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P05124

- KCRB_CANFA

UniProt

P05124 - KCRB_CANFA

Protein

Creatine kinase B-type

Gene

CKB

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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

    GO - Biological processi

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

    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
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Chromosome 8

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: AgBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase B-typePRO_0000211965Add
    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

    PaxDbiP05124.
    PRIDEiP05124.

    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

    STRINGi9615.ENSCAFP00000026998.

    Structurei

    3D structure databases

    ProteinModelPortaliP05124.
    SMRiP05124. 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.
    InParanoidiP05124.
    KOiK00933.
    OMAiQCLSDVR.
    OrthoDBiEOG7XM2XW.
    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.

    P05124-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG    50
    FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY 100
    KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE 150
    RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP 200
    LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF 250
    TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 300
    HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV 350
    QMVVDGVKLL IEMEQRLEQG QAIDDLVPAQ K 381
    Length:381
    Mass (Da):42,701
    Last modified:August 13, 1987 - v1
    Checksum:i2C2F925C78F16364
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13453 mRNA. Translation: AAA30837.1.
    PIRiA24227. B24686.
    RefSeqiXP_003639259.1. XM_003639211.2.

    Genome annotation databases

    EnsembliENSCAFT00000029035; ENSCAFP00000026998; ENSCAFG00000018277.
    GeneIDi100855552.
    KEGGicfa:100855552.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13453 mRNA. Translation: AAA30837.1 .
    PIRi A24227. B24686.
    RefSeqi XP_003639259.1. XM_003639211.2.

    3D structure databases

    ProteinModelPortali P05124.
    SMRi P05124. Positions 2-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9615.ENSCAFP00000026998.

    Proteomic databases

    PaxDbi P05124.
    PRIDEi P05124.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCAFT00000029035 ; ENSCAFP00000026998 ; ENSCAFG00000018277 .
    GeneIDi 100855552.
    KEGGi cfa:100855552.

    Organism-specific databases

    CTDi 1152.

    Phylogenomic databases

    eggNOGi COG3869.
    GeneTreei ENSGT00550000074561.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P05124.
    KOi K00933.
    OMAi QCLSDVR.
    OrthoDBi EOG7XM2XW.
    TreeFami TF314214.

    Miscellaneous databases

    NextBioi 20855457.

    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. "The complete nucleotide sequence of canine brain B creatine kinase mRNA: homology in the coding and 3' noncoding regions among species."
      Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W.
      Biochem. Biophys. Res. Commun. 138:392-398(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species."
      Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W.
      Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208; 224-236; 247-261; 268-287; 321-357 AND 364-381.
      Tissue: Brain.

    Entry informationi

    Entry nameiKCRB_CANFA
    AccessioniPrimary (citable) accession number: P05124
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 105 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3