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Gamma-aminobutyric acid receptor-associated protein (GABA(A) receptor-associated protein) (MM46)

 GBRAP_HUMAN             Reviewed;         117 AA.
O95166;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=Gamma-aminobutyric acid receptor-associated protein;
AltName: Full=GABA(A) receptor-associated protein;
AltName: Full=MM46;
Flags: Precursor;
Name=GABARAP; Synonyms=FLC3B; ORFNames=HT004;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
GABRG2 AND BETA-TUBULIN.
TISSUE=Brain;
PubMed=9892355; DOI=10.1038/16264;
Wang H., Bedford F.K., Brandon N.J., Moss S.J., Olsen R.W.;
"GABA(A)-receptor-associated protein links GABA(A) receptors and the
cytoskeleton.";
Nature 397:69-72(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
ULK1.
TISSUE=Frontal cortex;
PubMed=11146101; DOI=10.1016/S0169-328X(00)00218-7;
Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y.,
Koga H., Muramatsu M.-A.;
"Interaction of the Unc-51-like kinase and microtubule-associated
protein light chain 3 related proteins in the brain: possible role of
vesicular transport in axonal elongation.";
Brain Res. Mol. Brain Res. 85:1-12(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Iijima M., Mitsui Y.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Ye M., Fu G., Wu J., Zhou J., Zhang Q., Shen Y., Kan L., He K., Gu B.,
Chen S., Mao M., Chen Z.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hypothalamus;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[6]
INTERACTION WITH ATG7.
PubMed=11096062; DOI=10.1074/jbc.C000752200;
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
activating enzyme for multiple substrates including human Apg12p,
GATE-16, GABARAP, and MAP-LC3.";
J. Biol. Chem. 276:1701-1706(2001).
[7]
INTERACTION WITH ATG3.
PubMed=11825910; DOI=10.1074/jbc.M200385200;
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
conjugation of hApg12p to hApg5p.";
J. Biol. Chem. 277:13739-13744(2002).
[8]
LIPIDATION AT GLY-116, INTERACTION WITH ATG3 AND ATG7, AND SUBCELLULAR
LOCATION.
PubMed=12507496; DOI=10.1016/S0006-291X(02)02907-8;
Tanida I., Komatsu M., Ueno T., Kominami E.;
"GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and
Apg3.";
Biochem. Biophys. Res. Commun. 300:637-644(2003).
[9]
CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-116.
PubMed=15169837; DOI=10.1242/jcs.01131;
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y.,
Yoshimori T.;
"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending
on form-II formation.";
J. Cell Sci. 117:2805-2812(2004).
[10]
FUNCTION, AND INTERACTION WITH DDX47.
PubMed=15977068; DOI=10.1007/s10529-005-3628-2;
Lee J.H., Rho S.B., Chun T.;
"GABAA receptor-associated protein (GABARAP) induces apoptosis by
interacting with DEAD (Asp-Glu-Ala-Asp/His) box polypeptide 47 (DDX
47).";
Biotechnol. Lett. 27:623-628(2005).
[11]
INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=17580304; DOI=10.1074/jbc.M702824200;
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
Overvatn A., Bjorkoy G., Johansen T.;
"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
ubiquitinated protein aggregates by autophagy.";
J. Biol. Chem. 282:24131-24145(2007).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH TP53INP2.
PubMed=19056683; DOI=10.1091/mbc.E08-07-0671;
Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P.,
Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
"The TP53INP2 protein is required for autophagy in mammalian cells.";
Mol. Biol. Cell 20:870-881(2009).
[13]
INTERACTION WITH TECPR2, AND MUTAGENESIS OF 49-TYR-LEU-50 AND ARG-67.
PubMed=20562859; DOI=10.1038/nature09204;
Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
"Network organization of the human autophagy system.";
Nature 466:68-76(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH TBC1D25.
PubMed=21383079; DOI=10.1083/jcb.201008107;
Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
"OATL1, a novel autophagosome-resident Rab33B-GAP, regulates
autophagosomal maturation.";
J. Cell Biol. 192:839-853(2011).
[16]
INTERACTION WITH MAPK15.
PubMed=22948227; DOI=10.4161/auto.21857;
Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M.,
Dall'Armi C., Piccioni F., Verrotti di Pianella A., Chiariello M.;
"MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP
proteins.";
Autophagy 8:1724-1740(2012).
[17]
INTERACTION WITH TP53INP1.
