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Protein

Creatine kinase M-type

Gene

Ckm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.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

  • ATP binding Source: UniProtKB-KW
  • creatine kinase activity Source: RGD

GO - Biological processi

  • phosphocreatine biosynthetic process Source: RGD
  • response to heat Source: AgBase
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
Synonyms:Ckmm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2358. Ckm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2176800.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002119792 – 381Creatine kinase M-typeAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei164PhosphoserineBy similarity1
Modified residuei166PhosphothreonineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei180PhosphothreonineCombined sources1
Modified residuei199PhosphoserineCombined sources1
Modified residuei313PhosphothreonineCombined sources1
Modified residuei322PhosphothreonineCombined sources1
Modified residuei372PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00564.
PRIDEiP00564.

PTM databases

iPTMnetiP00564.
PhosphoSitePlusiP00564.

Expressioni

Gene expression databases

BgeeiENSRNOG00000016837.

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

BioGridi246449. 1 interactor.
STRINGi10116.ENSRNOP00000022895.

Structurei

3D structure databases

ProteinModelPortaliP00564.
SMRiP00564.
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.
InParanoidiP00564.
KOiK00933.
PhylomeDBiP00564.
TreeFamiTF314214.

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.

P00564-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKF KLNYKPQEEY PDLSKHNNHM AKVLTPDLYN KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGY
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE
160 170 180 190 200
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF
260 270 280 290 300
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA
310 320 330 340 350
NLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GAVFDISNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):43,045
Last modified:January 23, 2007 - v2
Checksum:iB573FEB1D2A41056
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16P → S in AAA40935 (PubMed:6209281).Curated1
Sequence conflicti87D → N in AAA40936 (Ref. 3) Curated1
Sequence conflicti100Y → F in AAA40935 (PubMed:6209281).Curated1
Sequence conflicti100Y → F in AAA40936 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10140 mRNA. Translation: AAA40935.1.
BC062058 mRNA. Translation: AAH62058.1.
M14864 mRNA. Translation: AAA40936.1.
PIRiA00674. KIRTCM.
RefSeqiNP_036662.1. NM_012530.2.
UniGeneiRn.10756.

Genome annotation databases

GeneIDi24265.
KEGGirno:24265.
UCSCiRGD:2358. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10140 mRNA. Translation: AAA40935.1.
BC062058 mRNA. Translation: AAH62058.1.
M14864 mRNA. Translation: AAA40936.1.
PIRiA00674. KIRTCM.
RefSeqiNP_036662.1. NM_012530.2.
UniGeneiRn.10756.

3D structure databases

ProteinModelPortaliP00564.
SMRiP00564.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246449. 1 interactor.
STRINGi10116.ENSRNOP00000022895.

Chemistry databases

ChEMBLiCHEMBL2176800.

PTM databases

iPTMnetiP00564.
PhosphoSitePlusiP00564.

Proteomic databases

PaxDbiP00564.
PRIDEiP00564.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24265.
KEGGirno:24265.
UCSCiRGD:2358. rat.

Organism-specific databases

CTDi1158.
RGDi2358. Ckm.

Phylogenomic databases

eggNOGiKOG3581. Eukaryota.
COG3869. LUCA.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP00564.
KOiK00933.
PhylomeDBiP00564.
TreeFamiTF314214.

Miscellaneous databases

PROiP00564.

Gene expression databases

BgeeiENSRNOG00000016837.

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_RAT
AccessioniPrimary (citable) accession number: P00564
Secondary accession number(s): Q6P6R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 127 of the entry and version 2 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.