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

 GBRL2_HUMAN             Reviewed;         117 AA.
P60520; O08765; Q6FG91; Q9DCP8; Q9UQF7;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 1.
07-APR-2021, entry version 163.
RecName: Full=Gamma-aminobutyric acid receptor-associated protein-like 2;
AltName: Full=GABA(A) receptor-associated protein-like 2;
AltName: Full=Ganglioside expression factor 2;
Short=GEF-2;
AltName: Full=General protein transport factor p16;
AltName: Full=Golgi-associated ATPase enhancer of 16 kDa;
Short=GATE-16;
AltName: Full=MAP1 light chain 3-related protein;
Flags: Precursor;
Name=GABARAPL2; Synonyms=FLC3A, GEF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH ULK1.
TISSUE=Frontal cortex;
PubMed=11146101; DOI=10.1016/s0169-328x(00)00218-7;
Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H.,
Muramatsu M.-A.;
"Interaction of the Unc-51-like kinase and microtubule-associated protein
light chain 3 related proteins in the brain: possible role of vesicular
transport in axonal elongation.";
Brain Res. Mol. Brain Res. 85:1-12(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11414770; DOI=10.1006/geno.2001.6555;
Xin Y., Yu L., Chen Z., Zheng L., Fu Q., Jiang J., Zhang P., Gong R.,
Zhao S.;
"Cloning, expression patterns, and chromosome localization of three human
and two mouse homologues of GABA(A) receptor-associated protein.";
Genomics 74:408-413(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Storch S., Braulke T.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Pituitary;
Song H., Peng Y., Yu Y., Fu G., Mao M., Zhang Q., Zhu H., Li G., Luo M.,
Chen J., Hu R.;
"Human GEF2 homolog gene.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH ATG7.
PubMed=11096062; DOI=10.1074/jbc.c000752200;
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
activating enzyme for multiple substrates including human Apg12p, GATE-16,
GABARAP, and MAP-LC3.";
J. Biol. Chem. 276:1701-1706(2001).
[10]
INTERACTION WITH ATG3.
PubMed=11825910; DOI=10.1074/jbc.m200385200;
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation
of hApg12p to hApg5p.";
J. Biol. Chem. 277:13739-13744(2002).
[11]
LIPIDATION AT GLY-116, INTERACTION WITH ATG3 AND ATG7, AND SUBCELLULAR
LOCATION.
PubMed=12507496; DOI=10.1016/s0006-291x(02)02907-8;
Tanida I., Komatsu M., Ueno T., Kominami E.;
"GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3.";
Biochem. Biophys. Res. Commun. 300:637-644(2003).
[12]
CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-116.
PubMed=15169837; DOI=10.1242/jcs.01131;
Kabeya Y., Mizushima N., Yamamoto A., Oshitani-Okamoto S., Ohsumi Y.,
Yoshimori T.;
"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on
form-II formation.";
J. Cell Sci. 117:2805-2812(2004).
[13]
INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=17580304; DOI=10.1074/jbc.m702824200;
Pankiv S., Clausen T.H., Lamark T., Brech A., Bruun J.A., Outzen H.,
Overvatn A., Bjorkoy G., Johansen T.;
"p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of
ubiquitinated protein aggregates by autophagy.";
J. Biol. Chem. 282:24131-24145(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH TP53INP2.
PubMed=19056683; DOI=10.1091/mbc.e08-07-0671;
Nowak J., Archange C., Tardivel-Lacombe J., Pontarotti P., Pebusque M.J.,
Vaccaro M.I., Velasco G., Dagorn J.C., Iovanna J.L.;
"The TP53INP2 protein is required for autophagy in mammalian cells.";
Mol. Biol. Cell 20:870-881(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
FUNCTION.
PubMed=20418806; DOI=10.1038/emboj.2010.74;
Weidberg H., Shvets E., Shpilka T., Shimron F., Shinder V., Elazar Z.;
"LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently
in autophagosome biogenesis.";
EMBO J. 29:1792-1802(2010).
[18]
INTERACTION WITH TECPR2.
PubMed=20562859; DOI=10.1038/nature09204;
Behrends C., Sowa M.E., Gygi S.P., Harper J.W.;
"Network organization of the human autophagy system.";
Nature 466:68-76(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
INTERACTION WITH TBC1D25.
