| Tag |
Content |
LipidDB ID |
LipidDB-559292-00215 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
5.44 |
Molecular Weight |
46404.65 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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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 |
01-FEB-1994 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGTTTSHPA | [1] | N-Myristoylation |
|
Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID |
559292 |
Reference |
[1] Lin SS, Manchester JK, Gordon JI. Sip2, an N-myristoylated beta subunit ofSnf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellularhistone kinase activity, recombination at rDNA loci, and silencing. J Biol Chem. 2003 Apr 11;278(15):13390-7. Epub 2003 Jan 31.[ PMID:12562756]
|
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);required for interaction with SNF1.
Region: 336 415 Association with SNF1 kinase complex(ASC) domain; required for interactionwith SNF4.
Modified residue: 66 66 Phosphoserine.
Modified residue: 298 298 Phosphoserine.
|
Protein Length |
415 AA. |
Protein Sequence
(Canonical) |
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
|
FASTA
(Canonical) |
>LipidDB-559292-00215|P34164
MGTTTSHPAQKKQTTKKCRAPIMSDVREKPSNAQGCEPQEMDAVSKKVTELSLNKCSDSQ
DAGQPSREGSITKKKSTLLLRDEDEPTMPKLSVMETAVDTDSGSSSTSDDEEGDIIAQTT
EPKQDASPDDDRSGHSSPREEGQQQIRAKEASGGPSEIKSSLMVPVEIRWQQGGSKVYVT
GSFTKWRKMIGLIPDSDNNGSFHVKLRLLPGTHRFRFIVDNELRVSDFLPTATDQMGNFV
NYIEVRQPEKNPTNEKIRSKEADSMRPPTSDRSSIALQIGKDPDDFGDGYTRFHEDLSPR
PPLEYTTDIPAVFTDPSVMERYYYTLDRQQSNTDTSWLTPPQLPPQLENVILNKYYATQD
QFNENNSGALPIPNHVVLNHLVTSSIKHNTLCVASIVRYKQKYVTQILYTPIESS
|
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 |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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