Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

5'-AMP-activated protein kinase subunit gamma-2

Gene

PRKAG2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei302AMP 1By similarity1
Binding sitei302ATP 1By similarity1
Binding sitei383AMP 2By similarity1
Binding sitei383AMP 3By similarity1
Binding sitei383ATP 2By similarity1
Binding sitei384ATP 1By similarity1
Binding sitei384ATP 2By similarity1
Binding sitei402AMP 1By similarity1
Binding sitei402ATP 1By similarity1
Binding sitei530AMP 3By similarity1
Binding sitei531AMP 1By similarity1
Binding sitei531ATP 1By similarity1

GO - Molecular functioni

  • ADP binding Source: BHF-UCL
  • AMP-activated protein kinase activity Source: Ensembl
  • AMP binding Source: Ensembl
  • ATP binding Source: BHF-UCL
  • cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  • cAMP-dependent protein kinase regulator activity Source: BHF-UCL
  • phosphorylase kinase regulator activity Source: BHF-UCL
  • protein kinase activator activity Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL

GO - Biological processi

  • ATP biosynthetic process Source: BHF-UCL
  • carnitine shuttle Source: Reactome
  • cell cycle arrest Source: Reactome
  • fatty acid biosynthetic process Source: UniProtKB-KW
  • glycogen metabolic process Source: BHF-UCL
  • intracellular signal transduction Source: BHF-UCL
  • macroautophagy Source: Reactome
  • negative regulation of protein kinase activity Source: BHF-UCL
  • positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of protein kinase activity Source: BHF-UCL
  • regulation of fatty acid biosynthetic process Source: Reactome
  • regulation of fatty acid metabolic process Source: BHF-UCL
  • regulation of fatty acid oxidation Source: BHF-UCL
  • regulation of glucose import Source: BHF-UCL
  • regulation of glycolytic process Source: BHF-UCL
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • sterol biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106617-MONOMER.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1632852. Macroautophagy.
R-HSA-163680. AMPK inhibits chREBP transcriptional activation activity.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2151209. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ9UGJ0.
SIGNORiQ9UGJ0.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-2
Short name:
AMPK gamma2
Short name:
AMPK subunit gamma-2
Alternative name(s):
H91620p
Gene namesi
Name:PRKAG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9386. PRKAG2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular space Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Wolff-Parkinson-White syndrome (WPWS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA supernormal conduction disorder characterized by the presence of one or several accessory atrioventricular connections, which can lead to episodes of sporadic tachycardia.
See also OMIM:194200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013264302R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 3 PublicationsCorresponds to variant rs121908987dbSNPEnsembl.1
Natural variantiVAR_032909531R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs121908990dbSNPEnsembl.1
Cardiomyopathy, familial hypertrophic 6 (CMH6)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. CMH6 patients present Wolff-Parkinson-White ventricular preexcitation, enlarged myocytes without myofiber disarray, and glycogen-containing cytosolic vacuoles within cardiomyocytes.
See also OMIM:600858
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013264302R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 3 PublicationsCorresponds to variant rs121908987dbSNPEnsembl.1
Natural variantiVAR_013265350R → RL in CMH6; severe. 1 Publication1
Natural variantiVAR_013266383H → R in CMH6; severe; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs121908988dbSNPEnsembl.1
Natural variantiVAR_013267400T → N in CMH6; severe; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs28938173dbSNPEnsembl.1
Natural variantiVAR_013268488N → I in CMH6; severe. 1 PublicationCorresponds to variant rs121908989dbSNPEnsembl.1
Glycogen storage disease of heart lethal congenital (GSDH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare disease which leads to death within a few weeks to a few months after birth, through heart failure and respiratory compromise.
See also OMIM:261740
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013269531R → Q in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit. 1 PublicationCorresponds to variant rs121908991dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi387V → S: Induces phosphorylation by AMPK. 1 Publication1

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Glycogen storage disease

Organism-specific databases

DisGeNETi51422.
MalaCardsiPRKAG2.
MIMi194200. phenotype.
261740. phenotype.
600858. phenotype.
OpenTargetsiENSG00000106617.
Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
907. Wolff-Parkinson-White syndrome.
PharmGKBiPA33752.

Chemistry databases

ChEMBLiCHEMBL3038451.
DrugBankiDB00945. Acetylsalicylic acid.

Polymorphism and mutation databases

BioMutaiPRKAG2.
DMDMi14285344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043811 – 5695'-AMP-activated protein kinase subunit gamma-2Add BLAST569

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei65PhosphoserineBy similarity1
Modified residuei71PhosphoserineCombined sources1
Modified residuei73PhosphoserineBy similarity1
Modified residuei90PhosphoserineBy similarity1
Modified residuei138PhosphoserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei161PhosphoserineBy similarity1
Modified residuei162PhosphoserineBy similarity1
Modified residuei165PhosphothreonineBy similarity1
Modified residuei196PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9UGJ0.
PeptideAtlasiQ9UGJ0.
PRIDEiQ9UGJ0.

PTM databases

iPTMnetiQ9UGJ0.
PhosphoSitePlusiQ9UGJ0.

Expressioni

Tissue specificityi

Isoform B is ubiquitously expressed except in liver and thymus. The highest level is detected in heart with abundant expression in placenta and testis.

Gene expression databases

BgeeiENSG00000106617.
CleanExiHS_PRKAG2.
ExpressionAtlasiQ9UGJ0. baseline and differential.
GenevisibleiQ9UGJ0. HS.

Organism-specific databases

HPAiCAB018641.
HPA004246.

Interactioni

Subunit structurei

AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.

GO - Molecular functioni

  • protein kinase binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi119531. 24 interactors.
IntActiQ9UGJ0. 15 interactors.
MINTiMINT-4831646.
STRINGi9606.ENSP00000287878.

Structurei

3D structure databases

ProteinModelPortaliQ9UGJ0.
SMRiQ9UGJ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini275 – 335CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini357 – 415CBS 2PROSITE-ProRule annotationAdd BLAST59
Domaini430 – 492CBS 3PROSITE-ProRule annotationAdd BLAST63
Domaini504 – 562CBS 4PROSITE-ProRule annotationAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi370 – 391AMPK pseudosubstrateAdd BLAST22

Domaini

The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1.
The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP.

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
GeneTreeiENSGT00390000009849.
HOVERGENiHBG050431.
KOiK07200.
OMAiXVQIYEL.
OrthoDBiEOG091G0CZV.
PhylomeDBiQ9UGJ0.
TreeFamiTF313247.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q9UGJ0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG
60 70 80 90 100
DLEGSGKHSS RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG
110 120 130 140 150
SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP ATSPGGIRFF
160 170 180 190 200
SRSRKTSGLS SSPSTPTQVT KQHTFPLESY KHEPERLENR IYASSSPPDT
210 220 230 240 250
GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA GMLEKLEFED
260 270 280 290 300
EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG
310 320 330 340 350
VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR
360 370 380 390 400
ELYLQETFKP LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT
410 420 430 440 450
HKRILKFLQL FMSDMPKPAF MKQNLDELGI GTYHNIAFIH PDTPIIKALN
460 470 480 490 500
IFVERRISAL PVVDESGKVV DIYSKFDVIN LAAEKTYNNL DITVTQALQH
510 520 530 540 550
RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS IVGIISLSDI
560
LQALILTPAG AKQKETETE
Length:569
Mass (Da):63,066
Last modified:May 1, 2000 - v1
Checksum:iF51C30668C294089
GO
Isoform B (identifier: Q9UGJ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-241: Missing.

Show »
Length:328
Mass (Da):37,509
Checksum:iD8402E96E46DB5A5
GO
Isoform C (identifier: Q9UGJ0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Show »
Length:525
Mass (Da):58,439
Checksum:i873DEE12F27F133D
GO

Sequence cautioni

The sequence AAH20540 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAS02032 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAA84695 differs from that shown. Reason: Frameshift at positions 228 and 233. Frameshifts are upstream of the initiating Met of isoform B.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0482506M → L.Corresponds to variant rs3207363dbSNPEnsembl.1
Natural variantiVAR_013264302R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 3 PublicationsCorresponds to variant rs121908987dbSNPEnsembl.1
Natural variantiVAR_013265350R → RL in CMH6; severe. 1 Publication1
Natural variantiVAR_013266383H → R in CMH6; severe; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs121908988dbSNPEnsembl.1
Natural variantiVAR_013267400T → N in CMH6; severe; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs28938173dbSNPEnsembl.1
Natural variantiVAR_013268488N → I in CMH6; severe. 1 PublicationCorresponds to variant rs121908989dbSNPEnsembl.1
Natural variantiVAR_032909531R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. 2 PublicationsCorresponds to variant rs121908990dbSNPEnsembl.1
Natural variantiVAR_013269531R → Q in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit. 1 PublicationCorresponds to variant rs121908991dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0002611 – 241Missing in isoform B. 5 PublicationsAdd BLAST241
Alternative sequenceiVSP_0155891 – 44Missing in isoform C. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025580 mRNA. Translation: BAA84695.1. Frameshift.
AJ249976 mRNA. Translation: CAB65116.1.
AF087875 mRNA. Translation: AAK00413.1.
AK001887 mRNA. Translation: BAA91962.1.
BT007127 mRNA. Translation: AAP35791.1.
AC006358 Genomic DNA. Translation: AAS02032.1. Sequence problems.
AC006966 Genomic DNA. Translation: AAF03528.2.
AC093583 Genomic DNA. No translation available.
BC020540 mRNA. Translation: AAH20540.2. Different initiation.
BC068598 mRNA. Translation: AAH68598.1.
CCDSiCCDS43683.1. [Q9UGJ0-3]
CCDS47752.1. [Q9UGJ0-2]
CCDS5928.1. [Q9UGJ0-1]
RefSeqiNP_001035723.1. NM_001040633.1. [Q9UGJ0-3]
NP_001291456.1. NM_001304527.1.
NP_001291460.1. NM_001304531.1. [Q9UGJ0-2]
NP_057287.2. NM_016203.3. [Q9UGJ0-1]
NP_077747.1. NM_024429.1. [Q9UGJ0-2]
XP_016867759.1. XM_017012270.1. [Q9UGJ0-3]
UniGeneiHs.647072.

