Skip Header

Contribute Send feedback
Read comments (?) or add your own

P05122 (KCRB_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase B-type
EC=2.7.3.2
Alternative name(s):
B-CK
Creatine kinase B chain
Gene names
Name:CKB
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Tissue specificity

Expressed in almost all tissues and found enriched in various region of the brain, retina heart, gizzard, gut and sperm.

Post-translational modification

Ba-CK and Bb-CK are phosphorylated. Ref.4 Ref.5

The N-terminus of BA-CK is blocked.

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 componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

creatine kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform Bb-CK-1 (identifier: P05122-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Ba-CK (identifier: P05122-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MPFSNSHNLL...VIQTGVDNPG → MAQLNNQRLP...VIQTGVDNPG
Isoform Bb-CK-2 (identifier: P05122-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
Isoform Bb-CK-3 (identifier: P05122-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
Isoform Bb-CK-4 (identifier: P05122-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 381381Creatine kinase B-type
PRO_0000211971

Regions

Domain11 – 9888Phosphagen kinase N-terminal
Domain125 – 367243Phosphagen kinase C-terminal
Nucleotide binding128 – 1325ATP By similarity
Nucleotide binding320 – 3256ATP By similarity

Sites

Binding site1301ATP By similarity
Binding site1321ATP By similarity
Binding site1911ATP By similarity
Binding site2321Substrate By similarity
Binding site2361ATP By similarity
Binding site2851Substrate By similarity
Binding site2921ATP By similarity
Binding site3201ATP By similarity
Binding site3351ATP By similarity

Amino acid modifications

Modified residue2821Phosphothreonine; by autocatalysis Probable
Modified residue2851Phosphoserine; by autocatalysis Probable
Modified residue2891Phosphothreonine; by autocatalysis Probable

Natural variations

Alternative sequence1 – 6969Missing in isoform Bb-CK-4.
VSP_010770
Alternative sequence1 – 6565MPFSN…VDNPG → MAQLNNQRLPPEEEYPDLST HNNHMAKVLTLDLYKKLRDR VTPSGFTLDDVIQTGVDNPG in isoform Ba-CK.
VSP_002814
Alternative sequence1 – 2929Missing in isoform Bb-CK-3.
VSP_010769
Alternative sequence1 – 1111Missing in isoform Bb-CK-2.
VSP_010768

Secondary structure

1 ............................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Bb-CK-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 313BCCB46BCDD02B

FASTA38142,871
        10         20         30         40         50         60 
MPFSNSHNLL KMKYSVDDEY PDLSVHNNHM AKVLTLDLYK KLRDRQTSSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PVIEDRHGGY KPTDEHKTDL NADNLQGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLSVE ALGSLGGDLK GKYYALRNMT 

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

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

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

       370        380 
IEMEKRLEKG QSIDDLMPAQ K

« Hide

Isoform Ba-CK [UniParc].

Checksum: 5A107A22ABCB046F
Show »

FASTA37642,267
Isoform Bb-CK-2 [UniParc].

Checksum: A08833EFEBB99797
Show »

FASTA37041,601
Isoform Bb-CK-3 [UniParc].

Checksum: D0BE655ACDE7C082
Show »

FASTA35239,456
Isoform Bb-CK-4 [UniParc].

Checksum: 0FDE036FF4AD60C6
Show »

FASTA31234,983

References

[1]"The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA."
Hossle J.P., Rosenberg U.B., Schaefer B.W., Eppenberger H.M., Perriard J.-C.
Nucleic Acids Res. 14:1449-1463(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BB-CK-1).
[2]"A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing."
Wirz T., Braendle U., Soldati T., Hossle J.P., Perriard J.-C.
J. Biol. Chem. 265:11656-11666(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BA-CK AND BB-CK-1).
Strain: White leghorn.
Tissue: Brain.
[3]"Accumulation of creatine kinase mRNA during myogenesis: molecular cloning of a B-creatine kinase cDNA."
Kwiatkowski R.W., Ehrismann R., Schweinfest C.W., Dottin R.P.
Dev. Biol. 112:84-88(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-381.
Tissue: Brain.
[4]"Autophosphorylation of creatine kinase: characterization and identification of a specifically phosphorylated peptide."
Hemmer W., Furter-Graves E.M., Frank G., Wallimann T., Furter R.
Biochim. Biophys. Acta 1251:81-90(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9; 12-20; 266-277 AND 320-329, AUTOPHOSPHORYLATION.
[5]"Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini."
Soldati T., Schaefer B.W., Perriard J.-C.
J. Biol. Chem. 265:4498-4506(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS BA-CK-2; BA-CK-3 AND BA-CK-4), PHOSPHORYLATION.
[6]"Crystal structure of brain-type creatine kinase at 1.41-A resolution."
Eder M., Schlattner U., Becker A., Wallimann T., Kabsch W., Fritz-Wolf K.
Protein Sci. 8:2258-2269(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X03509 mRNA. Translation: CAA27221.1.
M33714 expand/collapse EMBL AC list , M33711, M33712, M33713 Genomic DNA. Translation: AAA48613.1.
M33714 expand/collapse EMBL AC list , M33711, M33712, M33713 Genomic DNA. Translation: AAA48614.1.
M35381 Genomic DNA. Translation: AAA48687.1.
IPIIPI00573166.
IPI00577121.
IPI00594985.
IPI00599522.
IPI00604016.
PIRA24793. A37059.
RefSeqNP_990641.1. NM_205310.1.
UniGeneGga.2722.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QH4X-ray1.41A/B/C/D2-381[»]
ProteinModelPortalP05122.
SMRP05122. Positions 2-381.
ModBaseSearch...

Protein-protein interaction databases

IntActP05122. 1 interaction.

Proteomic databases

PaxDbP05122.
PRIDEP05122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396248.
KEGGgga:396248.

Organism-specific databases

CTD1152.

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
KOK00933.

Gene expression databases

ArrayExpressP05122.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR000749. 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]
PANTHERPTHR11547. PTHR11547. 1 hit.
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. ATP-gua_Ptrans. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05122.
NextBio20816300.

Entry information

Entry nameKCRB_CHICK
AccessionPrimary (citable) accession number: P05122
Secondary accession number(s): Q92061
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents