ID KCRB_HUMAN Reviewed; 381 AA. AC P12277; A8K236; B2R5R4; Q2LE07; Q6FG40; Q9UC66; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 27-MAR-2024, entry version 229. DE RecName: Full=Creatine kinase B-type {ECO:0000305}; DE EC=2.7.3.2 {ECO:0000269|PubMed:8186255}; DE AltName: Full=Brain creatine kinase {ECO:0000303|PubMed:2828370}; DE Short=B-CK; DE AltName: Full=Creatine kinase B chain {ECO:0000303|PubMed:3692484}; DE AltName: Full=Creatine phosphokinase B-type; DE Short=CPK-B; GN Name=CKB {ECO:0000312|HGNC:HGNC:1991}; Synonyms=CKBB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3034271; DOI=10.1016/0006-291x(87)91427-6; RA Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B.; RT "Human creatine kinase: isolation and sequence analysis of cDNA clones for RT the B subunit, development of subunit specific probes and determination of RT gene copy number."; RL Biochem. Biophys. Res. Commun. 144:1116-1127(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3692484; DOI=10.1016/0888-7543(87)90004-8; RA Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I., Wieringa B.; RT "Structure and expression of the human creatine kinase B gene."; RL Genomics 1:126-137(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2883200; DOI=10.1172/jci112969; RA Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A.; RT "Human creatine kinase-B complementary DNA. Nucleotide sequence, gene RT expression in lung cancer, and chromosomal assignment to two distinct RT loci."; RL J. Clin. Invest. 79:1412-1420(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=2771648; DOI=10.1093/nar/17.15.6385; RA Mariman E.C.M., Schepens J.T.G., Wieringa B.; RT "Complete nucleotide sequence of the human creatine kinase B gene."; RL Nucleic Acids Res. 17:6385-6385(1989). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum, and Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-177 AND LEU-309. RG NIEHS SNPs program; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Eye, and Lung; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97. RX PubMed=2828370; DOI=10.1016/s0021-9258(18)69226-9; RA Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P.; RT "Isolation of a functional human gene for brain creatine kinase."; RL J. Biol. Chem. 263:2442-2446(1988). RN [11] RP PROTEIN SEQUENCE OF 2-22. RC TISSUE=Eye; RX PubMed=7637327; RA Kliffen M., de Jong P.T.V.M., Luider T.M.; RT "Protein analysis of human maculae in relation to age-related RT maculopathy."; RL Lab. Invest. 73:267-272(1995). RN [12] RP PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314 AND RP 342-366, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Heiserich L., Gottlieb E.; RL Submitted (MAR-2008) to UniProtKB. RN [13] RP PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 157-172; 224-236; 253-265; RP 320-341 AND 359-381, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-283; ARG-292 AND RP ASP-340. RX PubMed=8186255; DOI=10.1016/0167-4838(94)90077-9; RA Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S.; RT "Determination of the catalytic site of creatine kinase by site-directed RT mutagenesis."; RL Biochim. Biophys. Acta 1206:97-104(1994). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-35, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CREATINE, RP ATP-BINDING SITES, SUBSTRATE-BINDING SITES, AND SUBUNIT. RX PubMed=18977227; DOI=10.1016/j.febslet.2008.10.039; RA Bong S.M., Moon J.H., Nam K.H., Lee K.S., Chi Y.M., Hwang K.Y.; RT "Structural studies of human brain-type creatine kinase complexed with the RT ADP-Mg2+-NO3- -creatine transition-state analogue complex."; RL FEBS Lett. 582:3959-3965(2008). RN [21] RP INTERACTION WITH SLC12A6, AND SUBCELLULAR LOCATION. 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). CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP CC and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). 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 (By similarity). During CC the futile creatine cycle, creatine and N-phosphocreatine are in a CC futile cycle, which dissipates the high energy charge of N- CC phosphocreatine as heat without performing any mechanical or chemical CC work (By similarity). {ECO:0000250|UniProtKB:Q04447, CC ECO:0000269|PubMed:8186255, ECO:0000305}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; 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:8186255}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17158; CC Evidence={ECO:0000269|PubMed:8186255}; 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 (PubMed:18566107). CC {ECO:0000269|PubMed:18566107, ECO:0000269|PubMed:18977227}. CC -!- INTERACTION: CC P12277; Q96DX5: ASB9; NbExp=10; IntAct=EBI-357706, EBI-745641; CC P12277; PRO_0000278738 [Q03463]; Xeno; NbExp=3; IntAct=EBI-357706, EBI-9081620; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q04447}. Mitochondrion CC {ECO:0000250|UniProtKB:Q04447}. Cell membrane CC {ECO:0000269|PubMed:18566107}. Note=Localizes to the mitochondria of CC thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. CC {ECO:0000250|UniProtKB:Q04447}. CC -!- DOMAIN: The internal MTS-like signal (iMTS-L) mediates targeting to CC mitochondria thermogenic fat cells. {ECO:0000250|UniProtKB:Q04447}. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE- CC ProRule:PRU00843}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ckb/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry; CC URL="https://en.wikipedia.org/wiki/Creatine_kinase"; 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; M16451; AAA76851.1; -; mRNA. DR EMBL; M21243; AAC31758.1; -; Genomic_DNA. DR EMBL; M21237; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; M21238; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; M21239; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; M21240; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; M21241; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; M21242; AAC31758.1; JOINED; Genomic_DNA. DR EMBL; L47647; AAA76852.1; -; mRNA. DR EMBL; M16364; AAA76850.1; -; mRNA. DR EMBL; X15334; CAA33389.1; -; Genomic_DNA. DR EMBL; AK290101; BAF82790.1; -; mRNA. DR EMBL; AK312282; BAG35211.1; -; mRNA. DR EMBL; CR542268; CAG47064.1; -; mRNA. DR EMBL; DQ333313; ABC67465.1; -; Genomic_DNA. DR EMBL; CH471061; EAW81822.1; -; Genomic_DNA. DR EMBL; BC001190; AAH01190.1; -; mRNA. DR EMBL; BC004914; AAH04914.1; -; mRNA. DR EMBL; BC008323; AAH08323.1; -; mRNA. DR EMBL; BC010002; AAH10002.1; -; mRNA. DR EMBL; BC019259; AAH19259.1; -; mRNA. DR EMBL; BC019281; AAH19281.1; -; mRNA. DR EMBL; M22356; AAA52024.1; -; Genomic_DNA. DR EMBL; M22355; AAA52024.1; JOINED; Genomic_DNA. DR CCDS; CCDS9981.1; -. DR PIR; S15935; KIHUCB. DR RefSeq; NP_001814.2; NM_001823.4. DR PDB; 3B6R; X-ray; 2.00 A; A/B=1-381. DR PDB; 3DRB; X-ray; 2.00 A; A/B=1-381. DR PDB; 3DRE; X-ray; 2.20 A; A/B=1-381. DR PDB; 6V9H; EM; 4.10 A; A/B=1-381. DR PDB; 7BF1; X-ray; 1.24 A; CCC/DDD=301-318. DR PDB; 7TUN; X-ray; 2.93 A; A/B=1-381. DR PDBsum; 3B6R; -. DR PDBsum; 3DRB; -. DR PDBsum; 3DRE; -. DR PDBsum; 6V9H; -. DR PDBsum; 7BF1; -. DR PDBsum; 7TUN; -. DR AlphaFoldDB; P12277; -. DR EMDB; EMD-21120; -. DR SMR; P12277; -. DR BioGRID; 107572; 250. DR CORUM; P12277; -. DR DIP; DIP-52968N; -. DR IntAct; P12277; 82. DR MINT; P12277; -. DR STRING; 9606.ENSP00000299198; -. DR ChEMBL; CHEMBL6049; -. DR DrugBank; DB00787; Acyclovir. DR DrugBank; DB00148; Creatine. DR DrugBank; DB13749; Magnesium gluconate. DR DrugBank; DB13191; Phosphocreatine. DR DrugBank; DB00300; Tenofovir disoproxil. DR CarbonylDB; P12277; -. DR GlyGen; P12277; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P12277; -. DR PhosphoSitePlus; P12277; -. DR SwissPalm; P12277; -. DR BioMuta; CKB; -. DR DMDM; 125294; -. DR REPRODUCTION-2DPAGE; IPI00022977; -. DR REPRODUCTION-2DPAGE; P12277; -. DR CPTAC; CPTAC-476; -. DR CPTAC; CPTAC-477; -. DR EPD; P12277; -. DR jPOST; P12277; -. DR MassIVE; P12277; -. DR PaxDb; 9606-ENSP00000299198; -. DR PeptideAtlas; P12277; -. DR ProteomicsDB; 52846; -. DR Pumba; P12277; -. DR TopDownProteomics; P12277; -. DR Antibodypedia; 28; 919 antibodies from 39 providers. DR CPTC; P12277; 3 antibodies. DR DNASU; 1152; -. DR Ensembl; ENST00000348956.7; ENSP00000299198.2; ENSG00000166165.14. DR GeneID; 1152; -. DR KEGG; hsa:1152; -. DR MANE-Select; ENST00000348956.7; ENSP00000299198.2; NM_001823.5; NP_001814.2. DR AGR; HGNC:1991; -. DR CTD; 1152; -. DR DisGeNET; 1152; -. DR GeneCards; CKB; -. DR HGNC; HGNC:1991; CKB. DR HPA; ENSG00000166165; Tissue enhanced (brain). DR MIM; 123280; gene. DR neXtProt; NX_P12277; -. DR OpenTargets; ENSG00000166165; -. DR PharmGKB; PA26528; -. DR VEuPathDB; HostDB:ENSG00000166165; -. DR eggNOG; KOG3581; Eukaryota. DR GeneTree; ENSGT00950000182772; -. DR HOGENOM; CLU_019868_4_2_1; -. DR InParanoid; P12277; -. DR OMA; NRGHEFM; -. DR OrthoDB; 35839at2759; -. DR PhylomeDB; P12277; -. DR TreeFam; TF314214; -. DR BioCyc; MetaCyc:HS09344-MONOMER; -. DR BRENDA; 2.7.3.2; 2681. DR PathwayCommons; P12277; -. DR Reactome; R-HSA-71288; Creatine metabolism. DR Reactome; R-HSA-9696264; RND3 GTPase cycle. DR SABIO-RK; P12277; -. DR SignaLink; P12277; -. DR SIGNOR; P12277; -. DR BioGRID-ORCS; 1152; 5 hits in 1161 CRISPR screens. DR ChiTaRS; CKB; human. DR EvolutionaryTrace; P12277; -. DR GeneWiki; CKB_(gene); -. DR GenomeRNAi; 1152; -. DR Pharos; P12277; Tbio. DR PRO; PR:P12277; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P12277; Protein. DR Bgee; ENSG00000166165; Expressed in right hemisphere of cerebellum and 200 other cell types or tissues. DR ExpressionAtlas; P12277; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; ISS:AgBase. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0140651; P:futile creatine cycle; IEA:Ensembl. DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB. DR CDD; cd00716; creatine_kinase_like; 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. DR UCD-2DPAGE; P12277; -. DR Genevisible; P12277; HS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Cytoplasm; KW Direct protein sequencing; Kinase; Membrane; Mitochondrion; Nitration; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7637327, ECO:0000269|Ref.12" FT CHAIN 2..381 FT /note="Creatine kinase B-type" FT /id="PRO_0000211966" 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..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 130..138 FT /note="Internal MTS-like signal" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT COMPBIAS 96..113 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:0000269|PubMed:18977227" FT BINDING 128..132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 130 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 232 FT /ligand="creatine" FT /ligand_id="ChEBI:CHEBI:57947" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 236 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 285 FT /ligand="creatine" FT /ligand_id="ChEBI:CHEBI:57947" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 320..325 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 320 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT BINDING 335 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18977227" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 35 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 125 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 269 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07335" FT MOD_RES 322 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q04447" FT VARIANT 177 FT /note="K -> R (in dbSNP:rs36002620)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025838" FT VARIANT 309 FT /note="S -> L (in dbSNP:rs35156510)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_025839" FT VARIANT 360 FT /note="L -> F (in dbSNP:rs12505)" FT /id="VAR_049674" FT MUTAGEN 283 FT /note="C->S,Y: Complete loss of activity." FT /evidence="ECO:0000269|PubMed:8186255" FT MUTAGEN 292 FT /note="R->H,L,Q: Complete loss of activity." FT /evidence="ECO:0000269|PubMed:8186255" FT MUTAGEN 292 FT /note="R->K: 42% of wild-type activity." FT /evidence="ECO:0000269|PubMed:8186255" FT MUTAGEN 340 FT /note="D->E: No change in activity." FT /evidence="ECO:0000269|PubMed:8186255" FT CONFLICT 41..42 FT /note="EL -> DV (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 78 FT /note="D -> G (in Ref. 3; AAA76850 and 10; AAA52024)" FT /evidence="ECO:0000305" FT CONFLICT 98..99 FT /note="GG -> RR (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 105..106 FT /note="EH -> DD (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="R -> G (in Ref. 3; AAA76850)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="R -> A (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="P -> Q (in Ref. 6; CAG47064)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="L -> S (in Ref. 2; AAC31758)" FT /evidence="ECO:0000305" FT CONFLICT 215..216 FT /note="RG -> AR (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 296 FT /note="H -> D (in Ref. 1; AAA76851)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="K -> R (in Ref. 5; BAG35211)" FT /evidence="ECO:0000305" FT HELIX 7..11 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 29..33 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 36..42 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 86..96 FT /evidence="ECO:0007829|PDB:3B6R" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:7TUN" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:3B6R" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 126..135 FT /evidence="ECO:0007829|PDB:3B6R" FT TURN 143..145 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 148..162 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 181..189 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:3B6R" FT TURN 204..214 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 216..220 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 223..244 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 246..266 FT /evidence="ECO:0007829|PDB:3B6R" FT TURN 275..277 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 308..314 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 325..330 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 333..338 FT /evidence="ECO:0007829|PDB:3B6R" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 346..368 FT /evidence="ECO:0007829|PDB:3B6R" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:3B6R" SQ SEQUENCE 381 AA; 42644 MW; 637AA67A86AE3059 CRC64; MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K //