Full text data of GABARAPL1
GABARAPL1
(GEC1)
[Confidence: low (only semi-automatic identification from reviews)]
Gamma-aminobutyric acid receptor-associated protein-like 1 (Early estrogen-regulated protein; GABA(A) receptor-associated protein-like 1; Glandular epithelial cell protein 1; GEC-1; Flags: Precursor)
Gamma-aminobutyric acid receptor-associated protein-like 1 (Early estrogen-regulated protein; GABA(A) receptor-associated protein-like 1; Glandular epithelial cell protein 1; GEC-1; Flags: Precursor)
UniProt
Q9H0R8
ID GBRL1_HUMAN Reviewed; 117 AA.
AC Q9H0R8; B4E0Y7; Q6FIE6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 1;
DE AltName: Full=Early estrogen-regulated protein;
DE AltName: Full=GABA(A) receptor-associated protein-like 1;
DE AltName: Full=Glandular epithelial cell protein 1;
DE Short=GEC-1;
DE Flags: Precursor;
GN Name=GABARAPL1; Synonyms=GEC1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11374880; DOI=10.1006/bbrc.2001.4908;
RA Vernier-Magnin S., Muller S., Sallot M., Radom J., Musard J.-F.,
RA Adami P., Dulieu P., Remy-Martin J.-P., Jouvenot M., Fraichard A.;
RT "A novel early estrogen-regulated gene gec1 encodes a protein related
RT to GABARAP.";
RL Biochem. Biophys. Res. Commun. 284:118-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 2).
RA Liu C., Yu L.;
RT "Alternative splicing pattern analysis of human Atg8 family
RT proteins.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [10]
RP FUNCTION, AND INTERACTION WITH OPRK1.
RX PubMed=16431922; DOI=10.1074/jbc.M509805200;
RA Chen C., Li J.-G., Chen Y., Huang P., Wang Y., Liu-Chen L.-Y.;
RT "GEC1 interacts with the kappa opioid receptor and enhances expression
RT of the receptor.";
RL J. Biol. Chem. 281:7983-7993(2006).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, LIPIDATION, AND
RP MUTAGENESIS OF GLY-116.
RX PubMed=20404487; DOI=10.4161/auto.6.4.11819;
RA Chakrama F.Z., Seguin-Py S., Le Grand J.N., Fraichard A.,
RA Delage-Mourroux R., Despouy G., Perez V., Jouvenot M.,
RA Boyer-Guittaut M.;
RT "GABARAPL1 (GEC1) associates with autophagic vesicles.";
RL Autophagy 6:495-505(2010).
RN [13]
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 [14]
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 [15]
RP INTERACTION WITH MAPK15.
RX PubMed=22948227; DOI=10.4161/auto.21857;
RA Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M.,
RA Dall'Armi C., Piccioni F., Verrotti di Pianella A., Chiariello M.;
RT "MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP
RT proteins.";
RL Autophagy 8:1724-1740(2012).
RN [16]
RP INTERACTION WITH ATG13; RB1CC1 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 [17]
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 [18]
RP DECONJUGATION BY LEGIONELLA RAVZ.
RX PubMed=23112293; DOI=10.1126/science.1227026;
RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J.,
RA Roy C.R.;
RT "The Legionella effector RavZ inhibits host autophagy through
RT irreversible Atg8 deconjugation.";
RL Science 338:1072-1076(2012).
RN [19]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23690988; DOI=10.1371/journal.pone.0063133;
RA Le Grand J.N., Bon K., Fraichard A., Zhang J., Jouvenot M.,
RA Risold P.Y., Boyer-Guittaut M., Delage-Mourroux R.;
RT "Specific distribution of the autophagic protein GABARAPL1/GEC1 in the
RT developing and adult mouse brain and identification of neuronal
RT populations expressing GABARAPL1/GEC1.";
RL PLoS ONE 8:E63133-E63133(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-111.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human gamma-aminobutyric acid receptor-
RT associated protein-like 1 (GABARAP1).";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: Ubiquitin-like modifier that increases cell-surface
CC expression of kappa-type opioid receptor through facilitating
CC anterograde intracellular trafficking of the receptor. Involved in
CC formation of autophagosomal vacuoles. Whereas LC3s are involved in
CC elongation of the phagophore membrane, the GABARAP/GATE-16
CC subfamily is essential for a later stage in autophagosome
CC maturation.
