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Q9XSC6 (KCRM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity.

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 By similarity. Ref.4

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processphosphocreatine biosynthetic process

Inferred from sequence or structural similarity. Source: AgBase

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

creatine kinase activity

Inferred from sequence or structural similarity. Source: AgBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380Creatine kinase M-type
PRO_0000211973

Regions

Domain11 – 9888Phosphagen kinase N-terminal
Domain125 – 367243Phosphagen kinase C-terminal
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

Natural variations

Natural variant3771I → M. Ref.1

Experimental info

Sequence conflict3761M → L in AAD30974. Ref.1

Secondary structure

1 ........................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9XSC6 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: C97EBBFB00BCF2FC

FASTA38142,989
        10         20         30         40         50         60 
MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF KPTDKHKTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 

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

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 

       310        320        330        340        350        360 
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K

« Hide

References

« Hide 'large scale' references
[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]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF120106 mRNA. Translation: AAD30974.1.
BT020785 mRNA. Translation: AAX08802.1.
BT021173 mRNA. Translation: AAX31355.1.
BC102907 mRNA. Translation: AAI02908.1.
IPIIPI00685709.
RefSeqNP_777198.2. NM_174773.4.
UniGeneBt.3651.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0WX-ray2.30A2-381[»]
ProteinModelPortalQ9XSC6.
SMRQ9XSC6. Positions 2-381.
ModBaseSearch...

Proteomic databases

PaxDbQ9XSC6.
PRIDEQ9XSC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921.
GeneID286822.
KEGGbta:286822.

Organism-specific databases

CTD1158.

Phylogenomic databases

eggNOGCOG3869.
GeneTreeENSGT00550000074561.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidQ9XSC6.
KOK00933.
OMAIRASVMM.
OrthoDBEOG4R7V9X.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERPTHR11547. PTHR11547. 1 hit.
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. ATP-gua_Ptrans. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9XSC6.
NextBio20806476.

Entry information

Entry nameKCRM_BOVIN
AccessionPrimary (citable) accession number: Q9XSC6
Secondary accession number(s): Q5E9Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: April 3, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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