CPLM-008508

Genbank Nucleotide ID

Rho GDP-dissociation inhibitor 1

Protein Synonyms/Alias

Rho GDI 1; Rho-GDI alpha

Homo sapiens (Human)

Position	Peptide	Type	References
28	DEHSVNYKPPAQKSI	ubiquitination	[1]
50	KDDESLRKYKEALLG	methylation	[2]
50	KDDESLRKYKEALLG	ubiquitination	[1]
52	DESLRKYKEALLGRV	methylation	[2]
52	DESLRKYKEALLGRV	ubiquitination	[1, 3]
99	GDLESFKKQSFVLKE	ubiquitination	[1, 4]
105	KKQSFVLKEGVEYRI	acetylation	[5]
127	REIVSGMKYIQHTYR	acetylation	[5]
127	REIVSGMKYIQHTYR	ubiquitination	[1, 3, 4]
141	RKGVKIDKTDYMVGS	acetylation	[5, 6, 7]
141	RKGVKIDKTDYMVGS	ubiquitination	[1, 3, 8, 9, 10, 11]
167	TPVEEAPKGMLARGS	ubiquitination	[1, 3, 4, 9, 11, 12]
178	ARGSYSIKSRFTDDD	acetylation	[5]
178	ARGSYSIKSRFTDDD	ubiquitination	[1]
186	SRFTDDDKTDHLSWE	ubiquitination	[4, 12, 13]

[1] 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]
[2] Proteomics study reveals cross-talk between Rho guanidine nucleotide dissociation inhibitor 1 post-translational modifications in epidermal growth factor stimulated fibroblasts.
Guerrera IC, Keep NH, Godovac-Zimmermann J.
J Proteome Res. 2007 Jul;6(7):2623-30. [PMID: 17506542]
[3] 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]
[4] 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]
[5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[7] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[9] 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]
[10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[11] 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]
[12] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[13] 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]

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).

MOD_RES 2 2 N-acetylalanine.
MOD_RES 105 105 N6-acetyllysine.
MOD_RES 127 127 N6-acetyllysine.
MOD_RES 141 141 N6-acetyllysine.
MOD_RES 178 178 N6-acetyllysine.

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0001772; C:immunological synapse; IEA:Compara.
GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO:0005094; F:Rho GDP-dissociation inhibitor activity; TAS:ProtInc.
GO:0006928; P:cellular component movement; TAS:UniProtKB.
GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome.
GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
GO:0032880; P:regulation of protein localization; IEA:Compara.
GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.

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