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Q04447

- KCRB_MOUSE

UniProt

Q04447 - KCRB_MOUSE

Protein

Creatine kinase B-type

Gene

Ckb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + creatine = ADP + phosphocreatine.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei130 – 1301ATPPROSITE-ProRule annotation
    Binding sitei132 – 1321ATPPROSITE-ProRule annotation
    Binding sitei191 – 1911ATPPROSITE-ProRule annotation
    Binding sitei232 – 2321SubstrateBy similarity
    Binding sitei236 – 2361ATPPROSITE-ProRule annotation
    Binding sitei285 – 2851SubstrateBy similarity
    Binding sitei292 – 2921ATPPROSITE-ProRule annotation
    Binding sitei320 – 3201ATPPROSITE-ProRule annotation
    Binding sitei335 – 3351ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi128 – 1325ATPPROSITE-ProRule annotation
    Nucleotide bindingi320 – 3256ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. creatine kinase activity Source: UniProtKB-EC
    3. protein binding Source: MGI

    GO - Biological processi

    1. brain development Source: Ensembl
    2. cellular chloride ion homeostasis Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase B-type (EC:2.7.3.2)
    Alternative name(s):
    B-CK
    Creatine kinase B chain
    Gene namesi
    Name:Ckb
    Synonyms:Ckbb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:88407. Ckb.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase B-typePRO_0000211967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei4 – 41PhosphoserineBy similarity
    Modified residuei35 – 351PhosphothreonineBy similarity
    Modified residuei125 – 1251Phosphotyrosine1 Publication
    Modified residuei199 – 1991PhosphoserineBy similarity
    Modified residuei269 – 2691Nitrated tyrosine1 Publication

    Keywords - PTMi

    Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiQ04447.
    PaxDbiQ04447.
    PRIDEiQ04447.

    2D gel databases

    REPRODUCTION-2DPAGEQ04447.
    UCD-2DPAGEQ04447.

    PTM databases

    PhosphoSiteiQ04447.

    Expressioni

    Gene expression databases

    BgeeiQ04447.
    CleanExiMM_CKB.
    GenevestigatoriQ04447.

    Interactioni

    Subunit structurei

    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.

    Protein-protein interaction databases

    BioGridi198725. 2 interactions.
    IntActiQ04447. 8 interactions.
    MINTiMINT-4099724.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04447.
    SMRiQ04447. Positions 6-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 9888Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 367243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3869.
    GeneTreeiENSGT00550000074561.
    HOGENOMiHOG000232165.
    HOVERGENiHBG001339.
    InParanoidiQ04447.
    KOiK00933.
    OMAiQCLSDVR.
    OrthoDBiEOG7XM2XW.
    PhylomeDBiQ04447.
    TreeFamiTF314214.

    Family and domain databases

    Gene3Di1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProiIPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view]
    PfamiPF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view]
    SUPFAMiSSF48034. SSF48034. 1 hit.
    PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q04447-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG    50
    FTLDDAIQTG VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY 100
    QPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE 150
    RRAIEKLAVE ALSSLDGDLS GRYYALKSMT EAEQQQLIDD HFLFDKPVSP 200
    LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF 250
    TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 300
    HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV 350
    QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K 381
    Length:381
    Mass (Da):42,713
    Last modified:October 1, 1993 - v1
    Checksum:iD901C5653054A490
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431P → H in BAE28690. (PubMed:16141072)Curated
    Sequence conflicti217 – 2171I → M in BAE39162. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74149 Genomic DNA. Translation: AAA37462.1.
    L09069 Genomic DNA. Translation: AAA37455.1.
    AK002467 mRNA. Translation: BAB22121.1.
    AK014299 mRNA. Translation: BAB29254.1.
    AK148885 mRNA. Translation: BAE28690.1.
    AK152388 mRNA. Translation: BAE31176.1.
    AK153484 mRNA. Translation: BAE32032.1.
    AK166980 mRNA. Translation: BAE39162.1.
    AK161990 mRNA. Translation: BAE36669.1.
    AK167034 mRNA. Translation: BAE39205.1.
    BC015271 mRNA. Translation: AAH15271.1.
    BC106109 mRNA. Translation: AAI06110.2.
    X04591 mRNA. Translation: CAA28259.1.
    CCDSiCCDS26183.1.
    PIRiA42078.
    RefSeqiNP_067248.1. NM_021273.4.
    UniGeneiMm.16831.

    Genome annotation databases

    EnsembliENSMUST00000001304; ENSMUSP00000001304; ENSMUSG00000001270.
    GeneIDi12709.
    KEGGimmu:12709.
    UCSCiuc007pdn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M74149 Genomic DNA. Translation: AAA37462.1 .
    L09069 Genomic DNA. Translation: AAA37455.1 .
    AK002467 mRNA. Translation: BAB22121.1 .
    AK014299 mRNA. Translation: BAB29254.1 .
    AK148885 mRNA. Translation: BAE28690.1 .
    AK152388 mRNA. Translation: BAE31176.1 .
    AK153484 mRNA. Translation: BAE32032.1 .
    AK166980 mRNA. Translation: BAE39162.1 .
    AK161990 mRNA. Translation: BAE36669.1 .
    AK167034 mRNA. Translation: BAE39205.1 .
    BC015271 mRNA. Translation: AAH15271.1 .
    BC106109 mRNA. Translation: AAI06110.2 .
    X04591 mRNA. Translation: CAA28259.1 .
    CCDSi CCDS26183.1.
    PIRi A42078.
    RefSeqi NP_067248.1. NM_021273.4.
    UniGenei Mm.16831.

    3D structure databases

    ProteinModelPortali Q04447.
    SMRi Q04447. Positions 6-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198725. 2 interactions.
    IntActi Q04447. 8 interactions.
    MINTi MINT-4099724.

    PTM databases

    PhosphoSitei Q04447.

    2D gel databases

    REPRODUCTION-2DPAGE Q04447.
    UCD-2DPAGE Q04447.

    Proteomic databases

    MaxQBi Q04447.
    PaxDbi Q04447.
    PRIDEi Q04447.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001304 ; ENSMUSP00000001304 ; ENSMUSG00000001270 .
    GeneIDi 12709.
    KEGGi mmu:12709.
    UCSCi uc007pdn.2. mouse.

    Organism-specific databases

    CTDi 1152.
    MGIi MGI:88407. Ckb.

    Phylogenomic databases

    eggNOGi COG3869.
    GeneTreei ENSGT00550000074561.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi Q04447.
    KOi K00933.
    OMAi QCLSDVR.
    OrthoDBi EOG7XM2XW.
    PhylomeDBi Q04447.
    TreeFami TF314214.

    Miscellaneous databases

    NextBioi 281980.
    PROi Q04447.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q04447.
    CleanExi MM_CKB.
    Genevestigatori Q04447.

    Family and domain databases

    Gene3Di 1.10.135.10. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR022415. ATP-guanido_PTrfase_AS.
    IPR022414. ATP-guanido_PTrfase_cat.
    IPR022413. ATP-guanido_PTrfase_N.
    IPR014746. Gln_synth/guanido_kin_cat_dom.
    [Graphical view ]
    Pfami PF00217. ATP-gua_Ptrans. 1 hit.
    PF02807. ATP-gua_PtransN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48034. SSF48034. 1 hit.
    PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
    PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
    PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genetic variability of the murine creatine kinase B gene locus and related pseudogenes in different inbred strains of mice."
      van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G., Hendriks W., Wieringa B.
      Genomics 12:340-349(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Pentecost B.T.
      Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryonic head, Kidney, Sympathetic ganglion and Wolffian duct.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    5. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209; 224-236; 253-265; 268-292 AND 320-381, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. "The 3' non-coding region of the mouse brain B creatine kinase mRNA: a sequence with exceptional homology among species."
      Papenbrock T., Wille W.
      Nucleic Acids Res. 14:8690-8690(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    7. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
      Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
      Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.

    Entry informationi

    Entry nameiKCRB_MOUSE
    AccessioniPrimary (citable) accession number: Q04447
    Secondary accession number(s): Q3KQP4
    , Q3TKI3, Q3U5P5, Q3UF71, Q9CXK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3