Reviewed, UniProtKB/Swiss-Prot P05122 (KCRB_CHICK)

Names and origin

Protein names

Recommended name:
    Creatine kinase B-type
    EC=2.7.3.2
Alternative name(s):
    Creatine kinase B chain
    B-CK

Gene names

Name:

CKB

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 381

381

Creatine kinase B-type

PRO_0000211971

Regions

Nucleotide binding

128 – 132

5

ATP By similarity

Nucleotide binding

320 – 325

6

ATP By similarity

Sites

Binding site

191

1

ATP By similarity

Binding site

236

1

ATP By similarity

Binding site

292

1

ATP By similarity

Binding site

335

1

ATP By similarity

Amino acid modifications

Modified residue

282

1

Phosphothreonine; by autocatalysis Probable

Modified residue

285

1

Phosphoserine; by autocatalysis Probable

Modified residue

289

1

Phosphothreonine; by autocatalysis Probable

Natural variations

Alternative sequence

1 – 69

69

Missing in isoform Bb-CK-4.

VSP_010770

Alternative sequence

1 – 65

65

MPFSN…VDNPG → MAQLNNQRLPPEEEYPDLST HNNHMAKVLTLDLYKKLRDR VTPSGFTLDDVIQTGVDNPG in isoform Ba-CK.

VSP_002814

Alternative sequence

1 – 29

29

Missing in isoform Bb-CK-3.

VSP_010769

Alternative sequence

1 – 11

11

Missing in isoform Bb-CK-2.

VSP_010768

Secondary structure

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381

Helix Strand Turn

Details...

Helix

6 – 13

8

Helix

16 – 19

4

Helix

29 – 33

5

Helix

36 – 42

7

Helix

53 – 62

10

Beta strand

67 – 69

3

Helix

81 – 84

4

Helix

86 – 96

11

Helix

112 – 114

3

Turn

123 – 125

3

Beta strand

126 – 135

10

Turn

143 – 145

3

Helix

148 – 162

15

Helix

167 – 169

3

Beta strand

171 – 175

5

Helix

176 – 178

3

Helix

181 – 189

9

Helix

200 – 203

4

Turn

204 – 214

11

Beta strand

216 – 220

5

Beta strand

223 – 244

22

Helix

246 – 266

21

Turn

275 – 277

3

Helix

284 – 286

3

Beta strand

292 – 298

7

Helix

300 – 303

4

Helix

308 – 315

8

Beta strand

317 – 320

4

Turn

329 – 332

4

Beta strand

333 – 338

6

Beta strand

342 – 344

3

Helix

346 – 368

23

Helix

374 – 376

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Bb-CK-1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 313BCCB46BCDD02B	FASTA	381	42,871
	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
	Isoform Ba-CK. Checksum: 5A107A22ABCB046F	FASTA	376	42,267
	10 20 30 40 50 60 MAQLNNQRLP PEEEYPDLST HNNHMAKVLT LDLYKKLRDR VTPSGFTLDD VIQTGVDNPG 70 80 90 100 110 120 HPFIMTVGCV AGDEESYEVF KELFDPVIED RHGGYKPTDE HKTDLNADNL QGGDDLDPNY 130 140 150 160 170 180 VLSSRVRTGR SIRGFCLPPH CSRGERRAIE KLSVEALGSL GGDLKGKYYA LRNMTDAEQQ 190 200 210 220 230 240 QLIDDHFLFD KPVSPLLLAS GMARDWPDAR GIWHNDNKTF LVWINEEDHL RVISMQKGGN 250 260 270 280 290 300 MKEVFTRFCT GLTQIETLFK SKNYEFMWNP HLGYILTCPS NLGTGLRAGV HIKLPNLGKH 310 320 330 340 350 360 EKFGEVLKRL RLQKRGTGGV DTAAVGGVFD VSNADRLGFS EVELVQMVVD GVKLLIEMEK 370 RLEKGQSIDD LMPAQK
	Isoform Bb-CK-2. Checksum: A08833EFEBB99797	FASTA	370	41,601
	10 20 30 40 50 60 MKYSVDDEYP DLSVHNNHMA KVLTLDLYKK LRDRQTSSGF TLDDVIQTGV DNPGHPFIMT 70 80 90 100 110 120 VGCVAGDEES YEVFKELFDP VIEDRHGGYK PTDEHKTDLN ADNLQGGDDL DPNYVLSSRV 130 140 150 160 170 180 RTGRSIRGFC LPPHCSRGER RAIEKLSVEA LGSLGGDLKG KYYALRNMTD AEQQQLIDDH 190 200 210 220 230 240 FLFDKPVSPL LLASGMARDW PDARGIWHND NKTFLVWINE EDHLRVISMQ KGGNMKEVFT 250 260 270 280 290 300 RFCTGLTQIE TLFKSKNYEF MWNPHLGYIL TCPSNLGTGL RAGVHIKLPN LGKHEKFGEV 310 320 330 340 350 360 LKRLRLQKRG TGGVDTAAVG GVFDVSNADR LGFSEVELVQ MVVDGVKLLI EMEKRLEKGQ 370 SIDDLMPAQK
	Isoform Bb-CK-3. Checksum: D0BE655ACDE7C082	FASTA	352	39,456
	10 20 30 40 50 60 MAKVLTLDLY KKLRDRQTSS GFTLDDVIQT GVDNPGHPFI MTVGCVAGDE ESYEVFKELF 70 80 90 100 110 120 DPVIEDRHGG YKPTDEHKTD LNADNLQGGD DLDPNYVLSS RVRTGRSIRG FCLPPHCSRG 130 140 150 160 170 180 ERRAIEKLSV EALGSLGGDL KGKYYALRNM TDAEQQQLID DHFLFDKPVS PLLLASGMAR 190 200 210 220 230 240 DWPDARGIWH NDNKTFLVWI NEEDHLRVIS MQKGGNMKEV FTRFCTGLTQ IETLFKSKNY 250 260 270 280 290 300 EFMWNPHLGY ILTCPSNLGT GLRAGVHIKL PNLGKHEKFG EVLKRLRLQK RGTGGVDTAA 310 320 330 340 350 VGGVFDVSNA DRLGFSEVEL VQMVVDGVKL LIEMEKRLEK GQSIDDLMPA QK
	Isoform Bb-CK-4. Checksum: 0FDE036FF4AD60C6	FASTA	312	34,983
	10 20 30 40 50 60 MTVGCVAGDE ESYEVFKELF DPVIEDRHGG YKPTDEHKTD LNADNLQGGD DLDPNYVLSS 70 80 90 100 110 120 RVRTGRSIRG FCLPPHCSRG ERRAIEKLSV EALGSLGGDL KGKYYALRNM TDAEQQQLID 130 140 150 160 170 180 DHFLFDKPVS PLLLASGMAR DWPDARGIWH NDNKTFLVWI NEEDHLRVIS MQKGGNMKEV 190 200 210 220 230 240 FTRFCTGLTQ IETLFKSKNY EFMWNPHLGY ILTCPSNLGT GLRAGVHIKL PNLGKHEKFG 250 260 270 280 290 300 EVLKRLRLQK RGTGGVDTAA VGGVFDVSNA DRLGFSEVEL VQMVVDGVKL LIEMEKRLEK 310 GQSIDDLMPA QK

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: 3513124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BB-CK).
[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: 2365692] [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: 3840441] [Abstract] Cited for: NUCLEOTIDE SEQUENCE 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: 7669815] [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: 2307674] [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: 10595529] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03509 mRNA. Translation: CAA27221.1.
M35381 Genomic DNA. Translation: AAA48687.1.
M33714 , M33711, M33712, M33713 Genomic DNA. Translation: AAA48613.1.
M33714 , M33711, M33712, M33713 Genomic DNA. Translation: AAA48614.1.

IPI

IPI00573166.
IPI00577121.
IPI00594985.
IPI00599522.
IPI00604016.

PIR

A24793. A37059.

RefSeq

NP_990641.1.

UniGene

Gga.2722

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QH4	X-ray	1.41	A/B/C/D	2-381	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P05122.

Genome annotation databases

Ensembl

ENSGALT00000018765; ENSGALP00000018742; ENSGALG00000011511; Gallus gallus. [Genome view]
ENSGALT00000018766; ENSGALP00000018743; ENSGALG00000011511; Gallus gallus. [Genome view]

GeneID

396248.

KEGG

gga:396248.

Organism-specific databases

CTD

396248.

Phylogenomic databases

HOVERGEN

P05122.

Enzyme and pathway databases

BRENDA

2.7.3.2. 4.

Family and domain databases

InterPro

IPR000749. ATP-guanido_PTrfase.
IPR014746. Gln_synth/guanido_kin_cat.
[Graphical view]

Gene3D

G3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit.
G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.

PANTHER

PTHR11547. ATP-gua_Ptrans. 1 hit.

Pfam

PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]

PROSITE

PS00112. GUANIDO_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KCRB_CHICK

Accession

Primary (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:	September 1, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)