CC -!- SUBUNIT: Interacts with GABRG2 and beta-tubulin (By similarity).
CC Interacts with ATG13, OPRK1, RB1CC1 and ULK1. Interacts with
CC TP53INP1 and TP53INP2. Directly interacts with SQSTM1. Interacts
CC with ATG3, ATG7 and MAP15. Interacts with TECPR2.
CC -!- INTERACTION:
CC O75143:ATG13; NbExp=2; IntAct=EBI-746969, EBI-2798775;
CC Q2TAZ0:ATG2A; NbExp=3; IntAct=EBI-746969, EBI-2514077;
CC Q9NT62:ATG3; NbExp=3; IntAct=EBI-746969, EBI-988094;
CC Q9Y4P1:ATG4B; NbExp=7; IntAct=EBI-746969, EBI-712014;
CC O95352:ATG7; NbExp=6; IntAct=EBI-746969, EBI-987834;
CC Q9Z2F7:Bnip3l (xeno); NbExp=4; IntAct=EBI-3464833, EBI-1774669;
CC Q14677:CLINT1; NbExp=2; IntAct=EBI-746969, EBI-1171113;
CC Q8WXU2:DYX1C1; NbExp=2; IntAct=EBI-746969, EBI-2946907;
CC Q8TF40:FNIP1; NbExp=2; IntAct=EBI-746969, EBI-2946919;
CC Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-746969, EBI-2869338;
CC O75323:GBAS; NbExp=6; IntAct=EBI-746969, EBI-307133;
CC P40939:HADHA; NbExp=4; IntAct=EBI-746969, EBI-356720;
CC P55084:HADHB; NbExp=4; IntAct=EBI-746969, EBI-356635;
CC O00410:IPO5; NbExp=4; IntAct=EBI-746969, EBI-356424;
CC Q86V97:KBTBD6; NbExp=4; IntAct=EBI-746969, EBI-2514778;
CC Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-746969, EBI-473695;
CC Q14596:NBR1; NbExp=4; IntAct=EBI-746969, EBI-742698;
CC Q8NI08:NCOA7; NbExp=2; IntAct=EBI-746969, EBI-80799;
CC P46934:NEDD4; NbExp=6; IntAct=EBI-746969, EBI-726944;
CC Q8TD19:NEK9; NbExp=6; IntAct=EBI-746969, EBI-1044009;
CC Q92636:NSMAF; NbExp=6; IntAct=EBI-746969, EBI-2947053;
CC P41145:OPRK1; NbExp=5; IntAct=EBI-3464833, EBI-925028;
CC P10644:PRKAR1A; NbExp=2; IntAct=EBI-746969, EBI-476431;
CC Q9Y3P9:RABGAP1; NbExp=2; IntAct=EBI-746969, EBI-1057545;
CC Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-746969, EBI-367390;
CC Q14151:SAFB2; NbExp=2; IntAct=EBI-746969, EBI-352869;
CC Q13501:SQSTM1; NbExp=7; IntAct=EBI-746969, EBI-307104;
CC O95210:STBD1; NbExp=7; IntAct=EBI-746969, EBI-2947137;
CC Q13188:STK3; NbExp=2; IntAct=EBI-746969, EBI-992580;
CC Q13043:STK4; NbExp=2; IntAct=EBI-746969, EBI-367376;
CC Q8TC07:TBC1D15; NbExp=2; IntAct=EBI-746969, EBI-1048247;
CC Q9UPU7:TBC1D2B; NbExp=5; IntAct=EBI-746969, EBI-2947180;
CC O15040:TECPR2; NbExp=2; IntAct=EBI-746969, EBI-2946991;
CC Q9GZZ9:UBA5; NbExp=2; IntAct=EBI-746969, EBI-747805;
CC O75385:ULK1; NbExp=2; IntAct=EBI-746969, EBI-908831;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle
CC membrane; Lipid-anchor. Endoplasmic reticulum (By similarity).
CC Golgi apparatus (By similarity). Cytoplasmic vesicle,
CC autophagosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0R8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0R8-2; Sequence=VSP_044422;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in
CC the brain, heart, peripheral blood leukocytes, liver, kidney,
CC placenta and skeletal muscle. Expressed at very low levels in
CC thymus and small intestine. In the brain, expression is
CC particularly intense in motoneurons in the embryo and in neurons
CC involved in somatomotor and neuroendocrine functions in the adult,
CC particularly in the substantia nigra pars compacta.
CC -!- PTM: The precursor molecule is cleaved by ATG4B to form the
CC cytosolic form, GABARAPL1-I. This is activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phospholipid to form the
CC membrane-bound form, GABARAPL1-II (By similarity). ATG4B also
CC mediates the delipidation required for GABARAPL1 recycling when
CC autophagosomes 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.
CC -!- SIMILARITY: Belongs to the ATG8 family.
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DR EMBL; AF287012; AAK55962.1; -; mRNA.
DR EMBL; AF087847; AAK20399.1; -; mRNA.
DR EMBL; JN663881; AEZ06294.1; -; mRNA.
DR EMBL; AL136676; CAB66611.1; -; mRNA.
DR EMBL; AK303581; BAG64599.1; -; mRNA.
DR EMBL; CR533480; CAG38511.1; -; mRNA.
DR EMBL; AC115676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96164.1; -; Genomic_DNA.
DR EMBL; BC009309; AAH09309.1; -; mRNA.
DR EMBL; BC028315; AAH28315.1; -; mRNA.
DR RefSeq; NP_113600.1; NM_031412.2.
DR RefSeq; XP_005253401.1; XM_005253344.1.
DR UniGene; Hs.524250; -.
DR PDB; 2L8J; NMR; -; A=2-115.
DR PDB; 2R2Q; X-ray; 1.65 A; A/B=3-111.
DR PDBsum; 2L8J; -.
DR PDBsum; 2R2Q; -.
DR ProteinModelPortal; Q9H0R8; -.
DR SMR; Q9H0R8; 3-111.
DR IntAct; Q9H0R8; 500.
DR MINT; MINT-1456875; -.
DR PhosphoSite; Q9H0R8; -.
DR DMDM; 44887973; -.
DR PaxDb; Q9H0R8; -.
DR PRIDE; Q9H0R8; -.
DR DNASU; 23710; -.
DR Ensembl; ENST00000266458; ENSP00000266458; ENSG00000139112.
DR Ensembl; ENST00000421801; ENSP00000411256; ENSG00000139112.
DR Ensembl; ENST00000543602; ENSP00000445857; ENSG00000139112.
DR Ensembl; ENST00000545887; ENSP00000444186; ENSG00000139112.
DR GeneID; 23710; -.
DR KEGG; hsa:23710; -.
DR UCSC; uc001qxs.3; human.
DR CTD; 23710; -.
DR GeneCards; GC12P010365; -.
DR H-InvDB; HIX0036758; -.
DR HGNC; HGNC:4068; GABARAPL1.
DR HPA; HPA051386; -.
DR MIM; 607420; gene.
DR neXtProt; NX_Q9H0R8; -.
DR PharmGKB; PA28481; -.
DR eggNOG; NOG281408; -.
DR HOGENOM; HOG000232034; -.
DR HOVERGEN; HBG051706; -.
DR InParanoid; Q9H0R8; -.
DR KO; K08341; -.
DR OMA; SRIREKH; -.
DR ChiTaRS; GABARAPL1; human.
DR EvolutionaryTrace; Q9H0R8; -.
DR GenomeRNAi; 23710; -.
DR NextBio; 35476887; -.
DR PMAP-CutDB; Q9H0R8; -.
DR PRO; PR:Q9H0R8; -.
DR ArrayExpress; Q9H0R8; -.
DR Bgee; Q9H0R8; -.
DR CleanEx; HS_GABARAPL1; -.
DR Genevestigator; Q9H0R8; -.
DR GO; GO:0005776; C:autophagic vacuole; IDA:MGI.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; 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 3D-structure; Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Microtubule;
KW Reference proteome.
FT CHAIN 1 116 Gamma-aminobutyric acid receptor-
FT associated protein-like 1.
FT /FTId=PRO_0000212369.
FT PROPEP 117 117 Removed in mature form.
FT /FTId=PRO_0000420208.
FT REGION 1 22 Interaction with beta-tubulin (By
FT similarity).
