Reviewed, UniProtKB/Swiss-Prot P34164 (SIP2_YEAST)

Names and origin

Protein names

Recommended name:
    SNF1 protein kinase subunit beta-2
Alternative name(s):
    SNF1-interacting protein 2
    Protein SPM2

Gene names

Name:	SIP2
Synonyms:	SPM2
Ordered Locus Names:	YGL208W
ORF Names:	G1155

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Beta subunit of the SNF1 kinase complex, which is required for transcriptional, metabolic, and developmental adaptations in response to glucose limitation. Has a structural role, mediating heterotrimer formation, and a regulatory role, defining carbon source-regulated subcellular location and substrate specificity of the SNF1 kinase complex. Involved in the regulation of aging. Acts as a negative regulator of nuclear SNF1 activity in young cells by sequestering its activating gamma subunit at the plasma membrane.
Subunit structure	Component of the SNF1 kinase complex, a heterotrimeric complex composed of the catalytic alpha subunit SNF1, one of the three related beta subunits SIP1, SIP2 or GAL83, and the regulatory gamma subunit SNF4. The beta subunit serves as a bridge between the catalytic and the regulatory subunit. Interacts (via KIS domain) with SNF1. Interacts (via ASC domain) with SNF4.
Subcellular location	Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Resides in the cytosol during growth in glucose. Excluded from the nucleus. There is an age-associated shift in localization from the plasma membrane to the cytoplasm.
Induction	Induced upon shift to nonfermentable carbon sources.
Post-translational modification	Phosphorylated by SNF1 in vitro. Ref.12 Ref.13 Ref.14
Miscellaneous	Present with 300 molecules/cell in log phase SD medium. Ref.11
Sequence similarities	Belongs to the 5'-AMP-activated protein kinase beta subunit family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cellular response to glucose starvation Inferred from mutant phenotype. Source: SGD invasive growth in response to glucose limitation Inferred from genetic interaction. Source: SGD protein amino acid phosphorylation Ref.7 Inferred from genetic interaction. Source: SGD regulation of protein complex assembly Ref.6 Inferred from genetic interaction. Source: SGD replicative cell aging Ref.10 Inferred from mutant phenotype. Source: SGD signal transduction Ref.7 Inferred from genetic interaction. Source: SGD
Cellular component	AMP-activated protein kinase complex Ref.2 Ref.6 Ref.9 Inferred from direct assay. Source: SGD cytoplasm Ref.8 Inferred from direct assay. Source: SGD plasma membrane Ref.10 Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P43582	1	EBI-17187,EBI-22766
ESS1	P22696	1	EBI-17187,EBI-6679
PRP40	P33203	1	EBI-17187,EBI-701
RSP5	P39940	1	EBI-17187,EBI-16219
SET2	P46995	1	EBI-17187,EBI-16985
SNF4	P12904	1	EBI-17187,EBI-17537
URN1	Q06525	1	EBI-17187,EBI-35138

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 415

414

SNF1 protein kinase subunit beta-2

PRO_0000204375

Regions

Region

154 – 335

182

Kinase-interacting sequence (KIS); required for interaction with SNF1

Region

336 – 415

80

Association with SNF1 kinase complex (ASC) domain; required for interaction with SNF4

Amino acid modifications

Modified residue

49

1

Phosphothreonine Ref.13

Modified residue

52

1

Phosphoserine Ref.13

Modified residue

66

1

Phosphoserine Ref.14

Modified residue

72

1

Phosphothreonine Ref.14

Modified residue

76

1

Phosphoserine Ref.12

Modified residue

77

1

Phosphothreonine Ref.12

Modified residue

133

1

Phosphoserine Ref.13

Modified residue

137

1

Phosphoserine Ref.13

Lipidation

2

1

N-myristoyl glycine

Experimental info

Mutagenesis

2

1

G → A: Changes protein distribution from the plasma membrane to the cytoplasm and nucleus and alters the cellular life span.

Secondary structure

1

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415

Helix Strand Turn

Details...

