Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Creatine kinase S-type, mitochondrial

Gene

Ckmt2

Organism
Rattus norvegicus (Rat)
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 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

  1. ATP binding Source: UniProtKB-KW
  2. creatine kinase activity Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi61977. Ckmt2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
  2. mitochondrion Source: RGD
  3. sarcomere Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939Mitochondrion1 PublicationAdd
BLAST
Chaini40 – 419380Creatine kinase S-type, mitochondrialPRO_0000016598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei233 – 2331PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP09605.

Expressioni

Tissue specificityi

Sarcomere-specific. Found only in heart and skeletal muscles.

Gene expression databases

GenevestigatoriP09605.

Interactioni

Subunit structurei

Exists as an octamer composed of four CKMT2 homodimers.

Structurei

3D structure databases

ProteinModelPortaliP09605.
SMRiP09605. Positions 47-413.
ModBaseiSearch...
MobiDBiSearch...

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6425Cardiolipin-bindingAdd
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

HOVERGENiHBG001339.
InParanoidiP09605.
PhylomeDBiP09605.

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.

P09605-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASAFSKLLT GRNASLLFTT LGTSALTTGY LLNRQKVSAD AREQHKLFPP
60 70 80 90 100
SADYPDLRKH NNCMAECLTP TIYAKLRNKM TPSGYTLDQC IQTGVDNPGH
110 120 130 140 150
PFIKTVGMVA GDEESYEVFA DLFDPVIKLR HNGYDPRLMK HPADLDASKI
160 170 180 190 200
THGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAERREVEN VAITALGGLK
210 220 230 240 250
GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG MARDWPDARG
260 270 280 290 300
IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
310 320 330 340 350
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR
360 370 380 390 400
LQKRGTGGVD TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK
410
LERGQDIKVP PPLPQFGRK
Length:419
Mass (Da):47,385
Last modified:May 1, 1992 - v2
Checksum:i106041417F5D412F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451H → C AA sequence (PubMed:3338460).Curated
Sequence conflicti51 – 511S → H AA sequence (PubMed:3338460).Curated
Sequence conflicti71 – 722TI → IK AA sequence (PubMed:3338460).Curated
Sequence conflicti77 – 793RNK → NCG AA sequence (PubMed:3338460).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59736 mRNA. Translation: CAA42414.1.
PIRiS17188.
UniGeneiRn.162549.

Genome annotation databases

UCSCiRGD:61977. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59736 mRNA. Translation: CAA42414.1.
PIRiS17188.
UniGeneiRn.162549.

3D structure databases

ProteinModelPortaliP09605.
SMRiP09605. Positions 47-413.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP09605.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61977. rat.

Organism-specific databases

RGDi61977. Ckmt2.

Phylogenomic databases

HOVERGENiHBG001339.
InParanoidiP09605.
PhylomeDBiP09605.

Gene expression databases

GenevestigatoriP09605.

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. "Structural characterization and tissue-specific expression of the mRNAs encoding isoenzymes from two rat mitochondrial creatine kinase genes."
    Payne R.M., Haas R.C., Strauss A.W.
    Biochim. Biophys. Acta 1089:352-361(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Heart.
  2. "Identification and primary structure of the cardiolipin-binding domain of mitochondrial creatine kinase."
    Cheneval D., Carafoli E.
    Eur. J. Biochem. 171:1-9(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-79.
    Tissue: Heart.

Entry informationi

Entry nameiKCRS_RAT
AccessioniPrimary (citable) accession number: P09605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 1, 1992
Last modified: March 4, 2015
This is version 108 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.