PubMed=22421968; DOI=10.1038/cdd.2012.30;
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
Carrier A., Iovanna J.L., Dusetti N.J.;
"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family
proteins through the LC3-interacting region (LIR) and promotes
autophagy-dependent cell death.";
Cell Death Differ. 19:1525-1535(2012).
[18]
INTERACTION WITH ATG13; RB1CC1 AND ULK1.
PubMed=23043107; DOI=10.1074/jbc.M112.378109;
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
"ATG8 family proteins act as scaffolds for assembly of the ULK
complex: sequence requirements for LC3-interacting region (LIR)
motifs.";
J. Biol. Chem. 287:39275-39290(2012).
[19]
INTERACTION WITH TBC1D5.
PubMed=22354992; DOI=10.1128/MCB.06717-11;
Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.;
"Rab GTPase-activating proteins in autophagy: regulation of endocytic
and autophagy pathways by direct binding to human ATG8 modifiers.";
Mol. Cell. Biol. 32:1733-1744(2012).
[20]
INTERACTION WITH TP53INP1 AND TP53INP2.
PubMed=22470510; DOI=10.1371/journal.pone.0034034;
Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A.,
Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U.,
Palacin M., Johansen T., Zorzano A.;
"DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding
dual regulators of autophagy and transcription.";
PLoS ONE 7:E34034-E34034(2012).
[21]
INTERACTION WITH PCM1.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
[22]
INTERACTION WITH TRIM5.
PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T.,
Dinkins C., Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y.,
Levine B., Johansen T., Deretic V.;
"TRIM proteins regulate autophagy and can target autophagic substrates
by direct recognition.";
Dev. Cell 30:394-409(2014).
[23]
INTERACTION WITH MEFV AND TRIM21.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND INTERACTION WITH GABRG2;
ALPHA-TUBULIN AND BETA-TUBULIN.
PubMed=11729197; DOI=10.1074/jbc.M109753200;
Knight D., Harris R., McAlister M.S.B., Phelan J.P., Geddes S.,
Moss S.J., Driscoll P.C., Keep N.H.;
"The X-ray crystal structure and putative ligand-derived peptide
binding properties of gamma-aminobutyric acid receptor type A
receptor-associated protein.";
J. Biol. Chem. 277:5556-5561(2002).
[25]
STRUCTURE BY NMR.
PubMed=11875056; DOI=10.1074/jbc.C200050200;
Stangler T., Mayr L.M., Willbold D.;
"Solution structure of human GABA(A) receptor-associated protein
GABARAP: implications for biological function and its regulation.";
J. Biol. Chem. 277:13363-13366(2002).
[26]
STRUCTURE BY NMR.
PubMed=11885988; DOI=10.1023/A:1013884402033;
Kouno T., Miura K., Kanematsu T., Shirakawa M., Hirata M., Kawano K.;
"1H, 13C and '5N resonance assignments of GABARAP, GABAA receptor
associated protein.";
J. Biomol. NMR 22:97-98(2002).
[27]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
PubMed=18638487; DOI=10.1016/j.jmb.2008.06.086;
Weiergraber O.H., Stangler T., Thielmann Y., Mohrluder J.,
Wiesehan K., Willbold D.;
"Ligand binding mode of GABAA receptor-associated protein.";
J. Mol. Biol. 381:1320-1331(2008).
[28]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALR, AND
INTERACTION WITH CALR.
PubMed=19154346; DOI=10.1111/j.1742-4658.2008.06857.x;
Thielmann Y., Weiergraber O.H., Mohrluder J., Willbold D.;
"Structural framework of the GABARAP-calreticulin interface
-- implications for substrate binding to endoplasmic reticulum
chaperones.";
FEBS J. 276:1140-1152(2009).
[29] {ECO:0000244|PDB:3WIM}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH WDFY3,
INTERACTION WITH SQSTM1, AND MUTAGENESIS OF LYS-24; TYR-25 AND ASP-54.
PubMed=24668264; DOI=10.1002/embr.201338003;
Lystad A.H., Ichimura Y., Takagi K., Yang Y., Pankiv S., Kanegae Y.,
Kageyama S., Suzuki M., Saito I., Mizushima T., Komatsu M.,
Simonsen A.;
"Structural determinants in GABARAP required for the selective binding
and recruitment of ALFY to LC3B-positive structures.";
EMBO Rep. 15:557-565(2014).
