Full text data of GABARAPL2
GABARAPL2
(FLC3A, GEF2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P60520
ID GBRL2_HUMAN Reviewed; 117 AA.
AC P60520; O08765; Q6FG91; Q9DCP8; Q9UQF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
DE AltName: Full=GABA(A) receptor-associated protein-like 2;
DE AltName: Full=Ganglioside expression factor 2;
DE Short=GEF-2;
DE AltName: Full=General protein transport factor p16;
DE AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE Short=GATE-16;
DE AltName: Full=MAP1 light chain 3-related protein;
DE Flags: Precursor;
GN Name=GABARAPL2; Synonyms=FLC3A, GEF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP ULK1.
RC TISSUE=Frontal cortex;
RX PubMed=11146101; DOI=10.1016/S0169-328X(00)00218-7;
RA Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y.,
RA Koga H., Muramatsu M.-A.;
RT "Interaction of the Unc-51-like kinase and microtubule-associated
RT protein light chain 3 related proteins in the brain: possible role of
RT vesicular transport in axonal elongation.";
RL Brain Res. Mol. Brain Res. 85:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11414770; DOI=10.1006/geno.2001.6555;
RA Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
RA Zhao S.;
RT "Cloning, expression patterns, and chromosome localization of three
RT human and two mouse homologues of GABA(A) receptor-associated
RT protein.";
RL Genomics 74:408-413(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Storch S., Braulke T.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G.,
RA Luo M., Chen J., Hu R.;
RT "Human GEF2 homolog gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH ATG7.
RX PubMed=11096062; DOI=10.1074/jbc.C000752200;
RA Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
RT "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
RT activating enzyme for multiple substrates including human Apg12p,
RT GATE-16, GABARAP, and MAP-LC3.";
RL J. Biol. Chem. 276:1701-1706(2001).
RN [10]
RP INTERACTION WITH ATG3.
RX PubMed=11825910; DOI=10.1074/jbc.M200385200;
RA Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
RT conjugation of hApg12p to hApg5p.";
RL J. Biol. Chem. 277:13739-13744(2002).
RN [11]
RP POST-TRANSLATIONAL MODIFICATION, INTERACTION WITH ATG3 AND ATG7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12507496; DOI=10.1016/S0006-291X(02)02907-8;
RA Tanida I., Komatsu M., Ueno T., Kominami E.;
RT "GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and
RT Apg3.";
RL Biochem. Biophys. Res. Commun. 300:637-644(2003).
RN [12]
RP CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-116.
RX PubMed=15169837; DOI=10.1242/jcs.01131;
RA Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y.,
RA Yoshimori T.;
RT "LC3, GABARAP and GATE16 localize to autophagosomal membrane depending
RT on form-II formation.";
RL J. Cell Sci. 117:2805-2812(2004).
RN [13]
RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=17580304; DOI=10.1074/jbc.M702824200;
RA Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
RA Overvatn A., Bjorkoy G., Johansen T.;
RT "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
RT ubiquitinated protein aggregates by autophagy.";
RL J. Biol. Chem. 282:24131-24145(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TP53INP2.
RX PubMed=19056683; DOI=10.1091/mbc.E08-07-0671;
RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P.,
RA Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
RT "The TP53INP2 protein is required for autophagy in mammalian cells.";
RL Mol. Biol. Cell 20:870-881(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP FUNCTION.
RX PubMed=20418806; DOI=10.1038/emboj.2010.74;
RA Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
RT "LC3 and GATE-16/GABARAP subfamilies are both essential yet act
RT differently in autophagosome biogenesis.";
RL EMBO J. 29:1792-1802(2010).
RN [18]
RP INTERACTION WITH TECPR2.
RX PubMed=20562859; DOI=10.1038/nature09204;
RA Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
RT "Network organization of the human autophagy system.";
RL Nature 466:68-76(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH TBC1D25.
RX PubMed=21383079; DOI=10.1083/jcb.201008107;
RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates
RT autophagosomal maturation.";
RL J. Cell Biol. 192:839-853(2011).
RN [21]
RP INTERACTION PCM1.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from
RT centriolar satellites.";
RL Nature 502:254-257(2013).
RN [22]
RP INTERACTION WITH TP53INP1.
RX PubMed=22421968; DOI=10.1038/cdd.2012.30;
RA Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
RA Carrier A., Iovanna J.L., Dusetti N.J.;
RT "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family
RT proteins through the LC3-interacting region (LIR) and promotes
RT autophagy-dependent cell death.";
RL Cell Death Differ. 19:1525-1535(2012).
