Carbon catabolite-derepressing protein kinase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

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)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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. Ref.6
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. Source: SGD carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from mutant phenotype. Source: SGD cellular response to nitrogen starvation Inferred from direct assay. Source: SGD invasive growth in response to glucose limitation Inferred from mutant phenotype. Source: SGD negative regulation of translation Inferred from mutant phenotype. Source: SGD positive regulation of gluconeogenesis Inferred from mutant phenotype. Source: SGD pseudohyphal growth Inferred from mutant phenotype. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD signal transduction Traceable author statement. Source: SGD
Cellular component	AMP-activated protein kinase complex Inferred from direct assay. Source: SGD fungal-type vacuole Inferred from physical interaction. Source: SGD mitochondrion Inferred from direct assay. Source: SGD nuclear envelope lumen Inferred from direct assay. Source: SGD nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	AMP-activated protein kinase activity Inferred from direct assay. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CDC14	Q00684	2	EBI-17516,EBI-4192
GAL83	Q04739	6	EBI-17516,EBI-7244
NPR1	P22211	2	EBI-17516,EBI-12207
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

.

633

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P06782 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: F5C63565C986C4E3
Show »

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

« Hide

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: 3526554] [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. Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [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: 7905477] [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: 12748292] [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: 14562106] [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: 12872131] [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: 15719021] [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: 16182287] [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: 16847059] [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: 17330950] [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: 17563356] [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: 18407956] [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_010765.1. NM_001180785.1.

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 46-630.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-18N.

IntAct

P06782. 32 interactions.

MINT

MINT-364314.

STRING

P06782.

Proteomic databases

PeptideAtlas

P06782.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR477W; YDR477W; YDR477W.

GeneID

852088.

KEGG

sce:YDR477W.

NMPDR

fig|4932.3.peg.1538.

Organism-specific databases

CYGD

YDR477w.

SGD

S000002885. SNF1.

Phylogenomic databases

eggNOG

fuNOG05716.

GeneTree

EFGT00070000008711.

HOGENOM

HBG755340.

OMA

SKIGILP.

OrthoDB

EOG4Q5CXQ.

Enzyme and pathway databases

BRENDA

2.7.11.1. 984.

Gene expression databases

ArrayExpress

P06782.

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.
IPR017442. Se/Thr_kinase-like_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR002290. Ser/Thr_kinase_dom.
IPR013896. Ubiquitin-assoc_dom.
[Graphical view]

KO

K12761.

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

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:	January 25, 2012
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents