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Creatine kinase M-type (EC 2.7.3.2) (Creatine kinase M chain) (M-CK)

 KCRM_HUMAN              Reviewed;         381 AA.
P06732; Q96QL9;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Creatine kinase M-type;
EC=2.7.3.2;
AltName: Full=Creatine kinase M chain;
AltName: Full=M-CK;
Name=CKM; Synonyms=CKMM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3778496; DOI=10.1016/0006-291X(86)90732-1;
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;
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 variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
PROTEIN SEQUENCE OF 1-30.
TISSUE=Brain;
PubMed=1690725;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 257-327.
PubMed=3031982;
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).
[9]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=10089465; DOI=10.1107/S0907444998011044;
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).
-!- 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.
{ECO:0000255|PROSITE-ProRule:PRU10029}.
-!- SUBUNIT: 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.
-!- INTERACTION:
Q96DX5:ASB9; NbExp=6; IntAct=EBI-4287089, EBI-745641;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
{ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
ProRule:PRU00843}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry;
URL="https://en.wikipedia.org/wiki/Creatine_kinase";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ckm/";
-----------------------------------------------------------------------
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EMBL; M14780; AAA52025.1; -; mRNA.
EMBL; M21494; AAA96609.1; -; Genomic_DNA.
EMBL; M21488; AAA96609.1; JOINED; Genomic_DNA.
EMBL; M21489; AAA96609.1; JOINED; Genomic_DNA.
EMBL; M21490; AAA96609.1; JOINED; Genomic_DNA.
EMBL; M21491; AAA96609.1; JOINED; Genomic_DNA.
EMBL; M21492; AAA96609.1; JOINED; Genomic_DNA.
EMBL; M21493; AAA96609.1; JOINED; Genomic_DNA.
EMBL; BT006793; AAP35439.1; -; mRNA.
EMBL; AY585238; AAS79321.1; -; Genomic_DNA.
EMBL; AC005781; AAC62841.1; -; Genomic_DNA.
EMBL; BC007462; AAH07462.1; -; mRNA.
EMBL; M16440; AAA52026.1; ALT_SEQ; mRNA.
CCDS; CCDS12659.1; -.
PIR; A31793; KIHUCM.
RefSeq; NP_001815.2; NM_001824.4.
RefSeq; XP_016881729.1; XM_017026240.1.
UniGene; Hs.334347; -.
PDB; 1I0E; X-ray; 3.50 A; A/B/C/D=1-381.
PDBsum; 1I0E; -.
ProteinModelPortal; P06732; -.
SMR; P06732; -.
BioGrid; 107578; 28.
IntAct; P06732; 6.
STRING; 9606.ENSP00000221476; -.
BindingDB; P06732; -.
ChEMBL; CHEMBL2656; -.
DrugBank; DB02490; (Diaminomethyl-Methyl-Amino)-Acetic Acid.
DrugBank; DB00148; Creatine.
DrugBank; DB04027; D-Arginine.
iPTMnet; P06732; -.
PhosphoSitePlus; P06732; -.
BioMuta; CKM; -.
DMDM; 125305; -.
UCD-2DPAGE; P06732; -.
EPD; P06732; -.
MaxQB; P06732; -.
PaxDb; P06732; -.
PeptideAtlas; P06732; -.
PRIDE; P06732; -.
DNASU; 1158; -.
Ensembl; ENST00000221476; ENSP00000221476; ENSG00000104879.
GeneID; 1158; -.
KEGG; hsa:1158; -.
UCSC; uc002pbd.5; human.
CTD; 1158; -.
DisGeNET; 1158; -.
EuPathDB; HostDB:ENSG00000104879.4; -.
GeneCards; CKM; -.
HGNC; HGNC:1994; CKM.
HPA; HPA047859; -.
MIM; 123310; gene.
neXtProt; NX_P06732; -.
OpenTargets; ENSG00000104879; -.
PharmGKB; PA26532; -.
eggNOG; KOG3581; Eukaryota.
eggNOG; COG3869; LUCA.
GeneTree; ENSGT00550000074561; -.
HOGENOM; HOG000232165; -.
HOVERGEN; HBG001339; -.
InParanoid; P06732; -.
KO; K00933; -.
OMA; GNTHNNF; -.
OrthoDB; EOG091G0HZ0; -.
PhylomeDB; P06732; -.
TreeFam; TF314214; -.
BioCyc; MetaCyc:HS02640-MONOMER; -.
BRENDA; 2.7.3.2; 2681.
Reactome; R-HSA-71288; Creatine metabolism.
SABIO-RK; P06732; -.
ChiTaRS; CKM; human.
EvolutionaryTrace; P06732; -.
GeneWiki; CKM_(gene); -.
GenomeRNAi; 1158; -.
PRO; PR:P06732; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104879; -.
CleanEx; HS_CKM; -.
Genevisible; P06732; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004111; F:creatine kinase activity; TAS:Reactome.
GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:Ensembl.
Gene3D; 1.10.135.10; -; 1.
Gene3D; 3.30.590.10; -; 1.
InterPro; IPR000749; ATP-guanido_PTrfase.
InterPro; IPR022415; ATP-guanido_PTrfase_AS.
InterPro; IPR022414; ATP-guanido_PTrfase_cat.
InterPro; IPR022413; ATP-guanido_PTrfase_N.
InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
PANTHER; PTHR11547; PTHR11547; 1.
Pfam; PF00217; ATP-gua_Ptrans; 1.
