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P11009

- KCRS_CHICK

UniProt

P11009 - KCRS_CHICK

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Protein
Creatine kinase S-type, mitochondrial
Gene
CKMT2
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251ATP By similarity
Binding sitei270 – 2701ATP By similarity
Binding sitei326 – 3261ATP By similarity
Binding sitei369 – 3691ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665ATP By similarity
Nucleotide bindingi354 – 3596ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. creatine kinase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKP11009.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Creatine kinase S-type, mitochondrial (EC:2.7.3.2)
    Alternative name(s):
    Basic-type mitochondrial creatine kinase
    Short name:
    Mib-CK
    Sarcomeric mitochondrial creatine kinase
    Short name:
    S-MtCK
    Gene namesi
    Name:CKMT2
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939Mitochondrion2 Publications
    Add
    BLAST
    Chaini40 – 419380Creatine kinase S-type, mitochondrial
    PRO_0000016599Add
    BLAST

    Proteomic databases

    PaxDbiP11009.
    PRIDEiP11009.

    Expressioni

    Tissue specificityi

    Expressed in the leg muscle and heart.

    Interactioni

    Subunit structurei

    Exists as an octamer composed of four MTCK homodimers.1 Publication

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000032149.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi50 – 534
    Helixi63 – 675
    Helixi70 – 767
    Helixi87 – 9610
    Helixi115 – 1184
    Helixi120 – 13011
    Turni131 – 1333
    Turni136 – 1383
    Helixi147 – 1493
    Turni157 – 1593
    Beta strandi160 – 16910
    Turni177 – 1793
    Helixi182 – 19716
    Helixi201 – 2033
    Beta strandi205 – 2128
    Helixi215 – 2239
    Helixi234 – 2374
    Turni238 – 2403
    Turni243 – 2486
    Beta strandi250 – 2545
    Beta strandi259 – 27820
    Helixi280 – 30021
    Turni309 – 3113
    Helixi318 – 3203
    Beta strandi326 – 3327
    Helixi334 – 3385
    Helixi342 – 3498
    Beta strandi351 – 3544
    Turni359 – 3635
    Beta strandi367 – 3726
    Beta strandi375 – 3784
    Helixi380 – 40223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CRKX-ray3.00A/B/C/D40-419[»]
    ProteinModelPortaliP11009.
    SMRiP11009. Positions 40-419.

    Miscellaneous databases

    EvolutionaryTraceiP11009.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 13287Phosphagen kinase N-terminal
    Add
    BLAST
    Domaini159 – 401243Phosphagen kinase C-terminal
    Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG3869.
    HOGENOMiHOG000232165.
    HOVERGENiHBG001339.
    InParanoidiP11009.
    KOiK00933.
    PhylomeDBiP11009.

    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.

    P11009-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGTFGRLLA GRVTAALFAA AGSGVLTTGY LLNQQNVKAT VHEKRKLFPP    50
    SADYPDLRKH NNCMAECLTP AIYAKLRDKL TPNGYSLDQC IQTGVDNPGH 100
    PFIKTVGMVA GDEESYEVFA EIFDPVIKAR HNGYDPRTMK HHTDLDASKI 150
    THGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAERREVEN VVVTALAGLK 200
    GDLSGKYYSL TNMSERDQQQ LIDDHFLFDK PVSPLLTCAG MARDWPDARG 250
    IWHNNDKTFL VWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIKE 300
    RGWEFMWNER LGYVLTCPSN LGTGLRAGVH VKLPRLSKDP RFPKILENLR 350
    LQKRGTGGVD TAAVADVYDI SNLDRMGRSE VELVQIVIDG VNYLVDCEKK 400
    LEKGQDIKVP PPLPQFGRK 419
    Length:419
    Mass (Da):47,084
    Last modified:July 15, 1998 - v2
    Checksum:i9ACC60D709B9283F
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 234AAGS → CSRQ in AAA48688. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18866 mRNA. Translation: AAA48688.1.
    PIRiA27708.
    RefSeqiNP_001161216.1. NM_001167744.1.
    UniGeneiGga.869.

    Genome annotation databases

    GeneIDi396508.
    KEGGigga:396508.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18866 mRNA. Translation: AAA48688.1 .
    PIRi A27708.
    RefSeqi NP_001161216.1. NM_001167744.1.
    UniGenei Gga.869.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CRK X-ray 3.00 A/B/C/D 40-419 [» ]
    ProteinModelPortali P11009.
    SMRi P11009. Positions 40-419.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000032149.

    Proteomic databases

    PaxDbi P11009.
    PRIDEi P11009.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396508.
    KEGGi gga:396508.

    Organism-specific databases

    CTDi 1160.

    Phylogenomic databases

    eggNOGi COG3869.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi P11009.
    KOi K00933.
    PhylomeDBi P11009.

    Enzyme and pathway databases

    SABIO-RK P11009.

    Miscellaneous databases

    EvolutionaryTracei P11009.
    NextBioi 20816547.
    PROi P11009.

    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. "Evolution of the creative kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene."
      Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.
      J. Biol. Chem. 271:11920-11929(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
      Strain: White leghorn.
    2. "Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework."
      Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P., Eppenberger H.M., Wallimann T., Perriard J.-C.
      Biochem. Biophys. Res. Commun. 151:408-416(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-419, PROTEIN SEQUENCE OF 40-69.
      Tissue: Heart and Skeletal muscle.
    3. "The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization."
      Kaldis P., Furter R., Wallimann T.
      Biochemistry 33:952-959(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-48.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiKCRS_CHICK
    AccessioniPrimary (citable) accession number: P11009
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 15, 1998
    Last modified: April 16, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mitochondrial creatine kinase binds cardiolipin.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

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