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Autophagy-related protein 13

 ATG13_HUMAN             Reviewed;         517 AA.
O75143; B4DFI4; D3DQQ1; D3DQQ2; E9PQZ8; Q53EN6; Q9BRL3; Q9H8B0;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 141.
RecName: Full=Autophagy-related protein 13;
Name=ATG13; Synonyms=KIAA0652;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain cortex, and Thyroid;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Cervix, Lung, and Muscle;
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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
INTERACTION WITH ATG101; ULK1 AND RB1CC1, AND SUBUNIT.
PubMed=19597335; DOI=10.4161/auto.5.7.9296;
Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T.,
Mizushima N.;
"Atg101, a novel mammalian autophagy protein interacting with Atg13.";
Autophagy 5:973-979(2009).
[9]
FUNCTION AS AUTOPHAGY FACTOR, PHOSPHORYLATION, AND INTERACTION WITH
ULK1 AND ATG101.
PubMed=19287211; DOI=10.4161/auto.5.5.8249;
Mercer C.A., Kaliappan A., Dennis P.B.;
"A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and
is essential for macroautophagy.";
Autophagy 5:649-662(2009).
[10]
FUNCTION, INTERACTION WITH ULK1 AND RB1CC1, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=19211835; DOI=10.1091/mbc.E08-12-1248;
Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y.,
Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N.,
Mizushima N.;
"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
complex required for autophagy.";
Mol. Biol. Cell 20:1981-1991(2009).
[11]
INTERACTION WITH ULK1; ULK2 AND RB1CC1, PHOSPHORYLATION BY ULK1; ULK2
AND MTOR, AND FUNCTION.
PubMed=19225151; DOI=10.1091/mbc.E08-12-1249;
Jung C.H., Jun C.B., Ro S.H., Kim Y.M., Otto N.M., Cao J., Kundu M.,
Kim D.H.;
"ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy
machinery.";
Mol. Biol. Cell 20:1992-2003(2009).
[12]
FUNCTION, INTERACTION WITH ULK1, AND PHOSPHORYLATION AT SER-355 BY
ULK1.
PubMed=21855797; DOI=10.1016/j.molcel.2011.06.018;
Joo J.H., Dorsey F.C., Joshi A., Hennessy-Walters K.M., Rose K.L.,
McCastlain K., Zhang J., Iyengar R., Jung C.H., Suen D.F.,
Steeves M.A., Yang C.Y., Prater S.M., Kim D.H., Thompson C.B.,
Youle R.J., Ney P.A., Cleveland J.L., Kundu M.;
"Hsp90-Cdc37 chaperone complex regulates Ulk1- and Atg13-mediated
mitophagy.";
Mol. Cell 43:572-585(2011).
[13]
FUNCTION AS AUTOPHAGY FACTOR, INTERACTION WITH ULK1 AND ULK2, AND
PHOSPHORYLATION BY ULK1 AND ULK2.
PubMed=18936157; DOI=10.1128/MCB.01082-08;
Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
"Kinase-inactivated ULK proteins inhibit autophagy via their conserved
C-terminal domains using an Atg13-independent mechanism.";
Mol. Cell. Biol. 29:157-171(2009).
[14]
FUNCTION.
PubMed=21795849; DOI=10.4161/auto.7.10.16660;
Jung C.H., Seo M., Otto N.M., Kim D.H.;
"ULK1 inhibits the kinase activity of mTORC1 and cell proliferation.";
Autophagy 7:1212-1221(2011).
[15]
PHOSPHORYLATION, AND INTERACTION WITH ULK1 AND RB1CC1.
PubMed=21258367; DOI=10.1038/ncb2152;
Kim J., Kundu M., Viollet B., Guan K.L.;
"AMPK and mTOR regulate autophagy through direct phosphorylation of
Ulk1.";
Nat. Cell Biol. 13:132-141(2011).
[16]
INTERACTION WITH TAB2 AND TAB3.
PubMed=21976705; DOI=10.1093/jb/mvr123;
Takaesu G., Kobayashi T., Yoshimura A.;
"TGFbeta-activated kinase 1 (TAK1)-binding proteins (TAB) 2 and 3
negatively regulate autophagy.";
J. Biochem. 151:157-166(2012).
[17]
INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2 AND MAP1LC3A, DOMAIN,
AND MUTAGENESIS.
