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Protein

Creatine kinase M-type

Gene

CKM

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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 sitei191ATPPROSITE-ProRule annotation1
Binding sitei236ATPPROSITE-ProRule annotation1
Binding sitei292ATPPROSITE-ProRule annotation1
Binding sitei335ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 132ATPPROSITE-ProRule annotation5
Nucleotide bindingi320 – 325ATPPROSITE-ProRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
M-CK
Gene namesi
Name:CKM
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002119742 – 381Creatine kinase M-typeAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei164PhosphoserineBy similarity1
Modified residuei166PhosphothreonineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei180PhosphothreonineBy similarity1
Modified residuei199PhosphoserineBy similarity1
Modified residuei313PhosphothreonineBy similarity1
Modified residuei322PhosphothreonineBy similarity1
Modified residuei332PhosphoserineBy similarity1
Modified residuei372PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05123.
PRIDEiP05123.

2D gel databases

UCD-2DPAGEP05123.

Interactioni

Subunit structurei

Dimer of identical or non-identical chains. With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain.

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000006727.

Structurei

3D structure databases

ProteinModelPortaliP05123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 98Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd BLAST88
Domaini125 – 367Phosphagen 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

Phylogenomic databases

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP05123.
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.

P05123-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKF KLNYKPEEEY PDLTKHNNHM AKALTPEIYK KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYQVFKDLFD PIIQDRHGGY
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE
160 170 180 190 200
RRAVEKLSIE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
310 320 330 340 350
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):43,153
Last modified:January 23, 2007 - v3
Checksum:i83F8D227D27472C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11660 mRNA. Translation: AAA30836.1.
PIRiA24686.
RefSeqiNP_001300705.1. NM_001313776.1.

Genome annotation databases

GeneIDi476435.
KEGGicfa:476435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11660 mRNA. Translation: AAA30836.1.
PIRiA24686.
RefSeqiNP_001300705.1. NM_001313776.1.

3D structure databases

ProteinModelPortaliP05123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000006727.

2D gel databases

UCD-2DPAGEP05123.

Proteomic databases

PaxDbiP05123.
PRIDEiP05123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi476435.
KEGGicfa:476435.

Organism-specific databases

CTDi1158.

Phylogenomic databases

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP05123.
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...

Entry informationi

Entry nameiKCRM_CANLF
AccessioniPrimary (citable) accession number: P05123
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.