FT REGION 36 68 Interaction with GABRG2 (By similarity).
FT SITE 115 116 Cleavage; by RavZ.
FT SITE 116 117 Cleavage; by ATG4B.
FT LIPID 116 116 Phosphatidylethanolamine amidated glycine
FT (Probable).
FT VAR_SEQ 97 117 DNHEEDYFLYVAYSDESVYGK -> VMVLVAQYWMPSSAVW
FT HPLALVLDALITHLRSGAEGVIYPDPLTYGSVRL (in
FT isoform 2).
FT /FTId=VSP_044422.
FT MUTAGEN 116 116 G->A: No processing of precursor.
FT HELIX 4 8
FT HELIX 11 24
FT STRAND 28 35
FT STRAND 48 52
FT HELIX 57 67
FT STRAND 77 80
FT HELIX 91 98
FT STRAND 105 110
SQ SEQUENCE 117 AA; 14044 MW; 7F56E345255F564B CRC64;
MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
//
ID GBRL1_HUMAN Reviewed; 117 AA.
AC Q9H0R8; B4E0Y7; Q6FIE6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 1;
DE AltName: Full=Early estrogen-regulated protein;
DE AltName: Full=GABA(A) receptor-associated protein-like 1;
DE AltName: Full=Glandular epithelial cell protein 1;
DE Short=GEC-1;
DE Flags: Precursor;
GN Name=GABARAPL1; Synonyms=GEC1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11374880; DOI=10.1006/bbrc.2001.4908;
RA Vernier-Magnin S., Muller S., Sallot M., Radom J., Musard J.-F.,
RA Adami P., Dulieu P., Remy-Martin J.-P., Jouvenot M., Fraichard A.;
RT "A novel early estrogen-regulated gene gec1 encodes a protein related
RT to GABARAP.";
RL Biochem. Biophys. Res. Commun. 284:118-125(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 2).
RA Liu C., Yu L.;
RT "Alternative splicing pattern analysis of human Atg8 family
RT proteins.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [10]
RP FUNCTION, AND INTERACTION WITH OPRK1.
RX PubMed=16431922; DOI=10.1074/jbc.M509805200;
RA Chen C., Li J.-G., Chen Y., Huang P., Wang Y., Liu-Chen L.-Y.;
RT "GEC1 interacts with the kappa opioid receptor and enhances expression
RT of the receptor.";
RL J. Biol. Chem. 281:7983-7993(2006).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, LIPIDATION, AND
RP MUTAGENESIS OF GLY-116.
RX PubMed=20404487; DOI=10.4161/auto.6.4.11819;
RA Chakrama F.Z., Seguin-Py S., Le Grand J.N., Fraichard A.,
RA Delage-Mourroux R., Despouy G., Perez V., Jouvenot M.,
RA Boyer-Guittaut M.;
RT "GABARAPL1 (GEC1) associates with autophagic vesicles.";
RL Autophagy 6:495-505(2010).
RN [13]
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 [14]
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 [15]
RP INTERACTION WITH MAPK15.
RX PubMed=22948227; DOI=10.4161/auto.21857;
RA Colecchia D., Strambi A., Sanzone S., Iavarone C., Rossi M.,
RA Dall'Armi C., Piccioni F., Verrotti di Pianella A., Chiariello M.;
RT "MAPK15/ERK8 stimulates autophagy by interacting with LC3 and GABARAP
RT proteins.";
RL Autophagy 8:1724-1740(2012).
RN [16]
RP INTERACTION WITH ATG13; RB1CC1 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 [17]
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 [18]
RP DECONJUGATION BY LEGIONELLA RAVZ.
RX PubMed=23112293; DOI=10.1126/science.1227026;
RA Choy A., Dancourt J., Mugo B., O'Connor T.J., Isberg R.R., Melia T.J.,
RA Roy C.R.;
RT "The Legionella effector RavZ inhibits host autophagy through
RT irreversible Atg8 deconjugation.";
RL Science 338:1072-1076(2012).
