 190 190 Cysteine methyl ester.
 LIPID 190 190 S-geranylgeranyl cysteine.  

Keyword

 3D-structure; ADP-ribosylation; Cell cycle; Cell division; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding; Host-virus interaction; Lipoprotein; Magnesium; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Prenylation; Proto-oncogene; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 193 AA 

Protein Sequence

Gene Ontology

 GO:0043296; C:apical junction complex; IDA:UniProtKB.
 GO:0030424; C:axon; IEA:Compara.
 GO:0005938; C:cell cortex; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; TAS:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; TAS:UniProtKB.
 GO:0030521; P:androgen receptor signaling pathway; IEA:Compara.
 GO:0043297; P:apical junction assembly; IMP:UniProtKB.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007160; P:cell-matrix adhesion; IEA:Compara.
 GO:0036089; P:cleavage furrow formation; IDA:UniProtKB.
 GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
 GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Compara.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0045665; P:negative regulation of neuron differentiation; IEA:Compara.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0043931; P:ossification involved in bone maturation; ISS:BHF-UCL.
 GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome.
 GO:0045785; P:positive regulation of cell adhesion; IEA:Compara.
 GO:0030307; P:positive regulation of cell growth; IEA:Compara.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara.
 GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEP:UniProtKB.
 GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Compara.
 GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
 GO:0042346; P:positive regulation of NF-kappaB import into nucleus; NAS:UniProtKB.
 GO:0071803; P:positive regulation of podosome assembly; IEA:Compara.
 GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI.
 GO:0045727; P:positive regulation of translation; IEA:Compara.
 GO:0045907; P:positive regulation of vasoconstriction; IEA:Compara.
 GO:0051924; P:regulation of calcium ion transport; IEA:Compara.
 GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
 GO:0050773; P:regulation of dendrite development; IEA:Compara.
 GO:0033688; P:regulation of osteoblast proliferation; ISS:BHF-UCL.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0009749; P:response to glucose stimulus; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0009612; P:response to mechanical stimulus; IEA:Compara.
 GO:0007266; P:Rho protein signal transduction; TAS:UniProtKB.
 GO:0007519; P:skeletal muscle tissue development; IEA:Compara.
 GO:0090307; P:spindle assembly involved in mitosis; IMP:BHF-UCL.
 GO:0043149; P:stress fiber assembly; IEA:Compara.
 GO:0031098; P:stress-activated protein kinase signaling cascade; IEA:Compara.
 GO:0061383; P:trabecula morphogenesis; ISS:BHF-UCL.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR003578; Small_GTPase_Rho. 

Pfam

 PF00071; Ras 

SMART

 SM00174; RHO 

PROSITE

 PS51420; RHO 

PRINTS

 PR00449; RASTRNSFRMNG.