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P05123

- KCRM_CANFA

UniProt

P05123 - KCRM_CANFA

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Protein
Creatine kinase M-type
Gene
CKM
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
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: 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
Gene namesi
Name:CKM
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

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 – 11Removed1 Publication
Chaini2 – 381380Creatine kinase M-type
PRO_0000211974Add
BLAST

Proteomic databases

PaxDbiP05123.
PRIDEiP05123.

2D gel databases

UCD-2DPAGEP05123.

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

STRINGi9615.ENSCAFP00000032827.

Structurei

3D structure databases

ProteinModelPortaliP05123.
SMRiP05123. Positions 2-381.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP05123.
KOiK00933.

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.

P05123-1 [UniParc]FASTAAdd to Basket

« Hide

MPFGNTHNKF KLNYKPEEEY PDLTKHNNHM AKALTPEIYK KLRDKETPSG    50
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYQVFKDLFD PIIQDRHGGY 100
KPTDKHKTDL NHENLKGGDD LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE 150
RRAVEKLSIE ALNSLTGEFK GKYYPLKSMT EQEQQQLIDD HFLFDKPVSP 200
LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF 250
RRFCVGLQKI EEIFKKAGHP FMWNEHLGYV LTCPSNLGTG LRGGVHVKLA 300
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDISNAD RLGSSEVEQV 350
QLVVDGVKLM VEMEKKLEKG QSIDDMIPAQ K 381
Length:381
Mass (Da):43,153
Last modified:January 23, 2007 - v3
Checksum:i83F8D227D27472C2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11660 mRNA. Translation: AAA30836.1.
PIRiA24686.
RefSeqiXP_005616506.1. XM_005616449.1.

Genome annotation databases

GeneIDi476435.
KEGGicfa:476435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11660 mRNA. Translation: AAA30836.1 .
PIRi A24686.
RefSeqi XP_005616506.1. XM_005616449.1.

3D structure databases

ProteinModelPortali P05123.
SMRi P05123. Positions 2-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9615.ENSCAFP00000032827.

2D gel databases

UCD-2DPAGE P05123.

Proteomic databases

PaxDbi P05123.
PRIDEi P05123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 476435.
KEGGi cfa:476435.

Organism-specific databases

CTDi 1158.

Phylogenomic databases

eggNOGi COG3869.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi P05123.
KOi K00933.

Miscellaneous databases

NextBioi 20852095.

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 dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species."
    Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W.
    Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins."
    Dunn M.J., Corbett J.M., Wheeler C.H.
    Electrophoresis 18:2795-2802(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-23.
    Tissue: Heart.
  3. "Characterization of MB creatine kinase isoform conversion in vitro and in vivo in dogs."
    Billadello J.J., Fontanet H.L., Strauss A.W., Abendschein D.R.
    J. Clin. Invest. 83:1637-1643(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 377-381.
    Tissue: Myocardium.

Entry informationi

Entry nameiKCRM_CANFA
AccessioniPrimary (citable) accession number: P05123
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 106 of the entry and version 3 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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