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Basic Information:

Symbol	RAB7A
Synonyms	RAB7
Protein Name	Ras-related protein Rab-7a (EC 3.6.5.2)
Species	Human
Entrez ID	7879
Uniprot ID	P51149
Membrane Contact Site	ER-Endosome; Endosome-ER
Location (from literature)	Endosome
Cell line/Tissue	HEK293 cells; COS-7 cells; U2-OS cells; MelJuSo cells; HeLa cells; hTERT-RPE1 cells; HL60 cells
Experimental Method	Low throughput experimental methods
Protein Sequence
More related results

Complex Information:

Complex ID	Subunit of complex	Subcellular location	Species	More
CMCS00006	ZFYVE27; FYCO1; KIF5B; RAB7A; PI(3)P	ER-Endosome; Endosome-ER	Human	more
CMCS00018	PDZD8; RAB7A	ER-Endosome; Endosome-ER	Human	more
CMCS00020	ANO10; RAB7A	ER-Endosome; Endosome-ER	Human	more
CMCS00027	VAPB; VAPA; OSBPL1A; RAB7A; RILP	ER-Endosome; Endosome-ER	Human	more
CMCS00183	PDZD8; RAB7A; ZFYVE27	ER-Endosome; Endosome-ER	Human	more

Expression Overview of RAB7A:

Homology Information of RAB7A:

Uniprot ID	P51149
EggNOG	KOG0394
HOGENOM	/
OrthoDB	586759at2759
TreeFam	TF105605
GeneTree	ENSGT00940000155864

References:

Pubmed ID	32620747
DOI	10.1038/s41467-020-17016-8
Description	We identify endosomal transport as a major functional cluster of TMEM16K in proximity biotinylation proteomics analyses.TMEM16K forms contact sites with endosomes, reconstituting split-GFP with the small GTPase RAB7.
Description of experimental evidence	The protein was validated by microscopy, immunofluorescence, PLA, BioID, mass spectrometry and statistical analysis in HEK293 cells, COS-7 cells and U2-OS cells, and TMEM16K-containing ER-endosome contact sites represent clinically relevant platforms for regulating endosomal sorting.
More related results

Pubmed ID	31636202
DOI	10.1073/pnas.1913509116
Description	PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.
Description of experimental evidence	The protein was validated by microscopy, immunofluorescence and pull-down assay in HEK293 cells and HeLa cells.
More related results

Pubmed ID	19564404
DOI	10.1083/jcb.200811005
Description	We show that cholesterol in LEs is sensed by ORP1L, which transmits this information to the Rab7–RILP–p150Glued complex through the formation of ER–LE membrane contact sites (MCSs). At these sites, the ER protein VAP enters the Rab7–RILP complex to control p150Glued binding and positioning of LEs.
Description of experimental evidence	The protein was validated by microscopy, FLIM, Immuno-EM and filipin stainings in MelJuSo cells, and these data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells.
More related results