RN [23]
RP INTERACTION WITH ATG13 AND ULK1.
RX PubMed=23043107; DOI=10.1074/jbc.M112.378109;
RA Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
RA Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
RT "ATG8 family proteins act as scaffolds for assembly of the ULK
RT complex: sequence requirements for LC3-interacting region (LIR)
RT motifs.";
RL J. Biol. Chem. 287:39275-39290(2012).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22311637; DOI=10.1074/mcp.M111.014035;
RA Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
RA Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
RA Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
RA Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
RT "Identification of autophagosome-associated proteins and regulators by
RT quantitative proteomic analysis and genetic screens.";
RL Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
RN [25]
RP INTERACTION WITH TP53INP1 AND TP53INP2.
RX PubMed=22470510; DOI=10.1371/journal.pone.0034034;
RA Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A.,
RA Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U.,
RA Palacin M., Johansen T., Zorzano A.;
RT "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding
RT dual regulators of autophagy and transcription.";
RL PLoS ONE 7:E34034-E34034(2012).
RN [26]
RP INTERACTION WITH BNIP3, AND FUNCTION.
RX PubMed=23209295; DOI=10.1074/jbc.M112.399345;
RA Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
RA Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
RT "Modulation of serines 17 and 24 in the LC3-interacting region of
RT Bnip3 determines pro-survival mitophagy versus apoptosis.";
RL J. Biol. Chem. 288:1099-1113(2013).
CC -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic.
CC Modulates intra-Golgi transport through coupling between NSF
CC activity and SNAREs activation. It first stimulates the ATPase
CC activity of NSF which in turn stimulates the association with
CC GOSR1 (By similarity). Involved in autophagy. Plays a role in
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to
CC fulfill cellular energy requirements and preventing excess ROS
CC production. Whereas LC3s are involved in elongation of the
CC phagophore membrane, the GABARAP/GATE-16 subfamily is essential
CC for a later stage in autophagosome maturation.
CC -!- SUBUNIT: Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-
CC tubulin (By similarity). Interacts with ATG3, ATG7, ATG13 and
CC ULK1. Interacts with TP53INP1 and TP53INP2. Interacts with
CC TBC1D25. Directly interacts with SQSTM1 and BNIP3. Interacts with
CC TECPR2 and PCM1.
CC -!- INTERACTION:
CC Q9P2R3:ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908;
CC O75143:ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775;
CC Q676U5:ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909;
CC Q2TAZ0:ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077;
CC Q9NT62:ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094;
CC Q9Y4P1:ATG4B; NbExp=7; IntAct=EBI-720116, EBI-712014;
CC O95352:ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834;
CC Q9Z2F7:Bnip3l (xeno); NbExp=2; IntAct=EBI-720116, EBI-1774669;
CC Q8WXU2:DYX1C1; NbExp=2; IntAct=EBI-720116, EBI-2946907;
CC P00533:EGFR; NbExp=2; IntAct=EBI-720116, EBI-297353;
CC Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338;
CC O75323:GBAS; NbExp=6; IntAct=EBI-720116, EBI-307133;
CC P40939:HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720;
CC O00410:IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424;
CC Q86V97:KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778;
CC Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695;
CC Q14596:NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698;
CC P46934:NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944;
CC Q8TD19:NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009;
CC Q9NS23:RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363;
CC Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390;
CC Q14257:RCN2; NbExp=3; IntAct=EBI-720116, EBI-356710;
CC Q13501:SQSTM1; NbExp=12; IntAct=EBI-720116, EBI-307104;
CC O95210:STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137;
CC Q13188:STK3; NbExp=2; IntAct=EBI-720116, EBI-992580;
CC Q13043:STK4; NbExp=2; IntAct=EBI-720116, EBI-367376;
CC Q8TC07:TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247;
CC Q9UPU7:TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180;
CC O15040:TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991;
CC Q9GZZ9:UBA5; NbExp=10; IntAct=EBI-720116, EBI-747805;
CC O75385:ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasmic
CC vesicle, autophagosome.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
CC brain, heart, prostate, ovary, spleen and skeletal muscle.
CC Expressed at very low levels in lung, thymus and small intestine.
CC -!- PTM: The precursor molecule is cleaved by ATG4B to form the
CC cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phospholipid to form the
CC membrane-bound form, GABARAPL2-II. ATG4B also mediates the
CC delipidation required for GABARAPL1 recycling when autophagosomes
CC fuse with lysosomes.