PubMed=21383079; DOI=10.1083/jcb.201008107;
Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.;
"OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal
maturation.";
J. Cell Biol. 192:839-853(2011).
[21]
INTERACTION WITH TP53INP1.
PubMed=22421968; DOI=10.1038/cdd.2012.30;
Seillier M., Peuget S., Gayet O., Gauthier C., N'guessan P., Monte M.,
Carrier A., Iovanna J.L., Dusetti N.J.;
"TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-family proteins
through the LC3-interacting region (LIR) and promotes autophagy-dependent
cell death.";
Cell Death Differ. 19:1525-1535(2012).
[22]
INTERACTION WITH ATG13 AND ULK1.
PubMed=23043107; DOI=10.1074/jbc.m112.378109;
Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B.,
Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.;
"ATG8 family proteins act as scaffolds for assembly of the ULK complex:
sequence requirements for LC3-interacting region (LIR) motifs.";
J. Biol. Chem. 287:39275-39290(2012).
[23]
INTERACTION WITH TBC1D5.
PubMed=22354992; DOI=10.1128/mcb.06717-11;
Popovic D., Akutsu M., Novak I., Harper J.W., Behrends C., Dikic I.;
"Rab GTPase-activating proteins in autophagy: regulation of endocytic and
autophagy pathways by direct binding to human ATG8 modifiers.";
Mol. Cell. Biol. 32:1733-1744(2012).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=22311637; DOI=10.1074/mcp.m111.014035;
Dengjel J., Hoyer-Hansen M., Nielsen M.O., Eisenberg T., Harder L.M.,
Schandorff S., Farkas T., Kirkegaard T., Becker A.C., Schroeder S.,
Vanselow K., Lundberg E., Nielsen M.M., Kristensen A.R., Akimov V.,
Bunkenborg J., Madeo F., Jaattela M., Andersen J.S.;
"Identification of autophagosome-associated proteins and regulators by
quantitative proteomic analysis and genetic screens.";
Mol. Cell. Proteomics 11:M111.014035.1-M111.014035.17(2012).
[25]
INTERACTION WITH TP53INP1 AND TP53INP2.
PubMed=22470510; DOI=10.1371/journal.pone.0034034;
Sancho A., Duran J., Garcia-Espana A., Mauvezin C., Alemu E.A., Lamark T.,
Macias M.J., Desalle R., Royo M., Sala D., Chicote J.U., Palacin M.,
Johansen T., Zorzano A.;
"DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual
regulators of autophagy and transcription.";
PLoS ONE 7:E34034-E34034(2012).
[26]
INTERACTION WITH BNIP3, AND FUNCTION.
PubMed=23209295; DOI=10.1074/jbc.m112.399345;
Zhu Y., Massen S., Terenzio M., Lang V., Chen-Lindner S., Eils R.,
Novak I., Dikic I., Hamacher-Brady A., Brady N.R.;
"Modulation of serines 17 and 24 in the LC3-interacting region of Bnip3
determines pro-survival mitophagy versus apoptosis.";
J. Biol. Chem. 288:1099-1113(2013).
[27]
INTERACTION WITH PCM1.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar
satellites.";
Nature 502:254-257(2013).
[28]
INTERACTION WITH TRIM5.
PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C.,
Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B.,
Johansen T., Deretic V.;
"TRIM proteins regulate autophagy and can target autophagic substrates by
direct recognition.";
Dev. Cell 30:394-409(2014).
[29]
INTERACTION WITH WDFY3.
PubMed=24668264; DOI=10.1002/embr.201338003;
Lystad A.H., Ichimura Y., Takagi K., Yang Y., Pankiv S., Kanegae Y.,
Kageyama S., Suzuki M., Saito I., Mizushima T., Komatsu M., Simonsen A.;
"Structural determinants in GABARAP required for the selective binding and
recruitment of ALFY to LC3B-positive structures.";
EMBO Rep. 15:557-565(2014).
[30]
INTERACTION WITH MEFV AND TRIM21.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of innate
immunity.";
J. Cell Biol. 210:973-989(2015).
[31]
INTERACTION WITH UBA5.
PubMed=26929408; DOI=10.1074/jbc.m116.715474;
Habisov S., Huber J., Ichimura Y., Akutsu M., Rogova N., Loehr F.,
McEwan D.G., Johansen T., Dikic I., Doetsch V., Komatsu M., Rogov V.V.,
Kirkin V.;
"Structural and functional analysis of a novel interaction motif within
UFM1-activating enzyme 5 (UBA5) required for binding to ubiquitin-like
proteins and ufmylation.";
J. Biol. Chem. 291:9025-9041(2016).
[32] {ECO:0007744|PDB:6H8C}
STRUCTURE BY NMR OF 1-116 IN COMPLEX WITH UBA5, INTERACTION WITH UBA5,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-47.
PubMed=30990354; DOI=10.1080/15548627.2019.1606637;
Huber J., Obata M., Gruber J., Akutsu M., Lohr F., Rogova N., Guntert P.,
Dikic I., Kirkin V., Komatsu M., Dotsch V., Rogov V.V.;
"An atypical LIR motif within UBA5 (ubiquitin like modifier activating
enzyme 5) interacts with GABARAP proteins and mediates membrane
localization of UBA5.";
Autophagy 16:256-270(2020).
-!- FUNCTION: Ubiquitin-like modifier involved in intra-Golgi traffic (By
similarity). Modulates intra-Golgi transport through coupling between
NSF activity and SNAREs activation (By similarity). It first stimulates
the ATPase activity of NSF which in turn stimulates the association
with GOSR1 (By similarity). Involved in autophagy (PubMed:20418806,
PubMed:23209295). Plays a role in mitophagy which contributes to
regulate mitochondrial quantity and quality by eliminating the
mitochondria to a basal level to fulfill cellular energy requirements
and preventing excess ROS production (PubMed:20418806,
PubMed:23209295). Whereas LC3s are involved in elongation of the
phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a
later stage in autophagosome maturation (PubMed:20418806,
PubMed:23209295). {ECO:0000250|UniProtKB:P60519,
ECO:0000269|PubMed:20418806, ECO:0000269|PubMed:23209295}.
-!- SUBUNIT: Monomer. Interacts with ATG3, ATG7, ATG13 and ULK1
(PubMed:11146101, PubMed:11825910, PubMed:11096062, PubMed:12507496,
PubMed:23043107). Interacts with TP53INP1 and TP53INP2
(PubMed:19056683, PubMed:22421968, PubMed:22470510). Interacts with
TBC1D25 (PubMed:21383079). Directly interacts with SQSTM1 and BNIP3
(PubMed:17580304, PubMed:23209295). Interacts with TECPR2 and PCM1
(PubMed:20562859, PubMed:24089205). Interacts with TBC1D5
(PubMed:22354992). Interacts with TRIM5 (PubMed:25127057). Interacts
with MEFV and TRIM21 (PubMed:26347139). Interacts with WDFY3
(PubMed:24668264). Interacts with UBA5; promoting recruitment of UBA5
to the endoplasmic reticulum membrane (PubMed:26929408,
PubMed:30990354). Interacts with GOSR1 (By similarity).
{ECO:0000250|UniProtKB:P60519, ECO:0000269|PubMed:11096062,
ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11825910,
ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:17580304,
ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:20562859,
ECO:0000269|PubMed:21383079, ECO:0000269|PubMed:22354992,
ECO:0000269|PubMed:22421968, ECO:0000269|PubMed:22470510,
ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:23209295,
ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24668264,
ECO:0000269|PubMed:25127057, ECO:0000269|PubMed:26347139,
ECO:0000269|PubMed:26929408, ECO:0000269|PubMed:30990354}.
