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Protein

Creatine kinase M-type

Gene

CKM

Organism
Oryctolagus cuniculus (Rabbit)
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 annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei191ATP1
Binding sitei236ATP1
Binding sitei292ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi128 – 132ATP5
Nucleotide bindingi320 – 325ATP6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.3.2. 1749.
SABIO-RKP00563.

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075201.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002119782 – 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

PRIDEiP00563.

Miscellaneous databases

PMAP-CutDBP00563.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PKMP119742EBI-2750756,EBI-7133357

Protein-protein interaction databases

IntActiP00563. 1 interactor.
MINTiMINT-6824935.

Chemistry databases

BindingDBiP00563.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Helixi16 – 19Combined sources4
Helixi29 – 33Combined sources5
Helixi36 – 42Combined sources7
Helixi53 – 62Combined sources10
Beta strandi77 – 79Combined sources3
Helixi81 – 84Combined sources4
Helixi86 – 96Combined sources11
Turni97 – 99Combined sources3
Helixi112 – 114Combined sources3
Turni123 – 125Combined sources3
Beta strandi126 – 135Combined sources10
Turni143 – 145Combined sources3
Helixi148 – 163Combined sources16
Helixi167 – 169Combined sources3
Beta strandi171 – 175Combined sources5
Helixi176 – 178Combined sources3
Helixi181 – 189Combined sources9
Helixi200 – 203Combined sources4
Turni204 – 214Combined sources11
Beta strandi216 – 220Combined sources5
Beta strandi225 – 244Combined sources20
Helixi246 – 267Combined sources22
Turni275 – 277Combined sources3
Helixi284 – 286Combined sources3
Beta strandi292 – 298Combined sources7
Helixi300 – 303Combined sources4
Helixi308 – 315Combined sources8
Beta strandi317 – 320Combined sources4
Beta strandi322 – 324Combined sources3
Beta strandi333 – 338Combined sources6
Beta strandi342 – 344Combined sources3
Helixi346 – 369Combined sources24
Beta strandi374 – 376Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U6RX-ray1.65A/B2-381[»]
2CRKX-ray2.35A1-381[»]
ProteinModelPortaliP00563.
SMRiP00563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00563.

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

HOVERGENiHBG001339.
InParanoidiP00563.
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.

P00563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFGNTHNKY KLNYKSEEEY PDLSKHNNHM AKVLTPDLYK KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGF
110 120 130 140 150
KPTDKHKTDL NHENLKGGDD LDPHYVLSSR 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
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV
360 370 380
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K
Length:381
Mass (Da):43,112
Last modified:July 21, 1986 - v1
Checksum:i821447F395FE71CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02831 mRNA. Translation: AAA31205.1.
PIRiA00673. KIRBCM.
RefSeqiNP_001075708.1. NM_001082239.1.
UniGeneiOcu.6249.

Genome annotation databases

GeneIDi100009056.
KEGGiocu:100009056.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02831 mRNA. Translation: AAA31205.1.
PIRiA00673. KIRBCM.
RefSeqiNP_001075708.1. NM_001082239.1.
UniGeneiOcu.6249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U6RX-ray1.65A/B2-381[»]
2CRKX-ray2.35A1-381[»]
ProteinModelPortaliP00563.
SMRiP00563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00563. 1 interactor.
MINTiMINT-6824935.

Chemistry databases

BindingDBiP00563.
ChEMBLiCHEMBL1075201.

Proteomic databases

PRIDEiP00563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009056.
KEGGiocu:100009056.

Organism-specific databases

CTDi1158.

Phylogenomic databases

HOVERGENiHBG001339.
InParanoidiP00563.
KOiK00933.

Enzyme and pathway databases

BRENDAi2.7.3.2. 1749.
SABIO-RKP00563.

Miscellaneous databases

EvolutionaryTraceiP00563.
PMAP-CutDBP00563.
PROiP00563.

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_RABIT
AccessioniPrimary (citable) accession number: P00563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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.