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P34164

- SIP2_YEAST

UniProt

P34164 - SIP2_YEAST

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Protein
SNF1 protein kinase subunit beta-2
Gene
SIP2, SPM2, YGL208W, G1155
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. cellular response to glucose starvation Source: SGD
  2. invasive growth in response to glucose limitation Source: SGD
  3. protein phosphorylation Source: SGD
  4. regulation of protein complex assembly Source: SGD
  5. replicative cell aging Source: SGD
  6. signal transduction Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30685-MONOMER.
ReactomeiREACT_209479. Regulation of AMPK activity via LKB1.
REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
SNF1 protein kinase subunit beta-2
Alternative name(s):
Protein SPM2
SNF1-interacting protein 2
Gene namesi
Name:SIP2
Synonyms:SPM2
Ordered Locus Names:YGL208W
ORF Names:G1155
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003176. SIP2.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: SGD
  2. cytoplasm Source: SGD
  3. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21G → A: Changes protein distribution from the plasma membrane to the cytoplasm and nucleus and alters the cellular life span. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 415414SNF1 protein kinase subunit beta-2
PRO_0000204375Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei66 – 661Phosphoserine1 Publication
Modified residuei298 – 2981Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by SNF1 in vitro.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP34164.
PaxDbiP34164.
PeptideAtlasiP34164.

Expressioni

Inductioni

Induced upon shift to nonfermentable carbon sources.1 Publication

Gene expression databases

GenevestigatoriP34164.

Interactioni

Subunit structurei

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 SNF4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNF1P067829EBI-17187,EBI-17516
SNF4P129046EBI-17187,EBI-17537

Protein-protein interaction databases

BioGridi33048. 40 interactions.
DIPiDIP-865N.
IntActiP34164. 15 interactions.
MINTiMINT-404843.
STRINGi4932.YGL208W.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi164 – 1707
Beta strandi177 – 1815
Helixi182 – 1843
Beta strandi196 – 1983
Beta strandi202 – 2087
Beta strandi210 – 21910
Beta strandi222 – 2243
Beta strandi231 – 2333
Beta strandi240 – 2456
Beta strandi305 – 3073
Helixi311 – 3133
Helixi316 – 3249
Helixi336 – 3383
Helixi345 – 3473
Helixi349 – 36517
Helixi375 – 3773
Beta strandi380 – 3834
Beta strandi390 – 39910
Beta strandi402 – 41110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QLVX-ray2.60B/E161-412[»]
3T4NX-ray2.30B304-415[»]
3TDHX-ray2.30B304-415[»]
3TE5X-ray2.50B304-415[»]
ProteinModelPortaliP34164.
SMRiP34164. Positions 161-413.

Miscellaneous databases

EvolutionaryTraceiP34164.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 335182Kinase-interacting sequence (KIS); required for interaction with SNF1
Add
BLAST
Regioni336 – 41580Association with SNF1 kinase complex (ASC) domain; required for interaction with SNF4
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG238368.
GeneTreeiENSGT00390000001416.
HOGENOMiHOG000093748.
OrthoDBiEOG7BS4NQ.

Family and domain databases

InterProiIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTiSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34164-1 [UniParc]FASTAAdd to Basket

« Hide

MGTTTSHPAQ KKQTTKKCRA PIMSDVREKP SNAQGCEPQE MDAVSKKVTE    50
LSLNKCSDSQ DAGQPSREGS ITKKKSTLLL RDEDEPTMPK LSVMETAVDT 100
DSGSSSTSDD EEGDIIAQTT EPKQDASPDD DRSGHSSPRE EGQQQIRAKE 150
ASGGPSEIKS SLMVPVEIRW QQGGSKVYVT GSFTKWRKMI GLIPDSDNNG 200
SFHVKLRLLP GTHRFRFIVD NELRVSDFLP TATDQMGNFV NYIEVRQPEK 250
NPTNEKIRSK EADSMRPPTS DRSSIALQIG KDPDDFGDGY TRFHEDLSPR 300
PPLEYTTDIP AVFTDPSVME RYYYTLDRQQ SNTDTSWLTP PQLPPQLENV 350
ILNKYYATQD QFNENNSGAL PIPNHVVLNH LVTSSIKHNT LCVASIVRYK 400
QKYVTQILYT PIESS 415
Length:415
Mass (Da):46,405
Last modified:January 23, 2007 - v3
Checksum:iCBB4FCE0070A563F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS51792.
RefSeqiNP_011307.1. NM_001181073.2.

Genome annotation databases

EnsemblFungiiYGL208W; YGL208W; YGL208W.
GeneIDi852664.
KEGGisce:YGL208W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S51792.
RefSeqi NP_011307.1. NM_001181073.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QLV X-ray 2.60 B/E 161-412 [» ]
3T4N X-ray 2.30 B 304-415 [» ]
3TDH X-ray 2.30 B 304-415 [» ]
3TE5 X-ray 2.50 B 304-415 [» ]
ProteinModelPortali P34164.
SMRi P34164. Positions 161-413.
ModBasei Search...

Protein-protein interaction databases

BioGridi 33048. 40 interactions.
DIPi DIP-865N.
IntActi P34164. 15 interactions.
MINTi MINT-404843.
STRINGi 4932.YGL208W.

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.

Proteomic databases

MaxQBi P34164.
PaxDbi P34164.
PeptideAtlasi P34164.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL208W ; YGL208W ; YGL208W .
GeneIDi 852664.
KEGGi sce:YGL208W.

Organism-specific databases

SGDi S000003176. SIP2.

Phylogenomic databases

eggNOGi NOG238368.
GeneTreei ENSGT00390000001416.
HOGENOMi HOG000093748.
OrthoDBi EOG7BS4NQ.

Enzyme and pathway databases

BioCyci YEAST:G3O-30685-MONOMER.
Reactomei REACT_209479. Regulation of AMPK activity via LKB1.
REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

Miscellaneous databases

EvolutionaryTracei P34164.
NextBioi 971954.

Gene expression databases

Genevestigatori P34164.

Family and domain databases

InterProi IPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF04739. AMPKBI. 1 hit.
[Graphical view ]
SMARTi SM01010. AMPKBI. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 304-415 IN COMPLEX WITH SNF1 AND SNF4.

Entry informationi

Entry nameiSIP2_YEAST
AccessioniPrimary (citable) accession number: P34164
Secondary accession number(s): D6VTU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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