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P09605

- KCRS_RAT

UniProt

P09605 - KCRS_RAT

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Protein
Creatine kinase S-type, mitochondrial
Gene
Ckmt2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251ATP By similarity
Binding sitei270 – 2701ATP By similarity
Binding sitei326 – 3261ATP By similarity
Binding sitei369 – 3691ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1665ATP By similarity
Nucleotide bindingi354 – 3596ATP By similarity

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 Publication
Add
BLAST
Chaini40 – 419380Creatine kinase S-type, mitochondrial
PRO_0000016598Add
BLAST

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 13287Phosphagen kinase N-terminal
Add
BLAST
Domaini159 – 401243Phosphagen kinase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6425Cardiolipin-binding
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001339.
PhylomeDBiP09605.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
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

MASAFSKLLT GRNASLLFTT LGTSALTTGY LLNRQKVSAD AREQHKLFPP    50
SADYPDLRKH NNCMAECLTP TIYAKLRNKM TPSGYTLDQC IQTGVDNPGH 100
PFIKTVGMVA GDEESYEVFA DLFDPVIKLR HNGYDPRLMK HPADLDASKI 150
THGQFDERYV LSSRVRTGRS IRGLSLPPAC SRAERREVEN VAITALGGLK 200
GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG MARDWPDARG 250
IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE 300
RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR 350
LQKRGTGGVD TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK 400
LERGQDIKVP PPLPQFGRK 419
Length:419
Mass (Da):47,385
Last modified:May 1, 1992 - v2
Checksum:i106041417F5D412F
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451H → C AA sequence 1 Publication
Sequence conflicti51 – 511S → H AA sequence 1 Publication
Sequence conflicti71 – 722TI → IK AA sequence 1 Publication
Sequence conflicti77 – 793RNK → NCG AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59736 mRNA. Translation: CAA42414.1.
PIRiS17188.
UniGeneiRn.162549.

Genome annotation databases

UCSCiRGD:61977. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59736 mRNA. Translation: CAA42414.1 .
PIRi S17188.
UniGenei Rn.162549.

3D structure databases

ProteinModelPortali P09605.
SMRi P09605. Positions 47-413.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P09605.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

UCSCi RGD:61977. rat.

Organism-specific databases

RGDi 61977. Ckmt2.

Phylogenomic databases

HOVERGENi HBG001339.
PhylomeDBi P09605.

Gene expression databases

Genevestigatori P09605.

Family and domain databases

Gene3Di 1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view ]
Pfami PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view ]
SUPFAMi SSF48034. SSF48034. 1 hit.
PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: April 16, 2014
This is version 104 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

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