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Protein

Creatine kinase M-type

Gene

CKM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

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: ProtInc

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. creatine metabolic process Source: Reactome
  3. phosphocreatine biosynthetic process Source: Ensembl
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS02640-MONOMER.
BRENDAi2.7.3.2. 2681.
ReactomeiREACT_813. Creatine metabolism.
SABIO-RKP06732.

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
M-CK
Cleaved into the following chain:
Gene namesi
Name:CKM
Synonyms:CKMM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1994. CKM.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26532.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Creatine kinase M-typePRO_0000211975Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 381380Creatine kinase M-type, N-terminally processedPRO_0000421788Add
BLAST

Proteomic databases

MaxQBiP06732.
PaxDbiP06732.
PeptideAtlasiP06732.
PRIDEiP06732.

2D gel databases

UCD-2DPAGEP06732.

PTM databases

PhosphoSiteiP06732.

Expressioni

Gene expression databases

BgeeiP06732.
CleanExiHS_CKM.
GenevestigatoriP06732.

Organism-specific databases

HPAiHPA047859.

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.

Protein-protein interaction databases

BioGridi107578. 17 interactions.
IntActiP06732. 2 interactions.
STRINGi9606.ENSP00000221476.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 194Combined sources
Helixi29 – 335Combined sources
Helixi36 – 427Combined sources
Helixi53 – 6210Combined sources
Beta strandi67 – 693Combined sources
Helixi80 – 845Combined sources
Helixi86 – 938Combined sources
Turni94 – 963Combined sources
Beta strandi97 – 993Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 1327Combined sources
Turni143 – 1453Combined sources
Helixi148 – 16417Combined sources
Helixi167 – 1693Combined sources
Beta strandi171 – 1766Combined sources
Turni181 – 1833Combined sources
Helixi184 – 1896Combined sources
Turni200 – 2067Combined sources
Turni209 – 2146Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi223 – 24422Combined sources
Helixi246 – 26621Combined sources
Turni275 – 2773Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2987Combined sources
Turni300 – 3045Combined sources
Helixi308 – 3147Combined sources
Beta strandi333 – 3386Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 36823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0EX-ray3.50A/B/C/D1-381[»]
ProteinModelPortaliP06732.
SMRiP06732. Positions 8-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06732.

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.
InParanoidiP06732.
KOiK00933.
OMAiALTLEIY.
OrthoDBiEOG7XM2XW.
PhylomeDBiP06732.
TreeFamiTF314214.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR000749. 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]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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.

P06732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG
60 70 80 90 100
FTVDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE
160 170 180 190 200
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EKEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF
260 270 280 290 300
RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA
310 320 330 340 350
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):43,101
Last modified:November 1, 1990 - v2
Checksum:i418FEAD0C2E138C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471T → I in AAA52025 (PubMed:3778496).Curated
Sequence conflicti130 – 1301R → P in AAA52025 (PubMed:3778496).Curated
Sequence conflicti193 – 1931L → Q in AAA52025 (PubMed:3778496).Curated
Sequence conflicti210 – 2101D → H in AAA52025 (PubMed:3778496).Curated
Sequence conflicti215 – 2151R → P in AAA52025 (PubMed:3778496).Curated
Sequence conflicti225 – 2251F → L in AAP35439 (Ref. 3) Curated
Sequence conflicti225 – 2251F → L in AAH07462 (PubMed:15489334).Curated
Sequence conflicti324 – 3241G → A in AAA52025 (PubMed:3778496).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831E → G.1 Publication
Corresponds to variant rs11559024 [ dbSNP | Ensembl ].
VAR_018680
Natural varianti127 – 1271L → V.1 Publication
Corresponds to variant rs17875653 [ dbSNP | Ensembl ].
VAR_018681
Natural varianti166 – 1661T → M.
Corresponds to variant rs17357122 [ dbSNP | Ensembl ].
VAR_049675
Natural varianti243 – 2431G → A.1 Publication
Corresponds to variant rs17875625 [ dbSNP | Ensembl ].
VAR_018682

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14780 mRNA. Translation: AAA52025.1.
M21494
, 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.
CCDSiCCDS12659.1.
PIRiA31793. KIHUCM.
RefSeqiNP_001815.2. NM_001824.4.
UniGeneiHs.334347.

Genome annotation databases

EnsembliENST00000221476; ENSP00000221476; ENSG00000104879.
GeneIDi1158.
KEGGihsa:1158.
UCSCiuc002pbd.4. human.

Polymorphism databases

DMDMi125305.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Creatine kinase entry

SeattleSNPs
Wikipedia

CKM entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14780 mRNA. Translation: AAA52025.1.
M21494
, 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.
CCDSiCCDS12659.1.
PIRiA31793. KIHUCM.
RefSeqiNP_001815.2. NM_001824.4.
UniGeneiHs.334347.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I0EX-ray3.50A/B/C/D1-381[»]
ProteinModelPortaliP06732.
SMRiP06732. Positions 8-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107578. 17 interactions.
IntActiP06732. 2 interactions.
STRINGi9606.ENSP00000221476.

Chemistry

BindingDBiP06732.
ChEMBLiCHEMBL2656.
DrugBankiDB00148. Creatine.

PTM databases

PhosphoSiteiP06732.

Polymorphism databases

DMDMi125305.

2D gel databases

UCD-2DPAGEP06732.

Proteomic databases

MaxQBiP06732.
PaxDbiP06732.
PeptideAtlasiP06732.
PRIDEiP06732.

Protocols and materials databases

DNASUi1158.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221476; ENSP00000221476; ENSG00000104879.
GeneIDi1158.
KEGGihsa:1158.
UCSCiuc002pbd.4. human.

Organism-specific databases

CTDi1158.
GeneCardsiGC19M045809.
HGNCiHGNC:1994. CKM.
HPAiHPA047859.
MIMi123310. gene.
neXtProtiNX_P06732.
PharmGKBiPA26532.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3869.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP06732.
KOiK00933.
OMAiALTLEIY.
OrthoDBiEOG7XM2XW.
PhylomeDBiP06732.
TreeFamiTF314214.

Enzyme and pathway databases

BioCyciMetaCyc:HS02640-MONOMER.
BRENDAi2.7.3.2. 2681.
ReactomeiREACT_813. Creatine metabolism.
SABIO-RKP06732.

Miscellaneous databases

ChiTaRSiCKM. human.
EvolutionaryTraceiP06732.
GeneWikiiCKM_(gene).
GenomeRNAii1158.
NextBioi4804.
PROiP06732.
SOURCEiSearch...

Gene expression databases

BgeeiP06732.
CleanExiHS_CKM.
GenevestigatoriP06732.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR000749. 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]
PANTHERiPTHR11547. PTHR11547. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1985) [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(1987) [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 (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. SeattleSNPs variation discovery resource
    Submitted (FEB-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.
    , 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(2003) [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(2003) [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(1989) [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(1986) [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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

Entry informationi

Entry nameiKCRM_HUMAN
AccessioniPrimary (citable) accession number: P06732
Secondary accession number(s): Q96QL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: April 1, 2015
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.