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P34164 (SIP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 113. 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:
SNF1 protein kinase subunit beta-2
Alternative name(s):
Protein SPM2
SNF1-interacting protein 2
Gene names
Name:SIP2
Synonyms:SPM2
Ordered Locus Names:YGL208W
ORF Names:G1155
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.8 Ref.11

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. Ref.2 Ref.7 Ref.10

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. Ref.9 Ref.11

Induction

Induced upon shift to nonfermentable carbon sources. Ref.9

Post-translational modification

Phosphorylated by SNF1 in vitro. Ref.2

Miscellaneous

Present with 300 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the 5'-AMP-activated protein kinase beta subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNF1P067829EBI-17187,EBI-17516
SNF4P129046EBI-17187,EBI-17537

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 415414SNF1 protein kinase subunit beta-2
PRO_0000204375

Regions

Region154 – 335182Kinase-interacting sequence (KIS); required for interaction with SNF1
Region336 – 41580Association with SNF1 kinase complex (ASC) domain; required for interaction with SNF4

Amino acid modifications

Modified residue661Phosphoserine Ref.14
Modified residue2981Phosphoserine Ref.14
Lipidation21N-myristoyl glycine Ref.11

Experimental info

Mutagenesis21G → A: Changes protein distribution from the plasma membrane to the cytoplasm and nucleus and alters the cellular life span. Ref.11

Secondary structure

...................................... 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P34164 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CBB4FCE0070A563F

FASTA41546,405
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-284.
Strain: ATCC 204508 / S288c.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNF1 AND SNF4.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INDUCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN SNF1 KINASE COMPLEX.
[11]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2.
[12]"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].
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-66 AND SER-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 161-412 IN COMPLEX WITH SNF1 AND SNF4.
[16]"ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated protein kinase."
Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D., McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A., Haire L.F., Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., Carling D.
Cell Metab. 14:707-714(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 304-415 IN COMPLEX WITH SNF1 AND SNF4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z14128 Genomic DNA. Translation: CAA78503.1.
L31592 Genomic DNA. Translation: AAC37420.1.
Z72730 Genomic DNA. Translation: CAA96922.1.
U33754 Genomic DNA. Translation: AAC49497.1.
BK006941 Genomic DNA. Translation: DAA07908.1.
PIRS51792.
RefSeqNP_011307.1. NM_001181073.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QLVX-ray2.60B/E161-412[»]
3T4NX-ray2.30B304-415[»]
3TDHX-ray2.30B304-415[»]
3TE5X-ray2.50B304-415[»]
ProteinModelPortalP34164.
SMRP34164. Positions 161-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33048. 40 interactions.
DIPDIP-865N.
IntActP34164. 15 interactions.
MINTMINT-404843.
STRING4932.YGL208W.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.

Proteomic databases

PaxDbP34164.
PeptideAtlasP34164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL208W; YGL208W; YGL208W.
GeneID852664.
KEGGsce:YGL208W.

Organism-specific databases

SGDS000003176. SIP2.

Phylogenomic databases

eggNOGNOG238368.
GeneTreeENSGT00390000001416.
HOGENOMHOG000093748.
OrthoDBEOG7BS4NQ.

Enzyme and pathway databases

BioCycYEAST:G3O-30685-MONOMER.

Gene expression databases

GenevestigatorP34164.

Family and domain databases

InterProIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP34164.
NextBio971954.

Entry information

Entry nameSIP2_YEAST
AccessionPrimary (citable) accession number: P34164
Secondary accession number(s): D6VTU7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references