[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/(SICI)1097-0061(199701)13:1<55::AID-YEA48>3.3.CO;2-0; PubMed=9046087 [NCBI, ExPASy, EBI, Israel, Japan] Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.; "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII from Saccharomyces cerevisiae."; Yeast 13:55-64(1997).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-211 AND GLU-237. STRAIN=ATCC 26109 / X2180; DOI=10.1016/S0378-1119(97)00084-X; PubMed=9224897 [NCBI, ExPASy, EBI, Israel, Japan] Matsuura A., Tsukada M., Wada Y., Ohsumi Y.; "Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae."; Gene 192:245-250(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan] Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; Nature 387:81-84(1997).
[4]	FUNCTION. DOI=10.1016/0014-5793(93)80398-E; PubMed=8224160 [NCBI, ExPASy, EBI, Israel, Japan] Tsukada M., Ohsumi Y.; "Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae."; FEBS Lett. 333:169-174(1993).
[5]	FUNCTION. DOI=10.1074/jbc.271.30.17621; PubMed=8663607 [NCBI, ExPASy, EBI, Israel, Japan] Harding T.M., Hefner-Gravink A., Thumm M., Klionsky D.J.; "Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway."; J. Biol. Chem. 271:17621-17624(1996).
[6]	FUNCTION, AND SUBCELLULAR LOCATION. PubMed=9190802 [NCBI, ExPASy, EBI, Israel, Japan] Straub M., Bredschneider M., Thumm M.; "AUT3, a serine/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae."; J. Bacteriol. 179:3875-3883(1997).
[7]	SUBCELLULAR LOCATION. DOI=10.1074/jbc.M002813200; PubMed=10837477 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting."; J. Biol. Chem. 275:25840-25849(2000).
[8]	FUNCTION, ENZYME REGULATION, MUTAGENESIS OF LYS-54, AND INTERACTION WITH ATG11; ATG13 AND ATG17. DOI=10.1083/jcb.150.6.1507; PubMed=10995454 [NCBI, ExPASy, EBI, Israel, Japan] Kamada Y., Funakoshi T., Shintani T., Nagano K., Ohsumi M., Ohsumi Y.; "Tor-mediated induction of autophagy via an Apg1 protein kinase complex."; J. Cell Biol. 150:1507-1513(2000).
[9]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1093/emboj/20.21.5971; PubMed=11689437 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.; "The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation."; EMBO J. 20:5971-5981(2001).
[10]	INTERACTION WITH ATG11. DOI=10.1083/jcb.153.2.381; PubMed=11309418 [NCBI, ExPASy, EBI, Israel, Japan] Kim J., Kamada Y., Stromhaug P.E., Guan J., Hefner-Gravink A., Baba M., Scott S.V., Ohsumi Y., Dunn W.A. Jr., Klionsky D.J.; "Cvt9/Gsa9 functions in sequestering selective cytosolic cargo destined for the vacuole."; J. Cell Biol. 153:381-396(2001).
[11]	FUNCTION. DOI=10.1128/MCB.21.17.5742-5752.2001; PubMed=11486014 [NCBI, ExPASy, EBI, Israel, Japan] Wang Z., Wilson W.A., Fujino M.A., Roach P.J.; "Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p."; Mol. Cell. Biol. 21:5742-5752(2001).
[12]	NOMENCLATURE. DOI=10.1016/S1534-5807(03)00296-X; PubMed=14536056 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "A unified nomenclature for yeast autophagy-related genes."; Dev. Cell 5:539-545(2003).
[13]	FUNCTION, AND MUTAGENESIS OF LYS-54; MET-102; ASN-884 AND LEU-886. DOI=10.1091/mbc.E02-07-0413; PubMed=12589048 [NCBI, ExPASy, EBI, Israel, Japan] Abeliovich H., Zhang C., Dunn W.A. Jr., Shokat K.M., Klionsky D.J.; "Chemical genetic analysis of Apg1 reveals a non-kinase role in the induction of autophagy."; Mol. Biol. Cell 14:477-490(2003).
[14]	SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan] Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.; "Global analysis of protein localization in budding yeast."; Nature 425:686-691(2003).
[15]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[16]	FUNCTION. DOI=10.1016/S1534-5807(03)00402-7; PubMed=14723849 [NCBI, ExPASy, EBI, Israel, Japan] Reggiori F., Tucker K.A., Stromhaug P.E., Klionsky D.J.; "The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure."; Dev. Cell 6:79-90(2004).
[17]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan] Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.; "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."; Mol. Cell. Proteomics 4:310-327(2005).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-390; SER-508; SER-515; SER-517; SER-647; SER-677; SER-683 AND SER-783, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).

Comments

FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. ATG1 kinase activity is only essential in the Cvt pathway. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9. Finally, ATG1 is also required for the maintenance of cell viability under starvation and for glycogen storage during stationary phase.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Activated by hypophosphorylated form of ATG13 (present in nitrogen starvation conditions).
SUBUNIT: Interacts with ATG13. Interacts also with ATG11 and ATG17.
INTERACTION:
Q12527:ATG11; NbExp=1; IntAct=EBI-2657, EBI-31977;
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Preautophagosomal structure membrane; Peripheral membrane protein. Note=Found in pre-autophagosomal structure and other punctate structures.
PTM: Autophosphorylated. May be regulated by a second protein kinase. The phosphorylation state may play a role in the induction of protein degradation upon starvation.
MISCELLANEOUS: Present with 1070 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X91489; CAA62794.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D29991; BAA21481.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72702; CAA96892.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S61137; S61137.

RefSeq

NP_011335.1; -.

3D structure databases

ModBase

P53104.

Protein-protein interaction databases

DIP

DIP:1192N; -.

