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UniProtKB/Swiss-Prot entry P06732


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

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Entry information
Entry name KCRM_HUMAN
Primary accession number P06732
Secondary accession number Q96QL9
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on November 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 92)
Name and origin of the protein
Protein name Creatine kinase M-type
Synonyms EC 2.7.3.2
Creatine kinase M chain
M-CK
Gene name
Name: CKM
Synonyms: CKMM
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(86)90732-1; PubMed=3778496 [NCBI, ExPASy, EBI, Israel, Japan]
Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R.;
"Isolation and sequence analysis of a full-length cDNA for human M creatine kinase.";
Biochem. Biophys. Res. Commun. 140:981-989(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2903158 [NCBI, ExPASy, EBI, Israel, Japan]
Trask R.V., Strauss A.W., Billadello J.J.;
"Developmental regulation and tissue-specific expression of the human muscle creatine kinase gene.";
J. Biol. Chem. 263:17142-17149(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-83; VAL-127 AND ALA-243.
SeattleSNPs program for genomic applications;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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 [MRNA] OF 257-327.
PubMed=3031982 [NCBI, ExPASy, EBI, Israel, Japan]
Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S., Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D., Martin-Deleon P.;
"cDNA cloning and mapping of the human creatine kinase M gene to 19q13.";
Am. J. Hum. Genet. 40:115-125(1987).
[8]
NUCLEOTIDE SEQUENCE OF 1-30.
PubMed=1690725 [NCBI, ExPASy, EBI, Israel, Japan]
Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D., Goodman C., Puleo P.R., Perryman M.B.;
"Muscle creatine kinase isoenzyme expression in adult human brain.";
J. Biol. Chem. 265:6403-6409(1990).
[9]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
DOI=10.1107/S0907444998011044; PubMed=10089465 [NCBI, ExPASy, EBI, Israel, Japan]
Tang L., Zhou H.M., Lin Z.J.;
"Crystallization and preliminary X-ray analysis of human muscle creatine kinase.";
Acta Crystallogr. D 55:669-670(1999).
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
M14780; AAA52025.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21494; AAA96609.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21488; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21489; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21490; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21491; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21492; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M21493; AAA96609.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006793; AAP35439.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY585238; AAS79321.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005781; AAC62841.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007462; AAH07462.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16440; AAA52026.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31793; KIHUCM.
RefSeq NP_001815.2; -.
UniGene Hs.334347
3D structure databases
PDB
1I0E; X-ray; 3.50 A; A/B/C/D=1-381.[ExPASy / RCSB / EBI]
PDBsum 1I0E; -.
ModBase P06732.
PTM databases
PhosphoSite P06732; -.
Enzyme and pathway databases
Reactome REACT_13; Metabolism of amino acids.
2D gel databases
HSC-2DPAGE P06732; -.
Organism-specific databases
H-InvDB HIX0015228; -.
HGNC HGNC:1994; CKM.
GenAtlas CKM.
MIM 123310; gene. [NCBI / EBI]
PharmGKB PA26532; -.
GeneCards P06732.
Gene expression databases
CleanEx HS_CKM; -.
GermOnline ENSG00000104879; Homo sapiens.
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 P06732.
ProtoNet P06732.
Proteomic databases
PeptideAtlas P06732; -.
Genome annotation databases
Ensembl ENSG00000104879; Homo sapiens. [Contig view]
GeneID 1158; -.
KEGG hsa:1158; -.
Phylogenomic databases
HOGENOM P06732; -.
HOVERGEN P06732; -.
Other
DrugBank DB00148; Creatine.
NextBio 4804; -.
SOURCE CKM; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   381  381     Creatine kinase M-type. PRO_0000211975
NP_BIND   128   132  5     ATP (By similarity). 
NP_BIND   320   325  6     ATP (By similarity). 
BINDING   191   191        ATP (By similarity). 
BINDING   236   236        ATP (By similarity). 
BINDING   292   292        ATP (By similarity). 
BINDING   335   335        ATP (By similarity). 
VARIANT   83    83  1     E -> G (in dbSNP:rs11559024 [NCBI]). VAR_018680 [3D]
VARIANT   127   127  1     L -> V (in dbSNP:rs17875653 [NCBI]). VAR_018681 [3D]
VARIANT   243   243  1     G -> A (in dbSNP:rs17875625 [NCBI]). VAR_018682 [3D]
CONFLICT   47    47        T -> I (in Ref. 1; AAA52025). 
CONFLICT   130   130        R -> P (in Ref. 1; AAA52025). 
CONFLICT   193   193        L -> Q (in Ref. 1; AAA52025). 
CONFLICT   210   210        D -> H (in Ref. 1; AAA52025). 
CONFLICT   215   215        R -> P (in Ref. 1; AAA52025). 
CONFLICT   225   225        F -> L (in Ref. 3 and 6). 
CONFLICT   324   324        G -> A (in Ref. 1; AAA52025). 
HELIX   16    19  4      
HELIX   29    33  5      
HELIX   36    42  7      
HELIX   53    62  10      
STRAND   67    69  3      
HELIX   80    84  5      
HELIX   86    93  8      
TURN   94    96  3      
STRAND   97    99  3      
TURN   123   125  3      
STRAND   126   132  7      
TURN   143   145  3      
HELIX   148   164  17      
HELIX   167   169  3      
STRAND   171   176  6      
TURN   181   183  3      
HELIX   184   189  6      
TURN   200   206  7      
TURN   209   214  6      
STRAND   216   220  5      
STRAND   223   244  22      
HELIX   246   266  21      
TURN   275   277  3      
HELIX   284   286  3      
STRAND   292   298  7      
TURN   300   304  5      
HELIX   308   314  7      
STRAND   333   338  6      
STRAND   342   344  3      
HELIX   346   368  23      
Sequence information
Length: 381 AA [This is the length of the unprocessed precursor] Molecular weight: 43101 Da [This is the MW of the unprocessed precursor] CRC64: 418FEAD0C2E138C8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG 

        70         80         90        100        110        120 
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD 

       130        140        150        160        170        180 
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT 

       190        200        210        220        230        240 
EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM 

       250        260        270        280        290        300 
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA 

       310        320        330        340        350        360 
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM 

       370        380 
VEMEKKLEKG QSIDDMIPAQ K 

P06732 in FASTA format

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