P06782 (SNF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbon catabolite-derepressing protein kinase
EC=2.7.11.1

Gene names

Name:	SNF1
Synonyms:	CAT1, CCR1, GLC2, PAS14
Ordered Locus Names:	YDR477W
ORF Names:	D8035.20

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	633 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters. Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with CTK1, GAL83, SAK1, SIP1, SIP2 and SNF4. Ref.5 Ref.9 Ref.10
Subcellular location	Nucleus membrane; Peripheral membrane protein.
Miscellaneous	Present with 589 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	biofilm formation Inferred from mutant phenotype PubMed 12024013. Source: SGD carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from mutant phenotype PubMed 12556493. Source: SGD cellular response to nitrogen starvation Inferred from direct assay PubMed 12024013. Source: SGD invasive growth in response to glucose limitation Inferred from mutant phenotype PubMed 11095711PubMed 12556493. Source: SGD negative regulation of translation Inferred from mutant phenotype PubMed 18955495. Source: SGD positive regulation of filamentous growth of a population of unicellular organisms in response to starvation Inferred from mutant phenotype PubMed 22904036. Source: SGD positive regulation of gluconeogenesis Inferred from mutant phenotype PubMed 8628258PubMed 8710504PubMed 9111319. Source: SGD pseudohyphal growth Inferred from mutant phenotype PubMed 12024013. Source: SGD replicative cell aging Inferred from mutant phenotype PubMed 10921902. Source: SGD signal transduction Traceable author statement PubMed 10322167. Source: SGD
Cellular_component	AMP-activated protein kinase complex Inferred from direct assay PubMed 12393914PubMed 2481228. Source: SGD fungal-type vacuole Inferred from physical interaction PubMed 11331606. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD nuclear envelope lumen Inferred from direct assay PubMed 17237508. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	AMP-activated protein kinase activity Inferred from direct assay PubMed 2557546PubMed 7913470. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC14	Q00684	2	EBI-17516,EBI-4192
GAL83	Q04739	6	EBI-17516,EBI-7244
NPR1	P22211	2	EBI-17516,EBI-12207
REG1	Q00816	3	EBI-17516,EBI-8270
SIP2	P34164	11	EBI-17516,EBI-17187
SNF4	P12904	17	EBI-17516,EBI-17537

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 633

633

Carbon catabolite-derepressing protein kinase

PRO_0000086670

Regions

Domain

55 – 306

252

Protein kinase

Nucleotide binding

61 – 69

9

ATP By similarity

Compositional bias

18 – 32

15

Poly-His

Sites

Active site

177

1

Proton acceptor By similarity

Binding site

84

1

ATP By similarity

Amino acid modifications

Modified residue

203

1

Phosphothreonine Ref.13

Modified residue

210

1

Phosphothreonine; by autocatalysis Ref.4 Ref.5 Ref.13

Modified residue

211

1

Phosphoserine Ref.13

Modified residue

214

1

Phosphoserine Ref.13

Modified residue

401

1

Phosphoserine Ref.13

Modified residue

411

1

Phosphoserine Ref.13

Modified residue

413

1

Phosphoserine Ref.7 Ref.11 Ref.12 Ref.13

Modified residue

416

1

Phosphothreonine Ref.13

Modified residue

487

1

Phosphoserine Ref.13

Secondary structure

1

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633

Helix Strand Turn

Details...

