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P06732 (KCRM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase M-type

EC=2.7.3.2
Alternative name(s):
Creatine kinase M chain
M-CK

Cleaved into the following chain:

  1. Creatine kinase M-type, N-terminally processed
Gene names
Name:CKM
Synonyms:CKMM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

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.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Creatine kinase M-type
PRO_0000211975
Initiator methionine11Removed; alternate By similarity
Chain2 – 381380Creatine kinase M-type, N-terminally processed
PRO_0000421788

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 variant831E → G. Ref.4
Corresponds to variant rs11559024 [ dbSNP | Ensembl ].
VAR_018680
Natural variant1271L → V. Ref.4
Corresponds to variant rs17875653 [ dbSNP | Ensembl ].
VAR_018681
Natural variant1661T → M.
Corresponds to variant rs17357122 [ dbSNP | Ensembl ].
VAR_049675
Natural variant2431G → A. Ref.4
Corresponds to variant rs17875625 [ dbSNP | Ensembl ].
VAR_018682

Experimental info

Sequence conflict471T → I in AAA52025. Ref.1
Sequence conflict1301R → P in AAA52025. Ref.1
Sequence conflict1931L → Q in AAA52025. Ref.1
Sequence conflict2101D → H in AAA52025. Ref.1
Sequence conflict2151R → P in AAA52025. Ref.1
Sequence conflict2251F → L in AAP35439. Ref.3
Sequence conflict2251F → L in AAH07462. Ref.6
Sequence conflict3241G → A in AAA52025. Ref.1

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P06732 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 418FEAD0C2E138C8

FASTA38143,101
        10         20         30         40         50         60 
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD 

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

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

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV 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]"Isolation and sequence analysis of a full-length cDNA for human M creatine kinase."
Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R.
Biochem. Biophys. Res. Commun. 140:981-989(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene."
Trask R.V., Strauss A.W., Billadello J.J.
J. Biol. Chem. 263:17142-17149(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]SeattleSNPs variation discovery resource
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-83; VAL-127 AND ALA-243.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[7]"Muscle creatine kinase isoenzyme expression in adult human brain."
Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D., Goodman C., Puleo P.R., Perryman M.B.
J. Biol. Chem. 265:6403-6409(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30.
Tissue: Brain.
[8]"cDNA cloning and mapping of the human creatine kinase M gene to 19q13."
Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S., Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D., Martin-Deleon P.
Am. J. Hum. Genet. 40:115-125(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 257-327.
[9]"Crystallization and preliminary X-ray analysis of human muscle creatine kinase."
Tang L., Zhou H.M., Lin Z.J.
Acta Crystallogr. D 55:669-670(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Wikipedia

Creatine kinase entry

SeattleSNPs
Wikipedia

CKM entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14780 mRNA. Translation: AAA52025.1.
M21494 expand/collapse EMBL AC list , M21488, M21489, M21490, M21491, M21492, M21493 Genomic DNA. Translation: AAA96609.1.
BT006793 mRNA. Translation: AAP35439.1.
AY585238 Genomic DNA. Translation: AAS79321.1.
AC005781 Genomic DNA. Translation: AAC62841.1.
BC007462 mRNA. Translation: AAH07462.1.
M16440 mRNA. Translation: AAA52026.1. Sequence problems.
PIRKIHUCM. A31793.
RefSeqNP_001815.2. NM_001824.4.
UniGeneHs.334347.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0EX-ray3.50A/B/C/D1-381[»]
ProteinModelPortalP06732.
SMRP06732. Positions 8-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107578. 9 interactions.
IntActP06732. 2 interactions.
STRING9606.ENSP00000221476.

Chemistry

BindingDBP06732.
ChEMBLCHEMBL2656.
DrugBankDB00148. Creatine.

PTM databases

PhosphoSiteP06732.

Polymorphism databases

DMDM125305.

2D gel databases

UCD-2DPAGEP06732.

Proteomic databases

PaxDbP06732.
PeptideAtlasP06732.
PRIDEP06732.

Protocols and materials databases

DNASU1158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221476; ENSP00000221476; ENSG00000104879.
GeneID1158.
KEGGhsa:1158.
UCSCuc002pbd.4. human.

Organism-specific databases

CTD1158.
GeneCardsGC19M045809.
HGNCHGNC:1994. CKM.
HPAHPA047859.
MIM123310. gene.
neXtProtNX_P06732.
PharmGKBPA26532.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP06732.
KOK00933.
OMAMTQPGFL.
OrthoDBEOG7XM2XW.
PhylomeDBP06732.
TreeFamTF314214.

Enzyme and pathway databases

BioCycMetaCyc:HS02640-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP06732.

Gene expression databases

BgeeP06732.
CleanExHS_CKM.
GenevestigatorP06732.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCKM. human.
EvolutionaryTraceP06732.
GeneWikiCKM_(gene).
GenomeRNAi1158.
NextBio4804.
PROP06732.
SOURCESearch...

Entry information

Entry nameKCRM_HUMAN
AccessionPrimary (citable) accession number: P06732
Secondary accession number(s): Q96QL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM