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Q06628 (ATG13_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy-related protein 13
Gene names
Name:ATG13
Synonyms:APG13
Ordered Locus Names:YPR185W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Activates the ATG1 kinase in a nutritional condition dependent manner through the TOR pathway, leading to autophagy. Required for autophosphorylation of ATG1 at 'Thr-226' and its dimerization. May also be involved in the regulation of autophagy through SNF1. Involved in ATG9 and ATG23 cycling through the pre-autophagosomal structure. Also involved in cytoplasm to vacuole transport (Cvt) and more specifically in Cvt vesicle formation. Seems to play a role in the switching machinery regulating the conversion between the Cvt pathway and autophagy. Finally, ATG13 is also required for glycogen storage during stationary phase. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.12 Ref.13 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.33 Ref.35 Ref.38 Ref.39 Ref.40 Ref.41

Subunit structure

Hypophosphorylated form interacts with ATG1 to form the ATG1-ATG13 kinase complex. The ATG1-ATG13 complex interacts with the ATG17-ATG29-ATG31 complex through direct interaction with ATG17. Interacts with VAC8. Ref.5 Ref.7 Ref.13 Ref.14 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29 Ref.35 Ref.37 Ref.38 Ref.40

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein Ref.10 Ref.17 Ref.33.

Post-translational modification

Phosphorylated; hyperphosphorylated by the TORC1 kinase complex to repress the induction of autophagy. Starvation and TOR inactivation results in ATG13 partial dephosphorylation leading to ATG1-binding. Rephosphorylated by ATG1 during prolonged nitrogen starvation. Also phosphorylated by PKA. PKA phosphorylation regulates the association of ATG13 with the PAS. Within this regulatory network, mitochondrial respiratory deficiency suppresses autophagic flux. Hyperphosphorylation in rich medium is impaired in the absence of VAC8. Ref.7 Ref.19 Ref.25 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.39 Ref.41 Ref.42

Miscellaneous

Present with 149 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATG13 fungi family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATG1P5310413EBI-36188,EBI-2657
VAC8P399685EBI-36188,EBI-20212

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 738738Autophagy-related protein 13
PRO_0000157972

Regions

Region432 – 52089Interaction with ATG1
Compositional bias306 – 33833Poly-Gln
Compositional bias622 – 6254Poly-Asp
Compositional bias699 – 70810Poly-Asn

Amino acid modifications

Modified residue3441Phosphoserine; by PKA
Modified residue3481Phosphoserine; by TORC1 Ref.31
Modified residue3551Phosphoserine Ref.18 Ref.23 Ref.26
Modified residue3601Phosphoserine Ref.18
Modified residue4371Phosphoserine; by TORC1 and PKA Ref.31
Modified residue4381Phosphoserine; by TORC1 Ref.31
Modified residue4611Phosphoserine Ref.23 Ref.26
Modified residue4961Phosphoserine; by TORC1 Ref.31
Modified residue5351Phosphoserine; by TORC1 Ref.31
Modified residue5411Phosphoserine; by TORC1 Ref.31
Modified residue5541Phosphoserine Ref.23
Modified residue5811Phosphoserine; by PKA
Modified residue6461Phosphoserine; by TORC1 Ref.31
Modified residue6491Phosphoserine; by TORC1 Ref.15 Ref.23 Ref.26 Ref.31

Experimental info

Mutagenesis3441S → A: Decreases phosphorylation by PKA. Ref.25
Mutagenesis3481S → A: Leads to constitutive activation of autophagy; when associated with A-437; A-438; A-496; A-535; A-541; A-646 and A-649. Ref.31
Mutagenesis4371S → A: Decreases phosphorylation by PKA. Leads to constitutive activation of autophagy; when associated with A-348; A-438; A-496; A-535; A-541; A-646 and A-649. Ref.25 Ref.31
Mutagenesis4381S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-496; A-535; A-541; A-646 and A-649. Ref.31
Mutagenesis4681F → A: Impairs binding to ATG1; when associated with A-469. Ref.38
Mutagenesis4691V → A: Impairs binding to ATG1; when associated with A-468. Ref.38
Mutagenesis4961S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-438; A-535; A-541; A-646 and A-649. Ref.31
Mutagenesis5351S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-438; A-496; A-541; A-646 and A-649. Ref.31
Mutagenesis5411S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-438; A-496; A-535; A-646 and A-649. Ref.31
Mutagenesis5811S → A: Decreases phosphorylation by PKA. Ref.25
Mutagenesis6461S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-438; A-496; A-535; A-541 and A-649. Ref.31
Mutagenesis6491S → A: Leads to constitutive activation of autophagy; when associated with A-348; A-437; A-438; A-496; A-535; A-541, and A-646. Ref.31

Sequences

Sequence LengthMass (Da)Tools
Q06628 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 45CD16F69B795E62

FASTA73883,281
        10         20         30         40         50         60 
MVAEEDIEKQ VLQLIDSFFL KTTLLICSTE SSRYQSSTEN IFLFDDTWFE DHSELVSELP 

        70         80         90        100        110        120 
EIISKWSHYD GRKELPPLVV ETYLDLRQLN SSHLVRLKDH EGHLWNVCKG TKKQEIVMER 

       130        140        150        160        170        180 
WLIELDNSSP TFKSYSEDET DVNELSKQLV LLFRYLLTLI QLLPTTELYQ LLIKSYNGPQ 

       190        200        210        220        230        240 
NEGSSNPITS TGPLVSIRTC VLDGSKPILS KGRIGLSKPI INTYSNALNE SNLPAHLDQK 

       250        260        270        280        290        300 
KITPVWTKFG LLRVSVSYRR DWKFEINNTN DELFSARHAS VSHNSQGPQN QPEQEGQSDQ 

       310        320        330        340        350        360 
DIGKRQPQFQ QQQQPQQQQQ QQQQQQRQHQ VQTQQQRQIP DRRSLSLSPC TRANSFEPQS 

       370        380        390        400        410        420 
WQKKVYPISR PVQPFKVGSI GSQSASRNPS NSSFFNQPPV HRPSMSSNYG PQMNIEGTSV 

       430        440        450        460        470        480 
GSTSKYSSSF GNIRRHSSVK TTENAEKVSK AVKSPLQPQE SQEDLMDFVK LLEEKPDLTI 

       490        500        510        520        530        540 
KKTSGNNPPN INISDSLIRY QNLKPSNDLL SEDLSVSLSM DPNHTYHRGR SDSHSPLPSI 

       550        560        570        580        590        600 
SPSMHYGSLN SRMSQGANAS HLIARGGGNS STSALNSRRN SLDKSSNKQG MSGLPPIFGG 

       610        620        630        640        650        660 
ESTSYHHDNK IQKYNQLGVE EDDDDENDRL LNQMGNSATK FKSSISPRSI DSISSSFIKS 

       670        680        690        700        710        720 
RIPIRQPYHY SQPTTAPFQA QAKFHKPANK LIDNGNRSNS NNNNHNGNDA VGVMHNDEDD 

