ID   KCRB_MOUSE              Reviewed;         381 AA.
AC   Q04447; Q3KQP4; Q3TKI3; Q3U5P5; Q3UF71; Q9CXK6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 195.
DE   RecName: Full=Creatine kinase B-type {ECO:0000303|PubMed:33597756};
DE            EC=2.7.3.2 {ECO:0000269|PubMed:33597756};
DE   AltName: Full=B-CK;
DE   AltName: Full=Creatine kinase B chain;
DE   AltName: Full=Creatine phosphokinase B-type;
DE            Short=CPK-B;
GN   Name=Ckb {ECO:0000303|PubMed:33597756, ECO:0000312|MGI:MGI:88407};
GN   Synonyms=Ckbb;
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 [GENOMIC DNA].
RX   PubMed=1740343; DOI=10.1016/0888-7543(92)90383-4;
RA   van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G.,
RA   Hendriks W., Wieringa B.;
RT   "Genetic variability of the murine creatine kinase B gene locus and related
RT   pseudogenes in different inbred strains of mice.";
RL   Genomics 12:340-349(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pentecost B.T.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic head, Kidney, Sympathetic ganglion, and Wolffian
RC   duct;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   [5]
RP   PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209;
RP   224-236; 253-265; 268-292 AND 320-381, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=3641191; DOI=10.1093/nar/14.21.8690;
RA   Papenbrock T., Wille W.;
RT   "The 3' non-coding region of the mouse brain B creatine kinase mRNA: a
RT   sequence with exceptional homology among species.";
RL   Nucleic Acids Res. 14:8690-8690(1986).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine / threonine
RT   post-translational modifications through stable isotope labeling with
RT   dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA   Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA   Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT   disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [10]
RP   UBIQUITINATION.
RX   PubMed=17148442; DOI=10.1074/jbc.m609164200;
RA   Debrincat M.A., Zhang J.G., Willson T.A., Silke J., Connolly L.M.,
RA   Simpson R.J., Alexander W.S., Nicola N.A., Kile B.T., Hilton D.J.;
RT   "Ankyrin repeat and suppressors of cytokine signaling box protein asb-9
RT   targets creatine kinase B for degradation.";
RL   J. Biol. Chem. 282:4728-4737(2007).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=18566107; DOI=10.1093/hmg/ddn172;
RA   Salin-Cantegrel A., Shekarabi M., Holbert S., Dion P., Rochefort D.,
RA   Laganiere J., Dacal S., Hince P., Karemera L., Gaspar C., Lapointe J.Y.,
RA   Rouleau G.A.;
RT   "HMSN/ACC truncation mutations disrupt brain-type creatine kinase-dependant
RT   activation of K+/Cl- co-transporter 3.";
RL   Hum. Mol. Genet. 17:2703-2711(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-199 AND THR-322, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, INDUCTION,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 130-ARG--ARG-138 AND CYS-283.
RX   PubMed=33597756; DOI=10.1038/s41586-021-03221-y;
RA   Rahbani J.F., Roesler A., Hussain M.F., Samborska B., Dykstra C.B.,
RA   Tsai L., Jedrychowski M.P., Vergnes L., Reue K., Spiegelman B.M., Kazak L.;
RT   "Creatine kinase B controls futile creatine cycling in thermogenic fat.";
RL   Nature 590:480-485(2021).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC       and various phosphogens (e.g. creatine phosphate) (PubMed:33597756).
CC       Creatine kinase isoenzymes play a central role in energy transduction
CC       in tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa (Probable). Acts as a key
CC       regulator of adaptive thermogenesis as part of the futile creatine
CC       cycle: localizes to the mitochondria of thermogenic fat cells and acts
CC       by mediating phosphorylation of creatine to initiate a futile cycle of
CC       creatine phosphorylation and dephosphorylation (PubMed:33597756).
CC       During the futile creatine cycle, creatine and N-phosphocreatine are in
CC       a futile cycle, which dissipates the high energy charge of N-
CC       phosphocreatine as heat without performing any mechanical or chemical
CC       work (PubMed:33597756). {ECO:0000269|PubMed:33597756, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=creatine + ATP = N-phosphocreatine + ADP + H(+);
CC         Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10029,
CC         ECO:0000269|PubMed:33597756};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158;
CC         Evidence={ECO:0000269|PubMed:33597756};
CC   -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC       either B (brain type) or M (muscle type). With MM being the major form
CC       in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC       existing in many tissues, especially brain. Interacts with SLC12A6 (via
CC       C-terminus); the interaction may be required for SLC12A6 potassium-
CC       chloride cotransport activity (By similarity).
CC       {ECO:0000250|UniProtKB:P12277}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:33597756}.
CC       Mitochondrion {ECO:0000269|PubMed:33597756}. Cell membrane
CC       {ECO:0000250|UniProtKB:P12277}. Note=Localizes to the mitochondria of
CC       thermogenic fat cells via the internal MTS-like signal (iMTS-L) region.
CC       {ECO:0000269|PubMed:33597756}.
CC   -!- TISSUE SPECIFICITY: Expressed in hippocampus and corpus callosum (at
CC       protein level). {ECO:0000269|PubMed:18566107}.
CC   -!- INDUCTION: Strongly up-regulated in response to cold in fat cells;
CC       expression is dependent on cAMP. {ECO:0000269|PubMed:33597756}.
CC   -!- DOMAIN: The internal MTS-like signal (iMTS-L) mediates targeting to
CC       mitochondria thermogenic fat cells. {ECO:0000269|PubMed:33597756}.
CC   -!- PTM: Ubiquitinated by the ECS(ASB9) complex, leading to its degradation
CC       by the proteasome. {ECO:0000250|UniProtKB:P12277}.
CC   -!- DISRUPTION PHENOTYPE: Conditional deletion in adipocytes leads to
CC       defective adaptive thermogenesis: defects are caused by abolition of
CC       the futile creatine cycle, thereby reducing whole-body energy
CC       expenditure and leading to predisposition to obesity.
CC       {ECO:0000269|PubMed:33597756}.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
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DR   EMBL; M74149; AAA37462.1; -; Genomic_DNA.
DR   EMBL; L09069; AAA37455.1; -; Genomic_DNA.
DR   EMBL; AK002467; BAB22121.1; -; mRNA.
DR   EMBL; AK014299; BAB29254.1; -; mRNA.
DR   EMBL; AK148885; BAE28690.1; -; mRNA.
DR   EMBL; AK152388; BAE31176.1; -; mRNA.
DR   EMBL; AK153484; BAE32032.1; -; mRNA.
DR   EMBL; AK166980; BAE39162.1; -; mRNA.
DR   EMBL; AK161990; BAE36669.1; -; mRNA.
DR   EMBL; AK167034; BAE39205.1; -; mRNA.
DR   EMBL; BC015271; AAH15271.1; -; mRNA.
DR   EMBL; BC106109; AAI06110.2; -; mRNA.
DR   EMBL; X04591; CAA28259.1; -; mRNA.
DR   CCDS; CCDS26183.1; -.
DR   PIR; A42078; A42078.
DR   RefSeq; NP_067248.1; NM_021273.4.
DR   AlphaFoldDB; Q04447; -.
DR   SMR; Q04447; -.
DR   BioGRID; 198725; 37.
DR   CORUM; Q04447; -.
DR   FunCoup; Q04447; 714.
DR   IntAct; Q04447; 10.
DR   MINT; Q04447; -.
DR   STRING; 10090.ENSMUSP00000001304; -.
DR   GlyGen; Q04447; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q04447; -.
DR   PhosphoSitePlus; Q04447; -.
DR   SwissPalm; Q04447; -.
DR   REPRODUCTION-2DPAGE; Q04447; -.
DR   CPTAC; non-CPTAC-3977; -.
DR   jPOST; Q04447; -.
DR   PaxDb; 10090-ENSMUSP00000001304; -.
DR   PeptideAtlas; Q04447; -.
DR   ProteomicsDB; 263509; -.
DR   Pumba; Q04447; -.
DR   Antibodypedia; 28; 914 antibodies from 41 providers.
DR   DNASU; 12709; -.
DR   Ensembl; ENSMUST00000001304.9; ENSMUSP00000001304.8; ENSMUSG00000001270.10.
DR   GeneID; 12709; -.
DR   KEGG; mmu:12709; -.
DR   UCSC; uc007pdn.2; mouse.
DR   AGR; MGI:88407; -.
DR   CTD; 1152; -.
DR   MGI; MGI:88407; Ckb.
DR   VEuPathDB; HostDB:ENSMUSG00000001270; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   GeneTree; ENSGT00950000182772; -.
DR   HOGENOM; CLU_019868_4_2_1; -.
DR   InParanoid; Q04447; -.
DR   OMA; MRICAFN; -.
DR   OrthoDB; 430219at2759; -.
DR   PhylomeDB; Q04447; -.
DR   BRENDA; 2.7.3.2; 3474.
DR   Reactome; R-MMU-71288; Creatine metabolism.
DR   Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR   BioGRID-ORCS; 12709; 2 hits in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:Q04447; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q04447; protein.
DR   Bgee; ENSMUSG00000001270; Expressed in cerebellar cortex and 134 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0030425; C:dendrite; ISO:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004111; F:creatine kinase activity; IDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:GO_Central.
DR   GO; GO:0140651; P:futile creatine cycle; IDA:UniProt.
DR   GO; GO:0030644; P:intracellular chloride ion homeostasis; ISO:GO_Central.
DR   GO; GO:0046314; P:phosphocreatine biosynthetic process; ISO:GO_Central.
DR   CDD; cd00716; creatine_kinase_like; 1.
DR   FunFam; 3.30.590.10:FF:000026; Creatine kinase B-type; 1.
DR   FunFam; 1.10.135.10:FF:000001; Creatine kinase M-type; 1.
DR   Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1.
DR   PANTHER; PTHR11547:SF23; CREATINE KINASE B-TYPE; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Kinase; Membrane; Mitochondrion; Nitration;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..381
FT                   /note="Creatine kinase B-type"
FT                   /id="PRO_0000211967"
FT   DOMAIN          11..98
FT                   /note="Phosphagen kinase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT   DOMAIN          125..367
FT                   /note="Phosphagen kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   REGION          96..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..138
FT                   /note="Internal MTS-like signal"
FT                   /evidence="ECO:0000269|PubMed:33597756"
FT   COMPBIAS        96..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         128..132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         232
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         285
FT                   /ligand="creatine"
FT                   /ligand_id="ChEBI:CHEBI:57947"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         320..325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   BINDING         335
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   MOD_RES         35
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         125
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         269
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16800626"
FT   MOD_RES         309
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P07335"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        45
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   CROSSLNK        107
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   CROSSLNK        381
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P12277"
FT   MUTAGEN         130..138
FT                   /note="RVRTGRSIR->AVATGASIA: Abolishes localization to
FT                   mitochondria in fat cells."
FT                   /evidence="ECO:0000269|PubMed:33597756"
FT   MUTAGEN         283
FT                   /note="C->S: Abolished creatine kinase activity."
FT                   /evidence="ECO:0000269|PubMed:33597756"
FT   CONFLICT        143
FT                   /note="P -> H (in Ref. 3; BAE28690)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        217
FT                   /note="I -> M (in Ref. 3; BAE39162)"
FT                   /evidence="ECO:0000305"
SQ   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
//