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O75143

- ATG13_HUMAN

UniProt

O75143 - ATG13_HUMAN

Protein

Autophagy-related protein 13

Gene

ATG13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    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.6 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. autophagic vacuole assembly Source: UniProtKB

    Keywords - Biological processi

    Autophagy

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Autophagy-related protein 13
    Gene namesi
    Name:ATG13
    Synonyms:KIAA0652
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:29091. ATG13.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Preautophagosomal structure By similarity
    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.By similarity

    GO - Cellular componenti

    1. ATG1/UKL1 signaling complex Source: RefGenome
    2. cytosol Source: RefGenome
    3. pre-autophagosomal structure Source: UniProtKB
    4. ULK1-ATG13-FIP200 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165543187.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 517517Autophagy-related protein 13PRO_0000050767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei355 – 3551Phosphoserine; by ULK11 Publication
    Modified residuei361 – 3611PhosphoserineBy similarity

    Post-translational modificationi

    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.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75143.
    PaxDbiO75143.
    PRIDEiO75143.

    PTM databases

    PhosphoSiteiO75143.

    Expressioni

    Gene expression databases

    ArrayExpressiO75143.
    BgeeiO75143.
    CleanExiHS_KIAA0652.
    GenevestigatoriO75143.

    Organism-specific databases

    HPAiHPA039350.

    Interactioni

    Subunit structurei

    Part of a complex consisting of ATG13, ULK1 and RB1CC1. Interacts with ATG101. Interacts with ULK1 (via C-terminus). Interacts with ULK2 (via C-terminus). Interacts (via the LIR motif) with GABARAP, GABARAPL, GABARAPL2, and LC3A. Interacts with TAB2 and TAB3.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATG101Q9BSB46EBI-2798775,EBI-2946739
    GABARAPL1Q9H0R82EBI-2798775,EBI-746969
    GABARAPL2P605203EBI-2798775,EBI-720116
    MAP1LC3BQ9GZQ82EBI-2798775,EBI-373144
    RB1CC1Q8TDY28EBI-2798775,EBI-1047793
    ULK1O753853EBI-2798775,EBI-908831

    Protein-protein interaction databases

    BioGridi115120. 14 interactions.
    DIPiDIP-60540N.
    IntActiO75143. 13 interactions.
    MINTiMINT-8247472.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3WANX-ray1.77A/B436-447[»]
    3WAOX-ray2.60A/B/C/D436-447[»]
    3WAPX-ray3.10A436-447[»]
    ProteinModelPortaliO75143.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi444 – 4474LIR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 444Poly-Ser

    Domaini

    The LIR motif (LC3-interacting region) is required for the interaction with the ATG8 family proteins GABARAP, GABARAPL, GABARAPL2, and LC3A.1 Publication

    Sequence similaritiesi

    Belongs to the ATG13 metazoan family.Curated

    Phylogenomic databases

    eggNOGiNOG266388.
    HOGENOMiHOG000008446.
    KOiK08331.
    OMAiMCVEISL.
    OrthoDBiEOG744T8P.
    PhylomeDBiO75143.
    TreeFamiTF321599.

    Family and domain databases

    InterProiIPR018731. Autophagy-rel_p13.
    [Graphical view]
    PfamiPF10033. ATG13. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: O75143-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW    50
    FNLAIKDIPE VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC 100
    LEMNEKCDKE IKVSYTVYNR LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI 150
    LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV GTITLSCAYR INLAFMSTRQ 200
    FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV IYPSVEDSQE 250
    VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHPHQ 300
    LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDRTHCA ATPSSSEDTE 350
    TVSNSSEGRA SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK 400
    NLELEDTDPM VNPPDSPETE SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK 450
    PAFSKDDILP MDLGTFYREF QNPPQLSSLS IDIGAQSMAE DLDSLPEKLA 500
    VHEKNVREFD AFVETLQ 517
    Length:517
    Mass (Da):56,572
    Last modified:November 1, 1998 - v1
    Checksum:i4D6905985EAB78A7
    GO
    Isoform 2 (identifier: O75143-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         265-301: Missing.

    Show »
    Length:480
    Mass (Da):52,823
    Checksum:i4EB66893A99956A1
    GO
    Isoform 3 (identifier: O75143-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         265-301: Missing.
         428-442: HSDGSSGGSSGNTHD → PCSWPLPCLLSPSTV
         443-517: Missing.

    Show »
    Length:405
    Mass (Da):44,487
    Checksum:iF2CE69C9082ABFA5
    GO
    Isoform 4 (identifier: O75143-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.
         263-299: Missing.

    Show »
    Length:401
    Mass (Da):44,093
    Checksum:i157846C39C54650F
    GO
    Isoform 5 (identifier: O75143-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         262-262: S → SQCVFTVTKAHFQTPTPVVTDTLRVPMAGLAFSH

    Note: No experimental confirmation available.

    Show »
    Length:550
    Mass (Da):60,155
    Checksum:i0965E80906316BD0
    GO

    Sequence cautioni

    The sequence BAA31627.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD97323.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7979Missing in isoform 4. 1 PublicationVSP_044503Add
    BLAST
    Alternative sequencei262 – 2621S → SQCVFTVTKAHFQTPTPVVT DTLRVPMAGLAFSH in isoform 5. 1 PublicationVSP_044640
    Alternative sequencei263 – 29937Missing in isoform 4. 1 PublicationVSP_044504Add
    BLAST
    Alternative sequencei265 – 30137Missing in isoform 2 and isoform 3. 2 PublicationsVSP_002431Add
    BLAST
    Alternative sequencei428 – 44215HSDGS…GNTHD → PCSWPLPCLLSPSTV in isoform 3. 1 PublicationVSP_002432Add
    BLAST
    Alternative sequencei443 – 51775Missing in isoform 3. 1 PublicationVSP_002433Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014552 mRNA. Translation: BAA31627.2. Different initiation.
    AK023867 mRNA. Translation: BAB14707.1.
    AK294110 mRNA. Translation: BAG57445.1.
    AK223603 mRNA. Translation: BAD97323.1. Different initiation.
    AC115088 Genomic DNA. No translation available.
    AC127035 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW67985.1.
    CH471064 Genomic DNA. Translation: EAW67986.1.
    CH471064 Genomic DNA. Translation: EAW67987.1.
    CH471064 Genomic DNA. Translation: EAW67988.1.
    CH471064 Genomic DNA. Translation: EAW67989.1.
    CH471064 Genomic DNA. Translation: EAW67990.1.
    CH471064 Genomic DNA. Translation: EAW67991.1.
    BC001331 mRNA. Translation: AAH01331.1.
    BC002378 mRNA. Translation: AAH02378.1.
    BC006191 mRNA. Translation: AAH06191.1.
    CCDSiCCDS44582.1. [O75143-1]
    CCDS55760.1. [O75143-5]
    CCDS55761.1. [O75143-4]
    CCDS7921.1. [O75143-2]
    RefSeqiNP_001136145.1. NM_001142673.2. [O75143-1]
    NP_001192048.1. NM_001205119.1. [O75143-5]
    NP_001192049.1. NM_001205120.1. [O75143-1]
    NP_001192050.1. NM_001205121.1. [O75143-2]
    NP_001192051.1. NM_001205122.1. [O75143-4]
    NP_055556.2. NM_014741.4. [O75143-2]
    XP_005253319.1. XM_005253262.1. [O75143-5]
    XP_005253320.1. XM_005253263.1. [O75143-5]
    XP_005253322.1. XM_005253265.1. [O75143-5]
    XP_005253323.1. XM_005253266.1. [O75143-5]
    XP_005253325.1. XM_005253268.1. [O75143-5]
    XP_006718457.1. XM_006718394.1. [O75143-5]
    XP_006718458.1. XM_006718395.1. [O75143-5]
    XP_006718459.1. XM_006718396.1. [O75143-5]
    UniGeneiHs.127403.

    Genome annotation databases

    EnsembliENST00000359513; ENSP00000352500; ENSG00000175224. [O75143-1]
    ENST00000524625; ENSP00000433543; ENSG00000175224. [O75143-2]
    ENST00000526508; ENSP00000431974; ENSG00000175224. [O75143-1]
    ENST00000528494; ENSP00000432412; ENSG00000175224. [O75143-5]
    ENST00000529655; ENSP00000433756; ENSG00000175224. [O75143-2]
    ENST00000530500; ENSP00000434390; ENSG00000175224. [O75143-4]
    GeneIDi9776.
    KEGGihsa:9776.
    UCSCiuc001ncz.3. human. [O75143-2]
    uc001ndb.3. human. [O75143-1]
    uc010rgv.2. human. [O75143-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB014552 mRNA. Translation: BAA31627.2 . Different initiation.
    AK023867 mRNA. Translation: BAB14707.1 .
    AK294110 mRNA. Translation: BAG57445.1 .
    AK223603 mRNA. Translation: BAD97323.1 . Different initiation.
    AC115088 Genomic DNA. No translation available.
    AC127035 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW67985.1 .
    CH471064 Genomic DNA. Translation: EAW67986.1 .
    CH471064 Genomic DNA. Translation: EAW67987.1 .
    CH471064 Genomic DNA. Translation: EAW67988.1 .
    CH471064 Genomic DNA. Translation: EAW67989.1 .
    CH471064 Genomic DNA. Translation: EAW67990.1 .
    CH471064 Genomic DNA. Translation: EAW67991.1 .
    BC001331 mRNA. Translation: AAH01331.1 .
    BC002378 mRNA. Translation: AAH02378.1 .
    BC006191 mRNA. Translation: AAH06191.1 .
    CCDSi CCDS44582.1. [O75143-1 ]
    CCDS55760.1. [O75143-5 ]
    CCDS55761.1. [O75143-4 ]
    CCDS7921.1. [O75143-2 ]
    RefSeqi NP_001136145.1. NM_001142673.2. [O75143-1 ]
    NP_001192048.1. NM_001205119.1. [O75143-5 ]
    NP_001192049.1. NM_001205120.1. [O75143-1 ]
    NP_001192050.1. NM_001205121.1. [O75143-2 ]
    NP_001192051.1. NM_001205122.1. [O75143-4 ]
    NP_055556.2. NM_014741.4. [O75143-2 ]
    XP_005253319.1. XM_005253262.1. [O75143-5 ]
    XP_005253320.1. XM_005253263.1. [O75143-5 ]
    XP_005253322.1. XM_005253265.1. [O75143-5 ]
    XP_005253323.1. XM_005253266.1. [O75143-5 ]
    XP_005253325.1. XM_005253268.1. [O75143-5 ]
    XP_006718457.1. XM_006718394.1. [O75143-5 ]
    XP_006718458.1. XM_006718395.1. [O75143-5 ]
    XP_006718459.1. XM_006718396.1. [O75143-5 ]
    UniGenei Hs.127403.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3WAN X-ray 1.77 A/B 436-447 [» ]
    3WAO X-ray 2.60 A/B/C/D 436-447 [» ]
    3WAP X-ray 3.10 A 436-447 [» ]
    ProteinModelPortali O75143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115120. 14 interactions.
    DIPi DIP-60540N.
    IntActi O75143. 13 interactions.
    MINTi MINT-8247472.

    PTM databases

    PhosphoSitei O75143.

    Proteomic databases

    MaxQBi O75143.
    PaxDbi O75143.
    PRIDEi O75143.

    Protocols and materials databases

    DNASUi 9776.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359513 ; ENSP00000352500 ; ENSG00000175224 . [O75143-1 ]
    ENST00000524625 ; ENSP00000433543 ; ENSG00000175224 . [O75143-2 ]
    ENST00000526508 ; ENSP00000431974 ; ENSG00000175224 . [O75143-1 ]
    ENST00000528494 ; ENSP00000432412 ; ENSG00000175224 . [O75143-5 ]
    ENST00000529655 ; ENSP00000433756 ; ENSG00000175224 . [O75143-2 ]
    ENST00000530500 ; ENSP00000434390 ; ENSG00000175224 . [O75143-4 ]
    GeneIDi 9776.
    KEGGi hsa:9776.
    UCSCi uc001ncz.3. human. [O75143-2 ]
    uc001ndb.3. human. [O75143-1 ]
    uc010rgv.2. human. [O75143-4 ]

    Organism-specific databases

    CTDi 9776.
    GeneCardsi GC11P046638.
    HGNCi HGNC:29091. ATG13.
    HPAi HPA039350.
    MIMi 615088. gene.
    neXtProti NX_O75143.
    PharmGKBi PA165543187.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266388.
    HOGENOMi HOG000008446.
    KOi K08331.
    OMAi MCVEISL.
    OrthoDBi EOG744T8P.
    PhylomeDBi O75143.
    TreeFami TF321599.

    Miscellaneous databases

    ChiTaRSi ATG13. human.
    GeneWikii Autophagy-related_protein_13.
    GenomeRNAii 9776.
    NextBioi 36806.
    PROi O75143.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75143.
    Bgeei O75143.
    CleanExi HS_KIAA0652.
    Genevestigatori O75143.

    Family and domain databases

    InterProi IPR018731. Autophagy-rel_p13.
    [Graphical view ]
    Pfami PF10033. ATG13. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
      Tissue: Brain cortex and Thyroid.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Cervix, Lung and Muscle.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Atg101, a novel mammalian autophagy protein interacting with Atg13."
      Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.
      Autophagy 5:973-979(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG101; ULK1 AND RB1CC1.
    9. "A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy."
      Mercer C.A., Kaliappan A., Dennis P.B.
      Autophagy 5:649-662(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AUTOPHAGY FACTOR, PHOSPHORYLATION, INTERACTION WITH ULK1 AND ATG101.
    10. "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
      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.
      Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ULK1 AND RB1CC1, PHOSPHORYLATION.
    11. "ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery."
      Jung C.H., Jun C.B., Ro S.H., Kim Y.M., Otto N.M., Cao J., Kundu M., Kim D.H.
      Mol. Biol. Cell 20:1992-2003(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ULK1; ULK2 AND RB1CC1, PHOSPHORYLATION BY ULK1; ULK2 AND MTOR, FUNCTION.
    12. Cited for: FUNCTION, INTERACTION WITH ULK1, PHOSPHORYLATION AT SER-355 BY ULK1.
    13. "Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism."
      Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.
      Mol. Cell. Biol. 29:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AUTOPHAGY FACTOR, INTERACTION WITH ULK1 AND ULK2, PHOSPHORYLATION BY ULK1 AND ULK2.
    14. "ULK1 inhibits the kinase activity of mTORC1 and cell proliferation."
      Jung C.H., Seo M., Otto N.M., Kim D.H.
      Autophagy 7:1212-1221(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
      Kim J., Kundu M., Viollet B., Guan K.L.
      Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH ULK1 AND RB1CC1.
    16. "TGFbeta-activated kinase 1 (TAK1)-binding proteins (TAB) 2 and 3 negatively regulate autophagy."
      Takaesu G., Kobayashi T., Yoshimura A.
      J. Biochem. 151:157-166(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAB2 AND TAB3.
    17. "ATG8 family proteins act as scaffolds for assembly of the ULK complex: sequence requirements for LC3-interacting region (LIR) motifs."
      Alemu E.A., Lamark T., Torgersen K.M., Birgisdottir A.B., Larsen K.B., Jain A., Olsvik H., Overvatn A., Kirkin V., Johansen T.
      J. Biol. Chem. 287:39275-39290(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP; GABARAPL1; GABARAPL2 AND LC3A, DOMAIN, MUTAGENESIS.
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATG13_HUMAN
    AccessioniPrimary (citable) accession number: O75143
    Secondary accession number(s): B4DFI4
    , D3DQQ1, D3DQQ2, E9PQZ8, Q53EN6, Q9BRL3, Q9H8B0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3