CC -!- PTM: The Legionella effector RavZ is a deconjugating enzyme that
CC produces an ATG8 product that would be resistant to reconjugation
CC by the host machinery due to the cleavage of the reactive C-
CC terminal glycine (By similarity).
CC -!- SIMILARITY: Belongs to the ATG8 family.
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DR EMBL; AB030710; BAB21548.1; -; mRNA.
DR EMBL; AF087848; AAK20400.1; -; mRNA.
DR EMBL; AJ010569; CAA09249.1; -; mRNA.
DR EMBL; AF077046; AAD27779.1; -; mRNA.
DR EMBL; CR542217; CAG47013.1; -; mRNA.
DR EMBL; AK289788; BAF82477.1; -; mRNA.
DR EMBL; CH471114; EAW95630.1; -; Genomic_DNA.
DR EMBL; BC005985; AAH05985.1; -; mRNA.
DR EMBL; BC014594; AAH14594.1; -; mRNA.
DR EMBL; BC029601; AAH29601.1; -; mRNA.
DR RefSeq; NP_009216.1; NM_007285.6.
DR UniGene; Hs.461379; -.
DR ProteinModelPortal; P60520; -.
DR SMR; P60520; 1-117.
DR IntAct; P60520; 494.
DR MINT; MINT-1414121; -.
DR STRING; 9606.ENSP00000037243; -.
DR PhosphoSite; P60520; -.
DR DMDM; 44888808; -.
DR UCD-2DPAGE; P60520; -.
DR PaxDb; P60520; -.
DR PRIDE; P60520; -.
DR DNASU; 11345; -.
DR Ensembl; ENST00000037243; ENSP00000037243; ENSG00000034713.
DR GeneID; 11345; -.
DR KEGG; hsa:11345; -.
DR UCSC; uc002fen.3; human.
DR CTD; 11345; -.
DR GeneCards; GC16P075600; -.
DR HGNC; HGNC:13291; GABARAPL2.
DR HPA; HPA036726; -.
DR MIM; 607452; gene.
DR neXtProt; NX_P60520; -.
DR PharmGKB; PA28482; -.
DR eggNOG; NOG249730; -.
DR HOGENOM; HOG000232034; -.
DR HOVERGEN; HBG051706; -.
DR InParanoid; P60520; -.
DR KO; K08341; -.
DR OMA; IRRRITM; -.
DR OrthoDB; EOG70KGRK; -.
DR ChiTaRS; GABARAPL2; human.
DR GeneWiki; GABARAPL2; -.
DR GenomeRNAi; 11345; -.
DR NextBio; 43116; -.
DR PMAP-CutDB; P60520; -.
DR PRO; PR:P60520; -.
DR ArrayExpress; P60520; -.
DR Bgee; P60520; -.
DR CleanEx; HS_GABARAPL2; -.
DR Genevestigator; P60520; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; NAS:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004241; Atg8_like.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; Atg8; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Complete proteome; Cytoplasmic vesicle;
KW Golgi apparatus; Lipoprotein; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 116 Gamma-aminobutyric acid receptor-
FT associated protein-like 2.
FT /FTId=PRO_0000212373.
FT PROPEP 117 117 Removed in mature form.
FT /FTId=PRO_0000423070.
FT REGION 1 22 Interaction with beta-tubulin (By
FT similarity).
FT REGION 36 68 Interaction with GABRG2 (Potential).
FT SITE 116 117 Cleavage; by ATG4.
FT MOD_RES 24 24 N6-acetyllysine.
FT MOD_RES 39 39 Phosphoserine.
FT LIPID 116 116 Phosphatidylethanolamine amidated
FT glycine.
FT VARIANT 51 51 V -> A (in dbSNP:rs11556291).
FT /FTId=VAR_049756.
FT MUTAGEN 116 116 G->A: Impairs localization at the
FT autophagosomal membrane.
FT CONFLICT 29 29 V -> F (in Ref. 4; AAD27779).
SQ SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
//
ID GBRL2_HUMAN Reviewed; 117 AA.
AC P60520; O08765; Q6FG91; Q9DCP8; Q9UQF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
DE AltName: Full=GABA(A) receptor-associated protein-like 2;
DE AltName: Full=Ganglioside expression factor 2;
DE Short=GEF-2;
DE AltName: Full=General protein transport factor p16;
DE AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
DE Short=GATE-16;
DE AltName: Full=MAP1 light chain 3-related protein;
DE Flags: Precursor;
GN Name=GABARAPL2; Synonyms=FLC3A, GEF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP ULK1.
RC TISSUE=Frontal cortex;
RX PubMed=11146101; DOI=10.1016/S0169-328X(00)00218-7;
RA Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y.,
RA Koga H., Muramatsu M.-A.;
RT "Interaction of the Unc-51-like kinase and microtubule-associated
RT protein light chain 3 related proteins in the brain: possible role of
RT vesicular transport in axonal elongation.";
RL Brain Res. Mol. Brain Res. 85:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11414770; DOI=10.1006/geno.2001.6555;
RA Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
RA Zhao S.;
RT "Cloning, expression patterns, and chromosome localization of three
RT human and two mouse homologues of GABA(A) receptor-associated
RT protein.";
RL Genomics 74:408-413(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Storch S., Braulke T.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G.,
RA Luo M., Chen J., Hu R.;
RT "Human GEF2 homolog gene.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP INTERACTION WITH ATG7.
RX PubMed=11096062; DOI=10.1074/jbc.C000752200;
RA Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
RT "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
RT activating enzyme for multiple substrates including human Apg12p,
RT GATE-16, GABARAP, and MAP-LC3.";
RL J. Biol. Chem. 276:1701-1706(2001).
RN [10]
RP INTERACTION WITH ATG3.
RX PubMed=11825910; DOI=10.1074/jbc.M200385200;
RA Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
RT conjugation of hApg12p to hApg5p.";
RL J. Biol. Chem. 277:13739-13744(2002).
RN [11]
RP POST-TRANSLATIONAL MODIFICATION, INTERACTION WITH ATG3 AND ATG7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12507496; DOI=10.1016/S0006-291X(02)02907-8;
RA Tanida I., Komatsu M., Ueno T., Kominami E.;
RT "GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and
RT Apg3.";
RL Biochem. Biophys. Res. Commun. 300:637-644(2003).
RN [12]
RP CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-116.
RX PubMed=15169837; DOI=10.1242/jcs.01131;
RA Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y.,
RA Yoshimori T.;
RT "LC3, GABARAP and GATE16 localize to autophagosomal membrane depending
RT on form-II formation.";
RL J. Cell Sci. 117:2805-2812(2004).
RN [13]
RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=17580304; DOI=10.1074/jbc.M702824200;
RA Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
RA Overvatn A., Bjorkoy G., Johansen T.;
RT "p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
RT ubiquitinated protein aggregates by autophagy.";
RL J. Biol. Chem. 282:24131-24145(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TP53INP2.
RX PubMed=19056683; DOI=10.1091/mbc.E08-07-0671;
RA Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P.,
RA Pebusque M.J., Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
RT "The TP53INP2 protein is required for autophagy in mammalian cells.";
RL Mol. Biol. Cell 20:870-881(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP FUNCTION.
RX PubMed=20418806; DOI=10.1038/emboj.2010.74;
RA Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
RT "LC3 and GATE-16/GABARAP subfamilies are both essential yet act
RT differently in autophagosome biogenesis.";
RL EMBO J. 29:1792-1802(2010).
RN [18]
RP INTERACTION WITH TECPR2.
RX PubMed=20562859; DOI=10.1038/nature09204;
RA Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
RT "Network organization of the human autophagy system.";
RL Nature 466:68-76(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP INTERACTION WITH TBC1D25.
RX PubMed=21383079; DOI=10.1083/jcb.201008107;
RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates
RT autophagosomal maturation.";
RL J. Cell Biol. 192:839-853(2011).
RN [21]
RP INTERACTION PCM1.
RX PubMed=24089205; DOI=10.1038/nature12606;
RA Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
RA Zhong Q.;
RT "Autophagy promotes primary ciliogenesis by removing OFD1 from
RT centriolar satellites.";
RL Nature 502:254-257(2013).
RN [22]
RP INTERACTION WITH TP53INP1.
RX PubMed=22421968; DOI=10.1038/cdd.2012.30;
RA Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
RA Carrier A., Iovanna J.L., Dusetti N.J.;
RT "TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family
RT proteins through the LC3-interacting region (LIR) and promotes
RT autophagy-dependent cell death.";
RL Cell Death Differ. 19:1525-1535(2012).
RN [23]
RP INTERACTION WITH ATG13 AND ULK1.
RX PubMed=23043107; DOI=10.1074/jbc.M112.378109;
RA Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
RA Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
RT "ATG8 family proteins act as scaffolds for assembly of the ULK
RT complex: sequence requirements for LC3-interacting region (LIR)
RT motifs.";
RL J. Biol. Chem. 287:39275-39290(2012).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22311637; DOI=10.1074/mcp.M111.014035;
RA Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
RA Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
RA Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
RA Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
RT "Identification of autophagosome-associated proteins and regulators by
RT quantitative proteomic analysis and genetic screens.";
RL Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
RN [25]
RP INTERACTION WITH TP53INP1 AND TP53INP2.
RX PubMed=22470510; DOI=10.1371/journal.pone.0034034;
RA Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A.,
RA Lamark T., Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U.,
RA Palacin M., Johansen T., Zorzano A.;
RT "DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding
RT dual regulators of autophagy and transcription.";
RL PLoS ONE 7:E34034-E34034(2012).
RN [26]
RP INTERACTION WITH BNIP3, AND FUNCTION.
RX PubMed=23209295; DOI=10.1074/jbc.M112.399345;
RA Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
RA Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
RT "Modulation of serines 17 and 24 in the LC3-interacting region of
RT Bnip3 determines pro-survival mitophagy versus apoptosis.";
RL J. Biol. Chem. 288:1099-1113(2013).
CC -!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic.
CC Modulates intra-Golgi transport through coupling between NSF
CC activity and SNAREs activation. It first stimulates the ATPase
CC activity of NSF which in turn stimulates the association with
CC GOSR1 (By similarity). Involved in autophagy. Plays a role in
CC mitophagy which contributes to regulate mitochondrial quantity and
CC quality by eliminating the mitochondria to a basal level to
CC fulfill cellular energy requirements and preventing excess ROS
CC production. Whereas LC3s are involved in elongation of the
CC phagophore membrane, the GABARAP/GATE-16 subfamily is essential
CC for a later stage in autophagosome maturation.
CC -!- SUBUNIT: Monomer. Interacts with GABRG2, NSF, GOSR1 and beta-
CC tubulin (By similarity). Interacts with ATG3, ATG7, ATG13 and
CC ULK1. Interacts with TP53INP1 and TP53INP2. Interacts with
CC TBC1D25. Directly interacts with SQSTM1 and BNIP3. Interacts with
CC TECPR2 and PCM1.
CC -!- INTERACTION:
CC Q9P2R3:ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908;
CC O75143:ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775;
CC Q676U5:ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909;
CC Q2TAZ0:ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077;
CC Q9NT62:ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094;
CC Q9Y4P1:ATG4B; NbExp=7; IntAct=EBI-720116, EBI-712014;
CC O95352:ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834;
CC Q9Z2F7:Bnip3l (xeno); NbExp=2; IntAct=EBI-720116, EBI-1774669;
CC Q8WXU2:DYX1C1; NbExp=2; IntAct=EBI-720116, EBI-2946907;
CC P00533:EGFR; NbExp=2; IntAct=EBI-720116, EBI-297353;
CC Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338;
CC O75323:GBAS; NbExp=6; IntAct=EBI-720116, EBI-307133;
CC P40939:HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720;
CC O00410:IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424;
CC Q86V97:KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778;
CC Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695;
CC Q14596:NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698;
CC P46934:NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944;
CC Q8TD19:NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009;
CC Q9NS23:RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363;
CC Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390;
CC Q14257:RCN2; NbExp=3; IntAct=EBI-720116, EBI-356710;
CC Q13501:SQSTM1; NbExp=12; IntAct=EBI-720116, EBI-307104;
CC O95210:STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137;
CC Q13188:STK3; NbExp=2; IntAct=EBI-720116, EBI-992580;
CC Q13043:STK4; NbExp=2; IntAct=EBI-720116, EBI-367376;
CC Q8TC07:TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247;
CC Q9UPU7:TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180;
CC O15040:TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991;
CC Q9GZZ9:UBA5; NbExp=10; IntAct=EBI-720116, EBI-747805;
CC O75385:ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasmic
CC vesicle, autophagosome.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
CC brain, heart, prostate, ovary, spleen and skeletal muscle.
CC Expressed at very low levels in lung, thymus and small intestine.
CC -!- PTM: The precursor molecule is cleaved by ATG4B to form the
CC cytosolic form, GABARAPL2-I. This is activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phospholipid to form the
CC membrane-bound form, GABARAPL2-II. ATG4B also mediates the
CC delipidation required for GABARAPL1 recycling when autophagosomes
CC fuse with lysosomes.
CC -!- PTM: The Legionella effector RavZ is a deconjugating enzyme that
CC produces an ATG8 product that would be resistant to reconjugation
CC by the host machinery due to the cleavage of the reactive C-
CC terminal glycine (By similarity).
CC -!- SIMILARITY: Belongs to the ATG8 family.
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DR EMBL; AB030710; BAB21548.1; -; mRNA.
DR EMBL; AF087848; AAK20400.1; -; mRNA.
DR EMBL; AJ010569; CAA09249.1; -; mRNA.
DR EMBL; AF077046; AAD27779.1; -; mRNA.
DR EMBL; CR542217; CAG47013.1; -; mRNA.
DR EMBL; AK289788; BAF82477.1; -; mRNA.
DR EMBL; CH471114; EAW95630.1; -; Genomic_DNA.
DR EMBL; BC005985; AAH05985.1; -; mRNA.
DR EMBL; BC014594; AAH14594.1; -; mRNA.
DR EMBL; BC029601; AAH29601.1; -; mRNA.
DR RefSeq; NP_009216.1; NM_007285.6.
DR UniGene; Hs.461379; -.
DR ProteinModelPortal; P60520; -.
DR SMR; P60520; 1-117.
DR IntAct; P60520; 494.
DR MINT; MINT-1414121; -.
DR STRING; 9606.ENSP00000037243; -.
DR PhosphoSite; P60520; -.
DR DMDM; 44888808; -.
DR UCD-2DPAGE; P60520; -.
DR PaxDb; P60520; -.
DR PRIDE; P60520; -.
DR DNASU; 11345; -.
DR Ensembl; ENST00000037243; ENSP00000037243; ENSG00000034713.
DR GeneID; 11345; -.
DR KEGG; hsa:11345; -.
DR UCSC; uc002fen.3; human.
DR CTD; 11345; -.
DR GeneCards; GC16P075600; -.
DR HGNC; HGNC:13291; GABARAPL2.
DR HPA; HPA036726; -.
DR MIM; 607452; gene.
DR neXtProt; NX_P60520; -.
DR PharmGKB; PA28482; -.
DR eggNOG; NOG249730; -.
DR HOGENOM; HOG000232034; -.
DR HOVERGEN; HBG051706; -.
DR InParanoid; P60520; -.
DR KO; K08341; -.
DR OMA; IRRRITM; -.
DR OrthoDB; EOG70KGRK; -.
DR ChiTaRS; GABARAPL2; human.
DR GeneWiki; GABARAPL2; -.
DR GenomeRNAi; 11345; -.
DR NextBio; 43116; -.
DR PMAP-CutDB; P60520; -.
DR PRO; PR:P60520; -.
DR ArrayExpress; P60520; -.
DR Bgee; P60520; -.
DR CleanEx; HS_GABARAPL2; -.
DR Genevestigator; P60520; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; NAS:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004241; Atg8_like.
DR PANTHER; PTHR10969; PTHR10969; 1.
DR Pfam; PF02991; Atg8; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Complete proteome; Cytoplasmic vesicle;
KW Golgi apparatus; Lipoprotein; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 116 Gamma-aminobutyric acid receptor-
FT associated protein-like 2.
FT /FTId=PRO_0000212373.
FT PROPEP 117 117 Removed in mature form.
FT /FTId=PRO_0000423070.
FT REGION 1 22 Interaction with beta-tubulin (By
FT similarity).
FT REGION 36 68 Interaction with GABRG2 (Potential).
FT SITE 116 117 Cleavage; by ATG4.
FT MOD_RES 24 24 N6-acetyllysine.
FT MOD_RES 39 39 Phosphoserine.
FT LIPID 116 116 Phosphatidylethanolamine amidated
FT glycine.
FT VARIANT 51 51 V -> A (in dbSNP:rs11556291).
FT /FTId=VAR_049756.
FT MUTAGEN 116 116 G->A: Impairs localization at the
FT autophagosomal membrane.
FT CONFLICT 29 29 V -> F (in Ref. 4; AAD27779).
SQ SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF
//
MIM
607452
*RECORD*
*FIELD* NO
607452
*FIELD* TI
*607452 GABA-A RECEPTOR-ASSOCIATED PROTEIN-LIKE PROTEIN 2; GABARAPL2
;;GATE16, BOVINE, HOMOLOG OF; GATE16
read more*FIELD* TX
CLONING
By database searching for sequences showing homology to GABARAP
(605125), Xin et al. (2001) identified GABARAPL2. The deduced protein
contains 117 amino acids and has a calculated molecular mass of 13.7 kD.
