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Protein

Creatine kinase S-type, mitochondrial

Gene

CKMT2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 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: UniProtKB-EC
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):
Sarcomeric mitochondrial creatine kinase
Short name:
S-MtCK
Gene namesi
Name:CKMT2
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionAdd
BLAST
Chaini40 – 419380Creatine kinase S-type, mitochondrialPRO_0000016596Add
BLAST

Proteomic databases

PRIDEiQ5R7B5.

Interactioni

Subunit structurei

Exists as an octamer composed of four CKMT2 homodimers.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5R7B5.
SMRiQ5R7B5. 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-bindingBy similarityAdd
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.
InParanoidiQ5R7B5.
KOiK00933.

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.

Q5R7B5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASIFSKLLT GRNASLLFAT MGTSVLTTGY LLNQQKVCAE VREQPRLFPP
60 70 80 90 100
SADYPDLRKH NNCMAECLTP AIYAKLRNKV TPNGYTLDQC IQTGVDNPGH
110 120 130 140 150
PFIKTVGMVA GDEESYEVFA DLFDPVIKLR HNGYDPRVMK HTTDLDASKI
160 170 180 190 200
TQGQFDEHYV LSSRVRTGRS IRGLSLPPAC TRAERREVEN VAITALEGLK
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 PPLPQFGKK
Length:419
Mass (Da):47,476
Last modified:December 21, 2004 - v1
Checksum:iE10C42A26BD926FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860203 mRNA. Translation: CAH92345.1.
RefSeqiNP_001126380.1. NM_001132908.1.
XP_009239129.1. XM_009240854.1.
XP_009239130.1. XM_009240855.1.

Genome annotation databases

GeneIDi100173361.
KEGGipon:100173361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860203 mRNA. Translation: CAH92345.1.
RefSeqiNP_001126380.1. NM_001132908.1.
XP_009239129.1. XM_009240854.1.
XP_009239130.1. XM_009240855.1.

3D structure databases

ProteinModelPortaliQ5R7B5.
SMRiQ5R7B5. Positions 47-413.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5R7B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173361.
KEGGipon:100173361.

Organism-specific databases

CTDi1160.

Phylogenomic databases

HOVERGENiHBG001339.
InParanoidiQ5R7B5.
KOiK00933.

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiKCRS_PONAB
AccessioniPrimary (citable) accession number: Q5R7B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 21, 2004
Last modified: January 7, 2015
This is version 64 of the entry and version 1 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, 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.