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 07-JUN-2017, entry version 129. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RC 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 RT 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 CC chain may bind calmodulin. CC -!- ENZYME REGULATION: By phosphorylation of various serine residues CC and 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 CC (PHKB) are regulatory subunits, gamma (PHKG1 or PHKG2) is the CC catalytic subunit, and delta is calmodulin (By similarity). CC {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 UniGene; Mm.350712; -. DR ProteinModelPortal; Q8BWJ3; -. DR IntAct; Q8BWJ3; 1. DR MINT; MINT-4099919; -. DR STRING; 10090.ENSMUSP00000033652; -. DR iPTMnet; Q8BWJ3; -. DR PhosphoSitePlus; Q8BWJ3; -. DR EPD; Q8BWJ3; -. DR MaxQB; Q8BWJ3; -. DR PaxDb; Q8BWJ3; -. DR PRIDE; Q8BWJ3; -. 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 eggNOG; KOG3635; Eukaryota. DR eggNOG; ENOG410XPJZ; LUCA. DR GeneTree; ENSGT00520000055553; -. DR HOGENOM; HOG000231478; -. DR HOVERGEN; HBG000273; -. DR InParanoid; Q8BWJ3; -. DR KO; K07190; -. DR OMA; HVPQPEY; -. DR OrthoDB; EOG091G00NN; -. DR PhylomeDB; Q8BWJ3; -. DR TreeFam; TF313970; -. DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis). DR UniPathway; UPA00163; -. DR PRO; PR:Q8BWJ3; -. DR Proteomes; UP000000589; Chromosome X. DR Bgee; ENSMUSG00000031295; -. DR CleanEx; MM_PHKA2; -. 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:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006468; P:protein phosphorylation; IEA:GOC. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR011613; Glyco_hydro_15/PHK. DR InterPro; IPR008734; PHK_A/B_su. DR PANTHER; PTHR10749; PTHR10749; 1. DR Pfam; PF00723; Glyco_hydro_15; 1. DR SUPFAM; SSF48208; SSF48208; 1. PE 1: Evidence at protein level; KW Calmodulin-binding; Carbohydrate metabolism; Cell membrane; KW Complete proteome; Glycogen metabolism; Lipoprotein; Membrane; KW Phosphoprotein; Prenylation; Reference proteome. FT CHAIN 1 1235 Phosphorylase b kinase regulatory subunit FT alpha, liver isoform. FT /FTId=PRO_0000057731. FT REGION 807 837 Calmodulin-binding. {ECO:0000255}. FT REGION 1059 1099 Calmodulin-binding. {ECO:0000255}. FT MOD_RES 695 695 Phosphoserine. FT {ECO:0000250|UniProtKB:P46019}. FT MOD_RES 729 729 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 735 735 Phosphoserine. FT {ECO:0000250|UniProtKB:P46019}. FT MOD_RES 983 983 Phosphoserine. FT {ECO:0000250|UniProtKB:P46019}. FT MOD_RES 1015 1015 Phosphoserine. FT {ECO:0000244|PubMed:17242355, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 1044 1044 Phosphoserine. FT {ECO:0000250|UniProtKB:P46019}. FT LIPID 1232 1232 S-farnesyl cysteine. FT {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 //