Like GABARAP, it contains a basic N-terminal tubulin binding domain and
a GABA-A receptor binding domain. GABARAPL2 shares 57% identity with
GABARAP and 100% amino acid sequence identity with bovine brain GATE16
(Golgi-associated ATPase enhancer of 16 kD), rat Gabarapl2, and mouse
Gabarapl2. Northern blot analysis revealed ubiquitous expression of a
1.35-kb transcript with high levels in heart, brain, testis, prostate,
ovary, spleen, and skeletal muscle, and low levels in lung, thymus, and
small intestine. Xin et al. (2001) also cloned the mouse Gabarapl2 gene
from a mouse brain cDNA library.
GENE FUNCTION
Sagiv et al. (2000) cloned and characterized bovine brain GABARAPL2,
which they called GATE16. GABARAPL2 had activity as a soluble transport
factor, it interacted with N-ethylmaleimide-sensitive factor (NSF;
601633) and stimulated its ATPase activity, and interacted with the
Golgi v-SNARE (GOS28; 604026) in an NSF-dependent manner. Sagiv et al.
(2000) proposed that GABARAPL2 modulates intra-Golgi transport by
coupling NSF activity and SNARE activation.
Apg8 is a ubiquitin-like protein involved in autophagy in yeast. A
cysteine protease, Apg4, cleaves Apg8 to create a C-terminal glycine
required for ubiquitin-like modification reactions. There are at least 4
mammalian Apg8 homologs: GATE16, GABARAP, MAP1LC3 (see 601242), and
APG8L (GABARAPL1; 607420). Hemelaar et al. (2003) found that mouse Atg4b
(611338) acted on the C termini of these 4 Atg8 homologs, and that the
reaction required the active-site cysteine of Atg4b. Although the amino
acid sequences of these Apg8 homologs differ from one another by as much
as 71%, their affinities for Atg4b were roughly comparable in
competition experiments.
Behrends et al. (2010) reported a proteomic analysis of the autophagy
interaction network (AIN) in human cells under conditions of ongoing
(basal) autophagy, revealing a network of 751 interactions among 409
candidate interacting proteins with extensive connectivity among
subnetworks. Many new AIN components have roles in vesicle trafficking,
protein or lipid phosphorylation, and protein ubiquitination, and affect
autophagosome number or flux when depleted by RNA interference. The 6
human orthologs of yeast autophagy-8 (ATG8), MAP1LC3A, MAP1LC3B
(609604), MAP1LC3C (609605), GABARAP (605125), GABARAPL1, and GABARAPL2,
interact with a cohort of 67 proteins, with extensive binding partner
overlap between family members, and frequent involvement of a conserved
surface on ATG8 proteins known to interact with LC3-interacting regions
in partner proteins. Behrends et al. (2010) concluded that their studies
provided a global view of the mammalian autophagy interaction landscape
and a resource for mechanistic analysis of this critical protein
homeostasis pathway.
GENE STRUCTURE
Xin et al. (2001) determined that the GABARAPL2 gene contains 4 exons.
MAPPING
By radiation hybrid analysis, Xin et al. (2001) mapped the GABARAPL2
gene to chromosome 16q22.3-q24.1.
*FIELD* RF
1. Behrends, C.; Sowa, M. E.; Gygi, S. P.; Harper, J. W.: Network
organization of the human autophagy system. Nature 466: 68-76, 2010.
2. Hemelaar, J.; Lelyveld, V. S.; Kessler, B. M.; Ploegh, H. L.:
A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like
proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol. Chem. 278:
51841-51850, 2003.
3. Sagiv, Y.; Legesse-Miller, A.; Porat, A.; Elazar, Z.: GATE-16,
a membrane transport modulator, interacts with NSF and the Golgi v-SNARE
GOS-28. EMBO J. 19: 1494-1504, 2000.
4. 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.
*FIELD* CN
Ada Hamosh - updated: 9/27/2010
Patricia A. Hartz - updated: 8/3/2007
*FIELD* CD
Patricia A. Hartz: 12/27/2002
*FIELD* ED
alopez: 09/28/2010
terry: 9/27/2010
mgross: 8/16/2007
terry: 8/3/2007
mgross: 9/26/2005
joanna: 2/28/2003
cwells: 12/27/2002
*RECORD*
*FIELD* NO
607452
*FIELD* TI
*607452 GABA-A RECEPTOR-ASSOCIATED PROTEIN-LIKE PROTEIN 2; GABARAPL2
;;GATE16, BOVINE, HOMOLOG OF; GATE16
read more*FIELD* TX
CLONING
By database searching for sequences showing homology to GABARAP
(605125), Xin et al. (2001) identified GABARAPL2. The deduced protein
contains 117 amino acids and has a calculated molecular mass of 13.7 kD.