RN [19]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23690988; DOI=10.1371/journal.pone.0063133;
RA Le Grand J.N., Bon K., Fraichard A., Zhang J., Jouvenot M.,
RA Risold P.Y., Boyer-Guittaut M., Delage-Mourroux R.;
RT "Specific distribution of the autophagic protein GABARAPL1/GEC1 in the
RT developing and adult mouse brain and identification of neuronal
RT populations expressing GABARAPL1/GEC1.";
RL PLoS ONE 8:E63133-E63133(2013).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 3-111.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human gamma-aminobutyric acid receptor-
RT associated protein-like 1 (GABARAP1).";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: Ubiquitin-like modifier that increases cell-surface
CC expression of kappa-type opioid receptor through facilitating
CC anterograde intracellular trafficking of the receptor. Involved in
CC formation of autophagosomal vacuoles. Whereas LC3s are involved in
CC elongation of the phagophore membrane, the GABARAP/GATE-16
CC subfamily is essential for a later stage in autophagosome
CC maturation.
CC -!- SUBUNIT: Interacts with GABRG2 and beta-tubulin (By similarity).
CC Interacts with ATG13, OPRK1, RB1CC1 and ULK1. Interacts with
CC TP53INP1 and TP53INP2. Directly interacts with SQSTM1. Interacts
CC with ATG3, ATG7 and MAP15. Interacts with TECPR2.
CC -!- INTERACTION:
CC O75143:ATG13; NbExp=2; IntAct=EBI-746969, EBI-2798775;
CC Q2TAZ0:ATG2A; NbExp=3; IntAct=EBI-746969, EBI-2514077;
CC Q9NT62:ATG3; NbExp=3; IntAct=EBI-746969, EBI-988094;
CC Q9Y4P1:ATG4B; NbExp=7; IntAct=EBI-746969, EBI-712014;
CC O95352:ATG7; NbExp=6; IntAct=EBI-746969, EBI-987834;
CC Q9Z2F7:Bnip3l (xeno); NbExp=4; IntAct=EBI-3464833, EBI-1774669;
CC Q14677:CLINT1; NbExp=2; IntAct=EBI-746969, EBI-1171113;
CC Q8WXU2:DYX1C1; NbExp=2; IntAct=EBI-746969, EBI-2946907;
CC Q8TF40:FNIP1; NbExp=2; IntAct=EBI-746969, EBI-2946919;
CC Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-746969, EBI-2869338;
CC O75323:GBAS; NbExp=6; IntAct=EBI-746969, EBI-307133;
CC P40939:HADHA; NbExp=4; IntAct=EBI-746969, EBI-356720;
CC P55084:HADHB; NbExp=4; IntAct=EBI-746969, EBI-356635;
CC O00410:IPO5; NbExp=4; IntAct=EBI-746969, EBI-356424;
CC Q86V97:KBTBD6; NbExp=4; IntAct=EBI-746969, EBI-2514778;
CC Q8WVZ9:KBTBD7; NbExp=3; IntAct=EBI-746969, EBI-473695;
CC Q14596:NBR1; NbExp=4; IntAct=EBI-746969, EBI-742698;
CC Q8NI08:NCOA7; NbExp=2; IntAct=EBI-746969, EBI-80799;
CC P46934:NEDD4; NbExp=6; IntAct=EBI-746969, EBI-726944;
CC Q8TD19:NEK9; NbExp=6; IntAct=EBI-746969, EBI-1044009;
CC Q92636:NSMAF; NbExp=6; IntAct=EBI-746969, EBI-2947053;
CC P41145:OPRK1; NbExp=5; IntAct=EBI-3464833, EBI-925028;
CC P10644:PRKAR1A; NbExp=2; IntAct=EBI-746969, EBI-476431;
CC Q9Y3P9:RABGAP1; NbExp=2; IntAct=EBI-746969, EBI-1057545;
CC Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-746969, EBI-367390;
CC Q14151:SAFB2; NbExp=2; IntAct=EBI-746969, EBI-352869;
CC Q13501:SQSTM1; NbExp=7; IntAct=EBI-746969, EBI-307104;
CC O95210:STBD1; NbExp=7; IntAct=EBI-746969, EBI-2947137;
CC Q13188:STK3; NbExp=2; IntAct=EBI-746969, EBI-992580;
CC Q13043:STK4; NbExp=2; IntAct=EBI-746969, EBI-367376;
CC Q8TC07:TBC1D15; NbExp=2; IntAct=EBI-746969, EBI-1048247;
CC Q9UPU7:TBC1D2B; NbExp=5; IntAct=EBI-746969, EBI-2947180;
CC O15040:TECPR2; NbExp=2; IntAct=EBI-746969, EBI-2946991;
CC Q9GZZ9:UBA5; NbExp=2; IntAct=EBI-746969, EBI-747805;
CC O75385:ULK1; NbExp=2; IntAct=EBI-746969, EBI-908831;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasmic vesicle
CC membrane; Lipid-anchor. Endoplasmic reticulum (By similarity).
