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P07335

- KCRB_RAT

UniProt

P07335 - KCRB_RAT

Protein

Creatine kinase B-type

Gene

Ckb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      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: RGD
    3. protein binding Source: RGD

    GO - Biological processi

    1. brain development Source: RGD
    2. cellular chloride ion homeostasis Source: RGD
    3. phosphocreatine metabolic process Source: RGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_212547. Creatine metabolism.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi2357. Ckb.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl
    2. plasma membrane Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase B-typePRO_0000211970Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Nitration, Phosphoprotein

    Proteomic databases

    PaxDbiP07335.
    PRIDEiP07335.

    2D gel databases

    World-2DPAGE0004:P07335.

    PTM databases

    PhosphoSiteiP07335.

    Expressioni

    Tissue specificityi

    In the kidney localized primarily in the outer medulla in the thick ascending limb and distal convoluted tubule.1 Publication

    Gene expression databases

    GenevestigatoriP07335.

    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

    BioGridi246448. 1 interaction.
    IntActiP07335. 1 interaction.
    MINTiMINT-4586357.

    Structurei

    3D structure databases

    ProteinModelPortaliP07335.
    SMRiP07335. Positions 2-381.
    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.
    InParanoidiP07335.
    KOiK00933.
    OMAiYMAKILT.
    OrthoDBiEOG7XM2XW.
    PhylomeDBiP07335.
    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.

    P07335-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG    50
    FTLDDAIQTG VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEDRHGGY 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 QPIDDLMPAQ K 381
    Length:381
    Mass (Da):42,725
    Last modified:January 9, 2007 - v2
    Checksum:iA8C8A09F6FF1A4D1
    GO

    Sequence cautioni

    The sequence AAH87656.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181D → A in AAA40931. (PubMed:2284002)Curated
    Sequence conflicti18 – 181D → A in AAA40933. (PubMed:2284002)Curated
    Sequence conflicti183 – 1842EQ → DE in AAA40930. (PubMed:3005113)Curated
    Sequence conflicti183 – 1842EQ → DE in AAA40932. (PubMed:2838389)Curated
    Sequence conflicti206 – 2061G → A in AAA40932. (PubMed:2838389)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14400 mRNA. Translation: AAA40930.1.
    M18668 Genomic DNA. Translation: AAA40932.1.
    M57664 mRNA. Translation: AAA40933.1.
    M57665 Genomic DNA. Translation: AAA40931.1.
    BC065307 mRNA. Translation: AAH65307.2.
    BC070955 mRNA. Translation: AAH70955.2.
    BC087656 mRNA. Translation: AAH87656.1. Different initiation.
    BC099814 mRNA. Translation: AAH99814.2.
    BC127477 mRNA. Translation: AAI27478.2.
    PIRiA23980. KIRTCB.
    RefSeqiNP_036661.3. NM_012529.3.
    UniGeneiRn.1472.

    Genome annotation databases

    EnsembliENSRNOT00000015122; ENSRNOP00000015122; ENSRNOG00000010872.
    GeneIDi24264.
    KEGGirno:24264.
    UCSCiRGD:2357. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14400 mRNA. Translation: AAA40930.1 .
    M18668 Genomic DNA. Translation: AAA40932.1 .
    M57664 mRNA. Translation: AAA40933.1 .
    M57665 Genomic DNA. Translation: AAA40931.1 .
    BC065307 mRNA. Translation: AAH65307.2 .
    BC070955 mRNA. Translation: AAH70955.2 .
    BC087656 mRNA. Translation: AAH87656.1 . Different initiation.
    BC099814 mRNA. Translation: AAH99814.2 .
    BC127477 mRNA. Translation: AAI27478.2 .
    PIRi A23980. KIRTCB.
    RefSeqi NP_036661.3. NM_012529.3.
    UniGenei Rn.1472.

    3D structure databases

    ProteinModelPortali P07335.
    SMRi P07335. Positions 2-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246448. 1 interaction.
    IntActi P07335. 1 interaction.
    MINTi MINT-4586357.

    Chemistry

    ChEMBLi CHEMBL2176812.

    PTM databases

    PhosphoSitei P07335.

    2D gel databases

    World-2DPAGE 0004:P07335.

    Proteomic databases

    PaxDbi P07335.
    PRIDEi P07335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015122 ; ENSRNOP00000015122 ; ENSRNOG00000010872 .
    GeneIDi 24264.
    KEGGi rno:24264.
    UCSCi RGD:2357. rat.

    Organism-specific databases

    CTDi 1152.
    RGDi 2357. Ckb.

    Phylogenomic databases

    eggNOGi COG3869.
    GeneTreei ENSGT00550000074561.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P07335.
    KOi K00933.
    OMAi YMAKILT.
    OrthoDBi EOG7XM2XW.
    PhylomeDBi P07335.
    TreeFami TF314214.

    Enzyme and pathway databases

    Reactomei REACT_212547. Creatine metabolism.

    Miscellaneous databases

    NextBioi 602815.

    Gene expression databases

    Genevestigatori P07335.

    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. "Expression of a rat brain creatine kinase-beta-galactosidase fusion protein in Escherichia coli and derivation of the complete amino acid sequence of rat brain creatine kinase."
      Benfield P.A., Henderson L., Pearson M.L.
      Gene 39:263-267(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation of four rat creatine kinase genes and identification of multiple potential promoter sequences within the rat brain creatine kinase promoter region."
      Benfield P.A., Graf D., Korolkoff P.N., Hobson G., Pearson M.L.
      Gene 63:227-243(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Estrogen regulation of creatine kinase-B in the rat uterus."
      Pentecost B.T., Mattheiss L., Dickerman H.W., Kumar S.A.
      Mol. Endocrinol. 4:1000-1010(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Tissue: Uterus.
    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].
      Tissue: Brain, Embryonic brain, Heart and Prostate.
    5. Lubec G., Afjehi-Sadat L., Diao W., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 138-148; 157-172; 224-236; 253-265 AND 320-341, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.
    6. "The brain isoform of a key ATP-regulating enzyme, creatine kinase, is a phosphoprotein."
      Mahadevan L.C., Whatley S.A., Leung T.K.C., Lim L.
      Biochem. J. 222:139-144(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    7. "Compartmentation of multiple forms of creatine kinase in the distal nephron of the rat kidney."
      Friedman D.L., Perryman M.B.
      J. Biol. Chem. 266:22404-22410(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiKCRB_RAT
    AccessioniPrimary (citable) accession number: P07335
    Secondary accession number(s): A0JPK7
    , Q499P7, Q5PPJ5, Q6IRE0, Q6P139
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3