ID KPB2_MOUSE Reviewed; 1235 AA. AC Q8BWJ3; Q3TN65; Q810J6; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 25-MAY-2022, entry version 153. DE RecName: Full=Phosphorylase b kinase regulatory subunit alpha, liver isoform; DE Short=Phosphorylase kinase alpha L subunit; GN Name=Phka2; 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=Heart, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-1015, AND 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 [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-1015, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen; 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 alpha chain may CC bind calmodulin. CC -!- ACTIVITY REGULATION: By phosphorylation of various serine residues and CC by calcium. {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:P18688}. CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH50040.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AK052346; BAC34948.1; -; mRNA. DR EMBL; AK165506; BAE38224.1; -; mRNA. DR EMBL; BC050040; AAH50040.1; ALT_INIT; mRNA. DR CCDS; CCDS30504.1; -. DR RefSeq; NP_001171350.1; NM_001177879.1. DR RefSeq; NP_766371.1; NM_172783.3. DR RefSeq; XP_006528742.1; XM_006528679.3. DR AlphaFoldDB; Q8BWJ3; -. DR BioGRID; 225291; 2. DR STRING; 10090.ENSMUSP00000033652; -. DR iPTMnet; Q8BWJ3; -. DR PhosphoSitePlus; Q8BWJ3; -. DR EPD; Q8BWJ3; -. DR jPOST; Q8BWJ3; -. DR MaxQB; Q8BWJ3; -. DR PaxDb; Q8BWJ3; -. DR PRIDE; Q8BWJ3; -. DR ProteomicsDB; 265017; -. DR Antibodypedia; 24169; 96 antibodies from 25 providers. DR DNASU; 110094; -. DR Ensembl; ENSMUST00000033652; ENSMUSP00000033652; ENSMUSG00000031295. DR Ensembl; ENSMUST00000112377; ENSMUSP00000107996; ENSMUSG00000031295. DR GeneID; 110094; -. DR KEGG; mmu:110094; -. DR UCSC; uc009utk.1; mouse. DR CTD; 5256; -. DR MGI; MGI:97577; Phka2. DR VEuPathDB; HostDB:ENSMUSG00000031295; -. DR eggNOG; KOG3635; Eukaryota. DR GeneTree; ENSGT00950000183118; -. DR HOGENOM; CLU_004177_1_0_1; -. DR InParanoid; Q8BWJ3; -. DR OMA; QFEHIEC; -. DR OrthoDB; 55049at2759; -. DR PhylomeDB; Q8BWJ3; -. DR TreeFam; TF313970; -. DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis). DR UniPathway; UPA00163; -. DR BioGRID-ORCS; 110094; 4 hits in 72 CRISPR screens. DR ChiTaRS; Phka2; mouse. DR PRO; PR:Q8BWJ3; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q8BWJ3; protein. DR Bgee; ENSMUSG00000031295; Expressed in bone marrow macrophage and 298 other tissues. DR ExpressionAtlas; Q8BWJ3; baseline and differential. DR Genevisible; Q8BWJ3; MM. DR GO; GO:0005964; C:phosphorylase kinase complex; IBA:GO_Central. 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 Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase_sf. DR InterPro; IPR012341; 6hp_glycosidase-like_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..1235 FT /note="Phosphorylase b kinase regulatory subunit alpha, FT liver isoform" FT /id="PRO_0000057731" FT REGION 636..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 807..837 FT /note="Calmodulin-binding" FT /evidence="ECO:0000255" FT REGION 1033..1060 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1059..1099 FT /note="Calmodulin-binding" FT /evidence="ECO:0000255" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46019" FT MOD_RES 729 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 735 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46019" FT MOD_RES 983 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46019" FT MOD_RES 1015 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 1044 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46019" FT LIPID 1232 FT /note="S-farnesyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P18688" SQ SEQUENCE 1235 AA; 138492 MW; 81B6EC538B0228CC CRC64; MRSRSNSGVR LDGYARLVQQ TILCYQNPVT GLLSASHDQK DAWVRDNIYS ILAVWGLGMA YRKNADRDED KAKAYELEQN VVKLMRGLLQ CMMRQVDKVE KFKHTQSTKD SLHAKYNTAT CSTVVGDDQW GHLQVDATSL FLLFLAQMTA SGLRIIFTLD EVAFIQNLVF YIEAAYKVAD YGMWERGDKT NQGIPELNAS SVGVAKAALE AIDELDLFGA HGGRKSVIHV LPDEVEHCQS ILFSMLPRAS TSKEIDAGLL SIISFPAFAV EDVNLVNVTK NEIISKLQGR YGCCRFLRDG YKTPREDPHR LHYDPAELKL FENIECEWPV FWTYLIIDGI FNGDAVQVQE YREALEGILI RGKDGIHLVP ELYAIPPDKV DEEYKNPHTV DRVPLGKLPH LWGQSLYILS SLLAEGFLAT GEIDPLNRRF STSVKPDVVV QVAVLAENSH IKGLLKEHGM TVQSIADVHP IRVQPGRILS HIYAKLGRNK NMKLSGRPYR HIGVLGTSKL YVIRNHIFTF TPQFTDQHHF YLALDNEMIV EMLRIELAYL CTCWRMTGRP TLTFPVTHTM LTNDGSDIHP AVLSTIRKLE DGYFGGARVK LGNLAEFLTT SFYTHLTFLD PDCDEKLFGD ITDRSFSPDS EPDLGGYLED SSPQESQDEL DQYISHLLQS TSLKCYLPPL CKKSEDSHFF SAIHSTRDIL SVMAKAKGLE TTFFPMILPT KVLSGHRKSL NLVDSPQPLL KTTPEYDYQW PRDDHDEVDC EKLVGQLKDC SNLQDQADIL YILYVMKGPR WDTNLFGQHG VTVHSLLSEL YGKAGLNQEW SLIRYISGLL RKKVEVLAEA CADLLSHQKQ LTVGLPPEPR EKTISTPLPP EELTELIYEA SGQDISIAVL TQEIVVYLAM YVRAQPSLFA EMLRLRIGLI IQVMATELAR SLNCSGKEAS ESLMNLSPFD MKSLLHHILS GKEFGVERSV RPIHSSMSSP AISIHEVGHT GATKTERSGI TRLRSEMKQM NRRASADEQF FPLGQTMSNS LHSIKSVRSS TPSSPTGTSS TDSGGQHLGW GEQQGQWLRR RRLDGAINRV PVGFYQKVWK ILQKCHGLSI DGYVLPSSTT QEMTPCEIKF AVHVESVLNR VSQPEYRQLL VEAIMVLTLL SDTEMDSIGG IIHVDQIVQL ANQLFLQDQV SFGTTDILEK DQATGICHLF YDSAPSGAYG TMTYLTKAVA SHLQELLPSS GCQMQ //