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UniProtKB/Swiss-Prot entry P12277


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name KCRB_HUMAN
Primary accession number P12277
Secondary accession number Q2LE07
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on October 1, 1989 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 92)
Name and origin of the protein
Protein name Creatine kinase B-type
Synonyms EC 2.7.3.2
Creatine kinase B chain
B-CK
Gene name
Name: CKB
Synonyms: CKBB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0006-291X(87)91427-6; PubMed=3034271 [NCBI, ExPASy, EBI, Israel, Japan]
Villarreal-Levy G., Ma T.S., Kerner S.A., Roberts R., Perryman M.B.;
"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.";
Biochem. Biophys. Res. Commun. 144:1116-1127(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(87)90004-8; PubMed=3692484 [NCBI, ExPASy, EBI, Israel, Japan]
Mariman E.C.M., Broers C.A.M., Claesen C.A.A., Tesser G.I., Wieringa B.;
"Structure and expression of the human creatine kinase B gene.";
Genomics 1:126-137(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2883200 [NCBI, ExPASy, EBI, Israel, Japan]
Kaye F.J., McBride O.W., Battey J.F., Gazder A.F., Sausville E.A.;
"Human creatine kinase-B complementary DNA. Nucleotide sequence, gene expression in lung cancer, and chromosomal assignment to two distinct loci.";
J. Clin. Invest. 79:1412-1420(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
DOI=10.1093/nar/17.15.6385; PubMed=2771648 [NCBI, ExPASy, EBI, Israel, Japan]
Mariman E.C.M., Schepens J.T.G., Wieringa B.;
"Complete nucleotide sequence of the human creatine kinase B gene.";
Nucleic Acids Res. 17:6385-6385(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-177 AND LEU-309.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
PubMed=2828370 [NCBI, ExPASy, EBI, Israel, Japan]
Daouk G.H., Kaddurah-Daouk R., Putney S., Kingston R., Schimmel P.;
"Isolation of a functional human gene for brain creatine kinase.";
J. Biol. Chem. 263:2442-2446(1988).
[8]
PROTEIN SEQUENCE OF 2-11; 33-43; 157-172; 224-236; 253-265; 308-314 AND 342-366, CLEAVAGE OF INITIATOR METHIONINE, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 33-43; 108-130; 157-172; 224-236 AND 253-265, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
MUTAGENESIS OF CYS-283; ARG-292 AND ASP-340.
PubMed=8186255 [NCBI, ExPASy, EBI, Israel, Japan]
Lin L., Perryman M.B., Friedman D., Roberts R., Ma T.S.;
"Determination of the catalytic site of creatine kinase by site-directed mutagenesis.";
Biochim. Biophys. Acta 1206:97-104(1994).
Comments
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
M16451; AAA76851.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21243; AAC31758.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21237; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21238; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21239; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21240; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21241; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21242; AAC31758.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L47647; AAA76852.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16364; AAA76850.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15334; CAA33389.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ333313; ABC67465.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001190; AAH01190.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004914; AAH04914.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008323; AAH08323.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010002; AAH10002.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019259; AAH19259.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019281; AAH19281.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22356; AAA52024.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22355; AAA52024.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15935; KIHUCB.
RefSeq NP_001814.2; -.
UniGene Hs.173724
3D structure databases
HSSP P05122; 1QH4. [HSSP ENTRY / PDB]
SMR P12277; 2-381.
ModBase P12277.
PTM databases
PhosphoSite P12277; -.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
Polymorphism databases
NIEHS-SNPs CKB.
2D gel databases
HSC-2DPAGE P12277; -.
PHCI-2DPAGE P12277; -.
REPRODUCTION-2DPAGE IPI00022977; -.
P12277; -.
Organism-specific databases
H-InvDB HIX0012001; -.
HGNC HGNC:1991; CKB.
GenAtlas CKB.
HPA HPA001254; -.
MIM 123280; gene. [NCBI / EBI]
PharmGKB PA26528; -.
GeneCards P12277.
Gene expression databases
ArrayExpress P12277; -.
CleanEx HS_CKB; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004111; Molecular function: creatine kinase activity (traceable author statement from ProtInc).
GO:0006600; Biological process: creatine metabolic process (inferred from experiment from Reactome).
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 P12277.
Proteomic databases
PeptideAtlas P12277; -.
Genome annotation databases
Ensembl ENSG00000166165; Homo sapiens. [Contig view]
GeneID 1152; -.
KEGG hsa:1152; -.
Phylogenomic databases
HOGENOM P12277; -.
HOVERGEN P12277; -.
Other
DrugBank DB00148; Creatine.
SOURCE CKB; Homo sapiens.
ProtoNet P12277.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   381  380     Creatine kinase B-type. PRO_0000211966
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). 
VARIANT   177   177  1     K -> R. VAR_025838 [3D]
VARIANT   309   309  1     S -> L. VAR_025839 [3D]
MUTAGEN   283   283        C->S,Y: Complete loss of activity. 
MUTAGEN   292   292        R->H,L,Q: Complete loss of activity. 
MUTAGEN   292   292        R->K: 42% of wild-type activity. 
MUTAGEN   340   340        D->E: No change in activity. 
CONFLICT   41    42        EL -> DV (in Ref. 1; AAA76851). 
CONFLICT   78    78        D -> G (in Ref. 3 and 7). 
CONFLICT   98    99        GG -> RR (in Ref. 1; AAA76851). 
CONFLICT   105   106        EH -> DD (in Ref. 1; AAA76851). 
CONFLICT   130   130        R -> G (in Ref. 3; AAA76850). 
CONFLICT   132   132        R -> A (in Ref. 1; AAA76851). 
CONFLICT   203   203        L -> S (in Ref. 2; AAC31758). 
CONFLICT   215   216        RG -> AR (in Ref. 1; AAA76851). 
CONFLICT   296   296        H -> D (in Ref. 1; AAA76851). 
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 42644 Da [This is the MW of the unprocessed precursor] CRC64: 637AA67A86AE3059 [This is a checksum on the sequence]
        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 

P12277 in FASTA format

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