Beta strand

56 – 62

7

Helix

64 – 66

3

Beta strand

69 – 73

5

Turn

75 – 77

3

Beta strand

80 – 87

8

Helix

88 – 91

4

Helix

97 – 109

13

Beta strand

118 – 123

6

Beta strand

125 – 133

9

Helix

139 – 145

7

Helix

151 – 170

20

Turn

180 – 182

3

Beta strand

183 – 185

3

Beta strand

191 – 193

3

Turn

207 – 209

3

Helix

215 – 217

3

Helix

220 – 223

4

Beta strand

224 – 227

4

Helix

232 – 247

16

Helix

257 – 266

10

Helix

277 – 286

10

Helix

291 – 293

3

Helix

297 – 302

6

Helix

304 – 307

4

Helix

312 – 314

3

Turn

317 – 319

3

Helix

471 – 473

3

Helix

475 – 485

11

Helix

489 – 492

4

Beta strand

506 – 511

6

Helix

515 – 529

15

Beta strand

532 – 534

3

Helix

538 – 540

3

Beta strand

543 – 548

6

Beta strand

565 – 576

12

Beta strand

579 – 590

12

Helix

607 – 610

4

Helix

613 – 628

16

Sequences

	Sequence		Length	Mass (Da)
	P06782 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: F5C63565C986C4E3	FASTA	633	72,045
	10 20 30 40 50 60 MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA HIGNYQIVKT 70 80 90 100 110 120 LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI EREISYLRLL RHPHIIKLYD 130 140 150 160 170 180 VIKSKDEIIM VIEYAGNELF DYIVQRDKMS EQEARRFFQQ IISAVEYCHR HKIVHRDLKP 190 200 210 220 230 240 ENLLLDEHLN VKIADFGLSN IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV 250 260 270 280 290 300 ILYVMLCRRL PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI 310 320 330 340 350 360 MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN ILSSTMGYEK 370 380 390 400 410 420 DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK SVSDELDTFL SQSPPTFQQQ 430 440 450 460 470 480 SKSHQKSQVD HETAKQHARR MASAITQQRT YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA 490 500 510 520 530 540 NMLAQGSPAA SKISPLVTKK SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED 550 560 570 580 590 600 LWTIKLRWKY DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS 610 620 630 NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A yeast gene that is essential for release from glucose repression encodes a protein kinase." Celenza J.L., Carlson M. Science 233:1175-1180(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase." Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., Witters L.A., Kemp B.E. J. Biol. Chem. 269:2361-2364(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, PHOSPHORYLATION AT THR-210.
[5]	"Yeast Pak1 kinase associates with and activates Snf1." Nath N., McCartney R.R., Schmidt M.C. Mol. Cell. Biol. 23:3909-3917(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-210, INTERACTION WITH SAK1.
[6]	"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].
[7]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, MASS SPECTROMETRY. Strain: SUB592.
[8]	"Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms." Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L. EMBO J. 24:997-1008(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
[9]	"Glucose deprivation mediates interaction between CTDK-I and Snf1 in Saccharomyces cerevisiae." Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J. FEBS Lett. 579:5318-5324(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CTK1.
[10]	"Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity." Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C. J. Biol. Chem. 281:26170-26180(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH SAK1.
[11]	"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-413, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, MASS SPECTROMETRY.
[13]	"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 THR-203; THR-210; SER-211; SER-214; SER-401; SER-411; SER-413; THR-416 AND SER-487, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13971 Genomic DNA. Translation: AAA35058.1.
U33050 Genomic DNA. Translation: AAB64904.1.
BK006938 Genomic DNA. Translation: DAA12310.1.

PIR

A26030.

RefSeq

NP_010765.3. NM_001180785.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FH9	X-ray	2.80	A	46-319	[»]
2QLV	X-ray	2.60	A/D	460-630	[»]
3DAE	X-ray	2.90	A/B	41-315	[»]
3HYH	X-ray	2.20	A/B	41-315	[»]
3MN3	X-ray	2.38	A	50-320	[»]
3T4N	X-ray	2.30	A	457-633	[»]
3TDH	X-ray	2.30	A	457-633	[»]
3TE5	X-ray	2.50	A	457-633	[»]

ProteinModelPortal

P06782.

SMR

P06782. Positions 18-630.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-18N.

IntAct

P06782. 30 interactions.

MINT

MINT-364314.

STRING

4932.YDR477W.

Proteomic databases

PaxDb

P06782.

PeptideAtlas

P06782.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR477W; YDR477W; YDR477W.

GeneID

852088.

KEGG

sce:YDR477W.

Organism-specific databases

CYGD

YDR477w.

SGD

S000002885. SNF1.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00700000104077.

HOGENOM

HOG000233016.

KO

K12761.

OMA

QRDKMSE.

OrthoDB

EOG4Q5CXQ.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30003-MONOMER.

BRENDA

2.7.11.1. 984.

Gene expression databases

Genevestigator

P06782.

GermOnline

YDR477W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR013896. Ubiquitin-assoc_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF08587. UBA_2. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06782.

NextBio

970409.

Entry information

Entry name

SNF1_YEAST

Accession

Primary (citable) accession number: P06782
Secondary accession number(s): D6VTA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 29, 2013
This is version 155 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program