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P00567 (KCRB_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 381380Creatine kinase B-type
PRO_0000211969

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 residue41Phosphoserine By similarity
Modified residue351Phosphothreonine By similarity
Modified residue1251Phosphotyrosine By similarity
Modified residue1641Phosphoserine By similarity
Modified residue1991Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P00567 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0001F0FF3A1F3F40

FASTA38142,663
        10         20         30         40         50         60 
MPFSNTHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPEMDA ELRAKSTPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEAFKELFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAVEKLAVE 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 
HLGQHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 

       370        380 
IEMEQRLEQG QAIDDLMPAQ K

« Hide

References

[1]"Two tissue-specific isozymes of creatine kinase have closely matched amino acid sequences."
Pickering L., Pang H., Biemann K., Munro H., Schimmel P.
Proc. Natl. Acad. Sci. U.S.A. 82:2310-2314(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11306 mRNA. Translation: AAA31201.1.
PIRKIRBCB. A00678.
RefSeqNP_001075730.1. NM_001082261.1.
UniGeneOcu.3366.

3D structure databases

ProteinModelPortalP00567.
SMRP00567. Positions 2-381.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000007616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009085.

Organism-specific databases

CTD1152.

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
OrthoDBEOG4R7V9X.

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...

Entry information

Entry nameKCRB_RABIT
AccessionPrimary (citable) accession number: P00567
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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