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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)DescriptionActionsGraphical viewLength
Binding sitei141Adenine nucleotides1
Binding sitei163Adenine nucleotides1
Binding sitei191Adenine nucleotides1
Binding sitei196Adenine nucleotides; via amide nitrogen and carbonyl oxygen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi215 – 218Adenine nucleotides4
Nucleotide bindingi289 – 290Adenine nucleotides2
Nucleotide bindingi305 – 308Adenine nucleotides4

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002043901 – 3345'-AMP-activated protein kinase subunit gammaAdd BLAST334

Proteomic databases

MaxQBiQ10343.
PRIDEiQ10343.

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 interactors.
DIPiDIP-29522N.
IntActiQ10343. 1 interactor.
MINTiMINT-4698961.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 21Combined sources18
Helixi24 – 27Combined sources4
Beta strandi30 – 38Combined sources9
Helixi43 – 53Combined sources11
Beta strandi58 – 62Combined sources5
Turni63 – 66Combined sources4
Beta strandi67 – 72Combined sources6
Helixi74 – 87Combined sources14
Helixi91 – 98Combined sources8
Helixi102 – 111Combined sources10
Helixi128 – 137Combined sources10
Beta strandi141 – 148Combined sources8
Turni150 – 152Combined sources3
Beta strandi155 – 162Combined sources8
Helixi163 – 173Combined sources11
Helixi175 – 179Combined sources5
Helixi184 – 186Combined sources3
Helixi204 – 214Combined sources11
Beta strandi217 – 222Combined sources6
Beta strandi227 – 233Combined sources7
Helixi235 – 241Combined sources7
Helixi242 – 244Combined sources3
Helixi246 – 250Combined sources5
Helixi253 – 257Combined sources5
Beta strandi269 – 271Combined sources3
Helixi276 – 285Combined sources10
Beta strandi290 – 294Combined sources5
Beta strandi299 – 305Combined sources7
Helixi306 – 314Combined sources9
Beta strandi317 – 320Combined sources4
Beta strandi329 – 331Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10343.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 89CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini115 – 177CBS 2PROSITE-ProRule annotationAdd BLAST63
Domaini187 – 247CBS 3PROSITE-ProRule annotationAdd BLAST61
Domaini262 – 319CBS 4PROSITE-ProRule annotationAdd BLAST58

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi858067. 26 interactors.
DIPiDIP-29522N.
IntActiQ10343. 1 interactor.
MINTiMINT-4698961.

PTM databases

SwissPalmiQ10343.

Proteomic databases

MaxQBiQ10343.
PRIDEiQ10343.

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: November 30, 2016
This is version 104 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.