CPLM-008357

Genbank Nucleotide ID

Ras-related protein Rab-7a

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
21	LGDSGVGKTSLMNQY	ubiquitination	[1]
32	MNQYVNKKFSNQYKA	ubiquitination	[2]
38	KKFSNQYKATIGADF	ubiquitination	[1, 2, 3, 4, 5, 6]
48	IGADFLTKEVMVDDR	ubiquitination	[3, 7]
126	PFVVLGNKIDLENRQ	ubiquitination	[1, 3, 6]
137	ENRQVATKRAQAWCY	ubiquitination	[3, 6]
146	AQAWCYSKNNIPYFE	ubiquitination	[1]
157	PYFETSAKEAINVEQ	ubiquitination	[1, 3]
175	TIARNALKQETEVEL	ubiquitination	[3, 7]
191	NEFPEPIKLDKNDRA	ubiquitination	[1, 2, 3, 4, 6]
194	PEPIKLDKNDRAKAS	ubiquitination	[4, 6]

[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] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]

Functional Description

Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays a central role, not only in endosomal traffic, but also in many other cellular and physiological events, such as growth-factor-mediated cell signaling, nutrient- transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses. Microbial pathogens possess survival strategies governed by RAB7A, sometimes by employing RAB7A function (e.g. Salmonella) and sometimes by excluding RAB7A function (e.g. Mycobacterium). In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA. Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation.

NP_BIND 15 22 GTP (By similarity).
NP_BIND 63 67 GTP (By similarity).
NP_BIND 125 128 GTP (By similarity).
MOTIF 37 45 Effector region (By similarity).
MOD_RES 72 72 Phosphoserine.
MOD_RES 207 207 Cysteine methyl ester (By similarity).
LIPID 205 205 S-geranylgeranyl cysteine (By
LIPID 207 207 S-geranylgeranyl cysteine (By

3D-structure; Charcot-Marie-Tooth disease; Complete proteome; Cytoplasmic vesicle; Disease mutation; Endosome; GTP-binding; Lipoprotein; Lysosome; Membrane; Methylation; Neuropathy; Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport; Reference proteome; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0097208; C:alveolar lamellar body; IEA:Compara.
GO:0005794; C:Golgi apparatus; IDA:HPA.
GO:0005770; C:late endosome; IDA:UniProtKB.
GO:0005765; C:lysosomal membrane; TAS:Reactome.
GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO:0019003; F:GDP binding; IDA:BHF-UCL.
GO:0005525; F:GTP binding; IDA:BHF-UCL.
GO:0003924; F:GTPase activity; IDA:BHF-UCL.
GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO:0045453; P:bone resorption; IEA:Compara.
GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
GO:0008333; P:endosome to lysosome transport; IMP:BHF-UCL.
GO:0007174; P:epidermal growth factor catabolic process; IMP:BHF-UCL.
GO:0090383; P:phagosome acidification; IMP:UniProtKB.
GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
GO:0006622; P:protein targeting to lysosome; IMP:BHF-UCL.
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.