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Protein

5'-AMP-activated protein kinase subunit gamma

Gene

cbs2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411Adenine nucleotides
Binding sitei163 – 1631Adenine nucleotides
Binding sitei191 – 1911Adenine nucleotides
Binding sitei196 – 1961Adenine nucleotides; via amide nitrogen and carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 2184Adenine nucleotides
Nucleotide bindingi289 – 2902Adenine nucleotides
Nucleotide bindingi305 – 3084Adenine nucleotides

GO - Molecular functioni

  • AMP binding Source: PomBase
  • ATP binding Source: PomBase
  • catalytic activity Source: InterPro
  • protein kinase activator activity Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SPO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SPO-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma
Short name:
AMPK gamma
Short name:
AMPK subunit gamma
Gene namesi
Name:cbs2
ORF Names:SPAC1556.08c, SPAC1F12.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.08c.
PomBaseiSPAC1556.08c. cbs2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleotide-activated protein kinase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3343345'-AMP-activated protein kinase subunit gammaPRO_0000204390Add
BLAST

Proteomic databases

MaxQBiQ10343.

PTM databases

SwissPalmiQ10343.

Interactioni

Subunit structurei

AMPK is a heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits.By similarity

Protein-protein interaction databases

BioGridi858067. 26 interactions.
DIPiDIP-29522N.
IntActiQ10343. 1 interaction.
MINTiMINT-4698961.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2118Combined sources
Helixi24 – 274Combined sources
Beta strandi30 – 389Combined sources
Helixi43 – 5311Combined sources
Beta strandi58 – 625Combined sources
Turni63 – 664Combined sources
Beta strandi67 – 726Combined sources
Helixi74 – 8714Combined sources
Helixi91 – 988Combined sources
Helixi102 – 11110Combined sources
Helixi128 – 13710Combined sources
Beta strandi141 – 1488Combined sources
Turni150 – 1523Combined sources
Beta strandi155 – 1628Combined sources
Helixi163 – 17311Combined sources
Helixi175 – 1795Combined sources
Helixi184 – 1863Combined sources
Helixi204 – 21411Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi227 – 2337Combined sources
Helixi235 – 2417Combined sources
Helixi242 – 2443Combined sources
Helixi246 – 2505Combined sources
Helixi253 – 2575Combined sources
Beta strandi269 – 2713Combined sources
Helixi276 – 28510Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi299 – 3057Combined sources
Helixi306 – 3149Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi329 – 3313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOXX-ray2.60E/G3-334[»]
2OOYX-ray2.88E/G3-334[»]
2QR1X-ray2.70E/G3-334[»]
2QRCX-ray2.70E/G3-334[»]
2QRDX-ray2.41E/G3-334[»]
2QREX-ray3.01E/G3-334[»]
ProteinModelPortaliQ10343.
SMRiQ10343. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 8961CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini115 – 17763CBS 2PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 24761CBS 3PROSITE-ProRule annotationAdd
BLAST
Domaini262 – 31958CBS 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

HOGENOMiHOG000176880.
InParanoidiQ10343.
OMAiNCKETAM.
OrthoDBiEOG092C39BT.
PhylomeDBiQ10343.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDVQETQKG ALKEIQAFIR SRTSYDVLPT SFRLIVFDVT LFVKTSLSLL
60 70 80 90 100
TLNNIVSAPL WDSEANKFAG LLTMADFVNV IKYYYQSSSF PEAIAEIDKF
110 120 130 140 150
RLLGLREVER KIGAIPPETI YVHPMHSLMD ACLAMSKSRA RRIPLIDVDG
160 170 180 190 200
ETGSEMIVSV LTQYRILKFI SMNCKETAML RVPLNQMTIG TWSNLATASM
210 220 230 240 250
ETKVYDVIKM LAEKNISAVP IVNSEGTLLN VYESVDVMHL IQDGDYSNLD
260 270 280 290 300
LSVGEALLKR PANFDGVHTC RATDRLDGIF DAIKHSRVHR LFVVDENLKL
310 320 330
EGILSLADIL NYIIYDKTTT PGVPEQTDNF ESAV
Length:334
Mass (Da):37,427
Last modified:August 14, 2001 - v2
Checksum:i8D32CC6CE53F7916
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB61219.1.
PIRiT38059. S67444.
T50087.
RefSeqiXP_001713093.1. XM_001713041.2.

Genome annotation databases

EnsemblFungiiSPAC1556.08c.1; SPAC1556.08c.1:pep; SPAC1556.08c.
GeneIDi5802929.
KEGGispo:SPAC1556.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB61219.1.
PIRiT38059. S67444.
T50087.
RefSeqiXP_001713093.1. XM_001713041.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOXX-ray2.60E/G3-334[»]
2OOYX-ray2.88E/G3-334[»]
2QR1X-ray2.70E/G3-334[»]
2QRCX-ray2.70E/G3-334[»]
2QRDX-ray2.41E/G3-334[»]
2QREX-ray3.01E/G3-334[»]
ProteinModelPortaliQ10343.
SMRiQ10343. Positions 3-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi858067. 26 interactions.
DIPiDIP-29522N.
IntActiQ10343. 1 interaction.
MINTiMINT-4698961.

PTM databases

SwissPalmiQ10343.

Proteomic databases

MaxQBiQ10343.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1556.08c.1; SPAC1556.08c.1:pep; SPAC1556.08c.
GeneIDi5802929.
KEGGispo:SPAC1556.08c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.08c.
PomBaseiSPAC1556.08c. cbs2.

Phylogenomic databases

HOGENOMiHOG000176880.
InParanoidiQ10343.
OMAiNCKETAM.
OrthoDBiEOG092C39BT.
PhylomeDBiQ10343.

Enzyme and pathway databases

ReactomeiR-SPO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SPO-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SPO-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Miscellaneous databases

EvolutionaryTraceiQ10343.
PROiQ10343.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 2 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAKG_SCHPO
AccessioniPrimary (citable) accession number: Q10343
Secondary accession number(s): Q9UTJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 14, 2001
Last modified: September 7, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.