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).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-361, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-356, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 436-447, INTERACTION WITH
MAP1LC3A; MAP1LC3B AND MAP1LC3C, MOTIF, SUBUNIT, AND MUTAGENESIS OF
PHE-444 AND ILE-447.
PubMed=24290141; DOI=10.1016/j.str.2013.09.023;
Suzuki H., Tabata K., Morita E., Kawasaki M., Kato R., Dobson R.C.,
Yoshimori T., Wakatsuki S.;
"Structural basis of the autophagy-related LC3/Atg13 LIR complex:
recognition and interaction mechanism.";
Structure 22:47-58(2014).
[22]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
PubMed=26236954; DOI=10.1080/15548627.2015.1076605;
Michel M., Schwarten M., Decker C., Nagel-Steger L., Willbold D.,
Weiergraber O.H.;
"The mammalian autophagy initiator complex contains 2 HORMA domain
proteins.";
Autophagy 11:2300-2308(2015).
[23]
X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-198 IN COMPLEX WITH
ATG101, INTERACTION WITH ATG101, AND MUTAGENESIS OF SER-127; ILE-131;
ARG-133 AND VAL-134.
PubMed=26299944; DOI=10.1016/j.str.2015.07.011;
Qi S., Kim do J., Stjepanovic G., Hurley J.H.;
"Structure of the human Atg13-Atg101 HORMA heterodimer: an interaction
hub within the ULK1 complex.";
Structure 23:1848-1857(2015).
-!- FUNCTION: Autophagy factor required for autophagosome formation
and mitophagy. Target of the TOR kinase signaling pathway that
regulates autophagy through the control of the phosphorylation
status of ATG13 and ULK1, and the regulation of the ATG13-ULK1-
RB1CC1 complex. Through its regulation of ULK1 activity, plays a
role in the regulation of the kinase activity of mTORC1 and cell
proliferation. {ECO:0000269|PubMed:18936157,
ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:19225151,
ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:21795849,
ECO:0000269|PubMed:21855797}.
-!- SUBUNIT: Part of a complex consisting of ATG13, ULK1 and RB1CC1
(PubMed:19597335, PubMed:19211835, PubMed:19225151,
PubMed:24290141). Interacts with ATG101 (PubMed:19597335,
PubMed:19287211, PubMed:26299944). Interacts with ULK1 (via C-
terminus) (PubMed:19287211, PubMed:21855797, PubMed:18936157).
Interacts with ULK2 (via C-terminus) (PubMed:19225151,
PubMed:18936157). Interacts (via the LIR motif) with GABARAP,
GABARAPL, GABARAPL2 (PubMed:23043107). Interacts (via the LIR
motif) with MAP1LC3A, MAP1LC3B and MAP1LC3C (PubMed:24290141).
Interacts with TAB2 and TAB3 (PubMed:21976705).
{ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835,
ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211,
ECO:0000269|PubMed:19597335, ECO:0000269|PubMed:21258367,
ECO:0000269|PubMed:21855797, ECO:0000269|PubMed:21976705,
ECO:0000269|PubMed:23043107, ECO:0000269|PubMed:26299944}.
-!- INTERACTION:
Q9BSB4:ATG101; NbExp=16; IntAct=EBI-2798775, EBI-2946739;
O95166:GABARAP; NbExp=3; IntAct=EBI-2798775, EBI-712001;
Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-2798775, EBI-746969;
P60520:GABARAPL2; NbExp=3; IntAct=EBI-2798775, EBI-720116;
Q9H492-1:MAP1LC3A; NbExp=7; IntAct=EBI-2798775, EBI-16082793;
Q9GZQ8:MAP1LC3B; NbExp=5; IntAct=EBI-2798775, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=8; IntAct=EBI-2798775, EBI-2603996;
Q8TDY2:RB1CC1; NbExp=9; IntAct=EBI-2798775, EBI-1047793;
O75385:ULK1; NbExp=10; IntAct=EBI-2798775, EBI-908831;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19211835}. Preautophagosomal structure
{ECO:0000269|PubMed:19211835}. Note=Under starvation conditions,
is localized to puncate structures primarily representing the
isolation membrane; the isolation membrane sequesters a portion of
the cytoplasm resulting in autophagosome formation.
{ECO:0000269|PubMed:19211835}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=O75143-1; Sequence=Displayed;
Name=2;
IsoId=O75143-2; Sequence=VSP_002431;
Name=3;
IsoId=O75143-3; Sequence=VSP_002431, VSP_002432, VSP_002433;
Name=4;
IsoId=O75143-4; Sequence=VSP_044503, VSP_044504;
Name=5;
IsoId=O75143-5; Sequence=VSP_044640;
Note=No experimental confirmation available.;
-!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
interaction with the ATG8 family proteins GABARAP, GABARAPL,
GABARAPL2, and MAP1LC3A. {ECO:0000269|PubMed:23043107}.
-!- PTM: Phosphorylated by ULK1, ULK2 and mTOR. Phosphorylation status
depends on nutrient-rich conditions; dephosphorylated during
starvation or following treatment with rapamycin. ULK1-mediated
phosphorylation of ATG13 at Ser-355 is required for efficient
clearance of depolarized mitochondria.
{ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835,
ECO:0000269|PubMed:19225151, ECO:0000269|PubMed:19287211,
ECO:0000269|PubMed:21258367, ECO:0000269|PubMed:21855797}.
-!- SIMILARITY: Belongs to the ATG13 family. Metazoan subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31627.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAD97323.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB014552; BAA31627.2; ALT_INIT; mRNA.
EMBL; AK023867; BAB14707.1; -; mRNA.
EMBL; AK294110; BAG57445.1; -; mRNA.
EMBL; AK223603; BAD97323.1; ALT_INIT; mRNA.
EMBL; AC115088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW67985.1; -; Genomic_DNA.
EMBL; CH471064; EAW67986.1; -; Genomic_DNA.
EMBL; CH471064; EAW67987.1; -; Genomic_DNA.
EMBL; CH471064; EAW67988.1; -; Genomic_DNA.
EMBL; CH471064; EAW67989.1; -; Genomic_DNA.
EMBL; CH471064; EAW67990.1; -; Genomic_DNA.
EMBL; CH471064; EAW67991.1; -; Genomic_DNA.
EMBL; BC001331; AAH01331.1; -; mRNA.
EMBL; BC002378; AAH02378.1; -; mRNA.
EMBL; BC006191; AAH06191.1; -; mRNA.
CCDS; CCDS44582.1; -. [O75143-1]
CCDS; CCDS55760.1; -. [O75143-5]
CCDS; CCDS55761.1; -. [O75143-4]
CCDS; CCDS7921.1; -. [O75143-2]
RefSeq; NP_001136145.1; NM_001142673.2. [O75143-1]
RefSeq; NP_001192048.1; NM_001205119.1. [O75143-5]
RefSeq; NP_001192049.1; NM_001205120.1. [O75143-1]
RefSeq; NP_001192050.1; NM_001205121.1. [O75143-2]
RefSeq; NP_001192051.1; NM_001205122.1. [O75143-4]
RefSeq; NP_001333240.1; NM_001346311.1. [O75143-5]
RefSeq; NP_001333241.1; NM_001346312.1. [O75143-5]
RefSeq; NP_001333242.1; NM_001346313.1. [O75143-5]
RefSeq; NP_001333243.1; NM_001346314.1. [O75143-5]
RefSeq; NP_001333244.1; NM_001346315.1. [O75143-5]
RefSeq; NP_001333245.1; NM_001346316.1. [O75143-5]
RefSeq; NP_001333248.1; NM_001346319.1. [O75143-1]
RefSeq; NP_001333249.1; NM_001346320.1. [O75143-1]
RefSeq; NP_001333250.1; NM_001346321.1. [O75143-1]
RefSeq; NP_001333251.1; NM_001346322.1. [O75143-1]
RefSeq; NP_001333252.1; NM_001346323.1. [O75143-1]
RefSeq; NP_001333253.1; NM_001346324.1. [O75143-1]
RefSeq; NP_001333254.1; NM_001346325.1. [O75143-1]
RefSeq; NP_001333255.1; NM_001346326.1. [O75143-1]
RefSeq; NP_001333256.1; NM_001346327.1. [O75143-1]
RefSeq; NP_001333257.1; NM_001346328.1. [O75143-1]
RefSeq; NP_001333258.1; NM_001346329.1. [O75143-1]
RefSeq; NP_001333259.1; NM_001346330.1. [O75143-1]
RefSeq; NP_001333260.1; NM_001346331.1. [O75143-1]
RefSeq; NP_001333261.1; NM_001346332.1. [O75143-1]
RefSeq; NP_001333271.1; NM_001346342.1. [O75143-2]
RefSeq; NP_001333273.1; NM_001346344.1. [O75143-2]
RefSeq; NP_001333275.1; NM_001346346.1. [O75143-2]
RefSeq; NP_001333277.1; NM_001346348.1. [O75143-2]
RefSeq; NP_001333278.1; NM_001346349.1. [O75143-2]
RefSeq; NP_001333279.1; NM_001346350.1. [O75143-2]
RefSeq; NP_001333280.1; NM_001346351.1. [O75143-2]
RefSeq; NP_001333281.1; NM_001346352.1. [O75143-2]
RefSeq; NP_001333282.1; NM_001346353.1. [O75143-2]
RefSeq; NP_001333283.1; NM_001346354.1. [O75143-2]
RefSeq; NP_055556.2; NM_014741.4. [O75143-2]
RefSeq; XP_005253322.1; XM_005253265.2. [O75143-5]
RefSeq; XP_005253323.1; XM_005253266.2. [O75143-5]
RefSeq; XP_005253325.1; XM_005253268.2. [O75143-5]
RefSeq; XP_006718459.1; XM_006718396.2. [O75143-5]
RefSeq; XP_011518795.1; XM_011520493.1. [O75143-5]
RefSeq; XP_011518798.1; XM_011520496.2. [O75143-5]
RefSeq; XP_011518801.1; XM_011520499.2. [O75143-5]
RefSeq; XP_016874088.1; XM_017018599.1. [O75143-5]
RefSeq; XP_016874092.1; XM_017018603.1. [O75143-1]
RefSeq; XP_016874096.1; XM_017018607.1. [O75143-1]
UniGene; Hs.127403; -.
PDB; 3WAN; X-ray; 1.77 A; A/B=436-447.
PDB; 3WAO; X-ray; 2.60 A; A/B/C/D=436-447.
PDB; 3WAP; X-ray; 3.10 A; A=436-447.
PDB; 5C50; X-ray; 1.63 A; B=12-200.
PDBsum; 3WAN; -.
PDBsum; 3WAO; -.
PDBsum; 3WAP; -.
PDBsum; 5C50; -.
ProteinModelPortal; O75143; -.
SMR; O75143; -.
BioGrid; 115120; 21.
CORUM; O75143; -.
DIP; DIP-60540N; -.
ELM; O75143; -.
IntAct; O75143; 19.
MINT; MINT-8247472; -.
iPTMnet; O75143; -.
PhosphoSitePlus; O75143; -.
BioMuta; ATG13; -.
EPD; O75143; -.
MaxQB; O75143; -.
PeptideAtlas; O75143; -.
PRIDE; O75143; -.
DNASU; 9776; -.
Ensembl; ENST00000359513; ENSP00000352500; ENSG00000175224. [O75143-1]
Ensembl; ENST00000524625; ENSP00000433543; ENSG00000175224. [O75143-2]
Ensembl; ENST00000526508; ENSP00000431974; ENSG00000175224. [O75143-1]
Ensembl; ENST00000528494; ENSP00000432412; ENSG00000175224. [O75143-5]
Ensembl; ENST00000529655; ENSP00000433756; ENSG00000175224. [O75143-2]
Ensembl; ENST00000530500; ENSP00000434390; ENSG00000175224. [O75143-4]
GeneID; 9776; -.
KEGG; hsa:9776; -.
UCSC; uc001ncz.4; human. [O75143-1]
CTD; 9776; -.
DisGeNET; 9776; -.
EuPathDB; HostDB:ENSG00000175224.16; -.
GeneCards; ATG13; -.
HGNC; HGNC:29091; ATG13.
HPA; HPA039350; -.
MIM; 615088; gene.
neXtProt; NX_O75143; -.
OpenTargets; ENSG00000175224; -.
PharmGKB; PA165543187; -.
GeneTree; ENSGT00390000007055; -.
HOGENOM; HOG000008446; -.
InParanoid; O75143; -.
KO; K08331; -.
OMA; MCVEISL; -.
OrthoDB; EOG091G0TEK; -.
PhylomeDB; O75143; -.
TreeFam; TF321599; -.
Reactome; R-HSA-1632852; Macroautophagy.
SIGNOR; O75143; -.
ChiTaRS; ATG13; human.
GeneWiki; Autophagy-related_protein_13; -.
GenomeRNAi; 9776; -.
PRO; PR:O75143; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000175224; -.
CleanEx; HS_KIAA0652; -.
ExpressionAtlas; O75143; baseline and differential.
Genevisible; O75143; HS.
GO; GO:1990316; C:ATG1/ULK1 kinase complex; IPI:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0000407; C:pre-autophagosomal structure; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0000423; P:mitophagy; IEA:Ensembl.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl.
InterPro; IPR018731; Atg13.
Pfam; PF10033; ATG13; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Autophagy;
Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome.
CHAIN 1 517 Autophagy-related protein 13.
/FTId=PRO_0000050767.
REGION 127 134 Important for interaction with ATG101.
{ECO:0000269|PubMed:26299944}.
MOTIF 444 447 LIR. {ECO:0000305|PubMed:24290141}.
COMPBIAS 41 44 Poly-Ser.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 355 355 Phosphoserine; by ULK1.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:21855797}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 79 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044503.
VAR_SEQ 262 262 S -> SQCVFTVTKAHFQTPTPVVTDTLRVPMAGLAFSH
(in isoform 5). {ECO:0000303|Ref.3}.
/FTId=VSP_044640.
VAR_SEQ 263 299 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044504.
VAR_SEQ 265 301 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002431.
VAR_SEQ 428 442 HSDGSSGGSSGNTHD -> PCSWPLPCLLSPSTV (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_002432.
VAR_SEQ 443 517 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_002433.
MUTAGEN 127 127 S->H: Abolishes interaction with ATG101;
when associated with D-133.
{ECO:0000269|PubMed:26299944}.
MUTAGEN 131 131 I->D: Decreases interaction with ATG101;
when associated with D-134.
{ECO:0000269|PubMed:26299944}.
MUTAGEN 133 133 R->D: Abolishes interaction with ATG101;
when associated with H-127.
{ECO:0000269|PubMed:26299944}.
MUTAGEN 134 134 V->D: Decreases interaction with ATG101;
when associated with D-131.
{ECO:0000269|PubMed:26299944}.
MUTAGEN 444 444 F->A: Decreases interaction with
MAP1LC3A. {ECO:0000269|PubMed:24290141}.
MUTAGEN 447 447 I->A: Decreases interaction with
MAP1LC3A. {ECO:0000269|PubMed:24290141}.
HELIX 12 30 {ECO:0000244|PDB:5C50}.
STRAND 33 35 {ECO:0000244|PDB:5C50}.
STRAND 42 44 {ECO:0000244|PDB:5C50}.
HELIX 59 69 {ECO:0000244|PDB:5C50}.
STRAND 78 88 {ECO:0000244|PDB:5C50}.
STRAND 93 103 {ECO:0000244|PDB:5C50}.
HELIX 114 131 {ECO:0000244|PDB:5C50}.
TURN 132 134 {ECO:0000244|PDB:5C50}.
HELIX 137 142 {ECO:0000244|PDB:5C50}.
STRAND 145 158 {ECO:0000244|PDB:5C50}.
STRAND 169 178 {ECO:0000244|PDB:5C50}.
STRAND 181 189 {ECO:0000244|PDB:5C50}.
SEQUENCE 517 AA; 56572 MW; 4D6905985EAB78A7 CRC64;
METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE
VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR
LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV
GTITLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV
IYPSVEDSQE VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHPHQ
LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDRTHCA ATPSSSEDTE TVSNSSEGRA
SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK NLELEDTDPM VNPPDSPETE
SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK PAFSKDDILP MDLGTFYREF QNPPQLSSLS
IDIGAQSMAE DLDSLPEKLA VHEKNVREFD AFVETLQ


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