Reviewed, UniProtKB/Swiss-Prot P12277 (KCRB_HUMAN)

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
Synonyms:	CKBB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Sequence similarities	Belongs to the ATP:guanido phosphotransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	creatine metabolic process Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW creatine kinase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.11 Ref.12

Chain

2 – 381

380

Creatine kinase B-type

PRO_0000211966

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

4

1

Phosphoserine Ref.17

Modified residue

35

1

Phosphothreonine Ref.15

Modified residue

39

1

Phosphotyrosine By similarity

Modified residue

125

1

Phosphotyrosine By similarity

Modified residue

164

1

Phosphoserine By similarity

Modified residue

199

1

Phosphoserine Ref.15

Natural variations

Natural variant

177

1

K → R: dbSNP rs36002620. Ref.7

VAR_025838

Natural variant

309

1

S → L: dbSNP rs35156510. Ref.7

VAR_025839

Natural variant

360

1

L → F: dbSNP rs12505.

VAR_049674

Experimental info

Mutagenesis

283

1

C → S or Y: Complete loss of activity. Ref.14

Mutagenesis

292

1

R → H, L or Q: Complete loss of activity. Ref.14

Mutagenesis

292

1

R → K: 42% of wild-type activity. Ref.14

Mutagenesis

340

1

D → E: No change in activity. Ref.14

Sequence conflict

41 – 42

2

EL → DV in AAA76851. Ref.1

Sequence conflict

78

1

D → G in AAA76850. Ref.3

Sequence conflict

78

1

D → G in AAA52024. Ref.10

Sequence conflict

98 – 99

2

GG → RR in AAA76851. Ref.1

Sequence conflict

105 – 106

2

EH → DD in AAA76851. Ref.1

Sequence conflict

130

1

R → G in AAA76850. Ref.3

Sequence conflict

132

1

R → A in AAA76851. Ref.1

Sequence conflict

144

1

P → Q in CAG47064. Ref.6

Sequence conflict

203

1

L → S in AAC31758. Ref.2

Sequence conflict

215 – 216

2

RG → AR in AAA76851. Ref.1

Sequence conflict

296

1

H → D in AAA76851. Ref.1

Sequence conflict

358

1

K → R in BAG35211. Ref.5

Secondary structure

1

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381

Helix Strand Turn

Details...

Helix

7 – 11

5

Helix

16 – 19

4

Helix

29 – 33

5

Helix

36 – 42

7

Helix

53 – 57

5

Helix

81 – 84

4

Helix

86 – 96

11

Helix

112 – 114

3

Turn

123 – 125

3

Beta strand

126 – 133

8

Turn

143 – 145

3

Helix

151 – 162

12

Helix

181 – 189

9

Helix

200 – 203

4

Turn

209 – 214

6

Beta strand

223 – 241

19

Helix

246 – 254

9

Helix

258 – 266

9

Helix

284 – 286

3

Helix

308 – 314

7

Beta strand

317 – 320

4

Helix

326 – 329

4

Beta strand

334 – 338

5

Helix

346 – 354

9

Helix

358 – 368

11

Helix

374 – 376

3

Sequences

	Sequence		Length	Mass (Da)
	P12277-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 637AA67A86AE3059	FASTA	381	42,644
	10 20 30 40 50 60 MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG 70 80 90 100 110 120 VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD 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 DNKTFLVWVN EEDHLRVISM 250 260 270 280 290 300 QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP 310 320 330 340 350 360 NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL 370 380 IEMEQRLEQG QAIDDLMPAQ K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human creatine kinase: isolation and sequence analysis of cDNA clones for the B subunit, development of subunit specific probes and determination of gene copy number." Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B. Biochem. Biophys. Res. Commun. 144:1116-1127(1987) [PubMed: 3034271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and expression of the human creatine kinase B gene." Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I., Wieringa B. Genomics 1:126-137(1987) [PubMed: 3692484] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci." Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A. J. Clin. Invest. 79:1412-1420(1987) [PubMed: 2883200] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete nucleotide sequence of the human creatine kinase B gene." Mariman E.C.M., Schepens J.T.G., Wieringa B. Nucleic Acids Res. 17:6385-6385(1989) [PubMed: 2771648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum and Subthalamic nucleus.
[6]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	NIEHS SNPs program Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-177 AND LEU-309.
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Eye and Lung.
[10]	"Isolation of a functional human gene for brain creatine kinase." Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P. J. Biol. Chem. 263:2442-2446(1988) [PubMed: 2828370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
[11]	"Protein analysis of human maculae in relation to age-related maculopathy." Kliffen M., de Jong P.T.V.M., Luider T.M. Lab. Invest. 73:267-272(1995) [PubMed: 7637327] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22. Tissue: Eye.
[12]	Bienvenut W.V., Heiserich L., Gottlieb E. Submitted (MAR-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314 AND 342-366, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[13]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 33-43; 87-96; 108-130; 157-172; 224-236; 253-265; 320-341 AND 359-381, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[14]	"Determination of the catalytic site of creatine kinase by site-directed mutagenesis." Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S. Biochim. Biophys. Acta 1206:97-104(1994) [PubMed: 8186255] [Abstract] Cited for: MUTAGENESIS OF CYS-283; ARG-292 AND ASP-340.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, MASS SPECTROMETRY.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Wikipedia

Creatine kinase entry

Wikipedia

CKB entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

IPI

IPI00022977.

PIR

KIHUCB. S15935.

RefSeq

NP_001814.2.

UniGene

Hs.173724

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B6R	X-ray	2.00	A/B	1-381	[»]
3DRB	X-ray	2.00	A/B	1-381	[»]
3DRE	X-ray	2.20	A/B	1-381	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P12277. 5 interactions.

STRING

P12277.

PTM databases

PhosphoSite

P12277.

2-D gel databases

HSC-2DPAGE

P12277.

PHCI-2DPAGE

P12277.

REPRODUCTION-2DPAGE

IPI00022977.
P12277.

Proteomic databases

PeptideAtlas

P12277.

PRIDE

P12277.

Genome annotation databases

Ensembl

ENST00000348956; ENSP00000299198; ENSG00000166165; Homo sapiens. [Genome view]

GeneID

1152.

KEGG

hsa:1152.

UCSC

uc001ynf.1. human.

Organism-specific databases

CTD

1152.

GeneCards

GC14M103055.

H-InvDB

HIX0012001.

HGNC

HGNC:1991. CKB.

HPA

HPA001254.

MIM

123280. gene.

PharmGKB

PA26528.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07258.

HOGENOM

HBG445448.

HOVERGEN

P12277.

InParanoid

P12277.

OMA

SYGILAN.

OrthoDB

EOG986BZ7.

PhylomeDB

P12277.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14573.

BRENDA

2.7.3.2. 247.

Reactome

REACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpress

P12277.

Bgee

P12277.

CleanEx

HS_CKB.

Genevestigator

P12277.

Family and domain databases

InterPro

IPR000749. ATP-guanido_PTrfase.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[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...

Other Resources

DrugBank

DB00148. Creatine.

NextBio

4784.

SOURCE

Search...

Entry information

Entry name

KCRB_HUMAN

Accession

Primary (citable) accession number: P12277
Secondary accession number(s): A8K236 , B2R5R4, Q2LE07, Q6FG40, Q9UC66

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	January 19, 2010
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.