CANFA:RAB7A

Species (Taxon ID)	Canis familiaris (Dog) (Canis lupus familiaris). (9615)
Gene Name(s)	RAB7A (synonyms: RAB7)
Protein Name(s)	Ras-related protein Rab-7a
External Links
UniProt	P18067
EMBL	M35522
PIR	B30413
RefSeq	NP_001003316.1 XP_005632072.1
UniGene	Cfa.29293
ProteinModelPortal	P18067
SMR	P18067
IntAct	P18067
MINT	MINT-8387239
STRING	9615.ENSCAFP00000034211
BindingDB	P18067
PaxDb	P18067
PRIDE	P18067
Ensembl	ENSCAFT00000038482
GeneID	404007
KEGG	cfa:404007
CTD	7879
eggNOG	COG1100
GeneTree	ENSGT00760000119125
HOGENOM	HOG000233968
HOVERGEN	HBG009351
InParanoid	P18067
KO	K07897
OMA	DYPDPIK
OrthoDB	EOG7G4QG8
TreeFam	TF105605
Reactome	REACT_221251
NextBio	20817494
Proteomes	UP000002254
GO	GO:0070062 GO:0005794 GO:0005770 GO:0005764 GO:0042470 GO:0045335 GO:0030670 GO:0019003 GO:0005525 GO:0045022 GO:0008333 GO:0007174 GO:0090383 GO:0090385 GO:0006622 GO:0007264
Gene3D	3.40.50.300
InterPro	IPR027417 IPR005225 IPR001806 IPR003579
Pfam	PF00071
PRINTS	PR00449
SMART	SM00175
SUPFAM	SSF52540
TIGRFAMs	TIGR00231
PROSITE	PS51419