-!- INTERACTION:
P60520; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-720116, EBI-741181;
P60520; Q8IVF2-2: AHNAK2; NbExp=3; IntAct=EBI-720116, EBI-10217765;
P60520; Q9P2R3: ANKFY1; NbExp=2; IntAct=EBI-720116, EBI-2513908;
P60520; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-716933;
P60520; Q8N6T3-2: ARFGAP1; NbExp=3; IntAct=EBI-720116, EBI-6288865;
P60520; O75143: ATG13; NbExp=3; IntAct=EBI-720116, EBI-2798775;
P60520; Q676U5: ATG16L1; NbExp=2; IntAct=EBI-720116, EBI-535909;
P60520; Q2TAZ0: ATG2A; NbExp=2; IntAct=EBI-720116, EBI-2514077;
P60520; Q9NT62: ATG3; NbExp=5; IntAct=EBI-720116, EBI-988094;
P60520; Q9Y4P1: ATG4B; NbExp=10; IntAct=EBI-720116, EBI-712014;
P60520; O95352: ATG7; NbExp=7; IntAct=EBI-720116, EBI-987834;
P60520; Q9BXK5: BCL2L13; NbExp=4; IntAct=EBI-720116, EBI-747430;
P60520; O60238: BNIP3L; NbExp=3; IntAct=EBI-720116, EBI-849893;
P60520; Q9NW68: BSDC1; NbExp=3; IntAct=EBI-720116, EBI-721848;
P60520; Q9P1Z2: CALCOCO1; NbExp=3; IntAct=EBI-720116, EBI-749920;
P60520; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-720116, EBI-739580;
P60520; Q8WXU2: DNAAF4; NbExp=2; IntAct=EBI-720116, EBI-2946907;
P60520; P63167: DYNLL1; NbExp=3; IntAct=EBI-720116, EBI-349105;
P60520; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-720116, EBI-742371;
P60520; P00533: EGFR; NbExp=3; IntAct=EBI-720116, EBI-297353;
P60520; Q8IVP5: FUNDC1; NbExp=4; IntAct=EBI-720116, EBI-3059266;
P60520; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-720116, EBI-2869338;
P60520; P40939: HADHA; NbExp=4; IntAct=EBI-720116, EBI-356720;
P60520; P54257: HAP1; NbExp=3; IntAct=EBI-720116, EBI-712814;
P60520; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-720116, EBI-4311436;
P60520; O00410: IPO5; NbExp=5; IntAct=EBI-720116, EBI-356424;
P60520; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-720116, EBI-749265;
P60520; Q86V97: KBTBD6; NbExp=2; IntAct=EBI-720116, EBI-2514778;
P60520; Q8WVZ9: KBTBD7; NbExp=3; IntAct=EBI-720116, EBI-473695;
P60520; Q8N8K9: KIAA1958; NbExp=7; IntAct=EBI-720116, EBI-10181113;
P60520; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-720116, EBI-10988217;
P60520; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-720116, EBI-10172290;
P60520; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-720116, EBI-10172052;
P60520; Q8N653: LZTR1; NbExp=3; IntAct=EBI-720116, EBI-2350056;
P60520; Q9UH92: MLX; NbExp=5; IntAct=EBI-720116, EBI-741109;
P60520; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-720116, EBI-8852072;
P60520; Q14596: NBR1; NbExp=11; IntAct=EBI-720116, EBI-742698;
P60520; P46934: NEDD4; NbExp=6; IntAct=EBI-720116, EBI-726944;
P60520; P46934-3: NEDD4; NbExp=3; IntAct=EBI-720116, EBI-11980721;
P60520; Q8TD19: NEK9; NbExp=7; IntAct=EBI-720116, EBI-1044009;
P60520; O75323: NIPSNAP2; NbExp=6; IntAct=EBI-720116, EBI-307133;
P60520; Q9NV35: NUDT15; NbExp=3; IntAct=EBI-720116, EBI-3924801;
P60520; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-720116, EBI-1051317;
P60520; Q15154: PCM1; NbExp=2; IntAct=EBI-720116, EBI-741421;
P60520; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-720116, EBI-367363;
P60520; Q8WWW0: RASSF5; NbExp=2; IntAct=EBI-720116, EBI-367390;
P60520; Q14257: RCN2; NbExp=6; IntAct=EBI-720116, EBI-356710;
P60520; Q9H6L5-1: RETREG1; NbExp=2; IntAct=EBI-720116, EBI-16159046;
P60520; Q9H6L5-2: RETREG1; NbExp=3; IntAct=EBI-720116, EBI-13382642;
