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Reviewed, UniProtKB/Swiss-Prot P00565 (KCRM_CHICK)

Last modified June 16, 2009. Version 63. Feed History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Creatine kinase M-type
    EC=2.7.3.2
Alternative name(s):
    Creatine kinase M chain
    M-CK
Gene names
Name: CKM
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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 activity

ATP + creatine = ADP + phosphocreatine.

Subunit structure

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.

Subcellular location

Cytoplasm.

Tissue specificity

Predominantly found in skeletal muscle, but not in the heart.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

creatine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Creatine kinase M-type
PRO_0000211980

Regions

Nucleotide binding128 – 1325ATP By similarity
Nucleotide binding320 – 3256ATP By similarity

Sites

Binding site1911ATP By similarity
Binding site2361ATP By similarity
Binding site2921ATP By similarity
Binding site3351ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P00565-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 192C236BB46E2531

FASTA38143,328
        10         20         30         40         50         60 
MPFSSTHNKH KLKFSAEEEF PDLSKHNNHM AKVLTPELYK RLRDKETPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEVFKDLFD PVIQDRHGGY KPTDKHRTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPKYVLSSR VRTGRSIKGY SLPPHCSRGE RRAVEKLSVE ALNSLEGEFK GRYYPLKAMT 

       190        200        210        220        230        240 
EQEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM 

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLKKI EEIFKKAGHP FMWTEHLGYI LTCPSNLGTG LRGGVHVKLP 

       310        320        330        340        350        360 
KLSQHPKFEE ILHRLRLQKR GTGGVDTAAV GAVFDISNAD RLGFSEVEQV QMVVDGVKLM 

       370        380 
VEMEKKLEQN QPIDDMIPAQ K 

« Hide

References

[1]"Molecular cloning and the complete nucleotide sequence of the creatine kinase-M cDNA from chicken."
Kwiatkowski R.W., Schweinfest C.W., Dottin R.P.
Nucleic Acids Res. 12:6925-6934(1984) [PubMed: 6091045] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete cDNA-derived amino acid sequence of chick muscle creatine kinase."
Ordahl C.P., Evans G.L., Cooper T.A., Kunz G., Perriard J.-C.
J. Biol. Chem. 259:15224-15227(1984) [PubMed: 6096363] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

M10012 mRNA. Translation: AAA48689.1.
X00954 mRNA. Translation: CAA25465.1.
X00954 mRNA. Translation: CAA25466.2.
IPIIPI00592568.
PIRKICHCM. A00675.
RefSeqNP_990838.1.
UniGeneGga.4308

3D structure databases

HSSPHSSP built from PDB template 2CRK based on UniProtKB P00563.
SMRP00565. Positions 2-381.
ModBaseSearch...

Genome annotation databases

GeneID396507.
KEGGgga:396507.

Phylogenomic databases

HOVERGENP00565.

Enzyme and pathway databases

BRENDA2.7.3.2. 4.

Family and domain databases

InterProIPR000749. ATP-guanido_PTrfase.
IPR014746. Gln_synth/guanido_kin_cat.
[Graphical view]
Gene3DG3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit.
G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PANTHERPTHR11547. ATP-gua_Ptrans. 1 hit.
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
PROSITEPS00112. GUANIDO_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKCRM_CHICK
AccessionPrimary (citable) accession number: P00565
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents