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Gamma-aminobutyric acid receptor-associated protein-like 2 (GABA(A) receptor-associated protein-like 2) (Ganglioside expression factor 2) (GEF-2) (General protein transport factor p16) (Golgi-associated ATPase enhancer of 16 kDa) (GATE-16) (MAP1 light chain 3-related protein)

 GBRL2_HUMAN             Reviewed;         117 AA.
P60520; O08765; Q6FG91; Q9DCP8; Q9UQF7;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 1.
25-OCT-2017, entry version 136.
RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
AltName: Full=GABA(A) receptor-associated protein-like 2;
AltName: Full=Ganglioside expression factor 2;
Short=GEF-2;
AltName: Full=General protein transport factor p16;
AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
Short=GATE-16;
AltName: Full=MAP1 light chain 3-related protein;
Flags: Precursor;
Name=GABARAPL2; Synonyms=FLC3A, GEF2;
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
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11414770; DOI=10.1006/geno.2001.6555;
Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
Zhao S.;
"Cloning, expression patterns, and chromosome localization of three
human and two mouse homologues of GABA(A) receptor-associated
protein.";
Genomics 74:408-413(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Storch S., Braulke T.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G.,
Luo M., Chen J., Hu R.;
"Human GEF2 homolog gene.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
FUNCTION.
PubMed=20418806; DOI=10.1038/emboj.2010.74;
Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
"LC3 and GATE-16/GABARAP subfamilies are both essential yet act
differently in autophagosome biogenesis.";
EMBO J. 29:1792-1802(2010).
[18]
INTERACTION WITH TECPR2.
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).
[19]
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).
[20]
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).
[21]
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).
[22]
INTERACTION WITH ATG13 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).
[23]
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).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=22311637; DOI=10.1074/mcp.M111.014035;
Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
"Identification of autophagosome-associated proteins and regulators by
quantitative proteomic analysis and genetic screens.";
Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
[25]
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).
[26]
INTERACTION WITH BNIP3, AND FUNCTION.
PubMed=23209295; DOI=10.1074/jbc.M112.399345;
Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
"Modulation of serines 17 and 24 in the LC3-interacting region of
Bnip3 determines pro-survival mitophagy versus apoptosis.";
J. Biol. Chem. 288:1099-1113(2013).
[27]
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).
[28]
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).
[29]
INTERACTION WITH WDFY3.
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).
[30]
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).
-!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic.
Modulates intra-Golgi transport through coupling between NSF
activity and SNAREs activation. It first stimulates the ATPase
activity of NSF which in turn stimulates the association with
GOSR1 (By similarity). Involved in autophagy. Plays a role in
mitophagy which contributes to regulate mitochondrial quantity and
quality by eliminating the mitochondria to a basal level to
fulfill cellular energy requirements and preventing excess ROS
production. 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:0000250,
ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}.
-!- SUBUNIT: Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-
tubulin (By similarity). Interacts with ATG3, ATG7, ATG13 and
ULK1. Interacts with TP53INP1 and TP53INP2. Interacts with
TBC1D25. Directly interacts with SQSTM1 and BNIP3. Interacts with
TECPR2 and PCM1. Interacts with TBC1D5 (PubMed:22354992).
Interacts with TRIM5 (PubMed:25127057). Interacts with MEFV and
TRIM21 (PubMed:26347139). Interacts with WDFY3 (PubMed:24668264).
