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Protein

Creatine kinase S-type, mitochondrial

Gene

CKMT2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 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 sitei225 – 2251ATPPROSITE-ProRule annotation
Binding sitei270 – 2701ATPPROSITE-ProRule annotation
Binding sitei326 – 3261ATPPROSITE-ProRule annotation
Binding sitei369 – 3691ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665ATPPROSITE-ProRule annotation
Nucleotide bindingi354 – 3596ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.3.2. 1306.
SABIO-RKP11009.

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase S-type, mitochondrial (EC:2.7.3.2)
Alternative name(s):
Basic-type mitochondrial creatine kinase
Short name:
Mib-CK
Sarcomeric mitochondrial creatine kinase
Short name:
S-MtCK
Gene namesi
Name:CKMT2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939Mitochondrion2 PublicationsAdd
BLAST
Chaini40 – 419380Creatine kinase S-type, mitochondrialPRO_0000016599Add
BLAST

Proteomic databases

PaxDbiP11009.
PRIDEiP11009.

Expressioni

Tissue specificityi

Expressed in the leg muscle and heart.

Interactioni

Subunit structurei

Exists as an octamer composed of four MTCK homodimers.1 Publication

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025110.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 534Combined sources
Helixi63 – 675Combined sources
Helixi70 – 767Combined sources
Helixi87 – 9610Combined sources
Helixi115 – 1184Combined sources
Helixi120 – 13011Combined sources
Turni131 – 1333Combined sources
Turni136 – 1383Combined sources
Helixi147 – 1493Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 16910Combined sources
Turni177 – 1793Combined sources
Helixi182 – 19716Combined sources
Helixi201 – 2033Combined sources
Beta strandi205 – 2128Combined sources
Helixi215 – 2239Combined sources
Helixi234 – 2374Combined sources
Turni238 – 2403Combined sources
Turni243 – 2486Combined sources
Beta strandi250 – 2545Combined sources
Beta strandi259 – 27820Combined sources
Helixi280 – 30021Combined sources
Turni309 – 3113Combined sources
Helixi318 – 3203Combined sources
Beta strandi326 – 3327Combined sources
Helixi334 – 3385Combined sources
Helixi342 – 3498Combined sources
Beta strandi351 – 3544Combined sources
Turni359 – 3635Combined sources
Beta strandi367 – 3726Combined sources
Beta strandi375 – 3784Combined sources
Helixi380 – 40223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRKX-ray3.00A/B/C/D40-419[»]
ProteinModelPortaliP11009.
SMRiP11009. Positions 40-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 13287Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini159 – 401243Phosphagen 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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP11009.
KOiK00933.
PhylomeDBiP11009.

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.

P11009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTFGRLLA GRVTAALFAA AGSGVLTTGY LLNQQNVKAT VHEKRKLFPP
60 70 80 90 100
SADYPDLRKH NNCMAECLTP AIYAKLRDKL TPNGYSLDQC IQTGVDNPGH
110 120 130 140 150
PFIKTVGMVA GDEESYEVFA EIFDPVIKAR HNGYDPRTMK HHTDLDASKI
160 170 180 190 200
THGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAERREVEN VVVTALAGLK
210 220 230 240 250
GDLSGKYYSL TNMSERDQQQ LIDDHFLFDK PVSPLLTCAG MARDWPDARG
260 270 280 290 300
IWHNNDKTFL VWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIKE
310 320 330 340 350
RGWEFMWNER LGYVLTCPSN LGTGLRAGVH VKLPRLSKDP RFPKILENLR
360 370 380 390 400
LQKRGTGGVD TAAVADVYDI SNLDRMGRSE VELVQIVIDG VNYLVDCEKK
410
LEKGQDIKVP PPLPQFGRK
Length:419
Mass (Da):47,084
Last modified:July 15, 1998 - v2
Checksum:i9ACC60D709B9283F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 234AAGS → CSRQ in AAA48688 (PubMed:2831887).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18866 mRNA. Translation: AAA48688.1.
PIRiA27708.
RefSeqiNP_001161216.1. NM_001167744.1.
UniGeneiGga.869.

Genome annotation databases

GeneIDi396508.
KEGGigga:396508.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18866 mRNA. Translation: AAA48688.1.
PIRiA27708.
RefSeqiNP_001161216.1. NM_001167744.1.
UniGeneiGga.869.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CRKX-ray3.00A/B/C/D40-419[»]
ProteinModelPortaliP11009.
SMRiP11009. Positions 40-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025110.

Proteomic databases

PaxDbiP11009.
PRIDEiP11009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396508.
KEGGigga:396508.

Organism-specific databases

CTDi1160.

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP11009.
KOiK00933.
PhylomeDBiP11009.

Enzyme and pathway databases

BRENDAi2.7.3.2. 1306.
SABIO-RKP11009.

Miscellaneous databases

EvolutionaryTraceiP11009.
NextBioi20816547.
PROiP11009.

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

  1. "Evolution of the creative kinases. The chicken acidic type mitochondrial creatine kinase gene as the first nonmammalian gene."
    Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.
    J. Biol. Chem. 271:11920-11929(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-39.
    Strain: White leghorn.
  2. "Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework."
    Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P., Eppenberger H.M., Wallimann T., Perriard J.-C.
    Biochem. Biophys. Res. Commun. 151:408-416(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-419, PROTEIN SEQUENCE OF 40-69.
    Tissue: Heart and Skeletal muscle.
  3. "The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization."
    Kaldis P., Furter R., Wallimann T.
    Biochemistry 33:952-959(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-48.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiKCRS_CHICK
AccessioniPrimary (citable) accession number: P11009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 15, 1998
Last modified: June 24, 2015
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Mitochondrial creatine kinase binds cardiolipin.

Keywords - Technical termi

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