ID KPB2_MOUSE STANDARD; PRT; 1235 AA. AC Q8BWJ3; Q3TN65; Q810J6; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-JUN-2006, entry version 31. DE Phosphorylase b kinase alpha regulatory chain, liver isoform DE (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; Sciurognathi; OC Muroidea; Muridae; Murinae; 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 (By similarity). CC -!- PATHWAY: Glycogen metabolism. CC -!- SUBUNIT: Polymer of 16 chains, four each of alpha, beta, gamma, CC and delta. Alpha and beta are regulatory chains, gamma is the CC catalytic chain, and delta is calmodulin (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; cytoplasmic CC side (Potential). CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain CC family. 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 UniGene; Mm.350712; -. DR Ensembl; ENSMUSG00000031295; Mus musculus. DR MGI; MGI:97577; Phka2. DR InterPro; IPR008928; 6hp_glycosidase. DR InterPro; IPR008734; PHK_AB. DR PANTHER; PTHR10749; PHK_AB; 1. DR Pfam; PF05682; PHK_AB; 1. KW Calmodulin-binding; Carbohydrate metabolism; Glycogen metabolism; KW Lipoprotein; Membrane; Phosphorylation; Prenylation. FT CHAIN 1 1235 Phosphorylase b kinase alpha regulatory FT chain, liver isoform. FT /FTId=PRO_0000057731. FT REGION 807 837 Calmodulin-binding (Potential). FT REGION 1059 1099 Calmodulin-binding (Potential). FT MOD_RES 735 735 Phosphoserine (By similarity). FT LIPID 1232 1232 S-farnesyl cysteine (By similarity). 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 //