{ECO:0000250, ECO:0000269|PubMed:11096062,
ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11825910,
ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:17580304,
ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:20562859,
ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:22354992,
ECO:0000269|PubMed:22421968, ECO:0000269|PubMed:22470510,
ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:23209295,
ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24668264,
ECO:0000269|PubMed:25127057, ECO:0000269|PubMed:26347139}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-720116, EBI-741181;
Q8IVF2-2:AHNAK2; NbExp=3; IntAct=EBI-720116, EBI-10217765;
Q9P2R3:ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908;
Q8N6T3:ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-716933;
Q8N6T3-2:ARFGAP1; NbExp=4; IntAct=EBI-720116, EBI-6288865;
O75143:ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775;
Q676U5:ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909;
Q2TAZ0:ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077;
Q9NT62:ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094;
Q9Y4P1:ATG4B; NbExp=9; IntAct=EBI-720116, EBI-712014;
O95352:ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834;
Q9BXK5:BCL2L13; NbExp=4; IntAct=EBI-720116, EBI-747430;
O60238:BNIP3L; NbExp=4; IntAct=EBI-720116, EBI-849893;
Q9Z2F7:Bnip3l (xeno); NbExp=2; IntAct=EBI-720116, EBI-1774669;
Q2T9L4:C15orf59; NbExp=4; IntAct=EBI-720116, EBI-4311436;
Q9P1Z2:CALCOCO1; NbExp=3; IntAct=EBI-720116, EBI-749920;
Q13137:CALCOCO2; NbExp=6; IntAct=EBI-720116, EBI-739580;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-720116, EBI-749265;
Q8WXU2:DNAAF4; NbExp=2; IntAct=EBI-720116, EBI-2946907;
P00533:EGFR; NbExp=2; IntAct=EBI-720116, EBI-297353;
Q8IVP5:FUNDC1; NbExp=3; IntAct=EBI-720116, EBI-3059266;
Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338;
P40939:HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720;
O00410:IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424;
Q86V97:KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778;
Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695;
Q8N8K9:KIAA1958; NbExp=5; IntAct=EBI-720116, EBI-10181113;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-720116, EBI-10172290;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-720116, EBI-10172052;
Q9UH92:MLX; NbExp=4; IntAct=EBI-720116, EBI-741109;
Q9UH92-3:MLX; NbExp=4; IntAct=EBI-720116, EBI-8852072;
Q14596:NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698;
P46934:NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944;
Q8TD19:NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009;
O75323:NIPSNAP2; NbExp=6; IntAct=EBI-720116, EBI-307133;
Q15154:PCM1; NbExp=2; IntAct=EBI-720116, EBI-741421;
Q9NS23:RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363;
Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390;
Q14257:RCN2; NbExp=5; IntAct=EBI-720116, EBI-356710;
Q9H6L5-1:RETREG1; NbExp=2; IntAct=EBI-720116, EBI-16159046;
Q9H0K1:SIK2; NbExp=3; IntAct=EBI-720116, EBI-1181664;
Q13501:SQSTM1; NbExp=18; IntAct=EBI-720116, EBI-307104;
O95210:STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137;
Q13188:STK3; NbExp=2; IntAct=EBI-720116, EBI-992580;
Q13043:STK4; NbExp=2; IntAct=EBI-720116, EBI-367376;
Q8TC07:TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247;
Q9UPU7:TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180;
B9A6K1:TBC1D5; NbExp=3; IntAct=EBI-720116, EBI-10217641;
Q92609:TBC1D5; NbExp=3; IntAct=EBI-720116, EBI-742381;
Q66K14-2:TBC1D9B; NbExp=3; IntAct=EBI-720116, EBI-10217736;
O15040:TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991;
Q15025:TNIP1; NbExp=5; IntAct=EBI-720116, EBI-357849;
Q969E8:TSR2; NbExp=9; IntAct=EBI-720116, EBI-746981;
Q9GZZ9:UBA5; NbExp=15; IntAct=EBI-720116, EBI-747805;
O75385:ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831;
Q8IZQ1:WDFY3; NbExp=3; IntAct=EBI-720116, EBI-1569256;
-!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cytoplasmic
vesicle, autophagosome {ECO:0000269|PubMed:12507496,
ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304,
ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22311637}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
brain, heart, prostate, ovary, spleen and skeletal muscle.
Expressed at very low levels in lung, thymus and small intestine.
{ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11414770}.
-!- PTM: The precursor molecule is cleaved by ATG4B to form the
cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7,
transferred to ATG3 and conjugated to phospholipid to form the
membrane-bound form, GABARAPL2-II. ATG4B also mediates the
delipidation required for GABARAPL1 recycling when autophagosomes
fuse with lysosomes. {ECO:0000269|PubMed:15169837}.
-!- PTM: The Legionella effector RavZ is a deconjugating enzyme that
produces an ATG8 product that would be resistant to reconjugation
by the host machinery due to the cleavage of the reactive C-
terminal glycine. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB030710; BAB21548.1; -; mRNA.
EMBL; AF087848; AAK20400.1; -; mRNA.
EMBL; AJ010569; CAA09249.1; -; mRNA.
EMBL; AF077046; AAD27779.1; -; mRNA.
EMBL; CR542217; CAG47013.1; -; mRNA.
EMBL; AK289788; BAF82477.1; -; mRNA.
EMBL; CH471114; EAW95630.1; -; Genomic_DNA.
EMBL; BC005985; AAH05985.1; -; mRNA.
EMBL; BC014594; AAH14594.1; -; mRNA.
EMBL; BC029601; AAH29601.1; -; mRNA.
CCDS; CCDS10921.1; -.
RefSeq; NP_009216.1; NM_007285.6.
UniGene; Hs.461379; -.
PDB; 4CO7; X-ray; 2.00 A; A/B=1-117.
PDBsum; 4CO7; -.
ProteinModelPortal; P60520; -.
SMR; P60520; -.
BioGrid; 116473; 83.
DIP; DIP-35051N; -.
ELM; P60520; -.
IntAct; P60520; 527.
MINT; MINT-1414121; -.
STRING; 9606.ENSP00000037243; -.
iPTMnet; P60520; -.
PhosphoSitePlus; P60520; -.
BioMuta; GABARAPL2; -.
DMDM; 44888808; -.
UCD-2DPAGE; P60520; -.
EPD; P60520; -.
PaxDb; P60520; -.
PeptideAtlas; P60520; -.
PRIDE; P60520; -.
DNASU; 11345; -.
Ensembl; ENST00000037243; ENSP00000037243; ENSG00000034713.
GeneID; 11345; -.
KEGG; hsa:11345; -.
UCSC; uc002fen.3; human.
CTD; 11345; -.
DisGeNET; 11345; -.
EuPathDB; HostDB:ENSG00000034713.7; -.
GeneCards; GABARAPL2; -.
HGNC; HGNC:13291; GABARAPL2.
HPA; HPA036726; -.
MIM; 607452; gene.
neXtProt; NX_P60520; -.
OpenTargets; ENSG00000034713; -.
PharmGKB; PA28482; -.
eggNOG; KOG1654; Eukaryota.
eggNOG; ENOG4111JAT; LUCA.
GeneTree; ENSGT00390000012937; -.
HOGENOM; HOG000232034; -.
HOVERGEN; HBG051706; -.
InParanoid; P60520; -.
KO; K08341; -.
OMA; AAAMKWM; -.
OrthoDB; EOG091G10QX; -.
PhylomeDB; P60520; -.
TreeFam; TF312964; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-8854214; TBC/RABGAPs.
SIGNOR; P60520; -.
ChiTaRS; GABARAPL2; human.
GeneWiki; GABARAPL2; -.
GenomeRNAi; 11345; -.
PMAP-CutDB; P60520; -.
PRO; PR:P60520; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000034713; -.
CleanEx; HS_GABARAPL2; -.
ExpressionAtlas; P60520; baseline and differential.
Genevisible; P60520; HS.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
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:0006914; P:autophagy; NAS:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Acetylation; Autophagy; Complete proteome;
Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Transport.
CHAIN 1 116 Gamma-aminobutyric acid receptor-
associated protein-like 2.
/FTId=PRO_0000212373.
PROPEP 117 117 Removed in mature form.
/FTId=PRO_0000423070.
REGION 1 22 Interaction with beta-tubulin.
{ECO:0000250}.
REGION 36 68 Interaction with GABRG2. {ECO:0000255}.
SITE 116 117 Cleavage; by ATG4.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
LIPID 116 116 Phosphatidylethanolamine amidated
glycine. {ECO:0000269|PubMed:12507496}.
VARIANT 51 51 V -> A (in dbSNP:rs11556291).
/FTId=VAR_049756.
MUTAGEN 116 116 G->A: Impairs localization at the
autophagosomal membrane.
{ECO:0000269|PubMed:15169837}.
CONFLICT 29 29 V -> F (in Ref. 4; AAD27779).
{ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:4CO7}.
HELIX 11 24 {ECO:0000244|PDB:4CO7}.
STRAND 28 35 {ECO:0000244|PDB:4CO7}.
STRAND 48 52 {ECO:0000244|PDB:4CO7}.
HELIX 57 67 {ECO:0000244|PDB:4CO7}.
STRAND 77 80 {ECO:0000244|PDB:4CO7}.
HELIX 91 98 {ECO:0000244|PDB:4CO7}.
STRAND 105 111 {ECO:0000244|PDB:4CO7}.
SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF


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