CPLM-009292

Genbank Nucleotide ID

Ras-related protein Rab-10

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
102	KSFENISKWLRNIDE	acetylation	[1, 2]
102	KSFENISKWLRNIDE	ubiquitination	[3, 4, 5, 6]
129	NKCDMDDKRVVPKGK	ubiquitination	[4]
154	RFFETSAKANINIEK	ubiquitination	[4]
177	ILRKTPVKEPNSENV	ubiquitination	[4]

[1] 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]
[2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[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] 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]
[5] 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]
[6] 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]

Functional Description

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. According to PubMed:23263280, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion.

NP_BIND 16 23 GTP (By similarity).
NP_BIND 64 68 GTP (By similarity).
NP_BIND 122 125 GTP (By similarity).
MOTIF 38 46 Effector region (By similarity).
MOD_RES 102 102 N6-acetyllysine.
LIPID 199 199 S-geranylgeranyl cysteine (By
LIPID 200 200 S-geranylgeranyl cysteine (By

Acetylation; Cell projection; Complete proteome; Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB.
GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO:0032593; C:insulin-responsive compartment; IDA:UniProtKB.
GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO:0072372; C:primary cilium; IDA:UniProtKB.
GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
GO:0019003; F:GDP binding; IDA:UniProtKB.
GO:0005525; F:GTP binding; IDA:UniProtKB.
GO:0003924; F:GTPase activity; EXP:Reactome.
GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO:0061467; P:basolateral protein localization; ISS:UniProtKB.
GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IMP:UniProtKB.
GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.

IPR027417; P-loop_NTPase.
IPR005225; Small_GTP-bd_dom.
IPR001806; Small_GTPase.
IPR003579; Small_GTPase_Rab_type.

PR00449; RASTRNSFRMNG.