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   27-MAR-2024, entry version 141.
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,
RC   Spleen, and 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   GlyGen; Q7TSH2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7TSH2; -.
DR   PhosphoSitePlus; Q7TSH2; -.
DR   SwissPalm; Q7TSH2; -.
DR   EPD; Q7TSH2; -.
DR   jPOST; Q7TSH2; -.
DR   MaxQB; Q7TSH2; -.
DR   PaxDb; 10090-ENSMUSP00000050788; -.
DR   PeptideAtlas; Q7TSH2; -.
DR   ProteomicsDB; 265018; -.
DR   Pumba; Q7TSH2; -.
DR   Antibodypedia; 28116; 206 antibodies from 29 providers.
DR   DNASU; 102093; -.
DR   Ensembl; ENSMUST00000053771.14; ENSMUSP00000050788.8; ENSMUSG00000036879.16.
DR   GeneID; 102093; -.
DR   KEGG; mmu:102093; -.
DR   UCSC; uc009mqj.1; mouse.
DR   AGR; MGI:97578; -.
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; CWIKQAH; -.
DR   OrthoDB; 3640971at2759; -.
DR   PhylomeDB; Q7TSH2; -.
DR   TreeFam; TF313970; -.
DR   Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR   UniPathway; UPA00163; -.
DR   BioGRID-ORCS; 102093; 1 hit in 78 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 251 other cell types or tissues.
DR   ExpressionAtlas; Q7TSH2; baseline and differential.
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   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; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10749:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q7TSH2; MM.
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
//