CC Golgi apparatus (By similarity). Cytoplasmic vesicle,
CC autophagosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0R8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0R8-2; Sequence=VSP_044422;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at very high levels in
CC the brain, heart, peripheral blood leukocytes, liver, kidney,
CC placenta and skeletal muscle. Expressed at very low levels in
CC thymus and small intestine. In the brain, expression is
CC particularly intense in motoneurons in the embryo and in neurons
CC involved in somatomotor and neuroendocrine functions in the adult,
CC particularly in the substantia nigra pars compacta.
CC -!- PTM: The precursor molecule is cleaved by ATG4B to form the
CC cytosolic form, GABARAPL1-I. This is activated by APG7L/ATG7,
CC transferred to ATG3 and conjugated to phospholipid to form the
CC membrane-bound form, GABARAPL1-II (By similarity). ATG4B also
CC mediates the delipidation required for GABARAPL1 recycling when
CC autophagosomes 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.
CC -!- SIMILARITY: Belongs to the ATG8 family.
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DR EMBL; AF287012; AAK55962.1; -; mRNA.
DR EMBL; AF087847; AAK20399.1; -; mRNA.
DR EMBL; JN663881; AEZ06294.1; -; mRNA.
DR EMBL; AL136676; CAB66611.1; -; mRNA.
DR EMBL; AK303581; BAG64599.1; -; mRNA.
DR EMBL; CR533480; CAG38511.1; -; mRNA.
DR EMBL; AC115676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96164.1; -; Genomic_DNA.
DR EMBL; BC009309; AAH09309.1; -; mRNA.
DR EMBL; BC028315; AAH28315.1; -; mRNA.
DR RefSeq; NP_113600.1; NM_031412.2.
DR RefSeq; XP_005253401.1; XM_005253344.1.
DR UniGene; Hs.524250; -.
DR PDB; 2L8J; NMR; -; A=2-115.
DR PDB; 2R2Q; X-ray; 1.65 A; A/B=3-111.
DR PDBsum; 2L8J; -.
DR PDBsum; 2R2Q; -.
DR ProteinModelPortal; Q9H0R8; -.
DR SMR; Q9H0R8; 3-111.
DR IntAct; Q9H0R8; 500.
DR MINT; MINT-1456875; -.
DR PhosphoSite; Q9H0R8; -.
DR DMDM; 44887973; -.
DR PaxDb; Q9H0R8; -.
DR PRIDE; Q9H0R8; -.
DR DNASU; 23710; -.
DR Ensembl; ENST00000266458; ENSP00000266458; ENSG00000139112.
DR Ensembl; ENST00000421801; ENSP00000411256; ENSG00000139112.
DR Ensembl; ENST00000543602; ENSP00000445857; ENSG00000139112.
DR Ensembl; ENST00000545887; ENSP00000444186; ENSG00000139112.
DR GeneID; 23710; -.
DR KEGG; hsa:23710; -.
DR UCSC; uc001qxs.3; human.
DR CTD; 23710; -.
DR GeneCards; GC12P010365; -.
DR H-InvDB; HIX0036758; -.
DR HGNC; HGNC:4068; GABARAPL1.
DR HPA; HPA051386; -.
DR MIM; 607420; gene.
DR neXtProt; NX_Q9H0R8; -.
DR PharmGKB; PA28481; -.
DR eggNOG; NOG281408; -.
DR HOGENOM; HOG000232034; -.
DR HOVERGEN; HBG051706; -.
DR InParanoid; Q9H0R8; -.
DR KO; K08341; -.
DR OMA; SRIREKH; -.
DR ChiTaRS; GABARAPL1; human.
DR EvolutionaryTrace; Q9H0R8; -.
DR GenomeRNAi; 23710; -.
