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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)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

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
Proteomesi
  • UP000001595 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 – 39MitochondrionAdd BLAST39
ChainiPRO_000001659640 – 419Creatine kinase S-type, mitochondrialAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei255PhosphotyrosineBy similarity1
Modified residuei356PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5R7B5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000017443.

Structurei

3D structure databases

ProteinModelPortaliQ5R7B5.
SMRiQ5R7B5.
ModBaseiSearch...
MobiDBiSearch...

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni40 – 64Cardiolipin-bindingBy similarityAdd BLAST25

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.
HOVERGENiHBG001339.
InParanoidiQ5R7B5.
KOiK00933.
OrthoDBiEOG091G0HZ0.

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000017443.

Proteomic databases

PRIDEiQ5R7B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173361.
KEGGipon:100173361.

Organism-specific databases

CTDi1160.

Phylogenomic databases

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
HOVERGENiHBG001339.
InParanoidiQ5R7B5.
KOiK00933.
OrthoDBiEOG091G0HZ0.

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_PONAB
AccessioniPrimary (citable) accession number: Q5R7B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 72 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

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.