MOUSE:LAMP2

Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Lamp2 (synonyms: Lamp-2)
Protein Name(s)	Lysosome-associated membrane glycoprotein 2 LAMP-2 Lysosome-associated membrane protein 2 CD107 antigen-like family member B Lysosomal membrane glycoprotein type B LGP-B
External Links
UniProt	P17047
EMBL	J05287 AK159272 AK032974 AK163933 AL513356 AL513356 CH466570 CH466570 BC138718 BC138723 M32017 M32018
CCDS	CCDS30092.1 CCDS30093.1 CCDS72369.1
PIR	A35560
RefSeq	NP_001017959.1 NP_001277414.1 NP_034815.2
UniGene	Mm.414016 Mm.486
ProteinModelPortal	P17047
SMR	P17047
BioGrid	201106
IntAct	P17047
MINT	MINT-1857994
STRING	10090.ENSMUSP00000074448
PhosphoSite	P17047
MaxQB	P17047
PaxDb	P17047
PRIDE	P17047
Ensembl	ENSMUST00000016678 ENSMUST00000061755 ENSMUST00000074913
GeneID	16784
KEGG	mmu:16784
UCSC	uc009szw.1 uc009szx.1
CTD	3920
MGI	MGI:96748
eggNOG	NOG301998
GeneTree	ENSGT00530000063068
HOGENOM	HOG000230942
HOVERGEN	HBG052303
InParanoid	P17047
KO	K06528
OrthoDB	EOG7ZD1VH
TreeFam	TF316339
ChiTaRS	Lamp2
NextBio	290644
PRO	PR:P17047
Proteomes	UP000000589
Bgee	P17047
CleanEx	MM_LAMP2
ExpressionAtlas	P17047
Genevestigator	P17047
GO	GO:0070062 GO:0016021 GO:0005770 GO:0031902 GO:0005765 GO:0005764 GO:0016020 GO:0030670 GO:0005886 GO:0031088 GO:0019904 GO:0050821
InterPro	IPR018134 IPR002000
PANTHER	PTHR11506
Pfam	PF01299
PRINTS	PR00336
PROSITE	PS00310 PS00311 PS51407

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0010467	gene expression	PMID:25586965^[1]	ECO:0000315			P		As seen in Figure 6, the localization of the receptors for LAMP2A is decreased due to decrease of CNTS. It is therefore more localized in LAMP1.	complete CACAO 10668
involved_in	GO:0006605	protein targeting	PMID:27628032^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009267	cellular response to starvation	PMID:27628032^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061740	protein targeting to lysosome involved in chaperone-mediated autophagy	PMID:27628032^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061684	chaperone-mediated autophagy	PMID:27628032^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905146	lysosomal protein catabolic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
involved_in	GO:0061684	chaperone-mediated autophagy	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
involved_in	GO:0097352	autophagosome maturation	PMID:27628032^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006605	protein targeting	PMID:12221139^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	PMID:12221139^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097637	integral component of autophagosome membrane	PMID:12221139^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0061684	chaperone-mediated autophagy	PMID:18644871^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:22641697^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:Q9JJ59)	Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:22641697^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NP78	F		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:18022370^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990836	lysosomal matrix	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17046	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:1905146	lysosomal protein catabolic process	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0061742	chaperone-mediated autophagy translocation complex	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061740	protein targeting to lysosome involved in chaperone-mediated autophagy	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061740	protein targeting to lysosome involved in chaperone-mediated autophagy	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17046	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061684	chaperone-mediated autophagy	PMID:18579532^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061684	chaperone-mediated autophagy	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0061684	chaperone-mediated autophagy	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2990	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0046716	muscle cell cellular homeostasis	PMID:20060297^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2385811	P	occurs_in:(EMAPA:35786)	Seeded From UniProt	complete
colocalizes_with	GO:0045121	membrane raft	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2990	C		Seeded From UniProt	complete
part_of	GO:0044754	autolysosome	PMID:25327288^[9]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0032463	negative regulation of protein homooligomerization	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
part_of	GO:0031902	late endosome membrane	PMID:21896273^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0031902	late endosome membrane	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0031647	regulation of protein stability	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	P		Seeded From UniProt	complete
part_of	GO:0031088	platelet dense granule membrane	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0030670	phagocytic vesicle membrane	PMID:9670047^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion	MGI:MGI:2446573	C	part_of:(CL:0000235)	Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:23093945^[12]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005802	trans-Golgi network	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:14668490^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	PMID:15229288^[14]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2990	C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	PMID:21896273^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2990	C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P17046	C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:24334765^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:19549681^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:16399794^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:16093322^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:14557411^[19]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000236)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:12775715^[20]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(EMAPA:28407) part_of:(CL:0000075)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:15229288^[14]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:12536145^[21]	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	RGD:2990	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000008	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000096	ECO:0000266	sequence orthology evidence used in manual assertion	UniProtKB:P13473	C		Seeded From UniProt	complete
involved_in	GO:1905146	lysosomal protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
involved_in	GO:0061740	protein targeting to lysosome involved in chaperone-mediated autophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	P		Seeded From UniProt	complete
involved_in	GO:0061684	chaperone-mediated autophagy	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	P		Seeded From UniProt	complete
part_of	GO:0044754	autolysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	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:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
involved_in	GO:0031647	regulation of protein stability	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	P		Seeded From UniProt	complete
part_of	GO:0031088	platelet dense granule membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
part_of	GO:0005765	lysosomal membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P13473 ensembl:ENSP00000408411	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002000	C		Seeded From UniProt	complete
part_of	GO:0061742	chaperone-mediated autophagy translocation complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13473-1	C		Seeded From UniProt	complete
involved_in	GO:0061684	chaperone-mediated autophagy	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P13473-1	P		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
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
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:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	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
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:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	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: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
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Notes

References

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

↑ Napolitano, G et al. (2015) Impairment of chaperone-mediated autophagy leads to selective lysosomal degradation defects in the lysosomal storage disease cystinosis. EMBO Mol Med 7 158-74 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Hubert, V et al. (2016) LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes. Biol Open 5 1516-1529 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Eskelinen, EL et al. (2002) Role of LAMP-2 in lysosome biogenesis and autophagy. Mol. Biol. Cell 13 3355-68 PubMed GONUTS page
↑ Bandyopadhyay, U et al. (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol. Cell. Biol. 28 5747-63 PubMed GONUTS page
↑ ^5.0 ^5.1 Demirel, Ö et al. (2012) The lysosomal polypeptide transporter TAPL is stabilized by interaction with LAMP-1 and LAMP-2. J. Cell. Sci. 125 4230-40 PubMed GONUTS page
↑ Reczek, D et al. (2007) LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase. Cell 131 770-83 PubMed GONUTS page
↑ Hayashi, H et al. (2008) The Foxc2 transcription factor regulates angiogenesis via induction of integrin beta3 expression. J. Biol. Chem. 283 23791-800 PubMed GONUTS page
↑ Arndt, V et al. (2010) Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr. Biol. 20 143-8 PubMed GONUTS page
↑ Dowdle, WE et al. (2014) Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo. Nat. Cell Biol. 16 1069-79 PubMed GONUTS page
↑ ^10.0 ^10.1 Behnke, J et al. (2011) Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. 585 2951-7 PubMed GONUTS page
↑ Hackam, DJ et al. (1998) Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification. J. Exp. Med. 188 351-64 PubMed GONUTS page
↑ Kuang, E et al. (2012) Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection. PLoS Genet. 8 e1003007 PubMed GONUTS page
↑ Richardson, SC et al. (2004) Mammalian late vacuole protein sorting orthologues participate in early endosomal fusion and interact with the cytoskeleton. Mol. Biol. Cell 15 1197-210 PubMed GONUTS page
↑ ^14.0 ^14.1 Coumailleau, F et al. (2004) Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment. Mol. Biol. Cell 15 4444-56 PubMed GONUTS page
↑ Qin, Y et al. (2014) The tumor susceptibility gene TMEM127 is mutated in renal cell carcinomas and modulates endolysosomal function. Hum. Mol. Genet. 23 2428-39 PubMed GONUTS page
↑ Sun-Wada, GH et al. (2009) Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification. J. Cell. Sci. 122 2504-13 PubMed GONUTS page
↑ Berger, P et al. (2006) Multi-level regulation of myotubularin-related protein-2 phosphatase activity by myotubularin-related protein-13/set-binding factor-2. Hum. Mol. Genet. 15 569-79 PubMed GONUTS page
↑ Pan, J et al. (2005) RNF17, a component of the mammalian germ cell nuage, is essential for spermiogenesis. Development 132 4029-39 PubMed GONUTS page
↑ Elewaut, D et al. (2003) The adaptor protein AP-3 is required for CD1d-mediated antigen presentation of glycosphingolipids and development of Valpha14i NKT cells. J. Exp. Med. 198 1133-46 PubMed GONUTS page
↑ Shirahama-Noda, K et al. (2003) Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice. J. Biol. Chem. 278 33194-9 PubMed GONUTS page
↑ Gurung, R et al. (2003) Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation. J. Biol. Chem. 278 11376-85 PubMed GONUTS page

[PMID:25586965-1] Napolitano, G et al. (2015) Impairment of chaperone-mediated autophagy leads to selective lysosomal degradation defects in the lysosomal storage disease cystinosis. EMBO Mol Med 7 158-74 PubMed GONUTS page

[PMID:27628032-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Hubert, V et al. (2016) LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and for their fusion with lysosomes. Biol Open 5 1516-1529 PubMed GONUTS page

[PMID:12221139-3] 3.0 ^3.1 ^3.2 Eskelinen, EL et al. (2002) Role of LAMP-2 in lysosome biogenesis and autophagy. Mol. Biol. Cell 13 3355-68 PubMed GONUTS page

[PMID:18644871-4] Bandyopadhyay, U et al. (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol. Cell. Biol. 28 5747-63 PubMed GONUTS page

[PMID:22641697-5] 5.0 ^5.1 Demirel, Ö et al. (2012) The lysosomal polypeptide transporter TAPL is stabilized by interaction with LAMP-1 and LAMP-2. J. Cell. Sci. 125 4230-40 PubMed GONUTS page

[PMID:18022370-6] Reczek, D et al. (2007) LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase. Cell 131 770-83 PubMed GONUTS page

[PMID:18579532-7] Hayashi, H et al. (2008) The Foxc2 transcription factor regulates angiogenesis via induction of integrin beta3 expression. J. Biol. Chem. 283 23791-800 PubMed GONUTS page

[PMID:20060297-8] Arndt, V et al. (2010) Chaperone-assisted selective autophagy is essential for muscle maintenance. Curr. Biol. 20 143-8 PubMed GONUTS page

[PMID:25327288-9] Dowdle, WE et al. (2014) Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo. Nat. Cell Biol. 16 1069-79 PubMed GONUTS page

[PMID:21896273-10] 10.0 ^10.1 Behnke, J et al. (2011) Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. 585 2951-7 PubMed GONUTS page

[PMID:9670047-11] Hackam, DJ et al. (1998) Host resistance to intracellular infection: mutation of natural resistance-associated macrophage protein 1 (Nramp1) impairs phagosomal acidification. J. Exp. Med. 188 351-64 PubMed GONUTS page

[PMID:23093945-12] Kuang, E et al. (2012) Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection. PLoS Genet. 8 e1003007 PubMed GONUTS page

[PMID:14668490-13] Richardson, SC et al. (2004) Mammalian late vacuole protein sorting orthologues participate in early endosomal fusion and interact with the cytoskeleton. Mol. Biol. Cell 15 1197-210 PubMed GONUTS page

[PMID:15229288-14] 14.0 ^14.1 Coumailleau, F et al. (2004) Over-expression of Rififylin, a new RING finger and FYVE-like domain-containing protein, inhibits recycling from the endocytic recycling compartment. Mol. Biol. Cell 15 4444-56 PubMed GONUTS page

[PMID:24334765-15] Qin, Y et al. (2014) The tumor susceptibility gene TMEM127 is mutated in renal cell carcinomas and modulates endolysosomal function. Hum. Mol. Genet. 23 2428-39 PubMed GONUTS page

[PMID:19549681-16] Sun-Wada, GH et al. (2009) Direct recruitment of H+-ATPase from lysosomes for phagosomal acidification. J. Cell. Sci. 122 2504-13 PubMed GONUTS page

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MOUSE:LAMP2

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