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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)DescriptionActionsGraphical viewLength
Binding sitei225ATPPROSITE-ProRule annotation1
Binding sitei270ATPPROSITE-ProRule annotation1
Binding sitei326ATPPROSITE-ProRule annotation1
Binding sitei369ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi162 – 166ATPPROSITE-ProRule annotation5
Nucleotide bindingi354 – 359ATPPROSITE-ProRule annotation6

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
Proteomesi
  • UP000000539 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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 39Mitochondrion2 PublicationsAdd BLAST39
ChainiPRO_000001659940 – 419Creatine kinase S-type, mitochondrialAdd BLAST380

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

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi50 – 53Combined sources4
Helixi63 – 67Combined sources5
Helixi70 – 76Combined sources7
Helixi87 – 96Combined sources10
Helixi115 – 118Combined sources4
Helixi120 – 130Combined sources11
Turni131 – 133Combined sources3
Turni136 – 138Combined sources3
Helixi147 – 149Combined sources3
Turni157 – 159Combined sources3
Beta strandi160 – 169Combined sources10
Turni177 – 179Combined sources3
Helixi182 – 197Combined sources16
Helixi201 – 203Combined sources3
Beta strandi205 – 212Combined sources8
Helixi215 – 223Combined sources9
Helixi234 – 237Combined sources4
Turni238 – 240Combined sources3
Turni243 – 248Combined sources6
Beta strandi250 – 254Combined sources5
Beta strandi259 – 278Combined sources20
Helixi280 – 300Combined sources21
Turni309 – 311Combined sources3
Helixi318 – 320Combined sources3
Beta strandi326 – 332Combined sources7
Helixi334 – 338Combined sources5
Helixi342 – 349Combined sources8
Beta strandi351 – 354Combined sources4
Turni359 – 363Combined sources5
Beta strandi367 – 372Combined sources6
Beta strandi375 – 378Combined sources4
Helixi380 – 402Combined sources23

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP11009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 132Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd BLAST87
Domaini159 – 401Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd BLAST243

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

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
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)DescriptionActionsGraphical viewLength
Sequence conflicti20 – 23AAGS → CSRQ in AAA48688 (PubMed:2831887).Curated4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CRKX-ray3.00A/B/C/D40-419[»]
ProteinModelPortaliP11009.
SMRiP11009.
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

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP11009.
KOiK00933.
PhylomeDBiP11009.

Enzyme and pathway databases

BRENDAi2.7.3.2. 1306.
SABIO-RKP11009.

Miscellaneous databases

EvolutionaryTraceiP11009.
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...

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: November 2, 2016
This is version 136 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

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 one 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.