P60520; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-720116, EBI-10192441;
P60520; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-720116, EBI-11959369;
P60520; Q9H0K1: SIK2; NbExp=3; IntAct=EBI-720116, EBI-1181664;
P60520; Q13501: SQSTM1; NbExp=19; IntAct=EBI-720116, EBI-307104;
P60520; O95210: STBD1; NbExp=5; IntAct=EBI-720116, EBI-2947137;
P60520; Q13188: STK3; NbExp=2; IntAct=EBI-720116, EBI-992580;
P60520; Q13043: STK4; NbExp=2; IntAct=EBI-720116, EBI-367376;
P60520; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-720116, EBI-529518;
P60520; Q8TC07: TBC1D15; NbExp=2; IntAct=EBI-720116, EBI-1048247;
P60520; Q3MII6: TBC1D25; NbExp=4; IntAct=EBI-720116, EBI-11899977;
P60520; Q9UPU7: TBC1D2B; NbExp=3; IntAct=EBI-720116, EBI-2947180;
P60520; B9A6K1: TBC1D5; NbExp=3; IntAct=EBI-720116, EBI-10217641;
P60520; Q92609: TBC1D5; NbExp=5; IntAct=EBI-720116, EBI-742381;
P60520; Q66K14-2: TBC1D9B; NbExp=3; IntAct=EBI-720116, EBI-10217736;
P60520; O15040: TECPR2; NbExp=2; IntAct=EBI-720116, EBI-2946991;
P60520; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-720116, EBI-10329860;
P60520; Q15025: TNIP1; NbExp=6; IntAct=EBI-720116, EBI-357849;
P60520; Q96A56: TP53INP1; NbExp=6; IntAct=EBI-720116, EBI-9986117;
P60520; Q9H8W5-2: TRIM45; NbExp=3; IntAct=EBI-720116, EBI-11993364;
P60520; Q969E8: TSR2; NbExp=11; IntAct=EBI-720116, EBI-746981;
P60520; Q9GZZ9: UBA5; NbExp=17; IntAct=EBI-720116, EBI-747805;
P60520; O75385: ULK1; NbExp=3; IntAct=EBI-720116, EBI-908831;
P60520; Q8IZQ1: WDFY3; NbExp=3; IntAct=EBI-720116, EBI-1569256;
P60520; Q8N680: ZBTB2; NbExp=3; IntAct=EBI-720116, EBI-2515601;
P60520; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-720116, EBI-10251462;
P60520; Q9Z2F7: Bnip3l; Xeno; NbExp=2; IntAct=EBI-720116, EBI-1774669;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837,
ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683,
ECO:0000269|PubMed:22311637}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:30990354}. Golgi apparatus
{ECO:0000250|UniProtKB:P60519}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the brain,
heart, prostate, ovary, spleen and skeletal muscle. Expressed at very
low levels in lung, thymus and small intestine.
{ECO:0000269|PubMed:11146101, ECO:0000269|PubMed:11414770}.
-!- PTM: The precursor molecule is cleaved by ATG4B to form the cytosolic
form, GABARAPL2-I. This is activated by APG7L/ATG7, transferred to ATG3
and conjugated to phospholipid to form the membrane-bound form,
GABARAPL2-II. ATG4B also mediates the delipidation required for
GABARAPL1 recycling when autophagosomes fuse with lysosomes.
{ECO:0000269|PubMed:15169837}.
-!- SIMILARITY: Belongs to the ATG8 family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; AB030710; BAB21548.1; -; mRNA.
EMBL; AF087848; AAK20400.1; -; mRNA.
EMBL; AJ010569; CAA09249.1; -; mRNA.
EMBL; AF077046; AAD27779.1; -; mRNA.
EMBL; CR542217; CAG47013.1; -; mRNA.
EMBL; AK289788; BAF82477.1; -; mRNA.
EMBL; CH471114; EAW95630.1; -; Genomic_DNA.
EMBL; BC005985; AAH05985.1; -; mRNA.
EMBL; BC014594; AAH14594.1; -; mRNA.
EMBL; BC029601; AAH29601.1; -; mRNA.
CCDS; CCDS10921.1; -.
RefSeq; NP_009216.1; NM_007285.6.
PDB; 4CO7; X-ray; 2.00 A; A/B=1-117.
PDB; 6H8C; NMR; -; A=1-116.
PDBsum; 4CO7; -.
PDBsum; 6H8C; -.
SMR; P60520; -.
BioGRID; 116473; 135.
DIP; DIP-35051N; -.
