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Reviewed, UniProtKB/Swiss-Prot P12277 (KCRB_HUMAN)

Last modified January 19, 2010. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcreatine metabolic process

Inferred from Experiment. Source: Reactome

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

   Molecular functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11 Ref.12
Chain2 – 381380Creatine kinase B-type
PRO_0000211966

Regions

Nucleotide binding128 – 1325ATP By similarity
Nucleotide binding320 – 3256ATP By similarity

Sites

Binding site1911ATP By similarity
Binding site2361ATP By similarity
Binding site2921ATP By similarity
Binding site3351ATP By similarity

Amino acid modifications

Modified residue41Phosphoserine Ref.17
Modified residue351Phosphothreonine Ref.15
Modified residue391Phosphotyrosine By similarity
Modified residue1251Phosphotyrosine By similarity
Modified residue1641Phosphoserine By similarity
Modified residue1991Phosphoserine Ref.15

Natural variations

Natural variant1771K → R: dbSNP rs36002620. Ref.7
VAR_025838
Natural variant3091S → L: dbSNP rs35156510. Ref.7
VAR_025839
Natural variant3601L → F: dbSNP rs12505.
VAR_049674

Experimental info

Mutagenesis2831C → S or Y: Complete loss of activity. Ref.14
Mutagenesis2921R → H, L or Q: Complete loss of activity. Ref.14
Mutagenesis2921R → K: 42% of wild-type activity. Ref.14
Mutagenesis3401D → E: No change in activity. Ref.14
Sequence conflict41 – 422EL → DV in AAA76851. Ref.1
Sequence conflict781D → G in AAA76850. Ref.3
Sequence conflict781D → G in AAA52024. Ref.10
Sequence conflict98 – 992GG → RR in AAA76851. Ref.1
Sequence conflict105 – 1062EH → DD in AAA76851. Ref.1
Sequence conflict1301R → G in AAA76850. Ref.3
Sequence conflict1321R → A in AAA76851. Ref.1
Sequence conflict1441P → Q in CAG47064. Ref.6
Sequence conflict2031L → S in AAC31758. Ref.2
Sequence conflict215 – 2162RG → AR in AAA76851. Ref.1
Sequence conflict2961H → D in AAA76851. Ref.1
Sequence conflict3581K → R in BAG35211. Ref.5

Secondary structure

.................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12277-1 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 637AA67A86AE3059

FASTA38142,644
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
IPIIPI00022977.
PIRKIHUCB. S15935.
RefSeqNP_001814.2.
UniGeneHs.173724

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B6RX-ray2.00A/B1-381[»]
3DRBX-ray2.00A/B1-381[»]
3DREX-ray2.20A/B1-381[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP12277. 5 interactions.
STRINGP12277.

PTM databases

PhosphoSiteP12277.

2-D gel databases

HSC-2DPAGEP12277.
PHCI-2DPAGEP12277.
REPRODUCTION-2DPAGEIPI00022977.
P12277.

Proteomic databases

PeptideAtlasP12277.
PRIDEP12277.

Genome annotation databases

EnsemblENST00000348956; ENSP00000299198; ENSG00000166165; Homo sapiens. [Genome view]
GeneID1152.
KEGGhsa:1152.
UCSCuc001ynf.1. human.

Organism-specific databases

CTD1152.
GeneCardsGC14M103055.
H-InvDBHIX0012001.
HGNCHGNC:1991. CKB.
HPAHPA001254.
MIM123280. gene.
PharmGKBPA26528.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07258.
HOGENOMHBG445448.
HOVERGENP12277.
InParanoidP12277.
OMASYGILAN.
OrthoDBEOG986BZ7.
PhylomeDBP12277.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14573.
BRENDA2.7.3.2. 247.
ReactomeREACT_13. Metabolism of amino acids.

Gene expression databases

ArrayExpressP12277.
BgeeP12277.
CleanExHS_CKB.
GenevestigatorP12277.

Family and domain databases

InterProIPR000749. ATP-guanido_PTrfase.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
Gene3DG3DSA:1.10.135.10. ATP-gua_Ptrans. 1 hit.
G3DSA:3.30.590.10. ATP-gua_Ptrans. 1 hit.
PANTHERPTHR11547. ATP-gua_Ptrans. 1 hit.
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
PROSITEPS00112. GUANIDO_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00148. Creatine.
NextBio4784.
SOURCESearch...

Entry information

Entry nameKCRB_HUMAN
AccessionPrimary (citable) accession number: P12277
Secondary accession number(s): A8K236 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents