Creatine kinase B-type - Canis familiaris (Dog)

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P05124 (KCRB_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Creatine kinase B-type
EC=2.7.3.2

Alternative name(s):
B-CK
Creatine kinase B chain

Gene names

Name:

CKB

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ATP + creatine = ADP + phosphocreatine.
Subunit structure	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.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family. Contains 1 phosphagen kinase C-terminal domain. Contains 1 phosphagen kinase N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain development Inferred from sequence or structural similarity. Source: AgBase cellular chloride ion homeostasis Inferred from sequence or structural similarity. Source: AgBase
Cellular_component	mitochondrion Inferred from sequence or structural similarity. Source: AgBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 381

380

Creatine kinase B-type

PRO_0000211965

Regions

Domain

11 – 98

Phosphagen kinase N-terminal

Domain

125 – 367

243

Phosphagen kinase C-terminal

Nucleotide binding

128 – 132

ATP By similarity

Nucleotide binding

320 – 325

ATP By similarity

Sites

Binding site

130

ATP By similarity

Binding site

132

ATP By similarity

Binding site

191

ATP By similarity

Binding site

232

Substrate By similarity

Binding site

236

ATP By similarity

Binding site

285

Substrate By similarity

Binding site

292

ATP By similarity

Binding site

320

ATP By similarity

Binding site

335

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

125

Phosphotyrosine By similarity

Modified residue

164

Phosphoserine By similarity

Modified residue

199

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P05124 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 2C2F925C78F16364
Show »

FASTA

381

42,701

        10         20         30         40         50         60 
MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT 

       190        200        210        220        230        240 
EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM 

       250        260        270        280        290        300 
QKGGNMKEVF TRFCNGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 

       310        320        330        340        350        360 
HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 

       370        380 
IEMEQRLEQG QAIDDLVPAQ K

« Hide

References

[1]

"The complete nucleotide sequence of canine brain B creatine kinase mRNA: homology in the coding and 3' noncoding regions among species."
Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W.
Biochem. Biophys. Res. Commun. 138:392-398(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.

[2]

"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: PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208; 224-236; 247-261; 268-287; 321-357 AND 364-381.
Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13453 mRNA. Translation: AAA30837.1.
PIR	B24686. A24227.
RefSeq	XP_003639259.1. XM_003639211.1.
3D structure databases
ProteinModelPortal	P05124.
SMR	P05124. Positions 2-381.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000026998.
Proteomic databases
PaxDb	P05124.
PRIDE	P05124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSCAFT00000029035; ENSCAFP00000026998; ENSCAFG00000018277.
GeneID	100855552.
KEGG	cfa:100855552.
Phylogenomic databases
eggNOG	COG3869.
GeneTree	ENSGT00550000074561.
HOGENOM	HOG000232165.
HOVERGEN	HBG001339.
InParanoid	P05124.
KO	K00933.
OMA	RGHEFMW.
OrthoDB	EOG4R7V9X.
Family and domain databases
Gene3D	1.10.135.10. 1 hit. 3.30.590.10. 1 hit.
InterPro	IPR000749. 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]
PANTHER	PTHR11547. PTHR11547. 1 hit.
Pfam	PF00217. ATP-gua_Ptrans. 1 hit. PF02807. ATP-gua_PtransN. 1 hit. [Graphical view]
SUPFAM	SSF48034. ATP-gua_Ptrans. 1 hit.
PROSITE	PS00112. PHOSPHAGEN_KINASE. 1 hit. PS51510. PHOSPHAGEN_KINASE_C. 1 hit. PS51509. PHOSPHAGEN_KINASE_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20855457.

Entry information

Entry name

KCRB_CANFA

Accession

Primary (citable) accession number: P05124

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents