KPBB_MOUSE
ID KPBB_MOUSE Reviewed; 1085 AA.
AC Q7TSH2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphorylase b kinase regulatory subunit beta;
DE Short=Phosphorylase kinase subunit beta;
GN Name=Phkb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The beta chain acts
CC as a regulatory unit and modulates the activity of the holoenzyme in
CC response to phosphorylation (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: By phosphorylation of various serine residues.
CC {ECO:0000250}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: Although the final Cys may be farnesylated, the terminal
CC tripeptide is probably not removed, and the C-terminus is not
CC methylated. {ECO:0000250|UniProtKB:P12798}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; BC053105; AAH53105.1; -; mRNA.
DR CCDS; CCDS22501.1; -.
DR RefSeq; NP_955517.1; NM_199446.1.
DR RefSeq; XP_006530595.1; XM_006530532.3.
DR RefSeq; XP_006530596.1; XM_006530533.3.
DR RefSeq; XP_006530597.1; XM_006530534.3.
DR AlphaFoldDB; Q7TSH2; -.
DR BioGRID; 221792; 5.
DR IntAct; Q7TSH2; 3.
DR MINT; Q7TSH2; -.
DR STRING; 10090.ENSMUSP00000050788; -.
DR iPTMnet; Q7TSH2; -.
DR PhosphoSitePlus; Q7TSH2; -.
DR SwissPalm; Q7TSH2; -.
DR EPD; Q7TSH2; -.
DR jPOST; Q7TSH2; -.
DR MaxQB; Q7TSH2; -.
DR PaxDb; Q7TSH2; -.
DR PeptideAtlas; Q7TSH2; -.
DR PRIDE; Q7TSH2; -.
DR ProteomicsDB; 265018; -.
DR Antibodypedia; 28116; 183 antibodies from 29 providers.
DR DNASU; 102093; -.
DR Ensembl; ENSMUST00000053771; ENSMUSP00000050788; ENSMUSG00000036879.
DR GeneID; 102093; -.
DR KEGG; mmu:102093; -.
DR UCSC; uc009mqj.1; mouse.
DR CTD; 5257; -.
DR MGI; MGI:97578; Phkb.
DR VEuPathDB; HostDB:ENSMUSG00000036879; -.
DR eggNOG; KOG3635; Eukaryota.
DR GeneTree; ENSGT00950000183118; -.
DR HOGENOM; CLU_004177_0_1_1; -.
DR InParanoid; Q7TSH2; -.
DR OMA; VIYTHHE; -.
DR OrthoDB; 55049at2759; -.
DR PhylomeDB; Q7TSH2; -.
DR TreeFam; TF313970; -.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR UniPathway; UPA00163; -.
DR BioGRID-ORCS; 102093; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Phkb; mouse.
DR PRO; PR:Q7TSH2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q7TSH2; protein.
DR Bgee; ENSMUSG00000036879; Expressed in quadriceps femoris and 248 other tissues.
DR ExpressionAtlas; Q7TSH2; baseline and differential.
DR Genevisible; Q7TSH2; MM.
DR GO; GO:0005964; C:phosphorylase kinase complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR PANTHER; PTHR10749; PTHR10749; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein; Prenylation;
KW Reference proteome.
FT CHAIN 1..1085
FT /note="Phosphorylase b kinase regulatory subunit beta"
FT /id="PRO_0000057737"
FT REGION 760..787
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 912..943
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
FT LIPID 1082
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P12798"
SQ SEQUENCE 1085 AA; 123889 MW; 8EC52645AD89FDF5 CRC64;
MANSPDAAFS SPALLRSGSV YEPLKSINLP RPDNETLWDK LDHYYRIVKS TMLMYQSPTT
GLFPTKTCGG EEKSKVHESL YCAAGAWALA LAYRRIDDDK GRTHELEHSA IKCMRGILYC
YMRQADKVQQ FKQDPRPTTC LHSVFSVHTG DELLSYEEYG HLQINAVSLF LLYLVEMISS
GLQIIYNTDE VSFIQNLVFC VERVYRVPDF GVWERGSKYN NGSTELHSSS VGLAKAALEA
INGFNLFGNQ GCSWSVIFVD LDAHNRNRQT LCSLLPRESR SHNTDAALLP CISYPAFALD
DEALFSQTLD KVIRKLKGKY GFKRFLRDGY RTPLEDPNRR YYKPAEIKLF DGIECEFPIF
FLYMMIDGVF RGNLEQVKEY QDLLTPLLHQ TTEGYPVVPK YYYVPADFVE CEKRNPGSQK
RFPSNCGRDG KLFLWGQALY IIAKLLADEL ISPKDIDPVQ RFVPLQNQRN VSMRYSNQGP
LENDLVVHVA LVAESQRLQV FLNTYGIQTQ TPQQVEPIQI WPQQELVKAY FHLGINEKLG
LSGRPDRPIG CLGTSKIYRI LGKTVVCYPI IFDLSDFYMS QDVLLLIDDI KNALQFIKQY
WKMHGRPLFL VLIREDNIRG SRFNPILDML AAFKKGIIGG VKVHVDRLQT LISGAVVEQL
DFLRISDTEK LPEFKSFEEL EFPKHSKVKR QSSTADAPEA QHEPGITITE WKNKSTHEIL
QKLNDCGCLA GQTILLGILL KREGPNFITM EGTVSDHIER VYRRAGSKKL WSVVRRAASL
LNKVVDSLAP SITNVLVQGK QVTLGAFGHE EEVISNPLSP RVIKNIIYYK CNTHDEREAV
IQQELVIHIG WIISNSPELF SGMLKIRIGW IIHAMEYELQ VRGGDKPAVD LYQLSPSEVK
QLLLDILQPQ QSGRCWLNRR QIDGSLNRTP PEFYDRVWQI LERTPNGIVV AGKHLPQQPT
LSDMTMYEMN FSLLVEDMLG NIDQPKYRQI IVELLMVVSI VLERNPELEF QDKVDLDRLV
KEAFHEFQKD ESRLKEIEKQ DDMTSFYNTP PLGKRGTCSY LTKVVMNSLL EGEVKPSNED
SCLVS
