Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P12277 (KCRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Creatine kinase B-type

EC=2.7.3.2
Alternative name(s):
B-CK
Creatine kinase B chain
Gene names
Name:CKB
Synonyms:CKBB
OrganismHomo sapiens (Human) [Reference 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.

Contains 1 phosphagen kinase C-terminal domain.

Contains 1 phosphagen kinase N-terminal domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q034633EBI-357706,EBI-9081620From a different organism.
ASB9Q96DX53EBI-357706,EBI-745641

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

Domain11 – 9888Phosphagen kinase N-terminal
Domain125 – 367243Phosphagen kinase C-terminal
Nucleotide binding128 – 1325ATP
Nucleotide binding320 – 3256ATP

Sites

Binding site721Substrate; via amide nitrogen
Binding site1301ATP
Binding site1321ATP
Binding site1911ATP
Binding site2321Substrate
Binding site2361ATP
Binding site2851Substrate
Binding site2921ATP
Binding site3201ATP
Binding site3351ATP By similarity

Amino acid modifications

Modified residue41Phosphoserine Ref.16
Modified residue351Phosphothreonine Ref.15
Modified residue1251Phosphotyrosine By similarity
Modified residue1991Phosphoserine Ref.15
Modified residue2691Nitrated tyrosine By similarity

Natural variations

Natural variant1771K → R. Ref.7
Corresponds to variant rs36002620 [ dbSNP | Ensembl ].
VAR_025838
Natural variant3091S → L. Ref.7
Corresponds to variant rs35156510 [ dbSNP | Ensembl ].
VAR_025839
Natural variant3601L → F.
Corresponds to variant rs12505 [ dbSNP | Ensembl ].
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3- -creatine transition-state analogue complex."
Bong S.M., Moon J.H., Nam K.H., Lee K.S., Chi Y.M., Hwang K.Y.
FEBS Lett. 582:3959-3965(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CREATINE, ATP-BINDING SITES, SUBSTRATE-BINDING SITES.
+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.
PIRKIHUCB. S15935.
RefSeqNP_001814.2. NM_001823.4.
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[»]
ProteinModelPortalP12277.
SMRP12277. Positions 6-381.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107572. 50 interactions.
IntActP12277. 25 interactions.
MINTMINT-1484821.
STRING9606.ENSP00000299198.

Chemistry

ChEMBLCHEMBL6049.
DrugBankDB00148. Creatine.

PTM databases

PhosphoSiteP12277.

Polymorphism databases

DMDM125294.

2D gel databases

REPRODUCTION-2DPAGEIPI00022977.
P12277.
UCD-2DPAGEP12277.

Proteomic databases

PaxDbP12277.
PeptideAtlasP12277.
PRIDEP12277.

Protocols and materials databases

DNASU1152.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348956; ENSP00000299198; ENSG00000166165.
GeneID1152.
KEGGhsa:1152.
UCSCuc001ynf.2. human.

Organism-specific databases

CTD1152.
GeneCardsGC14M103986.
HGNCHGNC:1991. CKB.
HPACAB047313.
HPA001254.
MIM123280. gene.
neXtProtNX_P12277.
PharmGKBPA26528.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3869.
HOGENOMHOG000232165.
HOVERGENHBG001339.
InParanoidP12277.
KOK00933.
OMARGHEFMW.
OrthoDBEOG7XM2XW.
PhylomeDBP12277.
TreeFamTF314214.

Enzyme and pathway databases

BioCycMetaCyc:HS09344-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP12277.

Gene expression databases

ArrayExpressP12277.
BgeeP12277.
CleanExHS_CKB.
GenevestigatorP12277.

Family and domain databases

Gene3D1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMSSF48034. SSF48034. 1 hit.
PROSITEPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCKB. human.
EvolutionaryTraceP12277.
GeneWikiCKB_(gene).
GenomeRNAi1152.
NextBio4784.
PROP12277.
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: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM