GABARAP
entrez
11337
canonical
uniprot
O95166
canonical
ensembl
ENSG00000170296
resolver
ensp
ENSP00000306866
resolver
enst
ENST00000302386
resolver
genesymbol
GABARAP
resolver
genesymbol_syn
FLC3B
resolver
hgnc
HGNC:4067
resolver
uniprot
Q6IAW1
resolver
uniprot_entry
GBRAP_HUMAN
resolver
uniprot_entry
Q6IAW1_HUMAN
resolver
amino_acid_sequence
MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
uniprot
proteins
function
FUNCTION: Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:15169837, PubMed:20562859, PubMed:22948227, PubMed:34597140). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538). Participates in selective ER-phagy through interaction with UBAC2, promoting recruitment of UBAC2-associated ER fragments to autophagosomes (PubMed:39284914). In addition to autophagy, also regulates lysosome biogenesis via interaction with FNIP1 (or FNIP2): interaction sequesters the FLCN-FNIP complex and prevents non-canonical mTORC1 signaling cascade activation, leading to activation of transcription factors TFEB and TFE3 (PubMed:39423796, PubMed:34597140). Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction (PubMed:25684205). Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation (PubMed:25684205). Involved in apoptosis (PubMed:15977068). {ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:22948227, ECO:0000269|PubMed:25684205, ECO:0000269|PubMed:31006538, ECO:0000269|PubMed:34597140, ECO:0000269|PubMed:39284914, ECO:0000269|PubMed:39423796, ECO:0000269|PubMed:9892355}.
uniprot
proteins
mass_dalton
13918
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="K->Q: No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with H-25 and H-54."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 25; /note="Y->A: Reduced interaction with UBAC2."; /evidence="ECO:0000269|PubMed:39284914"; MUTAGEN 25; /note="Y->H: No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with Q-24 and H-54."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 46; /note="K->A: Reduced interaction with UBAC2."; /evidence="ECO:0000269|PubMed:39284914"; MUTAGEN 49..50; /note="YL->AA: Inhibits interaction with TECPR2."; /evidence="ECO:0000269|PubMed:20562859"; MUTAGEN 54; /note="D->H: No effect on WDFY3-binding. Impaired WDFY3-binding, but no effect on SQSTM1-binding; when associated with Q-24 and H-25."; /evidence="ECO:0000269|PubMed:24668264"; MUTAGEN 67; /note="R->A: No effect on interaction with TECPR2."; /evidence="ECO:0000269|PubMed:20562859"; MUTAGEN 116; /note="G->A: Impairs localization at the autophagosomal membrane."; /evidence="ECO:0000269|PubMed:15169837
uniprot
proteins
post_translational_modification
PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or ATG4D) to expose the glycine at the C-terminus and form the cytosolic form, GABARAP-I (PubMed:15169837, PubMed:20818167, PubMed:30661429). The processed form is then activated by APG7L/ATG7, transferred to ATG3 and conjugated to phosphatidylethanolamine (PE) phospholipid to form the membrane-bound form, GABARAP-II (PubMed:15169837). During non-canonical autophagy, the processed form is conjugated to phosphatidylserine (PS) phospholipid (PubMed:33909989). ATG4 proteins also mediate the delipidation of PE-conjugated forms (PubMed:33909989). In addition, ATG4B and ATG4D mediate delipidation of ATG8 proteins conjugated to PS during non-canonical autophagy (PubMed:33909989). ATG4B constitutes the major protein for proteolytic activation (PubMed:30661429). ATG4D is the main enzyme for delipidation activity (By similarity). {ECO:0000250|UniProtKB:Q9DCD6, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:33909989}.; PTM: (Microbial infection) The Legionella effector RavZ is a deconjugating enzyme that hydrolyzes the amide bond between the C-terminal glycine residue and an adjacent aromatic residue in ATG8 proteins conjugated to phosphatidylethanolamine (PE), producing an ATG8 protein that is resistant to reconjugation by the host machinery due to the cleavage of the reactive C-terminal glycine (PubMed:31722778). RavZ is also able to mediate delipidation of ATG8 proteins conjugated to phosphatidylserine (PS) (PubMed:33909989). {ECO:0000269|PubMed:31722778, ECO:0000269|PubMed:33909989}.
uniprot
proteins
protein_family
ATG8 family
uniprot
proteins
pubmed
10931946
uniprot
proteins
pubmed
11096062
uniprot
proteins
pubmed
11146101
uniprot
proteins
pubmed
11729197
uniprot
proteins
pubmed
11825910
uniprot
proteins
pubmed
11875056
uniprot
proteins
pubmed
11885988
uniprot
proteins
pubmed
12507496
uniprot
proteins
pubmed
15169837
uniprot
proteins
pubmed
15977068
uniprot
proteins
pubmed
17580304
uniprot
proteins
pubmed
18638487
uniprot
proteins
pubmed
19056683
uniprot
proteins
pubmed
19154346
uniprot
proteins
pubmed
20562859
uniprot
proteins
pubmed
20818167
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21383079
uniprot
proteins
pubmed
22354992
uniprot
proteins
pubmed
22421968
uniprot
proteins
pubmed
22470510
uniprot
proteins
pubmed
22948227
uniprot
proteins
pubmed
23043107
uniprot
proteins
pubmed
24089205
uniprot
proteins
pubmed
24668264
uniprot
proteins
pubmed
25126726
uniprot
proteins
pubmed
25127057
uniprot
proteins
pubmed
25684205
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
26929408
uniprot
proteins
pubmed
29420192
uniprot
proteins
pubmed
30661429
uniprot
proteins
pubmed
31006538
uniprot
proteins
pubmed
31722778
uniprot
proteins
pubmed
32315611
uniprot
proteins
pubmed
32620754
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
34338405
uniprot
proteins
pubmed
34597140
uniprot
proteins
pubmed
36481789
uniprot
proteins
pubmed
37252361
uniprot
proteins
pubmed
39284914
uniprot
proteins
pubmed
39423796
uniprot
proteins
pubmed
9892355
uniprot
proteins
sequence_length
117
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683}. Endomembrane system {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60517}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae. Colocalizes with microtubules (By similarity). Also localizes to discrete punctae along the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:P60517, ECO:0000250|UniProtKB:Q9DCD6}.
uniprot
proteins