AAKB2_RAT
ID AAKB2_RAT Reviewed; 271 AA.
AC Q9QZH4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
DE Short=AMPK subunit beta-2;
GN Name=Prkab2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-183.
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=10544261; DOI=10.1016/s0014-5793(99)01371-x;
RA Chen Z., Heierhorst J., Mann R.J., Mitchelhill K.I., Michell B.J.,
RA Witters L.A., Lynch G.S., Kemp B.E., Stapleton D.;
RT "Expression of the AMP-activated protein kinase beta1 and beta2 subunits in
RT skeletal muscle.";
RL FEBS Lett. 460:343-348(1999).
RN [2]
RP PHOSPHORYLATION BY ULK1 AND ULK2, AND PHOSPHORYLATION AT SER-38; THR-39;
RP SER-68 AND SER-173.
RX PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC an energy sensor protein kinase that plays a key role in regulating
CC cellular energy metabolism. In response to reduction of intracellular
CC ATP levels, AMPK activates energy-producing pathways and inhibits
CC energy-consuming processes: inhibits protein, carbohydrate and lipid
CC biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC direct phosphorylation of metabolic enzymes, and by longer-term effects
CC via phosphorylation of transcription regulators. Also acts as a
CC regulator of cellular polarity by remodeling the actin cytoskeleton;
CC probably by indirectly activating myosin. Beta non-catalytic subunit
CC acts as a scaffold on which the AMPK complex assembles, via its C-
CC terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC (PRKAG1, PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC subunits (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000250}.
CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively
CC regulate AMPK activity and suggesting the existence of a regulatory
CC feedback loop between ULK1, ULK2 and AMPK.
CC {ECO:0000269|PubMed:10544261, ECO:0000269|PubMed:21460634}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AF182717; AAF01293.1; -; mRNA.
DR RefSeq; NP_072149.1; NM_022627.2.
DR PDB; 2LU3; NMR; -; A=67-163.
DR PDB; 2LU4; NMR; -; A=67-163.
DR PDB; 4Y0G; X-ray; 1.60 A; A/B=74-155.
DR PDB; 4YEE; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=74-155.
DR PDBsum; 2LU3; -.
DR PDBsum; 2LU4; -.
DR PDBsum; 4Y0G; -.
DR PDBsum; 4YEE; -.
DR AlphaFoldDB; Q9QZH4; -.
DR BMRB; Q9QZH4; -.
DR SMR; Q9QZH4; -.
DR STRING; 10116.ENSRNOP00000062137; -.
DR BindingDB; Q9QZH4; -.
DR ChEMBL; CHEMBL4523617; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q9QZH4; -.
DR PhosphoSitePlus; Q9QZH4; -.
DR PaxDb; Q9QZH4; -.
DR PRIDE; Q9QZH4; -.
DR DNASU; 64562; -.
DR GeneID; 64562; -.
DR KEGG; rno:64562; -.
DR CTD; 5565; -.
DR RGD; 620905; Prkab2.
DR eggNOG; KOG1616; Eukaryota.
DR InParanoid; Q9QZH4; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; Q9QZH4; -.
DR BRENDA; 2.7.11.31; 5301.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q9QZH4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR039160; AMPKB.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343:SF83; PTHR10343:SF83; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..271
FT /note="5'-AMP-activated protein kinase subunit beta-2"
FT /id="PRO_0000204370"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000269|PubMed:21460634,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphothreonine; by ULK1"
FT /evidence="ECO:0000269|PubMed:21460634"
FT MOD_RES 68
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000269|PubMed:21460634"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 173
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000269|PubMed:21460634"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10544261"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2LU4"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4Y0G"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2LU3"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:4Y0G"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2LU3"
SQ SEQUENCE 271 AA; 30227 MW; D881451A03287BEA CRC64;
MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS KLPGDKEFVP
WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST KIPLIKSHND FVAILDLPEG
EHQYKFFVDG QWVHDPSEPV VTSQLGTINN LIHVKKSDFE VFDALKLDSM ESSETSCRDL
SSSPPGPYGQ EMYVFRSEER FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL
YALSTKDSVM VLSATHRYKK KYVTTLLYKP I