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005525	GTP binding	PMID:18272684^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Figure1A: GTP overlay tested by SDS-page analysis showed that the Rab7 wild type isoform and the active mutant isoforms of the protein where able to bind to the radioactive GTP while the dominant negative mutant, Rab7T22N, (which had a reduced affinity to GTP) didn’t bind since no band was seen in the gel. Figure 1B: Western Blot analysis made with a monoclonal anti-Myc antibody showed the expression of the Myc-tagged Rab7 wild type protein as well.All this indicates that the Rab7 protein binds to GTP.	complete
	GO:0005097	Rab GTPase activator activity	PMID:18272684^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Figure 2 A: Mutated protein isoforms showed slower GTPase hydrolysis than the Rab7 wild type.	complete
	GO:0002057	guanine binding	PMID:18272684^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Figure 2 B&C: The figures demonstrating the measurement of the GTPase activity of the His-tagged proteins show that the wild type Rab7 protein had a high affinity for guanine nucleotides specifically when GDP was added compared to the mutated Rab7 proteins associated with Charcot Marie Tooth Disease Type 2B	complete
	GO:0005515	protein binding	PMID:18272684^[1]	ECO:0000021	physical interaction evidence	UniProtKB:Q96NA2	F	Figure. 4 : Using two hybrid assays ;the wild type of Rab7 and the CMT2B-associated Rab7 mutants were interacting strongly with RILP .Also Rab7 Q67L (which is an active mutated Rab7 protein impaired in GTP hydrolysis not GTP binding ) showed a strong interaction with RILP compared to the interaction of the dominant-negative mutant Rab7 T22N which was extremely weak .	complete
	GO:0005770	late endosome	PMID:18272684^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	(Figure. 6M–X): When co-expressed with RILP,the Rab7 wild type, Rab7 Q67L and the CMT2B-associated Rab7 mutant proteins were present on the clustered endosomal structures. Which indicates that Rab7 not only interacts with RILP but it also colocalizes with RILP.	complete
part_of	GO:0070382	exocytic vesicle	PMID:18504258^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0098993	anchored component of synaptic vesicle membrane	PMID:20926670^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0032419	extrinsic component of lysosome membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51150	C	Seeded From UniProt	complete
part_of	GO:0031902	late endosome membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51150	C	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51150	C	Seeded From UniProt	complete
involved_in	GO:0061724	lipophagy	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51150	P	Seeded From UniProt	complete
involved_in	GO:0090385	phagosome-lysosome fusion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51149	P	Seeded From UniProt	complete
involved_in	GO:0090383	phagosome acidification	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51149	P	Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51149	C	Seeded From UniProt	complete
involved_in	GO:0045022	early endosome to late endosome transport	PMID:8522602^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007174	epidermal growth factor catabolic process	PMID:16282324^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P51149	C	Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2442295 PANTHER:PTN000635769 UniProtKB:P51149 UniProtKB:Q96AH8 WB:WBGene00004271	C	Seeded From UniProt	complete
involved_in	GO:0032482	Rab protein signal transduction	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015790 PANTHER:PTN001292747 RGD:3529 dictyBase:DDB_G0269238	P	Seeded From UniProt	complete
involved_in	GO:0008333	endosome to lysosome transport	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015795 PANTHER:PTN001178536 UniProtKB:P51149	P	Seeded From UniProt	complete
involved_in	GO:0006886	intracellular protein transport	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1914292 PANTHER:PTN001292747 TAIR:locus:2094029 TAIR:locus:2123010 UniProtKB:Q9BW83	P	Seeded From UniProt	complete
part_of	GO:0005774	vacuolar membrane	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000635769 UniProtKB:C8VQY7	C	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015795 MGI:MGI:2442295 PANTHER:PTN000635769 UniProtKB:Q96AH8 WB:WBGene00004271	C	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015795 MGI:MGI:105068 MGI:MGI:2442295 PANTHER:PTN000635769 RGD:61908 UniProtKB:P51149 UniProtKB:Q96AH8 WB:WBGene00004271	C	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2442295 PANTHER:PTN000635769 UniProtKB:Q96AH8 WB:WBGene00004271 dictyBase:DDB_G0269236	C	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2442295 PANTHER:PTN000635769 UniProtKB:P51149 UniProtKB:Q96AH8 WB:WBGene00004271 dictyBase:DDB_G0269236	C	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015790 FB:FBgn0015797 FB:FBgn0016700 MGI:MGI:104606 MGI:MGI:105072 MGI:MGI:105926 MGI:MGI:1861441 MGI:MGI:1931295 MGI:MGI:2443036 MGI:MGI:99425 PANTHER:PTN001292747 PomBase:SPAC1565.06c PomBase:SPAC4C5.02c PomBase:SPBC1703.10 RGD:3529 RGD:619762 SGD:S000000833 SGD:S000001722 SGD:S000001856 SGD:S000001889 SGD:S000003178 SGD:S000004252 SGD:S000004460 SGD:S000004529 SGD:S000005037 SGD:S000005615 TAIR:locus:2041036 TAIR:locus:2082672 TAIR:locus:2202280 TAIR:locus:505006713 UniProtKB:P20336 UniProtKB:P20337 UniProtKB:P20338 UniProtKB:P20339 UniProtKB:P20340 UniProtKB:P51148 UniProtKB:P51149 UniProtKB:P51151 UniProtKB:P61006 UniProtKB:P61019 UniProtKB:P61020 UniProtKB:P61106 UniProtKB:P62491 UniProtKB:P62820 UniProtKB:Q13637 UniProtKB:Q14088 UniProtKB:Q15286 UniProtKB:Q15907 UniProtKB:Q86YS6 UniProtKB:Q96E17 UniProtKB:Q9H082 UniProtKB:Q9H0N0 UniProtKB:Q9H0T7 UniProtKB:Q9UL25 UniProtKB:Q9UL26 UniProtKB:Q9ULC3 WB:WBGene00004268 WB:WBGene00004271 WB:WBGene00006833	F	Seeded From UniProt	complete
involved_in	GO:0090385	phagosome-lysosome fusion	PMID:21873635^[6]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000635769 UniProtKB:P51149	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0045022	C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0045022	C	Seeded From UniProt	complete