Genome annotation databases

EnsembliENST00000287878; ENSP00000287878; ENSG00000106617. [Q9UGJ0-1]
ENST00000392801; ENSP00000376549; ENSG00000106617. [Q9UGJ0-3]
ENST00000418337; ENSP00000387386; ENSG00000106617. [Q9UGJ0-2]
GeneIDi51422.
KEGGihsa:51422.
UCSCiuc003wki.4. human. [Q9UGJ0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025580 mRNA. Translation: BAA84695.1. Frameshift.
AJ249976 mRNA. Translation: CAB65116.1.
AF087875 mRNA. Translation: AAK00413.1.
AK001887 mRNA. Translation: BAA91962.1.
BT007127 mRNA. Translation: AAP35791.1.
AC006358 Genomic DNA. Translation: AAS02032.1. Sequence problems.
AC006966 Genomic DNA. Translation: AAF03528.2.
AC093583 Genomic DNA. No translation available.
BC020540 mRNA. Translation: AAH20540.2. Different initiation.
BC068598 mRNA. Translation: AAH68598.1.
CCDSiCCDS43683.1. [Q9UGJ0-3]
CCDS47752.1. [Q9UGJ0-2]
CCDS5928.1. [Q9UGJ0-1]
RefSeqiNP_001035723.1. NM_001040633.1. [Q9UGJ0-3]
NP_001291456.1. NM_001304527.1.
NP_001291460.1. NM_001304531.1. [Q9UGJ0-2]
NP_057287.2. NM_016203.3. [Q9UGJ0-1]
NP_077747.1. NM_024429.1. [Q9UGJ0-2]
XP_016867759.1. XM_017012270.1. [Q9UGJ0-3]
UniGeneiHs.647072.

3D structure databases

ProteinModelPortaliQ9UGJ0.
SMRiQ9UGJ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119531. 24 interactors.
IntActiQ9UGJ0. 15 interactors.
MINTiMINT-4831646.
STRINGi9606.ENSP00000287878.

Chemistry databases

ChEMBLiCHEMBL3038451.
DrugBankiDB00945. Acetylsalicylic acid.

PTM databases

iPTMnetiQ9UGJ0.
PhosphoSitePlusiQ9UGJ0.

Polymorphism and mutation databases

BioMutaiPRKAG2.
DMDMi14285344.

Proteomic databases

PaxDbiQ9UGJ0.
PeptideAtlasiQ9UGJ0.
PRIDEiQ9UGJ0.

Protocols and materials databases

DNASUi51422.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000287878; ENSP00000287878; ENSG00000106617. [Q9UGJ0-1]
ENST00000392801; ENSP00000376549; ENSG00000106617. [Q9UGJ0-3]
ENST00000418337; ENSP00000387386; ENSG00000106617. [Q9UGJ0-2]
GeneIDi51422.
KEGGihsa:51422.
UCSCiuc003wki.4. human. [Q9UGJ0-1]

Organism-specific databases

CTDi51422.
DisGeNETi51422.
GeneCardsiPRKAG2.
GeneReviewsiPRKAG2.
HGNCiHGNC:9386. PRKAG2.
HPAiCAB018641.
HPA004246.
MalaCardsiPRKAG2.
MIMi194200. phenotype.
261740. phenotype.
600858. phenotype.
602743. gene.
neXtProtiNX_Q9UGJ0.
OpenTargetsiENSG00000106617.
Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
907. Wolff-Parkinson-White syndrome.
PharmGKBiPA33752.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
GeneTreeiENSGT00390000009849.
HOVERGENiHBG050431.
KOiK07200.
OMAiXVQIYEL.
OrthoDBiEOG091G0CZV.
PhylomeDBiQ9UGJ0.
TreeFamiTF313247.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000106617-MONOMER.
ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-1632852. Macroautophagy.
R-HSA-163680. AMPK inhibits chREBP transcriptional activation activity.
R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-HSA-2151209. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ9UGJ0.
SIGNORiQ9UGJ0.

Miscellaneous databases

ChiTaRSiPRKAG2. human.
GeneWikiiPRKAG2.
GenomeRNAii51422.
PROiQ9UGJ0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106617.
CleanExiHS_PRKAG2.
ExpressionAtlasiQ9UGJ0. baseline and differential.
GenevisibleiQ9UGJ0. HS.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAKG2_HUMAN
AccessioniPrimary (citable) accession number: Q9UGJ0
Secondary accession number(s): Q53Y07
, Q6NUI0, Q75MP4, Q9NUZ9, Q9UDN8, Q9ULX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.