Pfam; PF02807; ATP-gua_PtransN; 1.
SUPFAM; SSF48034; SSF48034; 1.
SUPFAM; SSF55931; SSF55931; 1.
PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Transferase.
CHAIN 1 381 Creatine kinase M-type.
/FTId=PRO_0000211975.
DOMAIN 11 98 Phosphagen kinase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00842}.
DOMAIN 125 367 Phosphagen kinase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00843}.
NP_BIND 128 132 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
NP_BIND 320 325 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 191 191 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 236 236 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 292 292 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
BINDING 335 335 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00843}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000250|UniProtKB:P07310}.
MOD_RES 166 166 Phosphothreonine.
{ECO:0000250|UniProtKB:P00564}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:P00564}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000250|UniProtKB:P00564}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:P07310}.
MOD_RES 313 313 Phosphothreonine.
{ECO:0000250|UniProtKB:P00564}.
MOD_RES 322 322 Phosphothreonine.
{ECO:0000250|UniProtKB:P07310}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:P07310}.
VARIANT 83 83 E -> G (in dbSNP:rs11559024).
{ECO:0000269|Ref.4}.
/FTId=VAR_018680.
VARIANT 127 127 L -> V (in dbSNP:rs17875653).
{ECO:0000269|Ref.4}.
/FTId=VAR_018681.
VARIANT 166 166 T -> M (in dbSNP:rs17357122).
/FTId=VAR_049675.
VARIANT 243 243 G -> A (in dbSNP:rs17875625).
{ECO:0000269|Ref.4}.
/FTId=VAR_018682.
CONFLICT 47 47 T -> I (in Ref. 1; AAA52025).
{ECO:0000305}.
CONFLICT 130 130 R -> P (in Ref. 1; AAA52025).
{ECO:0000305}.
CONFLICT 193 193 L -> Q (in Ref. 1; AAA52025).
{ECO:0000305}.
CONFLICT 210 210 D -> H (in Ref. 1; AAA52025).
{ECO:0000305}.
CONFLICT 215 215 R -> P (in Ref. 1; AAA52025).
{ECO:0000305}.
CONFLICT 225 225 F -> L (in Ref. 3; AAP35439 and 6;
AAH07462). {ECO:0000305}.
CONFLICT 324 324 G -> A (in Ref. 1; AAA52025).
{ECO:0000305}.
HELIX 16 19 {ECO:0000244|PDB:1I0E}.
HELIX 29 33 {ECO:0000244|PDB:1I0E}.
HELIX 36 42 {ECO:0000244|PDB:1I0E}.
HELIX 53 62 {ECO:0000244|PDB:1I0E}.
STRAND 67 69 {ECO:0000244|PDB:1I0E}.
HELIX 80 84 {ECO:0000244|PDB:1I0E}.
HELIX 86 93 {ECO:0000244|PDB:1I0E}.
TURN 94 96 {ECO:0000244|PDB:1I0E}.
STRAND 97 99 {ECO:0000244|PDB:1I0E}.
TURN 123 125 {ECO:0000244|PDB:1I0E}.
STRAND 126 132 {ECO:0000244|PDB:1I0E}.
TURN 143 145 {ECO:0000244|PDB:1I0E}.
HELIX 148 164 {ECO:0000244|PDB:1I0E}.
HELIX 167 169 {ECO:0000244|PDB:1I0E}.
STRAND 171 176 {ECO:0000244|PDB:1I0E}.
TURN 181 183 {ECO:0000244|PDB:1I0E}.
HELIX 184 189 {ECO:0000244|PDB:1I0E}.
TURN 200 206 {ECO:0000244|PDB:1I0E}.
TURN 209 214 {ECO:0000244|PDB:1I0E}.
STRAND 216 220 {ECO:0000244|PDB:1I0E}.
STRAND 223 244 {ECO:0000244|PDB:1I0E}.
HELIX 246 266 {ECO:0000244|PDB:1I0E}.
TURN 275 277 {ECO:0000244|PDB:1I0E}.
HELIX 284 286 {ECO:0000244|PDB:1I0E}.
STRAND 292 298 {ECO:0000244|PDB:1I0E}.
TURN 300 304 {ECO:0000244|PDB:1I0E}.
HELIX 308 314 {ECO:0000244|PDB:1I0E}.
STRAND 333 338 {ECO:0000244|PDB:1I0E}.
STRAND 342 344 {ECO:0000244|PDB:1I0E}.
HELIX 346 368 {ECO:0000244|PDB:1I0E}.
SEQUENCE 381 AA; 43101 MW; 418FEAD0C2E138C8 CRC64;
MPFGNTHNKF KLNYKPEEEY PDLSKHNNHM AKVLTLELYK KLRDKETPSG FTVDDVIQTG
VDNPGHPFIM TVGCVAGDEE SYEVFKELFD PIISDRHGGY KPTDKHKTDL NHENLKGGDD
LDPNYVLSSR VRTGRSIKGY TLPPHCSRGE RRAVEKLSVE ALNSLTGEFK GKYYPLKSMT
EKEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKSFLVWVN EEDHLRVISM
EKGGNMKEVF RRFCVGLQKI EEIFKKAGHP FMWNQHLGYV LTCPSNLGTG LRGGVHVKLA
HLSKHPKFEE ILTRLRLQKR GTGGVDTAAV GSVFDVSNAD RLGSSEVEQV QLVVDGVKLM
VEMEKKLEKG QSIDDMIPAQ K


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