IntAct

P53104; 17.

Organism-specific databases

YGL180w; -.

S000003148; ATG1.

Gene expression databases

ArrayExpress

P53104; -.

GermOnline

YGL180W; Saccharomyces cerevisiae.

Ontologies

GO:0034273;	Cellular component: Atg1p signaling complex (inferred from physical interaction from SGD).
GO:0005829;	Cellular component: cytosol (inferred from direct assay from SGD).
GO:0034045;	Cellular component: pre-autophagosomal structure membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0000045;	Biological process: autophagic vacuole formation (inferred from mutant phenotype from SGD).
GO:0034727;	Biological process: piecemeal microautophagy of nucleus (inferred from mutant phenotype from SGD).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0015031;	Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

YGL180W; Saccharomyces cerevisiae. [Contig view]

852695; -.

Y13135_GR; YGL180W.

sce:YGL180W; -.

fig|4932.3.peg.2439; -.

Phylogenomic databases

HOGENOM

P53104; -.

Other

P53104; -.

972032; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Protein transport; Serine/threonine-protein kinase; Transferase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 897`	`897`	`Serine/threonine-protein kinase ATG1.`	`PRO_0000085655`
`DOMAIN`	`24 325`	`302`	`Protein kinase.`
`NP_BIND`	`30 38`	`9`	`ATP (By similarity).`
`REGION`	`880 886`	`7`	`Required for Cvt trafficking.`
`COMPBIAS`	`542 548`	`7`	`Poly-Gln.`
`ACT_SITE`	`172 172`		`Proton acceptor (By similarity).`
`BINDING`	`54 54`		`ATP (By similarity).`
`MOD_RES`	`365 365`		`Phosphoserine.`
`MOD_RES`	`390 390`		`Phosphoserine.`
`MOD_RES`	`508 508`		`Phosphoserine.`
`MOD_RES`	`515 515`		`Phosphoserine.`
`MOD_RES`	`517 517`		`Phosphoserine.`
`MOD_RES`	`647 647`		`Phosphoserine.`
`MOD_RES`	`677 677`		`Phosphoserine.`
`MOD_RES`	`683 683`		`Phosphoserine.`
`MOD_RES`	`783 783`		`Phosphoserine.`
`MUTAGEN`	`54 54`		`K->A: Defect in the Cvt pathway.`
`MUTAGEN`	`102 102`		`M->A: Enables the binding of the inhibitor of the kinase activity 1-NA-PP1.`
`MUTAGEN`	`211 211`		`D->A: Loss of cell viability under starvation.`
`MUTAGEN`	`237 237`		`E->R: Loss of cell viability under starvation.`
`MUTAGEN`	`884 884`		`N->A: No effect.`
`MUTAGEN`	`886 886`		`L->G: Cvt pathway specific block.`

Sequence information

Length: 897 AA [This is the length of the unprocessed precursor]

Molecular weight: 101717 Da [This is the MW of the unprocessed precursor]

CRC64: 7F4C785AA3A7CC46 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGDIKNKDHT TSVNHNLMAS AGNYTAEKEI GKGSFATVYR GHLTSDKSQH VAIKEVSRAK 

        70         80         90        100        110        120 
LKNKKLLENL EIEIAILKKI KHPHIVGLID CERTSTDFYL IMEYCALGDL TFLLKRRKEL 

       130        140        150        160        170        180 
MENHPLLRTV FEKYPPPSEN HNGLHRAFVL SYLQQLASAL KFLRSKNLVH RDIKPQNLLL 

       190        200        210        220        230        240 
STPLIGYHDS KSFHELGFVG IYNLPILKIA DFGFARFLPN TSLAETLCGS PLYMAPEILN 

       250        260        270        280        290        300 
YQKYNAKADL WSVGTVVFEM CCGTPPFRAS NHLELFKKIK RANDVITFPS YCNIEPELKE 

       310        320        330        340        350        360 
LICSLLTFDP AQRIGFEEFF ANKVVNEDLS SYELEDDLPE LESKSKGIVE SNMFVSEYLS 

       370        380        390        400        410        420 
KQPKSPNSNL AGHQSMADNP AELSDALKNS NILTAPAVKT DHTQAVDKKA SNNKYHNSLV 

       430        440        450        460        470        480 
SDRSFEREYV VVEKKSVEVN SLADEVAQAG FNPNPIKHPT STQNQNVLLN EQFSPNNQQY 

       490        500        510        520        530        540 
FQNQGENPRL LRATSSSSGG SDGSRRPSLV DRRLSISSLN PSNALSRALG IASTRLFGGA 

       550        560        570        580        590        600 
NQQQQQQQIT SSPPYSQTLL NSQLFHELTE NIILRIDHLQ HPETLKLDNT NIVSILESLA 

       610        620        630        640        650        660 
AKAFVVYSYA EVKFSQIVPL STTLKGMANF ENRRSMDSNA IAEEQDSDDA EEEDETLKKY 

       670        680        690        700        710        720 
KEDCLSTKTF GKGRTLSATS QLSATFNKLP RSEMILLCNE AIVLYMKALS ILSKSMQVTS 

       730        740        750        760        770        780 
NWWYESQEKS CSLRVNVLVQ WLREKFNECL EKADFLRLKI NDLRFKHASE VAENQTLEEK 

       790        800        810        820        830        840 
GSSEEPVYLE KLLYDRALEI SKMAAHMELK GENLYNCELA YATSLWMLET SLDDDDFTNA 

       850        860        870        880        890 
YGDYPFKTNI HLKSNDVEDK EKYHSVLDEN DRIIIRKYID SIANRLKILR QKMNHQN

P53104 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools