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Q5XLD3

- KCRM_PIG

UniProt

Q5XLD3 - KCRM_PIG

Protein

Creatine kinase M-type

Gene

CKM

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 49 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      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: 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
    Gene namesi
    Name:CKM
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 381380Creatine kinase M-typePRO_0000211977Add
    BLAST

    Proteomic databases

    PRIDEiQ5XLD3.

    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

    3D structure databases

    ProteinModelPortaliQ5XLD3.
    SMRiQ5XLD3. 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

    HOVERGENiHBG001339.
    KOiK00933.

    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.

    Q5XLD3-1 [UniParc]FASTAAdd to Basket

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    MPFGNTHNKY KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG    50
    FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYVVFKDLFD PIIQDRHGGY 100
    KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE 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):43,059
    Last modified:November 23, 2004 - v1
    Checksum:iDF768FBFAF4E636D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY754869 mRNA. Translation: AAV28621.1.
    DQ153192 Genomic DNA. Translation: AAZ66747.1.
    RefSeqiNP_001123421.1. NM_001129949.1.
    UniGeneiSsc.415.

    Genome annotation databases

    GeneIDi397264.
    KEGGissc:397264.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY754869 mRNA. Translation: AAV28621.1 .
    DQ153192 Genomic DNA. Translation: AAZ66747.1 .
    RefSeqi NP_001123421.1. NM_001129949.1.
    UniGenei Ssc.415.

    3D structure databases

    ProteinModelPortali Q5XLD3.
    SMRi Q5XLD3. Positions 2-381.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5XLD3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397264.
    KEGGi ssc:397264.

    Organism-specific databases

    CTDi 1158.

    Phylogenomic databases

    HOVERGENi HBG001339.
    KOi K00933.

    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. "Molecular cloning and characterization of porcine CKM."
      Xu D.Q., Xiong Y.Z., Ling X.F., Lang J.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skeletal muscle.
    2. "Cloning and sequence analysis of genomic structure and the proximal promoter region of porcine CKM gene."
      Ling X.F., Xiong Y.Z., Xu D.Q.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiKCRM_PIG
    AccessioniPrimary (citable) accession number: Q5XLD3
    Secondary accession number(s): Q45EW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 49 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3