UniProt Accession

 GDIR1_MOUSE; Q99PT1; Q5M9P6; Q8BPI0; Q99KC4 

Genbank Protein ID

 AB055070; AK075656; AK077343; AK143516; AK156819; AK165241; AK170553; AK170718; AK172140; AL663030; BC004732; BC086755 

Genbank Nucleotide ID

 BAB21527.1; BAC35881.1; BAC36761.1; BAE25410.1; BAE33865.1; BAE38098.1; BAE41876.1; BAE41976.1; BAE42844.1; CAM27085.1; AAH04732.1; AAH86755.1 

Protein Name

 Rho GDP-dissociation inhibitor 1 

Protein Synonyms/Alias

 Rho GDI 1; GDI-1; Rho-GDI alpha 

Gene Name

 Arhgdia 

Gene Synonyms/Alias

 C87222; Gdi1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
28	DEHSVNYKPPAQKSI	acetylation	[1]
43	QEIQELDKDDESLRK	acetylation	[1, 2]
43	QEIQELDKDDESLRK	ubiquitination	[3]
52	DESLRKYKEALLGRV	acetylation	[2, 4]
52	DESLRKYKEALLGRV	succinylation	[2]
99	GDLESFKKQSFVLKE	acetylation	[4]
105	KKQSFVLKEGVEYRI	acetylation	[4]
127	REIVSGMKYIQHTYR	acetylation	[1, 4]
127	REIVSGMKYIQHTYR	ubiquitination	[3]
138	HTYRKGVKIDKTDYM	ubiquitination	[3]
141	RKGVKIDKTDYMVGS	acetylation	[1, 2, 4]
141	RKGVKIDKTDYMVGS	succinylation	[2]
141	RKGVKIDKTDYMVGS	ubiquitination	[3]
167	TPMEEAPKGMLARGS	acetylation	[1]
167	TPMEEAPKGMLARGS	ubiquitination	[3]
178	ARGSYNIKSRFTDDD	acetylation	[1, 2, 4]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 

Functional Description

 Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1 (By similarity). 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 105 105 N6-acetyllysine (By similarity).
 MOD_RES 127 127 N6-acetyllysine (By similarity).
 MOD_RES 141 141 N6-acetyllysine (By similarity).
 MOD_RES 178 178 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; GTPase activation; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 204 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0001772; C:immunological synapse; IDA:MGI.
 GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
 GO:0005094; F:Rho GDP-dissociation inhibitor activity; IDA:MGI.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0032880; P:regulation of protein localization; IDA:MGI.
 GO:0007266; P:Rho protein signal transduction; IDA:MGI. 

Interpro

 IPR014756; Ig_E-set.
 IPR000406; Rho_GDI.
 IPR024792; RhoGDI_domain. 

Pfam

 PF02115; Rho_GDI 

SMART

  

PROSITE

  

PRINTS

 PR00492; RHOGDI.