HUMAN:RAB7A

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	RAB7A (synonyms: RAB7)
Protein Name(s)	Ras-related protein Rab-7a
External Links
UniProt	P51149
EMBL	X93499 U44104 AF050175 AF498942 AK000826 AK290721 BC008721 CH471052
CCDS	CCDS3052.1
PIR	JC5268
RefSeq	NP_004628.4
UniGene	Hs.744853
PDB	1T91 1YHN 3LAW
PDBsum	1T91 1YHN 3LAW
ProteinModelPortal	P51149
SMR	P51149
BioGrid	113624
DIP	DIP-39879N
IntAct	P51149
MINT	MINT-4999676
STRING	9606.ENSP00000265062
PhosphoSite	P51149
DMDM	1709999
MaxQB	P51149
PaxDb	P51149
PeptideAtlas	P51149
PRIDE	P51149
DNASU	7879
Ensembl	ENST00000265062
GeneID	7879
KEGG	hsa:7879
UCSC	uc003eks.1
CTD	7879
GeneCards	GC03P128444
GeneReviews	RAB7A
HGNC	HGNC:9788
HPA	CAB037131 HPA006964
MIM	600882 602298
neXtProt	NX_P51149
Orphanet	99936
PharmGKB	PA162400619
eggNOG	COG1100
GeneTree	ENSGT00760000119125
HOGENOM	HOG000233968
HOVERGEN	HBG009351
InParanoid	P51149
KO	K07897
OMA	DYPDPIK
PhylomeDB	P51149
TreeFam	TF105605
Reactome	REACT_121399
SignaLink	P51149
ChiTaRS	RAB7A
EvolutionaryTrace	P51149
GeneWiki	RAB7A
GenomeRNAi	7879
NextBio	30336
PRO	PR:P51149
Proteomes	UP000005640
Bgee	P51149
CleanEx	HS_RAB7A
ExpressionAtlas	P51149
Genevestigator	P51149
GO	GO:0097208 GO:0070062 GO:0005794 GO:0043231 GO:0005770 GO:0005765 GO:0005764 GO:0042470 GO:0045335 GO:0030670 GO:0019003 GO:0005525 GO:0003924 GO:0019886 GO:0045453 GO:0045022 GO:0006897 GO:0008333 GO:0007174 GO:0006184 GO:0090383 GO:0090382 GO:0090385 GO:1903543 GO:0006622 GO:0015031 GO:2000785 GO:0042147 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	Extension	Notes	Status
	GO:0045732	positive regulation of protein catabolic process	PMID:22072966^[1]	ECO:0000315			P		Fig. 6A, and Fig. 7A	complete CACAO 3057
	GO:0009405	pathogenesis	PMID:22072966^[1]	ECO:0000315			P		Fig. 2C	complete CACAO 3059
	GO:0019076	release of virus from host	PMID:22072966^[1]	ECO:0000315			P		Fig. 2AB and Fig. 5	complete CACAO 3060
	GO:0048524	positive regulation of viral reproduction	PMID:22072966^[1]	ECO:0000315			P		Fig. 1A, 1B	complete CACAO 3061
part_of	GO:0010008	endosome membrane	PMID:22431521^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903542	negative regulation of exosomal secretion	PMID:26911690^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0010008	endosome membrane	PMID:26911690^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1905394	retromer complex binding	PMID:27385586^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:Q96QK1)	Seeded From UniProt	complete
involved_in	GO:0000045	autophagosome assembly	PMID:19956673^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		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
part_of	GO:0005770	late endosome	PMID:17010938^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(GO:0048471)	Seeded From UniProt	complete
involved_in	GO:0048524	positive regulation of viral process	PMID:22072966^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019076	viral release from host cell	PMID:22072966^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:22072966^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0022615	protein to membrane docking	PMID:24344282^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0030904	retromer complex	PMID:19531583^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0042147	retrograde transport, endosome to Golgi	PMID:19531583^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0030904	retromer complex	PMID:24344282^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903543	positive regulation of exosomal secretion	PMID:22660413^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
enables	GO:0019003	GDP binding	PMID:18272684^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008333	endosome to lysosome transport	PMID:18272684^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007174	epidermal growth factor catabolic process	PMID:18272684^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006622	protein targeting to lysosome	PMID:22115783^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q96S99)	Seeded From UniProt	complete
colocalizes_with	GO:0005770	late endosome	PMID:18272684^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0005764	lysosome	PMID:18272684^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	PMID:18272684^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:18272684^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090385	phagosome-lysosome fusion	PMID:21255211^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090383	phagosome acidification	PMID:21255211^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	PMID:21255211^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045022	early endosome to late endosome transport	PMID:14617358^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:14617358^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090385	phagosome-lysosome fusion	PMID:21873635^[17]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000635769 UniProtKB:P51149	P		Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	PMID:21873635^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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^[17]	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
part_of	GO:0005770	late endosome	PMID:15078902^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:15078902^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		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: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:1905366	negative regulation of intralumenal vesicle formation	PMID:26911690^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902583	multi-organism intracellular transport	PMID:22042847^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	PMID:2115402^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:2115402^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:8954989^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090382	phagosome maturation	PMID:19392663^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0015031	protein transport	PMID:19392663^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030667	secretory granule membrane	Reactome:R-HSA-6798743	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019886	antigen processing and presentation of exogenous peptide antigen via MHC class II	Reactome:R-HSA-2132295	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-6798743	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-8877451	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	Reactome:R-HSA-8877451 Reactome:R-HSA-8854329 Reactome:R-HSA-8854255 Reactome:R-HSA-2213248	ECO:0000304	author statement supported by traceable reference used in manual assertion		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: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: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
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
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: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
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
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
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: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: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: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: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
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: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
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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 ^1.5 ^1.6 Caillet, M et al. (2011) Rab7A is required for efficient production of infectious HIV-1. PLoS Pathog. 7 e1002347 PubMed GONUTS page
↑ Mamo, A et al. (2012) The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting. Mol. Cell. Biol. 32 1855-66 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Song, P et al. (2016) Parkin Modulates Endosomal Organization and Function of the Endo-Lysosomal Pathway. J. Neurosci. 36 2425-37 PubMed GONUTS page
↑ Follett, J et al. (2016) Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal Association of Retromer and Induces α-Synuclein Aggregation. J. Biol. Chem. 291 18283-98 PubMed GONUTS page
↑ Yamaguchi, H et al. (2009) An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7. PLoS Pathog. 5 e1000670 PubMed GONUTS page
↑ Wang, T & Hong, W (2006) RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment. Biochem. Biophys. Res. Commun. 350 413-23 PubMed GONUTS page
↑ ^7.0 ^7.1 Harrison, MS et al. (2014) A mechanism for retromer endosomal coat complex assembly with cargo. Proc. Natl. Acad. Sci. U.S.A. 111 267-72 PubMed GONUTS page
↑ ^8.0 ^8.1 Seaman, MN et al. (2009) Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. J. Cell. Sci. 122 2371-82 PubMed GONUTS page
↑ Baietti, MF et al. (2012) Syndecan-syntenin-ALIX regulates the biogenesis of exosomes. Nat. Cell Biol. 14 677-85 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 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
↑ Lin, WJ et al. (2012) Lysosomal targeting of phafin1 mediated by Rab7 induces autophagosome formation. Biochem. Biophys. Res. Commun. 417 35-42 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Seto, S et al. (2011) Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic 12 407-20 PubMed GONUTS page
↑ ^16.0 ^16.1 Stein, MP et al. (2003) Human VPS34 and p150 are Rab7 interacting partners. Traffic 4 754-71 PubMed GONUTS page
↑ ^17.00 ^17.01 ^17.02 ^17.03 ^17.04 ^17.05 ^17.06 ^17.07 ^17.08 ^17.09 ^17.10 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^18.0 ^18.1 Seaman, MN (2004) Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165 111-22 PubMed GONUTS page
↑ Spanò, S et al. (2011) Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella. Proc. Natl. Acad. Sci. U.S.A. 108 18418-23 PubMed GONUTS page
↑ ^20.0 ^20.1 Chavrier, P et al. (1990) Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62 317-29 PubMed GONUTS page
↑ Vitelli, R et al. (1996) Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid. Biochem. Biophys. Res. Commun. 229 887-90 PubMed GONUTS page
↑ ^22.0 ^22.1 Zhang, M et al. (2009) Rab7: roles in membrane trafficking and disease. Biosci. Rep. 29 193-209 PubMed GONUTS page

[PMID:22072966-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Caillet, M et al. (2011) Rab7A is required for efficient production of infectious HIV-1. PLoS Pathog. 7 e1002347 PubMed GONUTS page

[PMID:22431521-2] Mamo, A et al. (2012) The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting. Mol. Cell. Biol. 32 1855-66 PubMed GONUTS page

[PMID:26911690-3] 3.0 ^3.1 ^3.2 Song, P et al. (2016) Parkin Modulates Endosomal Organization and Function of the Endo-Lysosomal Pathway. J. Neurosci. 36 2425-37 PubMed GONUTS page

[PMID:27385586-4] Follett, J et al. (2016) Parkinson Disease-linked Vps35 R524W Mutation Impairs the Endosomal Association of Retromer and Induces α-Synuclein Aggregation. J. Biol. Chem. 291 18283-98 PubMed GONUTS page

[PMID:19956673-5] Yamaguchi, H et al. (2009) An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7. PLoS Pathog. 5 e1000670 PubMed GONUTS page

[PMID:17010938-6] Wang, T & Hong, W (2006) RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment. Biochem. Biophys. Res. Commun. 350 413-23 PubMed GONUTS page

[PMID:24344282-7] 7.0 ^7.1 Harrison, MS et al. (2014) A mechanism for retromer endosomal coat complex assembly with cargo. Proc. Natl. Acad. Sci. U.S.A. 111 267-72 PubMed GONUTS page

[PMID:19531583-8] 8.0 ^8.1 Seaman, MN et al. (2009) Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. J. Cell. Sci. 122 2371-82 PubMed GONUTS page

[PMID:22660413-9] Baietti, MF et al. (2012) Syndecan-syntenin-ALIX regulates the biogenesis of exosomes. Nat. Cell Biol. 14 677-85 PubMed GONUTS page

[PMID:23533145-10] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-11] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-12] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:18272684-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 ^13.6 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:22115783-14] Lin, WJ et al. (2012) Lysosomal targeting of phafin1 mediated by Rab7 induces autophagosome formation. Biochem. Biophys. Res. Commun. 417 35-42 PubMed GONUTS page

[PMID:21255211-15] 15.0 ^15.1 ^15.2 Seto, S et al. (2011) Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic 12 407-20 PubMed GONUTS page

[PMID:14617358-16] 16.0 ^16.1 Stein, MP et al. (2003) Human VPS34 and p150 are Rab7 interacting partners. Traffic 4 754-71 PubMed GONUTS page

[PMID:21873635-17] 17.00 ^17.01 ^17.02 ^17.03 ^17.04 ^17.05 ^17.06 ^17.07 ^17.08 ^17.09 ^17.10 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:15078902-18] 18.0 ^18.1 Seaman, MN (2004) Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165 111-22 PubMed GONUTS page

[PMID:22042847-19] Spanò, S et al. (2011) Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella. Proc. Natl. Acad. Sci. U.S.A. 108 18418-23 PubMed GONUTS page

[PMID:2115402-20] 20.0 ^20.1 Chavrier, P et al. (1990) Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62 317-29 PubMed GONUTS page

[PMID:8954989-21] Vitelli, R et al. (1996) Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid. Biochem. Biophys. Res. Commun. 229 887-90 PubMed GONUTS page

[PMID:19392663-22] 22.0 ^22.1 Zhang, M et al. (2009) Rab7: roles in membrane trafficking and disease. Biosci. Rep. 29 193-209 PubMed GONUTS page

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HUMAN:RAB7A

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