       730 
QDDDLVFFMS DMNLSKEG 

« Hide

References

« Hide 'large scale' references
[1]"Analyses of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae."
Funakoshi T., Matsuura A., Noda T., Ohsumi Y.
Gene 192:207-213(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae."
Tsukada M., Ohsumi Y.
FEBS Lett. 333:169-174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting."
Scott S.V., Nice D.C. III, Nau J.J., Weisman L.S., Kamada Y., Keizer-Gunnink I., Funakoshi T., Veenhuis M., Ohsumi Y., Klionsky D.J.
J. Biol. Chem. 275:25840-25849(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAC8.
[6]"Dissection of autophagosome biogenesis into distinct nucleation and expansion steps."
Abeliovich H., Dunn W.A. Jr., Kim J., Klionsky D.J.
J. Cell Biol. 151:1025-1034(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Tor-mediated induction of autophagy via an Apg1 protein kinase complex."
Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.
J. Cell Biol. 150:1507-1513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH ATG1.
[8]"Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p."
Wang Z., Wilson W.A., Fujino M.A., Roach P.J.
Mol. Cell. Biol. 21:5742-5752(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A unified nomenclature for yeast autophagy-related genes."
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.
Dev. Cell 5:539-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure."
Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.
Dev. Cell 6:79-90(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Atg17 functions in cooperation with Atg1 and Atg13 in yeast autophagy."
Kabeya Y., Kamada Y., Baba M., Takikawa H., Sasaki M., Ohsumi Y.
Mol. Biol. Cell 16:2544-2553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG1 AND ATG17.
[14]"Atg17 regulates the magnitude of the autophagic response."
Cheong H., Yorimitsu T., Reggiori F., Legakis J.E., Wang C.W., Klionsky D.J.
Mol. Biol. Cell 16:3438-3453(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG1 AND ATG17.
[15]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[16]"A cycling protein complex required for selective autophagy."
Legakis J.E., Yen W.L., Klionsky D.J.
Autophagy 3:422-432(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Hierarchy of Atg proteins in pre-autophagosomal structure organization."
Suzuki K., Kubota Y., Sekito T., Ohsumi Y.
Genes Cells 12:209-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[18]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-360, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[19]"Protein kinase A and Sch9 cooperatively regulate induction of autophagy in Saccharomyces cerevisiae."
Yorimitsu T., Zaman S., Broach J.R., Klionsky D.J.
Mol. Biol. Cell 18:4180-4189(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[20]"The Atg1 kinase complex is involved in the regulation of protein recruitment to initiate sequestering vesicle formation for nonspecific autophagy in Saccharomyces cerevisiae."
Cheong H., Nair U., Geng J., Klionsky D.J.
Mol. Biol. Cell 19:668-681(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Organization of the pre-autophagosomal structure responsible for autophagosome formation."
Kawamata T., Kamada Y., Kabeya Y., Sekito T., Ohsumi Y.
Mol. Biol. Cell 19:2039-2050(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE ATG1-ATG13 COMPLEX.
[22]"Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy."
He C., Baba M., Cao Y., Klionsky D.J.
Mol. Biol. Cell 19:5506-5516(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG1.
[23]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-461; SER-554 AND SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Characterization of the Atg17-Atg29-Atg31 complex specifically required for starvation-induced autophagy in Saccharomyces cerevisiae."
Kabeya Y., Noda N.N., Fujioka Y., Suzuki K., Inagaki F., Ohsumi Y.
Biochem. Biophys. Res. Commun. 389:612-615(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE ATG17-ATG29-ATG31 COMPLEX.
[25]"The Tor and PKA signaling pathways independently target the Atg1/Atg13 protein kinase complex to control autophagy."
Stephan J.S., Yeh Y.Y., Ramachandran V., Deminoff S.J., Herman P.K.
Proc. Natl. Acad. Sci. U.S.A. 106:17049-17054(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PKA AT SER-344; SER-437 AND SER-581, MUTAGENESIS OF SER-344; SER-437 AND SER-581, FUNCTION, INTERACTION WITH ATG17.
[26]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; SER-461 AND SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Induction of autophagic flux by amino acid deprivation is distinct from nitrogen starvation-induced macroautophagy."
Ecker N., Mor A., Journo D., Abeliovich H.
Autophagy 6:879-890(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"Activation of Atg1 kinase in autophagy by regulated phosphorylation."
Kijanska M., Dohnal I., Reiter W., Kaspar S., Stoffel I., Ammerer G., Kraft C., Peter M.
Autophagy 6:1168-1178(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG1.
