GenomeNet

Database: UniProt
Entry: G2HGR1_PANTR
LinkDB: G2HGR1_PANTR
Original site: G2HGR1_PANTR 
ID   G2HGR1_PANTR            Unreviewed;       270 AA.
AC   G2HGR1; A0A2J8MDY7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=5'-AMP-activated protein kinase subunit beta-1 {ECO:0000256|ARBA:ARBA00040010};
GN   Name=PRKAB1 {ECO:0000313|EMBL:JAA05002.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000009369.3, ECO:0000313|VGNC:VGNC:8503};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK62919.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000009369.3, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:BAK62919.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Testis {ECO:0000313|EMBL:BAK62919.1};
RX   PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA   Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA   Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA   Kim D.S., Park H.S.;
RT   "Major chimpanzee-specific structural changes in sperm development-
RT   associated genes.";
RL   Funct. Integr. Genomics 11:507-517(2011).
RN   [3] {ECO:0000313|EMBL:JAA05002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA05002.1}, Skeletal muscle
RC   {ECO:0000313|EMBL:JAA39650.1}, Skin {ECO:0000313|EMBL:JAA25395.1}, and
RC   Smooth vascular {ECO:0000313|EMBL:JAA17600.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSPTRP00000009369.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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). {ECO:0000256|ARBA:ARBA00025180}.
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). Interacts with FNIP1 and FNIP2.
CC       {ECO:0000256|ARBA:ARBA00025878}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000256|ARBA:ARBA00010926}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AACZ04070302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK305925; BAK62919.1; -; mRNA.
DR   EMBL; GABC01006336; JAA05002.1; -; mRNA.
DR   EMBL; GABF01004545; JAA17600.1; -; mRNA.
DR   EMBL; GABD01007705; JAA25395.1; -; mRNA.
DR   EMBL; GABE01005089; JAA39650.1; -; mRNA.
DR   RefSeq; NP_001233530.1; NM_001246601.1.
DR   STRING; 9598.ENSPTRP00000009369; -.
DR   PaxDb; 9598-ENSPTRP00000009369; -.
DR   Ensembl; ENSPTRT00000010133.4; ENSPTRP00000009369.3; ENSPTRG00000005520.4.
DR   GeneID; 452297; -.
DR   KEGG; ptr:452297; -.
DR   CTD; 5564; -.
DR   VGNC; VGNC:8503; PRKAB1.
DR   eggNOG; KOG1616; Eukaryota.
DR   GeneTree; ENSGT00940000155307; -.
DR   HOGENOM; CLU_070949_2_0_1; -.
DR   OMA; QPTVFRW; -.
DR   OrthoDB; 120305at2759; -.
DR   TreeFam; TF313827; -.
DR   Proteomes; UP000002277; Chromosome 12.
DR   Bgee; ENSPTRG00000005520; Expressed in cortex of kidney and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0035878; P:nail development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 6.20.250.60; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR032640; AMPK1_CBM.
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; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR   PANTHER; PTHR10343:SF96; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; AMPKBI-like; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   2: Evidence at transcript level;
KW   Kinase {ECO:0000313|EMBL:BAK62919.1};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transferase {ECO:0000313|EMBL:BAK62919.1}.
FT   DOMAIN          180..270
FT                   /note="Association with the SNF1 complex (ASC)"
FT                   /evidence="ECO:0000259|SMART:SM01010"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   270 AA;  30382 MW;  F0BCAA94D5BC15FC CRC64;
     MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE EIKAPEKEEF
     LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSHN NFVAILDLPE
     GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS
     SSPPGPYHQE PYVCKPEERF RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY
     ALSIKDGVMV LSATHRYKKK YVTTLLYKPI
//
DBGET integrated database retrieval system