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P00566

- KCRM_TORMA

UniProt

P00566 - KCRM_TORMA

Protein

Creatine kinase M-type

Gene
N/A
Organism
Torpedo marmorata (Marbled electric ray)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      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 sitei191 – 1911ATPPROSITE-ProRule annotation
    Binding sitei236 – 2361ATPPROSITE-ProRule annotation
    Binding sitei292 – 2921ATPPROSITE-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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase M-type (EC:2.7.3.2)
    Alternative name(s):
    Creatine kinase M chain
    M-CK
    NU-2 protein
    OrganismiTorpedo marmorata (Marbled electric ray)
    Taxonomic identifieri7788 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381Creatine kinase M-typePRO_0000211982Add
    BLAST

    Proteomic databases

    PRIDEiP00566.

    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.

    Structurei

    3D structure databases

    ProteinModelPortaliP00566.
    SMRiP00566. Positions 8-381.
    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

    HOVERGENiHBG001339.

    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.

    P00566-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG    50
    FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY 100
    KPTDKHKTDL NQDNLKGGDD LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE 150
    RRLVEKLCIE GLATLTGEFQ GKYYPLSTMS DAEQQQLIDD HFLFDKPISP 200
    LLLASGMARD WPDGRGIWHN NDKSFLVWVN EEDHLRVISM QKGGNMKEVF 250
    RRFCVGLKKI EEIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP 300
    HLCKHEKFSE VLKRTRLQKR GTGGVDTEAV GSIYDISNAD RLGFSEVEQV 350
    QMVVDGVKLM VEMEKRLENG KSIDDLIPAQ K 381
    Length:381
    Mass (Da):42,974
    Last modified:July 21, 1986 - v1
    Checksum:iAE0217EB65B8772C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11508 mRNA. Translation: AAA49277.1.
    PIRiA00676. KIRYCM.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11508 mRNA. Translation: AAA49277.1 .
    PIRi A00676. KIRYCM.

    3D structure databases

    ProteinModelPortali P00566.
    SMRi P00566. Positions 8-381.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P00566.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG001339.

    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. "Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase."
      Giraudat J., Devillers-Thiery A., Perriard J.-C., Changeux J.-P.
      Proc. Natl. Acad. Sci. U.S.A. 81:7313-7317(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Electric organ.

    Entry informationi

    Entry nameiKCRM_TORMA
    AccessioniPrimary (citable) accession number: P00566
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This electric ray muscle-specific creatine kinase (MM isozyme) is isolated from the electric organ, which derives embryologically from skeletal muscle. It may be involved in the electrical discharge process.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3