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Protein

Creatine kinase M-type

Gene

CKM

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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 (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: AgBase

GO - Biological processi

  1. phosphocreatine biosynthetic process Source: AgBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_207339. Creatine metabolism.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 18

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 381380Creatine kinase M-typePRO_0000211973Add
BLAST

Proteomic databases

PaxDbiQ9XSC6.
PRIDEiQ9XSC6.

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

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 115Combined sources
Helixi16 – 194Combined sources
Helixi29 – 335Combined sources
Helixi36 – 427Combined sources
Helixi53 – 6210Combined sources
Helixi81 – 844Combined sources
Helixi86 – 9611Combined sources
Turni97 – 993Combined sources
Helixi112 – 1143Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 13510Combined sources
Turni143 – 1453Combined sources
Helixi148 – 16215Combined sources
Helixi167 – 1693Combined sources
Beta strandi171 – 1755Combined sources
Helixi176 – 1783Combined sources
Helixi181 – 19010Combined sources
Helixi200 – 2034Combined sources
Turni204 – 21411Combined sources
Beta strandi216 – 2205Combined sources
Beta strandi225 – 24420Combined sources
Helixi246 – 26621Combined sources
Turni275 – 2773Combined sources
Helixi284 – 2863Combined sources
Beta strandi292 – 2987Combined sources
Turni300 – 3034Combined sources
Helixi308 – 3158Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi332 – 3387Combined sources
Beta strandi342 – 3443Combined sources
Helixi346 – 35914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0WX-ray2.30A7-359[»]
ProteinModelPortaliQ9XSC6.
SMRiQ9XSC6. Positions 2-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9XSC6.

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.
InParanoidiQ9XSC6.
KOiK00933.
OMAiALTLEIY.
OrthoDBiEOG7XM2XW.
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.

Q9XSC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKH KLNFKAEEEY PDLSKHNNHM AKALTLEIYK KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY ALPPHCSRGE
160 170 180 190 200
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF
260 270 280 290 300
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
310 320 330 340 350
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):42,989
Last modified:June 27, 2006 - v2
Checksum:iC97EBBFB00BCF2FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3761M → L in AAD30974 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti377 – 3771I → M.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120106 mRNA. Translation: AAD30974.1.
BT020785 mRNA. Translation: AAX08802.1.
BT021173 mRNA. Translation: AAX31355.1.
BC102907 mRNA. Translation: AAI02908.1.
RefSeqiNP_777198.2. NM_174773.4.
UniGeneiBt.3651.

Genome annotation databases

EnsembliENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921.
GeneIDi286822.
KEGGibta:286822.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120106 mRNA. Translation: AAD30974.1.
BT020785 mRNA. Translation: AAX08802.1.
BT021173 mRNA. Translation: AAX31355.1.
BC102907 mRNA. Translation: AAI02908.1.
RefSeqiNP_777198.2. NM_174773.4.
UniGeneiBt.3651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G0WX-ray2.30A7-359[»]
ProteinModelPortaliQ9XSC6.
SMRiQ9XSC6. Positions 2-381.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiQ9XSC6.
PRIDEiQ9XSC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018492; ENSBTAP00000018492; ENSBTAG00000013921.
GeneIDi286822.
KEGGibta:286822.

Organism-specific databases

CTDi1158.

Phylogenomic databases

eggNOGiCOG3869.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiQ9XSC6.
KOiK00933.
OMAiALTLEIY.
OrthoDBiEOG7XM2XW.
TreeFamiTF314214.

Enzyme and pathway databases

ReactomeiREACT_207339. Creatine metabolism.

Miscellaneous databases

EvolutionaryTraceiQ9XSC6.
NextBioi20806476.

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. "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. 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.

Entry informationi

Entry nameiKCRM_BOVIN
AccessioniPrimary (citable) accession number: Q9XSC6
Secondary accession number(s): Q5E9Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 27, 2006
Last modified: March 4, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.