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UniProtKB/Swiss-Prot entry P05122


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCRB_CHICK
Primary accession number P05122
Secondary accession number Q92061
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 75)
Name and origin of the protein
Protein name Creatine kinase B-type
Synonyms EC 2.7.3.2
Creatine kinase B chain
B-CK
Gene name
Name: CKB
From
Gallus gallus (Chicken) [TaxID: 9031] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BB-CK).
DOI=10.1093/nar/14.3.1449; PubMed=3513124 [NCBI, ExPASy, EBI, Israel, Japan]
Hossle J.P., Rosenberg U.B., Schaefer B.W., Eppenberger H.M., Perriard J.-C.;
"The primary structure of chicken B-creatine kinase and evidence for heterogeneity of its mRNA.";
Nucleic Acids Res. 14:1449-1463(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BA-CK AND BB-CK-1).
STRAIN=White leghorn;
TISSUE=Brain;
PubMed=2365692 [NCBI, ExPASy, EBI, Israel, Japan]
Wirz T., Braendle U., Soldati T., Hossle J.P., Perriard J.-C.;
"A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N termini by alternative splicing.";
J. Biol. Chem. 265:11656-11666(1990).
[3]
NUCLEOTIDE SEQUENCE OF 317-381.
TISSUE=Brain;
DOI=10.1016/0012-1606(85)90121-6; PubMed=3840441 [NCBI, ExPASy, EBI, Israel, Japan]
Kwiatkowski R.W., Ehrismann R., Schweinfest C.W., Dottin R.P.;
"Accumulation of creatine kinase mRNA during myogenesis: molecular cloning of a B-creatine kinase cDNA.";
Dev. Biol. 112:84-88(1985).
[4]
PROTEIN SEQUENCE OF 2-9; 12-20; 266-277 AND 320-329, AND AUTOPHOSPHORYLATION.
DOI=10.1016/0167-4838(95)00083-7; PubMed=7669815 [NCBI, ExPASy, EBI, Israel, Japan]
Hemmer W., Furter-Graves E.M., Frank G., Wallimann T., Furter R.;
"Autophosphorylation of creatine kinase: characterization and identification of a specifically phosphorylated peptide.";
Biochim. Biophys. Acta 1251:81-90(1995).
[5]
ALTERNATIVE SPLICING (ISOFORMS BA-CK-2; BA-CK-3 AND BA-CK-4), AND PHOSPHORYLATION.
PubMed=2307674 [NCBI, ExPASy, EBI, Israel, Japan]
Soldati T., Schaefer B.W., Perriard J.-C.;
"Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini.";
J. Biol. Chem. 265:4498-4506(1990).
[6]
X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS).
PubMed=10595529 [NCBI, ExPASy, EBI, Israel, Japan]
Eder M., Schlattner U., Becker A., Wallimann T., Kabsch W., Fritz-Wolf K.;
"Crystal structure of brain-type creatine kinase at 1.41-A resolution.";
Protein Sci. 8:2258-2269(1999).
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: 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.
  • ALTERNATIVE PRODUCTS: 5 named isoforms [FASTA] produced by alternative splicing.
    NameBb-CK-1
    Isoform IDP05122-1
    This is the isoform sequence displayed in this entry.
    NameBa-CK
    Isoform IDP05122-2
    Features which should be applied to build the isoform sequence: VSP_002814.
    NameBb-CK-2
    Isoform IDP05122-3
    Features which should be applied to build the isoform sequence: VSP_010768.
    NameBb-CK-3
    Isoform IDP05122-4
    Features which should be applied to build the isoform sequence: VSP_010769.
    NameBb-CK-4
    Isoform IDP05122-5
    Features which should be applied to build the isoform sequence: VSP_010770.
  • TISSUE SPECIFICITY: Expressed in almost all tissues and found enriched in various region of the brain, retina heart, gizzard, gut and sperm.
  • PTM: Ba-CK and Bb-CK are phosphorylated.
  • PTM: The N-terminus of BA-CK is blocked.
  • SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03509; CAA27221.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35381; AAA48687.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33714; AAA48613.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33711; AAA48613.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33712; AAA48613.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33713; AAA48613.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33714; AAA48614.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33711; AAA48614.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33712; AAA48614.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M33713; AAA48614.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37059; A24793.
RefSeq NP_990641.1; -.
UniGene Gga.2722
3D structure databases
PDB
1QH4; X-ray; 1.41 A; A/B/C/D=2-381.[ExPASy / RCSB / EBI]
PDBsum 1QH4; -.
ModBase P05122.
Family and domain databases
InterPro IPR000749; ATP-gua_Ptrans.
IPR014746; Gln_synth/guanido_kin_cat.
Graphical view of domain structure.
Gene3D G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
PANTHER PTHR11547; ATP-gua_Ptrans; 1.
Pfam PF00217; ATP-gua_Ptrans; 1.
PF02807; ATP-gua_PtransN; 1.
Pfam graphical view of domain structure.
PROSITE PS00112; GUANIDO_KINASE; 1.
BLOCKS P05122.
Genome annotation databases
Ensembl ENSGALG00000011511; Gallus gallus. [Contig view]
GeneID 396248; -.
KEGG gga:396248; -.
Phylogenomic databases
HOVERGEN P05122; -.
Other
LinkHub P05122; -.
ProtoNet P05122.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   381  381     Creatine kinase B-type. PRO_0000211971
NP_BIND   128   132  5     ATP (By similarity). 
NP_BIND   320   325  6     ATP (By similarity). 
ACT_SITE   283   283         
BINDING   191   191        ATP (By similarity). 
BINDING   292   292        ATP (By similarity). 
BINDING   335   335        ATP (By similarity). 
MOD_RES   282   282        Phosphothreonine; by autocatalysis (Probable). 
MOD_RES   285   285        Phosphoserine; by autocatalysis (Probable). 
MOD_RES   289   289        Phosphothreonine; by autocatalysis (Probable). 
VAR_SEQ   1    69        Missing (in isoform Bb-CK-4). VSP_010770
VAR_SEQ   1    65        MPFSNSHNLLKMKYSVDDEYPDLSVHNNHMAKVLTLDLYK KLRDRQTSSGFTLDDVIQTGVDNPG -> MAQLNNQRLPPEEEYPDLSTHNNHMAKVLTLDLYKKLRDR VTPSGFTLDDVIQTGVDNPG (in isoform Ba-CK). VSP_002814
VAR_SEQ   1    29        Missing (in isoform Bb-CK-3). VSP_010769
VAR_SEQ   1    11        Missing (in isoform Bb-CK-2). VSP_010768
HELIX   6    13  8      
HELIX   16    19  4      
HELIX   29    33  5      
HELIX   36    42  7      
HELIX   53    62  10      
STRAND   67    69  3      
HELIX   81    84  4      
HELIX   86    96  11      
HELIX   112   114  3      
TURN   123   125  3      
STRAND   126   135  10      
TURN   143   145  3      
HELIX   148   162  15      
HELIX   167   169  3      
STRAND   171   175  5      
HELIX   176   178  3      
HELIX   181   189  9      
HELIX   200   203  4      
TURN   204   214  11      
STRAND   216   220  5      
STRAND   223   244  22      
HELIX   246   266  21      
TURN   275   277  3      
HELIX   284   286  3      
STRAND   292   298  7      
HELIX   300   303  4      
HELIX   308   315  8      
STRAND   317   320  4      
TURN   329   332  4      
STRAND   333   338  6      
STRAND   342   344  3      
HELIX   346   368  23      
HELIX   374   376  3      
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 42871 Da [This is the MW of the unprocessed precursor] CRC64: 313BCCB46BCDD02B [This is a checksum on the sequence]
        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 

P05122 in FASTA format

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