involved_in	GO:0000045	autophagosome assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0061724	lipophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	P	Seeded From UniProt	complete
part_of	GO:0034045	phagophore assembly site membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0032419	extrinsic component of lysosome membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0031902	late endosome membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51150 ensembl:ENSMUSP00000109230	C	Seeded From UniProt	complete
enables	GO:1905394	retromer complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	F	Seeded From UniProt	complete
involved_in	GO:1903543	positive regulation of exosomal secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:1903542	negative regulation of exosomal secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0090385	phagosome-lysosome fusion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0090383	phagosome acidification	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0048524	positive regulation of viral process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
involved_in	GO:0045022	early endosome to late endosome transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0042147	retrograde transport, endosome to Golgi	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
part_of	GO:0030904	retromer complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
involved_in	GO:0022615	protein to membrane docking	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0019076	viral release from host cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
enables	GO:0019003	GDP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	F	Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
involved_in	GO:0008333	endosome to lysosome transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0007174	epidermal growth factor catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
involved_in	GO:0006622	protein targeting to lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	P	Seeded From UniProt	complete
part_of	GO:0005770	late endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	F	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P51149 ensembl:ENSP00000265062	F	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:A0A158RFU6 ensembl:ENSP00000265062	C	Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806	F	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001806 InterPro:IPR005225	F	Seeded From UniProt	complete
involved_in	GO:0016042	lipid catabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0442	P	Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0967	C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
involved_in	GO:0015031	protein transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0653	P	Seeded From UniProt	complete
involved_in	GO:0006629	lipid metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0443	P	Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F	Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0968	C	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0551 UniProtKB-SubCell:SL-0154	C	Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0072	P	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0458	C	Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0157	C	Seeded From UniProt	complete
part_of	GO:0031902	late endosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0151	C	Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0100	C	Seeded From UniProt	complete
part_of	GO:0000421	autophagosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0022	C	Seeded From UniProt	complete
part_of	GO:0033162	melanosome membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0160	C	Seeded From UniProt	complete
part_of	GO:0030670	phagocytic vesicle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0205	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Spinosa, MR et al. (2008) Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28 1640-8 PubMed GONUTS page
↑ Cao, Z et al. (2008) Use of fluorescence-activated vesicle sorting for isolation of Naked2-associated, basolaterally targeted exocytic vesicles for proteomics analysis. Mol. Cell Proteomics 7 1651-67 PubMed GONUTS page
↑ Pavlos, NJ et al. (2010) Quantitative analysis of synaptic vesicle Rabs uncovers distinct yet overlapping roles for Rab3a and Rab27b in Ca2+-triggered exocytosis. J. Neurosci. 30 13441-53 PubMed GONUTS page
↑ Feng, Y et al. (1995) Rab 7: an important regulator of late endocytic membrane traffic. J. Cell Biol. 131 1435-52 PubMed GONUTS page
↑ Ceresa, BP & Bahr, SJ (2006) rab7 activity affects epidermal growth factor:epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome. J. Biol. Chem. 281 1099-106 PubMed GONUTS page
↑ ^6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18272684-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Spinosa, MR et al. (2008) Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28 1640-8 PubMed GONUTS page

[PMID:18504258-2] Cao, Z et al. (2008) Use of fluorescence-activated vesicle sorting for isolation of Naked2-associated, basolaterally targeted exocytic vesicles for proteomics analysis. Mol. Cell Proteomics 7 1651-67 PubMed GONUTS page

[PMID:20926670-3] Pavlos, NJ et al. (2010) Quantitative analysis of synaptic vesicle Rabs uncovers distinct yet overlapping roles for Rab3a and Rab27b in Ca2+-triggered exocytosis. J. Neurosci. 30 13441-53 PubMed GONUTS page

[PMID:8522602-4] Feng, Y et al. (1995) Rab 7: an important regulator of late endocytic membrane traffic. J. Cell Biol. 131 1435-52 PubMed GONUTS page

[PMID:16282324-5] Ceresa, BP & Bahr, SJ (2006) rab7 activity affects epidermal growth factor:epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome. J. Biol. Chem. 281 1099-106 PubMed GONUTS page

[PMID:21873635-6] 6.00 ^6.01 ^6.02 ^6.03 ^6.04 ^6.05 ^6.06 ^6.07 ^6.08 ^6.09 ^6.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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CANFA:RAB7A

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