DR NextBio; 35476887; -.
DR PMAP-CutDB; Q9H0R8; -.
DR PRO; PR:Q9H0R8; -.
DR ArrayExpress; Q9H0R8; -.
DR Bgee; Q9H0R8; -.
DR CleanEx; HS_GABARAPL1; -.
DR Genevestigator; Q9H0R8; -.
DR GO; GO:0005776; C:autophagic vacuole; IDA:MGI.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; 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 3D-structure; Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Microtubule;
KW Reference proteome.
FT CHAIN 1 116 Gamma-aminobutyric acid receptor-
FT associated protein-like 1.
FT /FTId=PRO_0000212369.
FT PROPEP 117 117 Removed in mature form.
FT /FTId=PRO_0000420208.
FT REGION 1 22 Interaction with beta-tubulin (By
FT similarity).
FT REGION 36 68 Interaction with GABRG2 (By similarity).
FT SITE 115 116 Cleavage; by RavZ.
FT SITE 116 117 Cleavage; by ATG4B.
FT LIPID 116 116 Phosphatidylethanolamine amidated glycine
FT (Probable).
FT VAR_SEQ 97 117 DNHEEDYFLYVAYSDESVYGK -> VMVLVAQYWMPSSAVW
FT HPLALVLDALITHLRSGAEGVIYPDPLTYGSVRL (in
FT isoform 2).
FT /FTId=VSP_044422.
FT MUTAGEN 116 116 G->A: No processing of precursor.
FT HELIX 4 8
FT HELIX 11 24
FT STRAND 28 35
FT STRAND 48 52
FT HELIX 57 67
FT STRAND 77 80
FT HELIX 91 98
FT STRAND 105 110
SQ SEQUENCE 117 AA; 14044 MW; 7F56E345255F564B CRC64;
MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF
YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK
//
MIM
607420
*RECORD*
*FIELD* NO
607420
*FIELD* TI
*607420 GABA-A RECEPTOR-ASSOCIATED PROTEIN-LIKE PROTEIN 1; GABARAPL1
;;GABARAP-LIKE PROTEIN 1;;
read moreGLANDULAR EPITHELIAL CELL PROTEIN 1; GEC1;;
APG8-LIKE; APG8L
*FIELD* TX
CLONING
Pellerin et al. (1993) cloned guinea pig Gabarapl1, which they called
Gec1, through a differential screen of estrogen-regulated sequences
expressed by endometrial glandular epithelial cells. Using the guinea
pig sequence as probe, Vernier-Magnin et al. (2001) cloned human
GABARAPL1, which they called GEC1, from a placenta cDNA library. The
deduced 117-amino acid protein shares 100% amino acid identity with
guinea pig Gabarapl1 and 87% identity with GABARAP (605125). Northern
blot analysis revealed a 1.9-kb transcript in all tissues examined.
By Northern blot analysis, Xin et al. (2001) found a 2.3-kb GABARAPL1
transcript expressed in all tissues examined, with highest levels in
brain, heart, peripheral blood leukocytes, liver, kidney, placenta, and
skeletal muscle. Moderate expression was found in pancreas, prostate,
testis, ovary, lung, spleen, and colon, and low expression was found in
thymus and small intestine. In addition, a 4.2-kb transcript was found
in low abundance in ovary, peripheral blood leukocytes, and liver, and a
1.7-kb transcript was found in placenta at low levels. Xin et al. (2001)
noted that the amino acid sequence of the human and mouse proteins are
identical. Northern blot analysis of mouse tissues revealed high levels
of a 1.8-kb transcript in brain and kidney, and high levels of a 1.3-kb
transcript in testis and heart.
GENE FUNCTION
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 (GABARAPL2; 607452), GABARAP, MAP1LC3
(see 601242), and APG8L. 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 (601242), 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 GABARAPL1 gene contains 4 exons.
MAPPING
By genomic sequence analysis, Vernier-Magnin et al. (2001) mapped the
GABARAPL1 gene to chromosome 12.
By radiation hybrid analysis, Xin et al. (2001) mapped the GABARAPL1
gene to chromosome 12p12.3.
*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. Pellerin, I.; Vuillermoz, C.; Jouvenot, M.; Ordener, C.; Royez,
M.; Adessi, G. L.: Identification and characterization of an early
estrogen-regulated RNA in cultured guinea-pig endometrial cells. Molec.
