Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05122

- KCRB_CHICK

UniProt

P05122 - KCRB_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Creatine kinase B-type

Gene

CKB

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 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.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei130 – 1301ATPPROSITE-ProRule annotation
Binding sitei132 – 1321ATPPROSITE-ProRule annotation
Binding sitei191 – 1911ATPPROSITE-ProRule annotation
Binding sitei232 – 2321SubstrateBy similarity
Binding sitei236 – 2361ATPPROSITE-ProRule annotation
Binding sitei285 – 2851SubstrateBy similarity
Binding sitei292 – 2921ATPPROSITE-ProRule annotation
Binding sitei320 – 3201ATPPROSITE-ProRule annotation
Binding sitei335 – 3351ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi128 – 1325ATPPROSITE-ProRule annotation
Nucleotide bindingi320 – 3256ATPPROSITE-ProRule annotation

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 B-type (EC:2.7.3.2)
Alternative name(s):
B-CK
Creatine kinase B chain
Gene namesi
Name:CKB
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 381381Creatine kinase B-typePRO_0000211971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei282 – 2821Phosphothreonine; by autocatalysis1 Publication
Modified residuei285 – 2851Phosphoserine; by autocatalysis1 Publication
Modified residuei289 – 2891Phosphothreonine; by autocatalysis1 Publication

Post-translational modificationi

Ba-CK and Bb-CK are phosphorylated.1 Publication
The N-terminus of BA-CK is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05122.
PRIDEiP05122.

Expressioni

Tissue specificityi

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

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

BioGridi676508. 1 interaction.
IntActiP05122. 1 interaction.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 138
Helixi16 – 194
Helixi29 – 335
Helixi36 – 427
Helixi53 – 6210
Beta strandi67 – 693
Helixi81 – 844
Helixi86 – 9611
Helixi112 – 1143
Turni123 – 1253
Beta strandi126 – 13510
Turni143 – 1453
Helixi148 – 16215
Helixi167 – 1693
Beta strandi171 – 1755
Helixi176 – 1783
Helixi181 – 1899
Helixi200 – 2034
Turni204 – 21411
Beta strandi216 – 2205
Beta strandi223 – 24422
Helixi246 – 26621
Turni275 – 2773
Helixi284 – 2863
Beta strandi292 – 2987
Helixi300 – 3034
Helixi308 – 3158
Beta strandi317 – 3204
Turni329 – 3324
Beta strandi333 – 3386
Beta strandi342 – 3443
Helixi346 – 36823
Helixi374 – 3763

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QH4X-ray1.41A/B/C/D2-381[»]
ProteinModelPortaliP05122.
SMRiP05122. Positions 2-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05122.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 9888Phosphagen kinase N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 367243Phosphagen kinase C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
Contains 1 phosphagen kinase C-terminal domain.PROSITE-ProRule annotation
Contains 1 phosphagen kinase N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3869.
HOGENOMiHOG000232165.
HOVERGENiHBG001339.
InParanoidiP05122.
KOiK00933.
PhylomeDBiP05122.

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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform Bb-CK-1 (identifier: P05122-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPFSNSHNLL KMKYSVDDEY PDLSVHNNHM AKVLTLDLYK KLRDRQTSSG
60 70 80 90 100
FTLDDVIQTG VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PVIEDRHGGY
110 120 130 140 150
KPTDEHKTDL NADNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE
160 170 180 190 200
RRAIEKLSVE ALGSLGGDLK GKYYALRNMT DAEQQQLIDD HFLFDKPVSP
210 220 230 240 250
LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM QKGGNMKEVF
260 270 280 290 300
TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
310 320 330 340 350
NLGKHEKFGE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV
360 370 380
QMVVDGVKLL IEMEKRLEKG QSIDDLMPAQ K
Length:381
Mass (Da):42,871
Last modified:August 13, 1987 - v1
Checksum:i313BCCB46BCDD02B
GO
Isoform Ba-CK (identifier: P05122-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MPFSNSHNLL...VIQTGVDNPG → MAQLNNQRLP...VIQTGVDNPG

Show »
Length:376
Mass (Da):42,267
Checksum:i5A107A22ABCB046F
GO
Isoform Bb-CK-2 (identifier: P05122-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.

Show »
Length:370
Mass (Da):41,601
Checksum:iA08833EFEBB99797
GO
Isoform Bb-CK-3 (identifier: P05122-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:352
Mass (Da):39,456
Checksum:iD0BE655ACDE7C082
GO
Isoform Bb-CK-4 (identifier: P05122-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:312
Mass (Da):34,983
Checksum:i0FDE036FF4AD60C6
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969Missing in isoform Bb-CK-4. CuratedVSP_010770Add
BLAST
Alternative sequencei1 – 6565MPFSN…VDNPG → MAQLNNQRLPPEEEYPDLST HNNHMAKVLTLDLYKKLRDR VTPSGFTLDDVIQTGVDNPG in isoform Ba-CK. CuratedVSP_002814Add
BLAST
Alternative sequencei1 – 2929Missing in isoform Bb-CK-3. CuratedVSP_010769Add
BLAST
Alternative sequencei1 – 1111Missing in isoform Bb-CK-2. CuratedVSP_010768Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03509 mRNA. Translation: CAA27221.1.
M33714
, M33711, M33712, M33713 Genomic DNA. Translation: AAA48613.1.
M33714
, M33711, M33712, M33713 Genomic DNA. Translation: AAA48614.1.
M35381 Genomic DNA. Translation: AAA48687.1.
PIRiA37059. A24793.
RefSeqiNP_990641.1. NM_205310.1. [P05122-1]
UniGeneiGga.2722.

Genome annotation databases

GeneIDi396248.
KEGGigga:396248.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03509 mRNA. Translation: CAA27221.1 .
M33714
, M33711 , M33712 , M33713 Genomic DNA. Translation: AAA48613.1 .
M33714
, M33711 , M33712 , M33713 Genomic DNA. Translation: AAA48614.1 .
M35381 Genomic DNA. Translation: AAA48687.1 .
PIRi A37059. A24793.
RefSeqi NP_990641.1. NM_205310.1. [P05122-1 ]
UniGenei Gga.2722.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QH4 X-ray 1.41 A/B/C/D 2-381 [» ]
ProteinModelPortali P05122.
SMRi P05122. Positions 2-381.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 676508. 1 interaction.
IntActi P05122. 1 interaction.

Proteomic databases

PaxDbi P05122.
PRIDEi P05122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396248.
KEGGi gga:396248.

Organism-specific databases

CTDi 1152.

Phylogenomic databases

eggNOGi COG3869.
HOGENOMi HOG000232165.
HOVERGENi HBG001339.
InParanoidi P05122.
KOi K00933.
PhylomeDBi P05122.

Miscellaneous databases

EvolutionaryTracei P05122.
NextBioi 20816300.
PROi P05122.

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. "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).

Entry informationi

Entry nameiKCRB_CHICK
AccessioniPrimary (citable) accession number: P05122
Secondary accession number(s): Q92061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3