[29]"Autophosphorylation within the Atg1 activation loop is required for both kinase activity and the induction of autophagy in Saccharomyces cerevisiae."
Yeh Y.Y., Wrasman K., Herman P.K.
Genetics 185:871-882(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG1.
[30]"An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis."
Mari M., Griffith J., Rieter E., Krishnappa L., Klionsky D.J., Reggiori F.
J. Cell Biol. 190:1005-1022(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"Tor directly controls the Atg1 kinase complex to regulate autophagy."
Kamada Y., Yoshino K., Kondo C., Kawamata T., Oshiro N., Yonezawa K., Ohsumi Y.
Mol. Cell. Biol. 30:1049-1058(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-348; SER-437; SER-438; SER-496; SER-535; SER-541; SER-646 AND SER-649, MUTAGENESIS OF SER-348; SER-437; SER-438; SER-496; SER-535; SER-541; SER-646 AND SER-649, FUNCTION.
[32]"Bidirectional regulation between TORC1 and autophagy in Saccharomyces cerevisiae."
Shin C.S., Huh W.K.
Autophagy 7:854-862(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ATG1.
[33]"Mitochondria regulate autophagy by conserved signalling pathways."
Graef M., Nunnari J.
EMBO J. 30:2101-2114(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION OF THE ATG1-ATG13 COMPLEX.
[34]"Antagonistic interactions between the cAMP-dependent protein kinase and Tor signaling pathways modulate cell growth in Saccharomyces cerevisiae."
Ramachandran V., Herman P.K.
Genetics 187:441-454(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION.
[35]"An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy."
Yeh Y.Y., Shah K.H., Herman P.K.
J. Biol. Chem. 286:28931-28939(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG1.
[36]"Selective regulation of autophagy by the Iml1-Npr2-Npr3 complex in the absence of nitrogen starvation."
Wu X., Tu B.P.
Mol. Biol. Cell 22:4124-4133(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION.
[37]"Architecture of the Atg17 complex as a scaffold for autophagosome biogenesis."
Ragusa M.J., Stanley R.E., Hurley J.H.
Cell 151:1501-1512(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE ATG17-ATG29-ATG31 COMPLEX.
[38]"Binding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagy."
Kraft C., Kijanska M., Kalie E., Siergiejuk E., Lee S.S., Semplicio G., Stoffel I., Brezovich A., Verma M., Hansmann I., Ammerer G., Hofmann K., Tooze S., Peter M.
EMBO J. 31:3691-3703(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG1, MUTAGENESIS OF PHE-468 AND VAL-469, FUNCTION.
[39]"Ksp1 kinase regulates autophagy via the target of rapamycin complex 1 (TORC1) pathway."
Umekawa M., Klionsky D.J.
J. Biol. Chem. 287:16300-16310(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY TORC1 COMPLEX.
[40]"The autophagy-related protein kinase Atg1 interacts with the ubiquitin-like protein Atg8 via the Atg8 family interacting motif to facilitate autophagosome formation."
Nakatogawa H., Ohbayashi S., Sakoh-Nakatogawa M., Kakuta S., Suzuki S.W., Kirisako H., Kondo-Kakuta C., Noda N.N., Yamamoto H., Ohsumi Y.
J. Biol. Chem. 287:28503-28507(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG1.
[41]"The protein factor-arrest 11 (Far11) is essential for the toxicity of human caspase-10 in yeast and participates in the regulation of autophagy and the DNA damage signaling."
Lisa-Santamaria P., Jimenez A., Revuelta J.L.
J. Biol. Chem. 287:29636-29647(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[42]"Transient sequestration of TORC1 into stress granules during heat stress."
Takahara T., Maeda T.
Mol. Cell 47:242-252(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25842 Genomic DNA. Translation: AAB68118.1.
D88025 Genomic DNA. Translation: BAA21485.1.
BK006949 Genomic DNA. Translation: DAA11601.1.
PIRS59842.
RefSeqNP_015511.1. NM_001184282.1.

3D structure databases

ProteinModelPortalQ06628.
SMRQ06628. Positions 7-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36357. 77 interactions.
DIPDIP-1191N.
IntActQ06628. 8 interactions.
MINTMINT-384768.
STRING4932.YPR185W.

Protein family/group databases

TCDB9.A.15.1.1. the autophagy-related phagophore-formation transporter (apt) family.

Proteomic databases

MaxQBQ06628.
PaxDbQ06628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR185W; YPR185W; YPR185W.
GeneID856315.
KEGGsce:YPR185W.

Organism-specific databases

CYGDYPR185w.
SGDS000006389. ATG13.

Phylogenomic databases

eggNOGNOG318247.
HOGENOMHOG000034130.
KOK08331.
OMANIASHLE.
OrthoDBEOG744TJK.

Enzyme and pathway databases

BioCycYEAST:G3O-34308-MONOMER.

Gene expression databases

GenevestigatorQ06628.

Family and domain databases

InterProIPR018731. Autophagy-rel_p13.
[Graphical view]
PfamPF10033. ATG13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981697.

Entry information

Entry nameATG13_YEAST
AccessionPrimary (citable) accession number: Q06628
Secondary accession number(s): D6W4I5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families