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Creatine kinase B-type (EC 2.7.3.2) (B-CK) (Creatine kinase B chain)

 KCRB_MOUSE              Reviewed;         381 AA.
Q04447; Q3KQP4; Q3TKI3; Q3U5P5; Q3UF71; Q9CXK6;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=Creatine kinase B-type;
EC=2.7.3.2;
AltName: Full=B-CK;
AltName: Full=Creatine kinase B chain;
Name=Ckb; Synonyms=Ckbb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1740343; DOI=10.1016/0888-7543(92)90383-4;
van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G.,
Hendriks W., Wieringa B.;
"Genetic variability of the murine creatine kinase B gene locus and
related pseudogenes in different inbred strains of mice.";
Genomics 12:340-349(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Pentecost B.T.;
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Embryonic head, Kidney, Sympathetic ganglion, and
Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209;
224-236; 253-265; 268-292 AND 320-381, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=3641191; DOI=10.1093/nar/14.21.8690;
Papenbrock T., Wille W.;
"The 3' non-coding region of the mouse brain B creatine kinase mRNA: a
sequence with exceptional homology among species.";
Nucleic Acids Res. 14:8690-8690(1986).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15648052; DOI=10.1002/pmic.200401066;
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
Hart G.W., Burlingame A.L.;
"Quantitative analysis of both protein expression and serine /
threonine post-translational modifications through stable isotope
labeling with dithiothreitol.";
Proteomics 5:388-398(2005).
[8]
NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16800626; DOI=10.1021/bi060474w;
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
Squier T.C., Bigelow D.J.;
"Endogenously nitrated proteins in mouse brain: links to
neurodegenerative disease.";
Biochemistry 45:8009-8022(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-199 AND THR-322,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
ATP and various phosphogens (e.g. creatine phosphate). Creatine
kinase isoenzymes play a central role in energy transduction in
tissues with large, fluctuating energy demands, such as skeletal
muscle, heart, brain and spermatozoa.
-!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
the major form in skeletal muscle and myocardium, MB existing in
myocardium, and BB existing in many tissues, especially brain.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
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EMBL; M74149; AAA37462.1; -; Genomic_DNA.
EMBL; L09069; AAA37455.1; -; Genomic_DNA.
EMBL; AK002467; BAB22121.1; -; mRNA.
EMBL; AK014299; BAB29254.1; -; mRNA.
EMBL; AK148885; BAE28690.1; -; mRNA.
EMBL; AK152388; BAE31176.1; -; mRNA.
EMBL; AK153484; BAE32032.1; -; mRNA.
EMBL; AK166980; BAE39162.1; -; mRNA.
EMBL; AK161990; BAE36669.1; -; mRNA.
EMBL; AK167034; BAE39205.1; -; mRNA.
EMBL; BC015271; AAH15271.1; -; mRNA.
EMBL; BC106109; AAI06110.2; -; mRNA.
EMBL; X04591; CAA28259.1; -; mRNA.
CCDS; CCDS26183.1; -.
PIR; A42078; A42078.
RefSeq; NP_067248.1; NM_021273.4.
UniGene; Mm.16831; -.
ProteinModelPortal; Q04447; -.
SMR; Q04447; -.
BioGrid; 198725; 5.
CORUM; Q04447; -.
IntAct; Q04447; 9.
MINT; MINT-4099724; -.
STRING; 10090.ENSMUSP00000001304; -.
iPTMnet; Q04447; -.
PhosphoSitePlus; Q04447; -.
SwissPalm; Q04447; -.
REPRODUCTION-2DPAGE; Q04447; -.
UCD-2DPAGE; Q04447; -.
EPD; Q04447; -.
MaxQB; Q04447; -.
PaxDb; Q04447; -.
PeptideAtlas; Q04447; -.
PRIDE; Q04447; -.
Ensembl; ENSMUST00000001304; ENSMUSP00000001304; ENSMUSG00000001270.
GeneID; 12709; -.
KEGG; mmu:12709; -.
UCSC; uc007pdn.2; mouse.
CTD; 1152; -.
MGI; MGI:88407; Ckb.
eggNOG; KOG3581; Eukaryota.
eggNOG; COG3869; LUCA.
GeneTree; ENSGT00550000074561; -.
HOGENOM; HOG000232165; -.
HOVERGEN; HBG001339; -.
InParanoid; Q04447; -.
KO; K00933; -.
OMA; RGHEFMW; -.
OrthoDB; EOG091G0HZ0; -.
PhylomeDB; Q04447; -.
TreeFam; TF314214; -.
Reactome; R-MMU-71288; Creatine metabolism.
PRO; PR:Q04447; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000001270; -.
CleanEx; MM_CKB; -.
Genevisible; Q04447; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; IEA:UniProtKB-EC.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEA:Ensembl.
Gene3D; 1.10.135.10; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 1.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Kinase; Nitration; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transferase.
CHAIN 1 381 Creatine kinase B-type.
/FTId=PRO_0000211967.
DOMAIN 11 98 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
DOMAIN 125 367 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
NP_BIND 128 132 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
NP_BIND 320 325 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 130 130 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 132 132 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 191 191 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 232 232 Substrate. {ECO:0000250}.
BINDING 236 236 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 285 285 Substrate. {ECO:0000250}.
BINDING 292 292 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 320 320 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 335 335 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P12277}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 125 125 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 269 269 Nitrated tyrosine.
{ECO:0000244|PubMed:16800626}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:P07335}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 143 143 P -> H (in Ref. 3; BAE28690).
{ECO:0000305}.
CONFLICT 217 217 I -> M (in Ref. 3; BAE39162).
{ECO:0000305}.
SEQUENCE 381 AA; 42713 MW; D901C5653054A490 CRC64;
MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG
VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY QPSDEHKTDL NPDNLQGGDD
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLS GRYYALKSMT
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
IEMEQRLEQG QAIDDLMPAQ K


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