CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006367
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SNF1 protein kinase subunit beta-2 
Protein Synonyms/Alias
 Protein SPM2; SNF1-interacting protein 2 
Gene Name
 SIP2 
Gene Synonyms/Alias
 SPM2; YGL208W; G1155 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
12TSHPAQKKQTTKKCRacetylation[1]
16AQKKQTTKKCRAPIMacetylation[1]
17QKKQTTKKCRAPIMSacetylation[1]
29IMSDVREKPSNAQGCubiquitination[2]
55VTELSLNKCSDSQDAubiquitination[2]
256EKNPTNEKIRSKEADacetylation[1]
Reference
 [1] Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction.
 Lu JY, Lin YY, Sheu JC, Wu JT, Lee FJ, Chen Y, Lin MI, Chiang FT, Tai TY, Berger SL, Zhao Y, Tsai KS, Zhu H, Chuang LM, Boeke JD.
 Cell. 2011 Sep 16;146(6):969-79. [PMID: 21906795]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 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. 
Sequence Annotation
 REGION 154 335 Kinase-interacting sequence (KIS);
 REGION 336 415 Association with SNF1 kinase complex
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 3D-structure; Cell membrane; Complete proteome; Cytoplasm; Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 415 AA 
Protein Sequence
MGTTTSHPAQ KKQTTKKCRA PIMSDVREKP SNAQGCEPQE MDAVSKKVTE LSLNKCSDSQ 60
DAGQPSREGS ITKKKSTLLL RDEDEPTMPK LSVMETAVDT DSGSSSTSDD EEGDIIAQTT 120
EPKQDASPDD DRSGHSSPRE EGQQQIRAKE ASGGPSEIKS SLMVPVEIRW QQGGSKVYVT 180
GSFTKWRKMI GLIPDSDNNG SFHVKLRLLP GTHRFRFIVD NELRVSDFLP TATDQMGNFV 240
NYIEVRQPEK NPTNEKIRSK EADSMRPPTS DRSSIALQIG KDPDDFGDGY TRFHEDLSPR 300
PPLEYTTDIP AVFTDPSVME RYYYTLDRQQ SNTDTSWLTP PQLPPQLENV ILNKYYATQD 360
QFNENNSGAL PIPNHVVLNH LVTSSIKHNT LCVASIVRYK QKYVTQILYT PIESS 415 
Gene Ontology
 GO:0031588; C:AMP-activated protein kinase complex; IDA:SGD.
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
 GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
 GO:0006468; P:protein phosphorylation; IGI:SGD.
 GO:0043254; P:regulation of protein complex assembly; IGI:SGD.
 GO:0001302; P:replicative cell aging; IMP:SGD.
 GO:0007165; P:signal transduction; IGI:SGD. 
Interpro
 IPR006828; AMP_prot_kin_bsu_interact-dom. 
Pfam
 PF04739; AMPKBI 
SMART
 SM01010; AMPKBI 
PROSITE
  
PRINTS