NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/0006-291X(86)90294-9; PubMed=3755597 [NCBI, ExPASy, EBI, Israel, Japan]
Billadello J.J., Kelly D.P., Roman D.G., Strauss A.W.;
"The complete nucleotide sequence of canine brain B creatine kinase mRNA: homology in the coding and 3' noncoding regions among species.";
Biochem. Biophys. Res. Commun. 138:392-398(1986).

[2]

PROTEIN SEQUENCE OF 2-30; 44-61; 87-95; 138-149; 158-171; 178-208; 224-236; 247-261; 268-287; 321-357 AND 364-381.
TISSUE=Brain;
PubMed=3866230 [NCBI, ExPASy, EBI, Israel, Japan]
Roman D.G., Billadello J.J., Gordon J., Grace A., Sobel B., Strauss A.W.;
"Complete nucleotide sequence of dog heart creatine kinase mRNA: conservation of amino acid sequence within and among species.";
Proc. Natl. Acad. Sci. U.S.A. 82:8394-8398(1985).

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.
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

M13453; AAA30837.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24227; B24686.

3D structure databases

HSSP

P05122; 1QH4. [HSSP ENTRY / PDB]

SMR

P05124; 2-381.

ModBase

P05124.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from AgBase).
GO:0005515;	Molecular function: protein binding (inferred from sequence or structural similarity from AgBase).
GO:0007420;	Biological process: brain development (inferred from sequence or structural similarity from AgBase).
GO:0030644;	Biological process: cellular chloride ion homeostasis (inferred from sequence or structural similarity from AgBase).
QuickGo view.

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

P05124.

Genome annotation databases

Ensembl

ENSCAFG00000018277; Canis familiaris. [Contig view]

Phylogenomic databases

HOVERGEN

P05124; -.

Other

ProtoNet

P05124.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 381`	`380`	`Creatine kinase B-type.`	`PRO_0000211965`
`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`	`39 39`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`125 125`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`164 164`		`Phosphoserine (By similarity).`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 42701 Da [This is the MW of the unprocessed precursor]

CRC64: 2C2F925C78F16364 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPFSNSHNTL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPYIM TVGCVAGDEE SYDVFKELFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE 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 
HLGKHEKFPE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 

       370        380 
IEMEQRLEQG QAIDDLVPAQ K

P05124 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools