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O75143

- ATG13_HUMAN

UniProt

O75143 - ATG13_HUMAN

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Protein

Autophagy-related protein 13

Gene

ATG13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 kinase binding Source: UniProtKB

GO - Biological processi

  1. autophagic vacuole assembly Source: UniProtKB
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO75143.
CleanExiHS_KIAA0652.
ExpressionAtlasiO75143. baseline and differential.
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. 16 interactions.
DIPiDIP-60540N.
IntActiO75143. 14 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.
GeneTreeiENSGT00390000007055.
HOGENOMiHOG000008446.
InParanoidiO75143.
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

        10         20         30         40         50
METDLNSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW
60 70 80 90 100
FNLAIKDIPE VTHEAKKALA GQLPAVGRSM CVEISLKTSE GDSMELEIWC
110 120 130 140 150
LEMNEKCDKE IKVSYTVYNR LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI
160 170 180 190 200
LYRIYFGEVQ LSGLGEGFQT VRVGTVGTPV GTITLSCAYR INLAFMSTRQ
210 220 230 240 250
FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAGEDTGV IYPSVEDSQE
260 270 280 290 300
VCTTSFSTSP PSQLSSSRLS YQPAALGVGS ADLAYPVVFA AGLNATHPHQ
310 320 330 340 350
LMVPGKEGGV PLAPNQPVHG TQADQERLAT CTPSDRTHCA ATPSSSEDTE
360 370 380 390 400
TVSNSSEGRA SPHDVLETIF VRKVGAFVNK PINQVTLTSL DIPFAMFAPK
410 420 430 440 450
NLELEDTDPM VNPPDSPETE SPLQGSLHSD GSSGGSSGNT HDDFVMIDFK
460 470 480 490 500
PAFSKDDILP MDLGTFYREF QNPPQLSSLS IDIGAQSMAE DLDSLPEKLA
510
VHEKNVREFD AFVETLQ
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. 16 interactions.
DIPi DIP-60540N.
IntActi O75143. 14 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.
GeneTreei ENSGT00390000007055.
HOGENOMi HOG000008446.
InParanoidi O75143.
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

Bgeei O75143.
CleanExi HS_KIAA0652.
ExpressionAtlasi O75143. baseline and differential.
Genevestigatori O75143.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 113 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