KCRB_HUMAN
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 03-AUG-2022, entry version 220.
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).
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.
CC {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}. 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";
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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 PDBsum; 3B6R; -.
DR PDBsum; 3DRB; -.
DR PDBsum; 3DRE; -.
DR PDBsum; 6V9H; -.
DR PDBsum; 7BF1; -.
DR AlphaFoldDB; P12277; -.
DR SMR; P12277; -.
DR BioGRID; 107572; 205.
DR CORUM; P12277; -.
DR DIP; DIP-52968N; -.
DR IntAct; P12277; 76.
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 UCD-2DPAGE; P12277; -.
DR CPTAC; CPTAC-476; -.
DR CPTAC; CPTAC-477; -.
DR EPD; P12277; -.
DR jPOST; P12277; -.
DR MassIVE; P12277; -.
DR PaxDb; P12277; -.
DR PeptideAtlas; P12277; -.
DR PRIDE; P12277; -.
DR ProteomicsDB; 52846; -.
DR TopDownProteomics; P12277; -.
DR Antibodypedia; 28; 840 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 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 PhylomeDB; P12277; -.
DR TreeFam; TF314214; -.
DR BioCyc; MetaCyc:HS09344-MON; -.
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 1075 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 198 other tissues.
DR ExpressionAtlas; P12277; baseline and differential.
DR Genevisible; P12277; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
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:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; 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 Gene3D; 1.10.135.10; -; 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; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 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 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Mitochondrion; Nitration; Nucleotide-binding; Phosphoprotein;
KW 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 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