ELM; P60520; -.
IntAct; P60520; 535.
MINT; P60520; -.
STRING; 9606.ENSP00000037243; -.
MoonDB; P60520; Predicted.
iPTMnet; P60520; -.
PhosphoSitePlus; P60520; -.
BioMuta; GABARAPL2; -.
DMDM; 44888808; -.
UCD-2DPAGE; P60520; -.
EPD; P60520; -.
jPOST; P60520; -.
MassIVE; P60520; -.
PaxDb; P60520; -.
PeptideAtlas; P60520; -.
PRIDE; P60520; -.
ProteomicsDB; 57214; -.
Antibodypedia; 30328; 573 antibodies.
DNASU; 11345; -.
Ensembl; ENST00000037243; ENSP00000037243; ENSG00000034713.
GeneID; 11345; -.
KEGG; hsa:11345; -.
UCSC; uc002fen.3; human.
CTD; 11345; -.
DisGeNET; 11345; -.
GeneCards; GABARAPL2; -.
HGNC; HGNC:13291; GABARAPL2.
HPA; ENSG00000034713; Low tissue specificity.
MIM; 607452; gene.
neXtProt; NX_P60520; -.
OpenTargets; ENSG00000034713; -.
PharmGKB; PA28482; -.
VEuPathDB; HostDB:ENSG00000034713.7; -.
eggNOG; KOG1654; Eukaryota.
GeneTree; ENSGT00940000155010; -.
HOGENOM; CLU_119276_0_1_1; -.
InParanoid; P60520; -.
OMA; AKMKWMF; -.
OrthoDB; 1508198at2759; -.
PhylomeDB; P60520; -.
TreeFam; TF312964; -.
PathwayCommons; P60520; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-8854214; TBC/RABGAPs.
SIGNOR; P60520; -.
BioGRID-ORCS; 11345; 6 hits in 1003 CRISPR screens.
ChiTaRS; GABARAPL2; human.
GeneWiki; GABARAPL2; -.
GenomeRNAi; 11345; -.
Pharos; P60520; Tbio.
PRO; PR:P60520; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; P60520; protein.
Bgee; ENSG00000034713; Expressed in caudate nucleus and 249 other tissues.
ExpressionAtlas; P60520; baseline and differential.
Genevisible; P60520; HS.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
GO; GO:0050811; F:GABA receptor binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0097352; P:autophagosome maturation; TAS:Reactome.
GO; GO:0006914; P:autophagy; NAS:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; IBA:GO_Central.
GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
GO; GO:0070972; P:protein localization to endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR004241; Atg8-like.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10969; PTHR10969; 1.
Pfam; PF02991; Atg8; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Autophagy; Cytoplasmic vesicle;
Endoplasmic reticulum; Golgi apparatus; Lipoprotein; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Transport.
CHAIN 1..116
/note="Gamma-aminobutyric acid receptor-associated protein-
like 2"
/id="PRO_0000212373"
PROPEP 117
/note="Removed in mature form"
/evidence="ECO:0000269|PubMed:15169837"
/id="PRO_0000423070"
SITE 116..117
/note="Cleavage; by ATG4"
/evidence="ECO:0000269|PubMed:15169837"
MOD_RES 24
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 39
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17525332"
LIPID 116
/note="Phosphatidylethanolamine amidated glycine"
/evidence="ECO:0000269|PubMed:12507496"
VARIANT 51
/note="V -> A (in dbSNP:rs11556291)"
/id="VAR_049756"
MUTAGEN 47
/note="R->A: Strongly reduced interaction with UBA5."
/evidence="ECO:0000269|PubMed:30990354"
MUTAGEN 116
/note="G->A: Impairs localization at the autophagosomal
membrane."