-!- FUNCTION: Ubiquitin-like modifier that plays a role in
intracellular transport of GABA(A) receptors and its interaction
with the cytoskeleton. Involved in apoptosis. Involved in
autophagy. Whereas LC3s are involved in elongation of the
phagophore membrane, the GABARAP/GATE-16 subfamily is essential
for a later stage in autophagosome maturation.
{ECO:0000269|PubMed:15977068}.
-!- SUBUNIT: Interacts with GPHN and NSF (By similarity). Interacts
with ATG3, ATG7, ATG13 (PubMed:11096062, PubMed:11825910,
PubMed:12507496, PubMed:23043107). Interacts with alpha- and beta-
tubulin (PubMed:9892355, PubMed:11729197). Interacts with GABRG2
(PubMed:9892355, PubMed:11729197). Interacts with RB1CC1
(PubMed:23043107). Interacts with ULK1 (PubMed:11146101,
PubMed:23043107). Interacts with CALR (PubMed:19154346). Interacts
with DDX47 (PubMed:15977068). Interacts with TP53INP1 and TP53INP2
(PubMed:19056683, PubMed:22421968, PubMed:22470510). Interacts
with TBC1D5 and TBC1D25 (PubMed:21383079, PubMed:22354992).
Directly interacts with SQSTM1 (PubMed:17580304, PubMed:24668264).
Interacts with MAPK15 (PubMed:22948227). Interacts with TECPR2
(PubMed:20562859). Interacts with PCM1 (PubMed:24089205).
Interacts with TRIM5 and TRIM21 (PubMed:25127057,
PubMed:26347139). Interacts with MEFV (PubMed:26347139). Interacts
with KIF21B (By similarity). Interacts with WDFY3; this
interaction is required for WDFY3 recruitment to MAP1LC3B-positive
p62/SQSTM1 bodies (PubMed:24668264).
{ECO:0000250|UniProtKB:P60517, ECO:0000269|PubMed:11096062,
ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11729197,
ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12507496,
ECO:0000269|PubMed:15977068, ECO:0000269|PubMed:17580304,
ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:19154346,
ECO:0000269|PubMed:20562859, ECO:0000269|PubMed:21383079,
ECO:0000269|PubMed:22354992, ECO:0000269|PubMed:22421968,
ECO:0000269|PubMed:22470510, ECO:0000269|PubMed:22948227,
ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:24089205,
ECO:0000269|PubMed:24668264, ECO:0000269|PubMed:25127057,
ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:9892355}.
-!- INTERACTION:
O75143:ATG13; NbExp=3; IntAct=EBI-712001, EBI-2798775;
Q2TAZ0:ATG2A; NbExp=2; IntAct=EBI-712001, EBI-2514077;
Q9NT62:ATG3; NbExp=5; IntAct=EBI-712001, EBI-988094;
Q9Y4P1:ATG4B; NbExp=8; IntAct=EBI-712001, EBI-712014;
Q9H1Y0:ATG5; NbExp=2; IntAct=EBI-712001, EBI-1047414;
O95352:ATG7; NbExp=8; IntAct=EBI-712001, EBI-987834;
Q9Z2F7:Bnip3l (xeno); NbExp=2; IntAct=EBI-712001, EBI-1774669;
P27797:CALR; NbExp=4; IntAct=EBI-712001, EBI-1049597;
Q9H0S4:DDX47; NbExp=3; IntAct=EBI-712001, EBI-2515241;
Q8WXU2:DNAAF4; NbExp=4; IntAct=EBI-712001, EBI-2946907;
Q96RU3:FNBP1; NbExp=2; IntAct=EBI-712001, EBI-1111248;
Q8TF40:FNIP1; NbExp=5; IntAct=EBI-712001, EBI-2946919;
Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-712001, EBI-2869338;
P18507-2:GABRG2; NbExp=3; IntAct=EBI-712001, EBI-15096952;
P40939:HADHA; NbExp=5; IntAct=EBI-712001, EBI-356720;
O00410:IPO5; NbExp=6; IntAct=EBI-712001, EBI-356424;
Q86V97:KBTBD6; NbExp=3; IntAct=EBI-712001, EBI-2514778;
Q8WVZ9:KBTBD7; NbExp=2; IntAct=EBI-712001, EBI-473695;
Q86YT6:MIB1; NbExp=3; IntAct=EBI-712001, EBI-2129148;
Q14596:NBR1; NbExp=5; IntAct=EBI-712001, EBI-742698;
Q8NI08:NCOA7; NbExp=4; IntAct=EBI-712001, EBI-80799;
P46934:NEDD4; NbExp=6; IntAct=EBI-712001, EBI-726944;
Q8TD19:NEK9; NbExp=5; IntAct=EBI-712001, EBI-1044009;
O75323:NIPSNAP2; NbExp=5; IntAct=EBI-712001, EBI-307133;
Q92636:NSMAF; NbExp=2; IntAct=EBI-712001, EBI-2947053;
Q15154:PCM1; NbExp=8; IntAct=EBI-712001, EBI-741421;
Q9NS23:RASSF1; NbExp=2; IntAct=EBI-712001, EBI-367363;
Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-712001, EBI-367390;
Q13501:SQSTM1; NbExp=13; IntAct=EBI-712001, EBI-307104;
O95210:STBD1; NbExp=5; IntAct=EBI-712001, EBI-2947137;
Q13188:STK3; NbExp=2; IntAct=EBI-712001, EBI-992580;
Q13043:STK4; NbExp=2; IntAct=EBI-712001, EBI-367376;
Q8TC07:TBC1D15; NbExp=5; IntAct=EBI-712001, EBI-1048247;
Q9UPU7:TBC1D2B; NbExp=2; IntAct=EBI-712001, EBI-2947180;
O15040:TECPR2; NbExp=2; IntAct=EBI-712001, EBI-2946991;
Q969E8:TSR2; NbExp=4; IntAct=EBI-712001, EBI-746981;
Q9GZZ9:UBA5; NbExp=2; IntAct=EBI-712001, EBI-747805;
-!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60517}. Golgi
apparatus membrane {ECO:0000250}. Cytoplasmic vesicle,
autophagosome {ECO:0000269|PubMed:12507496,
ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304,
ECO:0000269|PubMed:19056683}. 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). Localizes also to discrete punctae along the ciliary
axoneme (By similarity). {ECO:0000250|UniProtKB:P60517,
ECO:0000250|UniProtKB:Q9DCD6}.
-!- TISSUE SPECIFICITY: Heart, brain, placenta, liver, skeletal
muscle, kidney and pancreas. {ECO:0000269|PubMed:11146101,
ECO:0000269|PubMed:9892355}.
-!- PTM: The precursor molecule is cleaved by ATG4B to form the
cytosolic form, GABARAP-I. This is activated by APG7L/ATG7,
transferred to ATG3 and conjugated to phospholipid to form the
membrane-bound form, GABARAP-II. {ECO:0000269|PubMed:15169837}.
-!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
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EMBL; AF161586; AAD47641.1; -; mRNA.
EMBL; AB030711; BAB21549.1; -; mRNA.
EMBL; AF044671; AAD02337.1; -; mRNA.
EMBL; AF067171; AAD32455.1; -; mRNA.
EMBL; AF183425; AAG09694.1; -; mRNA.
CCDS; CCDS11092.1; -.
RefSeq; NP_009209.1; NM_007278.1.
UniGene; Hs.647421; -.
PDB; 1GNU; X-ray; 1.75 A; A=1-117.
PDB; 1KLV; NMR; -; A=1-117.
PDB; 1KM7; NMR; -; A=1-117.
PDB; 1KOT; NMR; -; A=1-117.
PDB; 3D32; X-ray; 1.30 A; A/B=1-117.
PDB; 3DOW; X-ray; 2.30 A; A=1-117.
PDB; 3WIM; X-ray; 2.60 A; A=1-117.
PDB; 4XC2; X-ray; 1.90 A; A/B/C/D=3-116.
PDB; 5DPS; X-ray; 2.00 A; A/B/C=2-117.
PDBsum; 1GNU; -.
PDBsum; 1KLV; -.
PDBsum; 1KM7; -.
PDBsum; 1KOT; -.
PDBsum; 3D32; -.
PDBsum; 3DOW; -.
PDBsum; 3WIM; -.
PDBsum; 4XC2; -.
PDBsum; 5DPS; -.
ProteinModelPortal; O95166; -.
SMR; O95166; -.
BioGrid; 116465; 64.
DIP; DIP-35050N; -.
ELM; O95166; -.
IntAct; O95166; 483.
MINT; MINT-206256; -.
STRING; 9606.ENSP00000306866; -.
TCDB; 1.A.9.5.2; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
iPTMnet; O95166; -.
PhosphoSitePlus; O95166; -.
BioMuta; GABARAP; -.
EPD; O95166; -.
PaxDb; O95166; -.
PeptideAtlas; O95166; -.
PRIDE; O95166; -.
DNASU; 11337; -.
Ensembl; ENST00000302386; ENSP00000306866; ENSG00000170296.
