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P00564

- KCRM_RAT

UniProt

P00564 - KCRM_RAT

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Protein

Creatine kinase M-type

Gene
Ckm, Ckmm
Organism
Rattus norvegicus (Rat)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATP By similarity
Binding sitei236 – 2361ATP By similarity
Binding sitei292 – 2921ATP By similarity
Binding sitei335 – 3351ATP By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. creatine kinase activity Source: RGD

GO - Biological processi

  1. phosphocreatine biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_212547. Creatine metabolism.

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
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi2358. Ckm.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 381380Creatine kinase M-typePRO_0000211979Add
BLAST

Proteomic databases

PaxDbiP00564.
PRIDEiP00564.

PTM databases

PhosphoSiteiP00564.

Expressioni

Gene expression databases

GenevestigatoriP00564.

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 interaction.
STRINGi10116.ENSRNOP00000022895.

Structurei

3D structure databases

ProteinModelPortaliP00564.
SMRiP00564. Positions 2-381.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3869.
GeneTreeiENSGT00550000074561.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP00564.
KOiK00933.
OrthoDBiEOG7XM2XW.
PhylomeDBiP00564.
TreeFamiTF314214.

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.

P00564-1 [UniParc]FASTAAdd to Basket

« Hide

MPFGNTHNKF KLNYKPQEEY PDLSKHNNHM AKVLTPDLYN KLRDKETPSG    50
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYTVFKDLFD PIIQDRHGGY 100
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE 150
RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP 200
LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM EKGGNMKEVF 250
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 300
NLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GAVFDISNAD RLGSSEVEQV 350
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K 381
Length:381
Mass (Da):43,045
Last modified:January 23, 2007 - v2
Checksum:iB573FEB1D2A41056
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161P → S in AAA40935. 1 Publication
Sequence conflicti87 – 871D → N in AAA40936. 1 Publication
Sequence conflicti100 – 1001Y → F in AAA40935. 1 Publication
Sequence conflicti100 – 1001Y → F in AAA40936. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENSRNOT00000022895; ENSRNOP00000022895; ENSRNOG00000016837.
GeneIDi24265.
KEGGirno:24265.
UCSCiRGD:2358. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M10140 mRNA. Translation: AAA40935.1 .
BC062058 mRNA. Translation: AAH62058.1 .
M14864 mRNA. Translation: AAA40936.1 .
PIRi A00674. KIRTCM.
RefSeqi NP_036662.1. NM_012530.2.
UniGenei Rn.10756.

3D structure databases

ProteinModelPortali P00564.
SMRi P00564. Positions 2-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 246449. 1 interaction.
STRINGi 10116.ENSRNOP00000022895.

Chemistry

ChEMBLi CHEMBL2176800.

PTM databases

PhosphoSitei P00564.

Proteomic databases

PaxDbi P00564.
PRIDEi P00564.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000022895 ; ENSRNOP00000022895 ; ENSRNOG00000016837 .
GeneIDi 24265.
KEGGi rno:24265.
UCSCi RGD:2358. rat.

Organism-specific databases

CTDi 1158.
RGDi 2358. Ckm.

Phylogenomic databases

eggNOGi COG3869.
GeneTreei ENSGT00550000074561.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi P00564.
KOi K00933.
OrthoDBi EOG7XM2XW.
PhylomeDBi P00564.
TreeFami TF314214.

Enzyme and pathway databases

Reactomei REACT_212547. Creatine metabolism.

Miscellaneous databases

NextBioi 602819.

Gene expression databases

Genevestigatori P00564.

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

« Hide 'large scale' publications
  1. "Isolation and sequence analysis of cDNA clones coding for rat skeletal muscle creatine kinase."
    Benfield P.A., Zivin R.A., Miller L.S., Sowder R., Smythers G.W., Henderson L., Oroszlan S., Pearson M.L.
    J. Biol. Chem. 259:14979-14984(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Fischer 344.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "The nucleotide sequence of rat muscle creatine kinase cDNA and ckm transcription during myogenesis in an RNA polymerase II mutant of L6 myoblasts."
    Benfield P.A., Zivin R.A., Shearman C.W., Graf D., Henderson L., Oroszlan S., Pearson M.L.
    Exp. Biol. Med. 9:187-194(1984)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-381.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (DEC-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 87-96; 139-148; 157-170 AND 321-341, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

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: September 3, 2014
This is version 111 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

External Data

Dasty 3

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