Cell. Endocr. 90: R17-R21, 1993.
4. Vernier-Magnin, S.; Muller, S.; Sallot, M.; Radom, J.; Musard,
J.-F.; Adami, P.; Dulieu, P.; Remy-Martin, J.-P.; Jouvenot, M.; Fraichard,
A.: A novel early estrogen-regulated gene gec1 encodes a protein
related to GABARAP. Biochem. Biophys. Res. Commun. 284: 118-125,
2001.
5. 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
Patricia A. Hartz - updated: 12/30/2002
*FIELD* CD
Patricia A. Hartz: 12/12/2002
*FIELD* ED
alopez: 09/28/2010
terry: 9/27/2010
mgross: 8/16/2007
terry: 8/3/2007
cwells: 12/30/2002
mgross: 12/12/2002
*RECORD*
*FIELD* NO
607420
*FIELD* TI
*607420 GABA-A RECEPTOR-ASSOCIATED PROTEIN-LIKE PROTEIN 1; GABARAPL1
;;GABARAP-LIKE PROTEIN 1;;
read moreGLANDULAR EPITHELIAL CELL PROTEIN 1; GEC1;;
APG8-LIKE; APG8L
*FIELD* TX
CLONING
Pellerin et al. (1993) cloned guinea pig Gabarapl1, which they called
Gec1, through a differential screen of estrogen-regulated sequences
expressed by endometrial glandular epithelial cells. Using the guinea
pig sequence as probe, Vernier-Magnin et al. (2001) cloned human
GABARAPL1, which they called GEC1, from a placenta cDNA library. The
deduced 117-amino acid protein shares 100% amino acid identity with
guinea pig Gabarapl1 and 87% identity with GABARAP (605125). Northern
blot analysis revealed a 1.9-kb transcript in all tissues examined.
By Northern blot analysis, Xin et al. (2001) found a 2.3-kb GABARAPL1
transcript expressed in all tissues examined, with highest levels in
brain, heart, peripheral blood leukocytes, liver, kidney, placenta, and
skeletal muscle. Moderate expression was found in pancreas, prostate,
testis, ovary, lung, spleen, and colon, and low expression was found in
thymus and small intestine. In addition, a 4.2-kb transcript was found
in low abundance in ovary, peripheral blood leukocytes, and liver, and a
1.7-kb transcript was found in placenta at low levels. Xin et al. (2001)
noted that the amino acid sequence of the human and mouse proteins are
identical. Northern blot analysis of mouse tissues revealed high levels
of a 1.8-kb transcript in brain and kidney, and high levels of a 1.3-kb
transcript in testis and heart.
GENE FUNCTION
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 (GABARAPL2; 607452), GABARAP, MAP1LC3
(see 601242), and APG8L. 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 (601242), 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 GABARAPL1 gene contains 4 exons.
MAPPING
By genomic sequence analysis, Vernier-Magnin et al. (2001) mapped the
GABARAPL1 gene to chromosome 12.
By radiation hybrid analysis, Xin et al. (2001) mapped the GABARAPL1
gene to chromosome 12p12.3.
*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. Pellerin, I.; Vuillermoz, C.; Jouvenot, M.; Ordener, C.; Royez,
M.; Adessi, G. L.: Identification and characterization of an early
estrogen-regulated RNA in cultured guinea-pig endometrial cells. Molec.
Cell. Endocr. 90: R17-R21, 1993.
4. Vernier-Magnin, S.; Muller, S.; Sallot, M.; Radom, J.; Musard,
J.-F.; Adami, P.; Dulieu, P.; Remy-Martin, J.-P.; Jouvenot, M.; Fraichard,
A.: A novel early estrogen-regulated gene gec1 encodes a protein
related to GABARAP. Biochem. Biophys. Res. Commun. 284: 118-125,
2001.
5. 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
Patricia A. Hartz - updated: 12/30/2002
*FIELD* CD
Patricia A. Hartz: 12/12/2002
*FIELD* ED
alopez: 09/28/2010
terry: 9/27/2010
mgross: 8/16/2007
terry: 8/3/2007
cwells: 12/30/2002
mgross: 12/12/2002