Like GABARAP, it contains a basic N-terminal tubulin binding domain and
a GABA-A receptor binding domain. GABARAPL2 shares 57% identity with
GABARAP and 100% amino acid sequence identity with bovine brain GATE16
(Golgi-associated ATPase enhancer of 16 kD), rat Gabarapl2, and mouse
Gabarapl2. Northern blot analysis revealed ubiquitous expression of a
1.35-kb transcript with high levels in heart, brain, testis, prostate,
ovary, spleen, and skeletal muscle, and low levels in lung, thymus, and
small intestine. Xin et al. (2001) also cloned the mouse Gabarapl2 gene
from a mouse brain cDNA library.
GENE FUNCTION
Sagiv et al. (2000) cloned and characterized bovine brain GABARAPL2,
which they called GATE16. GABARAPL2 had activity as a soluble transport
factor, it interacted with N-ethylmaleimide-sensitive factor (NSF;
601633) and stimulated its ATPase activity, and interacted with the
Golgi v-SNARE (GOS28; 604026) in an NSF-dependent manner. Sagiv et al.
(2000) proposed that GABARAPL2 modulates intra-Golgi transport by
coupling NSF activity and SNARE activation.
Apg8 is a ubiquitin-like protein involved in autophagy in yeast. A
cysteine protease, Apg4, cleaves Apg8 to create a C-terminal glycine
required for ubiquitin-like modification reactions. There are at least 4
mammalian Apg8 homologs: GATE16, GABARAP, MAP1LC3 (see 601242), and
APG8L (GABARAPL1; 607420). Hemelaar et al. (2003) found that mouse Atg4b
(611338) acted on the C termini of these 4 Atg8 homologs, and that the
reaction required the active-site cysteine of Atg4b. Although the amino
acid sequences of these Apg8 homologs differ from one another by as much
as 71%, their affinities for Atg4b were roughly comparable in
competition experiments.
Behrends et al. (2010) reported a proteomic analysis of the autophagy
interaction network (AIN) in human cells under conditions of ongoing
(basal) autophagy, revealing a network of 751 interactions among 409
candidate interacting proteins with extensive connectivity among
subnetworks. Many new AIN components have roles in vesicle trafficking,
protein or lipid phosphorylation, and protein ubiquitination, and affect
autophagosome number or flux when depleted by RNA interference. The 6
human orthologs of yeast autophagy-8 (ATG8), MAP1LC3A, MAP1LC3B
(609604), MAP1LC3C (609605), GABARAP (605125), GABARAPL1, and GABARAPL2,
interact with a cohort of 67 proteins, with extensive binding partner
overlap between family members, and frequent involvement of a conserved
surface on ATG8 proteins known to interact with LC3-interacting regions
in partner proteins. Behrends et al. (2010) concluded that their studies
provided a global view of the mammalian autophagy interaction landscape
and a resource for mechanistic analysis of this critical protein
homeostasis pathway.
GENE STRUCTURE
Xin et al. (2001) determined that the GABARAPL2 gene contains 4 exons.
MAPPING
By radiation hybrid analysis, Xin et al. (2001) mapped the GABARAPL2
gene to chromosome 16q22.3-q24.1.
*FIELD* RF
1. Behrends, C.; Sowa, M. E.; Gygi, S. P.; Harper, J. W.: Network
organization of the human autophagy system. Nature 466: 68-76, 2010.
2. Hemelaar, J.; Lelyveld, V. S.; Kessler, B. M.; Ploegh, H. L.:
A single protease, Apg4B, is specific for the autophagy-related ubiquitin-like
proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L. J. Biol. Chem. 278:
51841-51850, 2003.
3. Sagiv, Y.; Legesse-Miller, A.; Porat, A.; Elazar, Z.: GATE-16,
a membrane transport modulator, interacts with NSF and the Golgi v-SNARE
GOS-28. EMBO J. 19: 1494-1504, 2000.
4. 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.
*FIELD* CN
Ada Hamosh - updated: 9/27/2010
Patricia A. Hartz - updated: 8/3/2007
*FIELD* CD
Patricia A. Hartz: 12/27/2002
*FIELD* ED
alopez: 09/28/2010
terry: 9/27/2010
mgross: 8/16/2007
terry: 8/3/2007
mgross: 9/26/2005
joanna: 2/28/2003
cwells: 12/27/2002