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P00566

- KCRM_TORMA

UniProt

P00566 - KCRM_TORMA

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Protein

Creatine kinase M-type

Gene
N/A
Organism
Torpedo marmorata (Marbled electric ray)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei191 – 1911ATPPROSITE-ProRule annotation
Binding sitei236 – 2361ATPPROSITE-ProRule annotation
Binding sitei292 – 2921ATPPROSITE-ProRule annotation
Binding sitei335 – 3351ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325ATPPROSITE-ProRule annotation
Nucleotide bindingi320 – 3256ATPPROSITE-ProRule annotation

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

Names & Taxonomyi

Protein namesi
Recommended name:
Creatine kinase M-type (EC:2.7.3.2)
Alternative name(s):
Creatine kinase M chain
M-CK
NU-2 protein
OrganismiTorpedo marmorata (Marbled electric ray)
Taxonomic identifieri7788 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTorpedo

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Creatine kinase M-typePRO_0000211982Add
BLAST

Proteomic databases

PRIDEiP00566.

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.

Structurei

3D structure databases

ProteinModelPortaliP00566.
SMRiP00566. Positions 8-381.
ModBaseiSearch...
MobiDBiSearch...

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

HOVERGENiHBG001339.

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.

P00566-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPFGNTHNKW KLNYSAAEEF PDLSKHNNHM AKALTLDIYK KLRDKETPSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE CYEVFKDLFD PVIEDRHGGY
110 120 130 140 150
KPTDKHKTDL NQDNLKGGDD LDPNYVLSSR VRTGRSIKGI ALPPHCSRGE
160 170 180 190 200
RRLVEKLCIE GLATLTGEFQ GKYYPLSTMS DAEQQQLIDD HFLFDKPISP
210 220 230 240 250
LLLASGMARD WPDGRGIWHN NDKSFLVWVN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
RRFCVGLKKI EEIFVKAGRG FMWNEHLGYV LTCPSNLGTG LRGGVHVKIP
310 320 330 340 350
HLCKHEKFSE VLKRTRLQKR GTGGVDTEAV GSIYDISNAD RLGFSEVEQV
360 370 380
QMVVDGVKLM VEMEKRLENG KSIDDLIPAQ K
Length:381
Mass (Da):42,974
Last modified:July 21, 1986 - v1
Checksum:iAE0217EB65B8772C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11508 mRNA. Translation: AAA49277.1.
PIRiA00676. KIRYCM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11508 mRNA. Translation: AAA49277.1 .
PIRi A00676. KIRYCM.

3D structure databases

ProteinModelPortali P00566.
SMRi P00566. Positions 8-381.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P00566.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001339.

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. "Complete nucleotide sequence of Torpedo marmorata mRNA coding for the 43,000-dalton nu 2 protein: muscle-specific creatine kinase."
    Giraudat J., Devillers-Thiery A., Perriard J.-C., Changeux J.-P.
    Proc. Natl. Acad. Sci. U.S.A. 81:7313-7317(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Electric organ.

Entry informationi

Entry nameiKCRM_TORMA
AccessioniPrimary (citable) accession number: P00566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This electric ray muscle-specific creatine kinase (MM isozyme) is isolated from the electric organ, which derives embryologically from skeletal muscle. It may be involved in the electrical discharge process.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3