P12277 · KCRB_HUMAN

  • Protein
    Creatine kinase B-type
  • Gene
    CKB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255).
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 (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity).
During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity).

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site72creatine (UniProtKB | ChEBI)
Binding site128-132ATP (UniProtKB | ChEBI)
Binding site130ATP (UniProtKB | ChEBI)
Binding site132ATP (UniProtKB | ChEBI)
Binding site191ATP (UniProtKB | ChEBI)
Binding site232creatine (UniProtKB | ChEBI)
Binding site236ATP (UniProtKB | ChEBI)
Binding site285creatine (UniProtKB | ChEBI)
Binding site292ATP (UniProtKB | ChEBI)
Binding site320ATP (UniProtKB | ChEBI)
Binding site320-325ATP (UniProtKB | ChEBI)
Binding site335ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentextracellular exosome
Cellular Componentextracellular space
Cellular Componentmitochondrion
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functioncreatine kinase activity
Molecular Functionubiquitin protein ligase binding
Biological Processfutile creatine cycle
Biological Processphosphocreatine biosynthetic process
Biological Processsubstantia nigra development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Creatine kinase B-type
  • EC number
  • Alternative names
    • Brain creatine kinase
      (B-CK)
    • Creatine kinase B chain
    • Creatine phosphokinase B-type (CPK-B)

Gene names

    • Name
      CKB
    • Synonyms
      CKBB

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P12277
  • Secondary accessions
    • A8K236
    • B2R5R4
    • Q2LE07
    • Q6FG40
    • Q9UC66

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Mitochondrion
Cell membrane
Note: Localizes to the mitochondria of thermogenic fat cells via the internal MTS-like signal (iMTS-L) region.

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_025838177in dbSNP:rs36002620
Mutagenesis283Complete loss of activity.
Mutagenesis292Complete loss of activity.
Mutagenesis29242% of wild-type activity.
Natural variantVAR_025839309in dbSNP:rs35156510
Mutagenesis340No change in activity.
Natural variantVAR_049674360in dbSNP:rs12505

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 386 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
ChainPRO_00002119662-381UniProtCreatine kinase B-type
Modified residue4UniProtPhosphoserine
Modified residue (large scale data)4PRIDEPhosphoserine
Modified residue (large scale data)6PRIDEPhosphoserine
Modified residue35UniProtPhosphothreonine
Modified residue (large scale data)35PRIDEPhosphothreonine
Modified residue (large scale data)39PRIDEPhosphotyrosine
Cross-link45UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link101UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link107UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue125UniProtPhosphotyrosine
Modified residue (large scale data)125PRIDEPhosphotyrosine
Modified residue (large scale data)163PRIDEPhosphoserine
Modified residue (large scale data)164PRIDEPhosphoserine
Modified residue (large scale data)178PRIDEPhosphoserine
Modified residue199UniProtPhosphoserine
Modified residue (large scale data)199PRIDEPhosphoserine
Modified residue269UniProt3'-nitrotyrosine
Modified residue309UniProtPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine
Modified residue322UniProtPhosphothreonine
Modified residue (large scale data)322PRIDEPhosphothreonine
Modified residue (large scale data)337PRIDEPhosphoserine
Cross-link381UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Ubiquitinated by the ECS(ASB9) complex, leading to its degradation by the proteasome.

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Dimer of identical or non-identical chains, which can be either B (brain type) or M (muscle type). With MM being the major form in skeletal muscle and myocardium, MB existing in myocardium, and BB existing in many tissues, especially brain. Interacts with SLC12A6 (via C-terminus); the interaction may be required for SLC12A6 potassium-chloride cotransport activity (PubMed:18566107).

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain11-98Phosphagen kinase N-terminal
Compositional bias96-113Basic and acidic residues
Region96-122Disordered
Domain125-367Phosphagen kinase C-terminal
Region130-138Internal MTS-like signal

Domain

The internal MTS-like signal (iMTS-L) mediates targeting to mitochondria thermogenic fat cells.

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    381
  • Mass (Da)
    42,644
  • Last updated
    1989-10-01 v1
  • Checksum
    637AA67A86AE3059
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0S2Z471A0A0S2Z471_HUMANCKB405
H0YJG0H0YJG0_HUMANCKB179
H0YJJ7H0YJJ7_HUMANCKB20
H0YJK0H0YJK0_HUMANCKB90
G3V461G3V461_HUMANCKB128
G3V4N7G3V4N7_HUMANCKB217
G3V2I1G3V2I1_HUMANCKB58

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict41-42in Ref. 1; AAA76851
Sequence conflict78in Ref. 3; AAA76850 and 10; AAA52024
Compositional bias96-113Basic and acidic residues
Sequence conflict98-99in Ref. 1; AAA76851
Sequence conflict105-106in Ref. 1; AAA76851
Sequence conflict130in Ref. 3; AAA76850
Sequence conflict132in Ref. 1; AAA76851
Sequence conflict144in Ref. 6; CAG47064
Sequence conflict203in Ref. 2; AAC31758
Sequence conflict215-216in Ref. 1; AAA76851
Sequence conflict296in Ref. 1; AAA76851
Sequence conflict358in Ref. 5; BAG35211

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M16451
EMBL· GenBank· DDBJ
AAA76851.1
EMBL· GenBank· DDBJ
mRNA
M21243
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21237
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21238
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21239
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21240
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21241
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
M21242
EMBL· GenBank· DDBJ
AAC31758.1
EMBL· GenBank· DDBJ
Genomic DNA
L47647
EMBL· GenBank· DDBJ
AAA76852.1
EMBL· GenBank· DDBJ
mRNA
M16364
EMBL· GenBank· DDBJ
AAA76850.1
EMBL· GenBank· DDBJ
mRNA
X15334
EMBL· GenBank· DDBJ
CAA33389.1
EMBL· GenBank· DDBJ
Genomic DNA
AK290101
EMBL· GenBank· DDBJ
BAF82790.1
EMBL· GenBank· DDBJ
mRNA
AK312282
EMBL· GenBank· DDBJ
BAG35211.1
EMBL· GenBank· DDBJ
mRNA
CR542268
EMBL· GenBank· DDBJ
CAG47064.1
EMBL· GenBank· DDBJ
mRNA
DQ333313
EMBL· GenBank· DDBJ
ABC67465.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471061
EMBL· GenBank· DDBJ
EAW81822.1
EMBL· GenBank· DDBJ
Genomic DNA
BC001190
EMBL· GenBank· DDBJ
AAH01190.1
EMBL· GenBank· DDBJ
mRNA
BC004914
EMBL· GenBank· DDBJ
AAH04914.1
EMBL· GenBank· DDBJ
mRNA
BC008323
EMBL· GenBank· DDBJ
AAH08323.1
EMBL· GenBank· DDBJ
mRNA
BC010002
EMBL· GenBank· DDBJ
AAH10002.1
EMBL· GenBank· DDBJ
mRNA
BC019259
EMBL· GenBank· DDBJ
AAH19259.1
EMBL· GenBank· DDBJ
mRNA
BC019281
EMBL· GenBank· DDBJ
AAH19281.1
EMBL· GenBank· DDBJ
mRNA
M22356
EMBL· GenBank· DDBJ
AAA52024.1
EMBL· GenBank· DDBJ
Genomic DNA
M22355
EMBL· GenBank· DDBJ
AAA52024.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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