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P00563

- KCRM_RABIT

UniProt

P00563 - KCRM_RABIT

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Protein

Creatine kinase M-type

Gene

CKM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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.1 PublicationPROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATP
Binding sitei236 – 2361ATP
Binding sitei292 – 2921ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325ATP
Nucleotide bindingi320 – 3256ATP

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

Enzyme and pathway databases

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
ProteomesiUP000001811: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 381380Creatine kinase M-typePRO_0000211978Add
BLAST

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 interaction.
MINTiMINT-6824935.
STRINGi9986.ENSOCUP00000020805.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 116
Helixi16 – 194
Helixi29 – 335
Helixi36 – 427
Helixi53 – 6210
Beta strandi77 – 793
Helixi81 – 844
Helixi86 – 9611
Turni97 – 993
Helixi112 – 1143
Turni123 – 1253
Beta strandi126 – 13510
Turni143 – 1453
Helixi148 – 16316
Helixi167 – 1693
Beta strandi171 – 1755
Helixi176 – 1783
Helixi181 – 1899
Helixi200 – 2034
Turni204 – 21411
Beta strandi216 – 2205
Beta strandi225 – 24420
Helixi246 – 26722
Turni275 – 2773
Helixi284 – 2863
Beta strandi292 – 2987
Helixi300 – 3034
Helixi308 – 3158
Beta strandi317 – 3204
Beta strandi322 – 3243
Beta strandi333 – 3386
Beta strandi342 – 3443
Helixi346 – 36924
Beta strandi374 – 3763

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00563.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9888Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 367243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
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

Phylogenomic databases

eggNOGiCOG3869.
HOVERGENiHBG001339.
InParanoidiP00563.

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
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:
EMBL
GenBank
DDBJ
Links Updated
K02831 mRNA. Translation: AAA31205.1.
PIRiA00673. KIRBCM.
RefSeqiNP_001075708.1. NM_001082239.1.
UniGeneiOcu.6249.

Genome annotation databases

GeneIDi100009056.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K02831 mRNA. Translation: AAA31205.1 .
PIRi A00673. KIRBCM.
RefSeqi NP_001075708.1. NM_001082239.1.
UniGenei Ocu.6249.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U6R X-ray 1.65 A/B 2-381 [» ]
2CRK X-ray 2.35 A 1-381 [» ]
ProteinModelPortali P00563.
SMRi P00563. Positions 2-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00563. 1 interaction.
MINTi MINT-6824935.
STRINGi 9986.ENSOCUP00000020805.

Chemistry

ChEMBLi CHEMBL1075201.

Proteomic databases

PRIDEi P00563.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009056.

Organism-specific databases

CTDi 1158.

Phylogenomic databases

eggNOGi COG3869.
HOVERGENi HBG001339.
InParanoidi P00563.

Enzyme and pathway databases

SABIO-RK P00563.

Miscellaneous databases

EvolutionaryTracei P00563.
PMAP-CutDB P00563.

Family and domain databases

Gene3Di 1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view ]
Pfami PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view ]
SUPFAMi SSF48034. SSF48034. 1 hit.
PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences."
    Pickering L., Pang H., Biemann K., Munro H., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Rabbit muscle creatine phosphokinase. cDNA cloning, primary structure and detection of human homologues."
    Putney S., Herlihy W., Royal N., Pang H., Aposhian H.V., Pickering L., Belagaje R., Biemann K., Page D., Kuby S., Schimmel P.
    J. Biol. Chem. 259:14317-14320(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Brain adenosine 5'-triphosphate-creatine phosphotransferase."
    Atherton R.S., Laws J.F., Miles B.J., Thomson A.R.
    Biochem. J. 120:589-600(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION.
  4. "Crystal structure of rabbit muscle creatine kinase."
    Rao J.K., Bujacz G., Wlodawer A.
    FEBS Lett. 439:133-137(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    Tissue: Muscle.
  5. "Structural asymmetry and intersubunit communication in muscle creatine kinase."
    Ohren J.F., Kundracik M.L., Borders C.L. Jr., Edmiston P., Viola R.E.
    Acta Crystallogr. D 63:381-389(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP.

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: October 29, 2014
This is version 101 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

External Data

Dasty 3