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Q9XSC6

- KCRM_BOVIN

UniProt

Q9XSC6 - KCRM_BOVIN

Protein

Creatine kinase M-type

Gene

CKM

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (27 Jun 2006)
      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 By similarity.By similarity

    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: AgBase

    GO - Biological processi

    1. phosphocreatine biosynthetic process Source: AgBase

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_207339. Creatine metabolism.

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 18

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase M-typePRO_0000211973Add
    BLAST

    Proteomic databases

    PaxDbiQ9XSC6.
    PRIDEiQ9XSC6.

    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 By similarity.By similarity

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 115
    Helixi16 – 194
    Helixi29 – 335
    Helixi36 – 427
    Helixi53 – 6210
    Helixi81 – 844
    Helixi86 – 9611
    Turni97 – 993
    Helixi112 – 1143
    Turni123 – 1253
    Beta strandi126 – 13510
    Turni143 – 1453
    Helixi148 – 16215
    Helixi167 – 1693
    Beta strandi171 – 1755
    Helixi176 – 1783
    Helixi181 – 19010
    Helixi200 – 2034
    Turni204 – 21411
    Beta strandi216 – 2205
    Beta strandi225 – 24420
    Helixi246 – 26621
    Turni275 – 2773
    Helixi284 – 2863
    Beta strandi292 – 2987
    Turni300 – 3034
    Helixi308 – 3158
    Beta strandi317 – 3204
    Beta strandi332 – 3387
    Beta strandi342 – 3443
    Helixi346 – 35914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G0WX-ray2.30A7-359[»]
    ProteinModelPortaliQ9XSC6.
    SMRiQ9XSC6. Positions 2-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9XSC6.

    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.
    InParanoidiQ9XSC6.
    KOiK00933.
    OMAiGNTHNNF.
    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.

    Q9XSC6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG    50
    FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF 100
    KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE 150
    RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP 200
    LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF 250
    RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 300
    HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV 350
    QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K 381
    Length:381
    Mass (Da):42,989
    Last modified:June 27, 2006 - v2
    Checksum:iC97EBBFB00BCF2FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti376 – 3761M → L in AAD30974. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti377 – 3771I → M.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF120106 mRNA. Translation: AAD30974.1.
    BT020785 mRNA. Translation: AAX08802.1.
    BT021173 mRNA. Translation: AAX31355.1.
    BC102907 mRNA. Translation: AAI02908.1.
    RefSeqiNP_777198.2. NM_174773.4.
    UniGeneiBt.3651.

    Genome annotation databases

    EnsembliENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921.
    GeneIDi286822.
    KEGGibta:286822.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF120106 mRNA. Translation: AAD30974.1 .
    BT020785 mRNA. Translation: AAX08802.1 .
    BT021173 mRNA. Translation: AAX31355.1 .
    BC102907 mRNA. Translation: AAI02908.1 .
    RefSeqi NP_777198.2. NM_174773.4.
    UniGenei Bt.3651.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G0W X-ray 2.30 A 7-359 [» ]
    ProteinModelPortali Q9XSC6.
    SMRi Q9XSC6. Positions 2-381.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9XSC6.
    PRIDEi Q9XSC6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000018492 ; ENSBTAP00000018492 ; ENSBTAG00000013921 .
    GeneIDi 286822.
    KEGGi bta:286822.

    Organism-specific databases

    CTDi 1158.

    Phylogenomic databases

    eggNOGi COG3869.
    GeneTreei ENSGT00550000074561.
    HOGENOMi HOG000232165.
    HOVERGENi HBG001339.
    InParanoidi Q9XSC6.
    KOi K00933.
    OMAi GNTHNNF.
    OrthoDBi EOG7XM2XW.
    TreeFami TF314214.

    Enzyme and pathway databases

    Reactomei REACT_207339. Creatine metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q9XSC6.
    NextBioi 20806476.

    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. "Bovine creatine kinase M."
      Towler E.M.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-377.
      Tissue: Heart.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Heart ventricle.
    4. "The three-dimensional structure of cytosolic bovine retinal creatine kinase."
      Tisi D., Bax B., Loew A.
      Acta Crystallogr. D 57:187-193(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-359, SUBUNIT.

    Entry informationi

    Entry nameiKCRM_BOVIN
    AccessioniPrimary (citable) accession number: Q9XSC6
    Secondary accession number(s): Q5E9Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: June 27, 2006
    Last modified: October 1, 2014
    This is version 101 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

    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