Beta strand

164 – 170

7

Beta strand

177 – 181

5

Helix

182 – 184

3

Beta strand

196 – 198

3

Beta strand

202 – 208

7

Beta strand

210 – 219

10

Beta strand

222 – 224

3

Beta strand

231 – 233

3

Beta strand

240 – 245

6

Helix

311 – 313

3

Helix

316 – 326

11

Beta strand

388 – 399

12

Beta strand

402 – 411

10

Sequences

	Sequence		Length	Mass (Da)
	P34164-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CBB4FCE0070A563F	FASTA	415	46,405
	10 20 30 40 50 60 MGTTTSHPAQ KKQTTKKCRA PIMSDVREKP SNAQGCEPQE MDAVSKKVTE LSLNKCSDSQ 70 80 90 100 110 120 DAGQPSREGS ITKKKSTLLL RDEDEPTMPK LSVMETAVDT DSGSSSTSDD EEGDIIAQTT 130 140 150 160 170 180 EPKQDASPDD DRSGHSSPRE EGQQQIRAKE ASGGPSEIKS SLMVPVEIRW QQGGSKVYVT 190 200 210 220 230 240 GSFTKWRKMI GLIPDSDNNG SFHVKLRLLP GTHRFRFIVD NELRVSDFLP TATDQMGNFV 250 260 270 280 290 300 NYIEVRQPEK NPTNEKIRSK EADSMRPPTS DRSSIALQIG KDPDDFGDGY TRFHEDLSPR 310 320 330 340 350 360 PPLEYTTDIP AVFTDPSVME RYYYTLDRQQ SNTDTSWLTP PQLPPQLENV ILNKYYATQD 370 380 390 400 410 QFNENNSGAL PIPNHVVLNH LVTSSIKHNT LCVASIVRYK QKYVTQILYT PIESS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Suppressors of yeast RNA polymerase II mutations belong to a family of gene products that interact with a protein kinase." Drebot M.A., Jansma D., Himmelfarb H.J., Friesen J.D. Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex." Yang X., Jiang R., Carlson M. EMBO J. 13:5878-5886(1994) [PubMed: 7813428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH SNF1, PHOSPHORYLATION. Strain: ATCC 204508 / S288c.
[3]	"Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII reveals 11 open reading frames: two correspond to new genes." Feuermann M., Simeonava L., Souciet J.-L., Potier S. Yeast 13:475-477(1997) [PubMed: 9153757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." 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. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and containing three novel transcribed open reading frames." Kail M., Juettner E., Vaux D. Yeast 12:799-807(1996) [PubMed: 8813766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-284. Strain: ATCC 204508 / S288c.
[6]	"The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex." Jiang R., Carlson M. Mol. Cell. Biol. 17:2099-2106(1997) [PubMed: 9121458] [Abstract] Cited for: INTERACTION WITH SNF1 AND SNF4.
[7]	"beta-subunits of Snf1 kinase are required for kinase function and substrate definition." Schmidt M.C., McCartney R.R. EMBO J. 19:4936-4943(2000) [PubMed: 10990457] [Abstract] Cited for: FUNCTION.
[8]	"Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism." Vincent O., Townley R., Kuchin S., Carlson M. Genes Dev. 15:1104-1114(2001) [PubMed: 11331606] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[9]	"Purification and characterization of Snf1 kinase complexes containing a defined beta subunit composition." Nath N., McCartney R.R., Schmidt M.C. J. Biol. Chem. 277:50403-50408(2002) [PubMed: 12393914] [Abstract] Cited for: IDENTIFICATION IN SNF1 KINASE COMPLEX.
[10]	"Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination at rDNA loci, and silencing." Lin S.S., Manchester J.K., Gordon J.I. J. Biol. Chem. 278:13390-13397(2003) [PubMed: 12562756] [Abstract] Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
[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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND THR-77, MASS SPECTROMETRY.
[13]	"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 THR-49; SER-52; SER-133 AND SER-137, MASS SPECTROMETRY.
[14]	"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 SER-66 AND THR-72, MASS SPECTROMETRY.
[15]	"Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1." Amodeo G.A., Rudolph M.J., Tong L. Nature 449:492-495(2007) [PubMed: 17851534] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 161-412 IN COMPLEX WITH SNF1 AND SNF4.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z14128 Genomic DNA. Translation: CAA78503.1.
L31592 Genomic DNA. Translation: AAC37420.1.
Z72730 Genomic DNA. Translation: CAA96922.1.
U33754 Genomic DNA. Translation: AAC49497.1.

PIR

S51792.

RefSeq

NP_011307.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QLV	X-ray	2.60	B/E	161-412	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:865N.

IntAct

P34164. 19 interactions.

Protein family/group databases

CAZy

CBM48. Carbohydrate-Binding Module Family 48.

Proteomic databases

PeptideAtlas

P34164.

PRIDE

P34164.

Genome annotation databases

Ensembl

YGL208W. Saccharomyces cerevisiae. [Contig view]

GeneID

852664.

GenomeReviews

Gene locus YGL208W in contig Y13135_GR.

KEGG

sce:YGL208W.

NMPDR

fig|4932.3.peg.2410.

Organism-specific databases

CYGD

YGL208w.

SGD

S000003176. SIP2.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P34164.

Gene expression databases

GermOnline

YGL208W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006828. AMPKBI.
[Graphical view]

Pfam

PF04739. AMPKBI. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

971954.

Entry information

Entry name

SIP2_YEAST

Accession

Primary (citable) accession number: P34164

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)