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P00563

- KCRM_RABIT

UniProt

P00563 - KCRM_RABIT

Protein

Creatine kinase M-type

Gene

CKM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (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.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei191 – 1911ATP
    Binding sitei236 – 2361ATP
    Binding sitei292 – 2921ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi128 – 1325ATP
    Nucleotide bindingi320 – 3256ATP

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP00563.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase M-type (EC:2.7.3.2)
    Alternative name(s):
    Creatine kinase M chain
    M-CK
    Gene namesi
    Name:CKM
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase M-typePRO_0000211978Add
    BLAST

    Proteomic databases

    PRIDEiP00563.

    Miscellaneous databases

    PMAP-CutDBP00563.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKMP119742EBI-2750756,EBI-7133357

    Protein-protein interaction databases

    IntActiP00563. 1 interaction.
    MINTiMINT-6824935.
    STRINGi9986.ENSOCUP00000020805.

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 116
    Helixi16 – 194
    Helixi29 – 335
    Helixi36 – 427
    Helixi53 – 6210
    Beta strandi77 – 793
    Helixi81 – 844
    Helixi86 – 9611
    Turni97 – 993
    Helixi112 – 1143
    Turni123 – 1253
    Beta strandi126 – 13510
    Turni143 – 1453
    Helixi148 – 16316
    Helixi167 – 1693
    Beta strandi171 – 1755
    Helixi176 – 1783
    Helixi181 – 1899
    Helixi200 – 2034
    Turni204 – 21411
    Beta strandi216 – 2205
    Beta strandi225 – 24420
    Helixi246 – 26722
    Turni275 – 2773
    Helixi284 – 2863
    Beta strandi292 – 2987
    Helixi300 – 3034
    Helixi308 – 3158
    Beta strandi317 – 3204
    Beta strandi322 – 3243
    Beta strandi333 – 3386
    Beta strandi342 – 3443
    Helixi346 – 36924
    Beta strandi374 – 3763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U6RX-ray1.65A/B2-381[»]
    2CRKX-ray2.35A1-381[»]
    ProteinModelPortaliP00563.
    SMRiP00563. Positions 2-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00563.

    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.
    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.

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

    P00563-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG    50
    FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF 100
    KPTDKHKTDL NHENLKGGDD LDPHYVLSSR VRTGRSIKGY TLPPHCSRGE 150
    RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP 200
    LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF 250
    RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 300
    HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV 350
    QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K 381
    Length:381
    Mass (Da):43,112
    Last modified:July 21, 1986 - v1
    Checksum:i821447F395FE71CC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02831 mRNA. Translation: AAA31205.1.
    PIRiA00673. KIRBCM.
    RefSeqiNP_001075708.1. NM_001082239.1.
    UniGeneiOcu.6249.

    Genome annotation databases

    GeneIDi100009056.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02831 mRNA. Translation: AAA31205.1 .
    PIRi A00673. KIRBCM.
    RefSeqi NP_001075708.1. NM_001082239.1.
    UniGenei Ocu.6249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U6R X-ray 1.65 A/B 2-381 [» ]
    2CRK X-ray 2.35 A 1-381 [» ]
    ProteinModelPortali P00563.
    SMRi P00563. Positions 2-381.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00563. 1 interaction.
    MINTi MINT-6824935.
    STRINGi 9986.ENSOCUP00000020805.

    Chemistry

    ChEMBLi CHEMBL1075201.

    Proteomic databases

    PRIDEi P00563.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009056.

    Organism-specific databases

    CTDi 1158.

    Phylogenomic databases

    eggNOGi COG3869.
    HOVERGENi HBG001339.

    Enzyme and pathway databases

    SABIO-RK P00563.

    Miscellaneous databases

    EvolutionaryTracei P00563.
    PMAP-CutDB P00563.

    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. "Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences."
      Pickering L., Pang H., Biemann K., Munro H., Schimmel P.
      Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and detection of human homologues."
      Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.
      J. Biol. Chem. 259:14317-14320(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Brain adenosine 5'-triphosphate-creatine phosphotransferase."
      Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.
      Biochem. J. 120:589-600(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION.
    4. "Crystal structure of rabbit muscle creatine kinase."
      Rao J.K., Bujacz G., Wlodawer A.
      FEBS Lett. 439:133-137(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
      Tissue: Muscle.
    5. "Structural asymmetry and intersubunit communication in muscle creatine kinase."
      Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.
      Acta Crystallogr. D 63:381-389(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiKCRM_RABIT
    AccessioniPrimary (citable) accession number: P00563
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 100 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3