/evidence="ECO:0000269|PubMed:15169837"
CONFLICT 29
/note="V -> F (in Ref. 4; AAD27779)"
/evidence="ECO:0000305"
HELIX 4..8
/evidence="ECO:0007744|PDB:4CO7"
HELIX 11..24
/evidence="ECO:0007744|PDB:4CO7"
STRAND 28..35
/evidence="ECO:0007744|PDB:4CO7"
STRAND 39..41
/evidence="ECO:0007744|PDB:6H8C"
STRAND 48..52
/evidence="ECO:0007744|PDB:4CO7"
HELIX 57..67
/evidence="ECO:0007744|PDB:4CO7"
STRAND 77..80
/evidence="ECO:0007744|PDB:4CO7"
HELIX 91..98
/evidence="ECO:0007744|PDB:4CO7"
STRAND 105..111
/evidence="ECO:0007744|PDB:4CO7"
SEQUENCE 117 AA; 13667 MW; 17ACB540FD5B975B CRC64;
MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF
MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF


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[MAP1LC3B MAP1ALC3] Microtubule-associated proteins 1A/1B light chain 3B (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (MAP1A/MAP1B light chain 3 B) (MAP1A/MAP1B LC3 B) (Microtubule-associated protein 1 light chain 3 beta)
[Gabrg2] Gamma-aminobutyric acid receptor subunit gamma-2 (GABA(A) receptor subunit gamma-2)
[Cdkn2a P16ink4a] Cyclin-dependent kinase inhibitor 2A (Cyclin-dependent kinase 4 inhibitor A) (CDK4I) (p16-INK4a) (p16-INK4)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[Gabra2 Gabra-2] Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2)
[GABRG2] Gamma-aminobutyric acid receptor subunit gamma-2 (GABA(A) receptor subunit gamma-2)
[GABRB2] Gamma-aminobutyric acid receptor subunit beta-2 (GABA(A) receptor subunit beta-2)
[GABBR2 GPR51 GPRC3B] Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51) (HG20)
[Gabrb3 Gabrb-3] Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p66) (p66-HEL); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p41); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); Non-structural protein 11 (nsp11)]
[Gabrg2] Gamma-aminobutyric acid receptor subunit gamma-2 (GABA(A) receptor subunit gamma-2)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[GABRB3] Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3)
[ORF1ab orf1ab] 3C-like proteinase (EC 3.4.19.12) (EC 3.4.22.69) (Growth factor-like peptide) (Leader protein) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (Papain-like proteinase) (p65 homolog)
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[nef] Protein Nef (3'ORF) (Negative factor) (F-protein) [Cleaved into: C-terminal core protein]
[GABRA2] Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2)
[] 3C-like proteinase (EC 2.7.7.48) (EC 3.6.4.12) (EC 3.6.4.13) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (Peptide HD2) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p10) (p16) (p195) (p24) (p33) (p34) (p41) (p87) (p9)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); Non-structural protein 11 (nsp11)]
[Gabra2 Gabra-2] Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p9); Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p34); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p5); Non-structural protein 8 (nsp8) (p23); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); Non-structural protein 11 (nsp11)]
[Gabrb3 Gabrb-3] Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3)
[Lrp1 A2mr] Prolow-density lipoprotein receptor-related protein 1 (LRP-1) (Alpha-2-macroglobulin receptor) (A2MR) (CD antigen CD91) [Cleaved into: Low-density lipoprotein receptor-related protein 1 85 kDa subunit (LRP-85); Low-density lipoprotein receptor-related protein 1 515 kDa subunit (LRP-515); Low-density lipoprotein receptor-related protein 1 intracellular domain (LRPICD)]
[1ab] 2'-O-methyltransferase (EC 3.4.22.69) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (M-PRO) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (Peptide HD2) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (nsp5) (p10) (p16) (p195) (p24) (p33) (p34) (p41) (p87) (p9)
[1ab] 3C-like proteinase (EC 2.7.7.48) (EC 3.6.4.12) (EC 3.6.4.13) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (Peptide HD2) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p10) (p16) (p195) (p24) (p33) (p34) (p41) (p87) (p9)
[1ab] 3C-like proteinase (EC 2.7.7.48) (EC 3.6.4.12) (EC 3.6.4.13) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (Peptide HD2) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p10) (p16) (p195) (p24) (p33) (p34) (p41) (p87) (p9)
[1ab] 3C-like proteinase (EC 2.7.7.48) (EC 3.6.4.12) (EC 3.6.4.13) (Growth factor-like peptide) (Helicase) (M-PRO) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (Peptide HD2) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (nsp12) (nsp13) (nsp14) (nsp15) (nsp16) (nsp5) (p10) (p16) (p195) (p24) (p33) (p34) (p41) (p87) (p9)

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