GeneID; 11337; -.
KEGG; hsa:11337; -.
CTD; 11337; -.
DisGeNET; 11337; -.
EuPathDB; HostDB:ENSG00000170296.9; -.
GeneCards; GABARAP; -.
HGNC; HGNC:4067; GABARAP.
HPA; HPA065883; -.
MIM; 605125; gene.
neXtProt; NX_O95166; -.
OpenTargets; ENSG00000170296; -.
PharmGKB; PA28480; -.
eggNOG; KOG1654; Eukaryota.
eggNOG; ENOG4111JAT; LUCA.
GeneTree; ENSGT00390000012937; -.
HOGENOM; HOG000232034; -.
HOVERGEN; HBG051706; -.
KO; K08341; -.
OMA; RVPVICE; -.
OrthoDB; EOG091G10QX; -.
PhylomeDB; O95166; -.
TreeFam; TF314556; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-8854214; TBC/RABGAPs.
SIGNOR; O95166; -.
ChiTaRS; GABARAP; human.
EvolutionaryTrace; O95166; -.
GeneWiki; GABARAP; -.
GenomeRNAi; 11337; -.
PMAP-CutDB; O95166; -.
PRO; PR:O95166; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000170296; -.
CleanEx; HS_GABARAP; -.
ExpressionAtlas; O95166; baseline and differential.
Genevisible; O95166; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
GO; GO:0005930; C:axoneme; ISS:UniProtKB.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
GO; GO:0050811; F:GABA receptor binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0097352; P:autophagosome maturation; TAS:Reactome.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:0006605; P:protein targeting; TAS:ProtInc.
CDD; cd01611; GABARAP; 1.
InterPro; IPR004241; Atg8-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR10969; PTHR10969; 1.
Pfam; PF02991; Atg8; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Autophagy; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus; Lipoprotein;
Membrane; Microtubule; Protein transport; Reference proteome;
Transport.
CHAIN 1 116 Gamma-aminobutyric acid receptor-
associated protein.
/FTId=PRO_0000212363.
PROPEP 117 117 Removed in mature form.
/FTId=PRO_0000423065.
REGION 1 22 Interaction with beta-tubulin.
REGION 36 117 Interaction with GPHN. {ECO:0000250}.
REGION 36 68 Interaction with GABRG2. {ECO:0000255}.
SITE 116 117 Cleavage; by ATG4B.
LIPID 116 116 Phosphatidylethanolamine amidated
glycine. {ECO:0000269|PubMed:12507496}.
MUTAGEN 24 24 K->Q: No effect on WDFY3-binding.
Impaired WDFY3-binding, but no effect on
SQSTM1-binding; when associated with H-25
and H-54. {ECO:0000269|PubMed:24668264}.
MUTAGEN 25 25 Y->H: No effect on WDFY3-binding.
Impaired WDFY3-binding, but no effect on
SQSTM1-binding; when associated with Q-24
and H-54. {ECO:0000269|PubMed:24668264}.
MUTAGEN 49 50 YL->AA: Inhibits interaction with TECPR2.
{ECO:0000269|PubMed:20562859}.
MUTAGEN 54 54 D->H: No effect on WDFY3-binding.
Impaired WDFY3-binding, but no effect on
SQSTM1-binding; when associated with Q-24
and H-25. {ECO:0000269|PubMed:24668264}.
MUTAGEN 67 67 R->A: No effect on interaction with
TECPR2. {ECO:0000269|PubMed:20562859}.
MUTAGEN 116 116 G->A: Impairs localization at the
autophagosomal membrane.
{ECO:0000269|PubMed:15169837}.
HELIX 4 8 {ECO:0000244|PDB:3D32}.
HELIX 11 24 {ECO:0000244|PDB:3D32}.
STRAND 28 35 {ECO:0000244|PDB:3D32}.
STRAND 47 52 {ECO:0000244|PDB:3D32}.
HELIX 57 68 {ECO:0000244|PDB:3D32}.
STRAND 77 80 {ECO:0000244|PDB:3D32}.
STRAND 87 90 {ECO:0000244|PDB:1KLV}.
HELIX 91 98 {ECO:0000244|PDB:3D32}.
STRAND 101 103 {ECO:0000244|PDB:1KM7}.
STRAND 105 111 {ECO:0000244|PDB:3D32}.
SEQUENCE 117 AA; 13918 MW; BC0B84B8A51C1E32 CRC64;
MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF
YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL


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