KCRM_HUMAN
ID KCRM_HUMAN Reviewed; 381 AA.
AC P06732; Q96QL9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Creatine kinase M-type;
DE EC=2.7.3.2 {ECO:0000250|UniProtKB:P00563};
DE AltName: Full=Creatine kinase M chain;
DE AltName: Full=Creatine phosphokinase M-type {ECO:0000305};
DE Short=CPK-M;
DE AltName: Full=M-CK;
GN Name=CKM; Synonyms=CKMM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3778496; DOI=10.1016/0006-291x(86)90732-1;
RA Perryman M.B., Kerner S.A., Bohlmeyer T.J., Roberts R.;
RT "Isolation and sequence analysis of a full-length cDNA for human M creatine
RT kinase.";
RL Biochem. Biophys. Res. Commun. 140:981-989(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2903158; DOI=10.1016/s0021-9258(18)37510-0;
RA Trask R.V., Strauss A.W., Billadello J.J.;
RT "Developmental regulation and tissue-specific expression of the human
RT muscle creatine kinase gene.";
RL J. Biol. Chem. 263:17142-17149(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-83; VAL-127 AND
RP ALA-243.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-30.
RC TISSUE=Brain;
RX PubMed=1690725; DOI=10.1016/s0021-9258(19)39340-8;
RA Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D., Goodman C.,
RA Puleo P.R., Perryman M.B.;
RT "Muscle creatine kinase isoenzyme expression in adult human brain.";
RL J. Biol. Chem. 265:6403-6409(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 257-327.
RX PubMed=3031982;
RA Nigro J.M., Schweinfest C.W., Rajkovic A., Pavlovic J., Jamal S.,
RA Dottin R.P., Hart J.T., Kamarck M.E., Rae P.M.M., Carty M.D.,
RA Martin-Deleon P.;
RT "cDNA cloning and mapping of the human creatine kinase M gene to 19q13.";
RL Am. J. Hum. Genet. 40:115-125(1987).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=10089465; DOI=10.1107/s0907444998011044;
RA Tang L., Zhou H.M., Lin Z.J.;
RT "Crystallization and preliminary X-ray analysis of human muscle creatine
RT kinase.";
RL Acta Crystallogr. D 55:669-670(1999).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC isoenzymes play a central role in energy transduction in tissues with
CC large, fluctuating energy demands, such as skeletal muscle, heart,
CC brain and spermatozoa. {ECO:0000250|UniProtKB:P00563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC Evidence={ECO:0000250|UniProtKB:P00563, ECO:0000255|PROSITE-
CC ProRule:PRU10029};
CC -!- SUBUNIT: Dimer of identical or non-identical chains, which can be
CC either B (brain type) or M (muscle type). With MM being the major form
CC in skeletal muscle and myocardium, MB existing in myocardium, and BB
CC existing in many tissues, especially brain.
CC {ECO:0000250|UniProtKB:P12277}.
CC -!- INTERACTION:
CC P06732; Q96DX5: ASB9; NbExp=10; IntAct=EBI-4287089, EBI-745641;
CC P06732; P12532: CKMT1B; NbExp=3; IntAct=EBI-4287089, EBI-1050662;
CC P06732; P42858: HTT; NbExp=3; IntAct=EBI-4287089, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry;
CC URL="https://en.wikipedia.org/wiki/Creatine_kinase";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ckm/";
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DR EMBL; M14780; AAA52025.1; -; mRNA.
DR EMBL; M21494; AAA96609.1; -; Genomic_DNA.
DR EMBL; M21488; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; M21489; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; M21490; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; M21491; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; M21492; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; M21493; AAA96609.1; JOINED; Genomic_DNA.
DR EMBL; BT006793; AAP35439.1; -; mRNA.
DR EMBL; AY585238; AAS79321.1; -; Genomic_DNA.
DR EMBL; AC005781; AAC62841.1; -; Genomic_DNA.
DR EMBL; BC007462; AAH07462.1; -; mRNA.
DR EMBL; M16440; AAA52026.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12659.1; -.
DR PIR; A31793; KIHUCM.
DR RefSeq; NP_001815.2; NM_001824.4.
DR RefSeq; XP_016881729.1; XM_017026240.1.
DR PDB; 1I0E; X-ray; 3.50 A; A/B/C/D=1-381.
DR PDB; 7BF2; X-ray; 1.43 A; CCC/DDD=301-318.
DR PDBsum; 1I0E; -.
DR PDBsum; 7BF2; -.
DR AlphaFoldDB; P06732; -.
DR SMR; P06732; -.
DR BioGRID; 107578; 63.
DR IntAct; P06732; 16.
DR MINT; P06732; -.
DR STRING; 9606.ENSP00000221476; -.
DR BindingDB; P06732; -.
DR ChEMBL; CHEMBL2656; -.
DR DrugBank; DB02490; (Diaminomethyl-Methyl-Amino)-Acetic Acid.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB00148; Creatine.
DR DrugBank; DB04027; D-arginine.
DR DrugBank; DB13191; Phosphocreatine.
DR DrugBank; DB00300; Tenofovir disoproxil.
DR GlyGen; P06732; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P06732; -.
DR PhosphoSitePlus; P06732; -.
DR BioMuta; CKM; -.
DR DMDM; 125305; -.
DR UCD-2DPAGE; P06732; -.
DR jPOST; P06732; -.
DR MassIVE; P06732; -.
DR MaxQB; P06732; -.
DR PaxDb; P06732; -.
DR PeptideAtlas; P06732; -.
DR PRIDE; P06732; -.
DR ProteomicsDB; 51918; -.
DR ABCD; P06732; 2 sequenced antibodies.
DR Antibodypedia; 17872; 901 antibodies from 39 providers.
DR DNASU; 1158; -.
DR Ensembl; ENST00000221476.4; ENSP00000221476.2; ENSG00000104879.5.
DR GeneID; 1158; -.
DR KEGG; hsa:1158; -.
DR MANE-Select; ENST00000221476.4; ENSP00000221476.2; NM_001824.5; NP_001815.2.
DR UCSC; uc002pbd.5; human.
DR CTD; 1158; -.
DR DisGeNET; 1158; -.
DR GeneCards; CKM; -.
DR HGNC; HGNC:1994; CKM.
DR HPA; ENSG00000104879; Group enriched (skeletal muscle, tongue).
DR MIM; 123310; gene.
DR neXtProt; NX_P06732; -.
DR OpenTargets; ENSG00000104879; -.
DR PharmGKB; PA26532; -.
DR VEuPathDB; HostDB:ENSG00000104879; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_4_2_1; -.
DR InParanoid; P06732; -.
DR OMA; IIMQERV; -.
DR OrthoDB; 825025at2759; -.
DR PhylomeDB; P06732; -.
DR TreeFam; TF314214; -.
DR BioCyc; MetaCyc:HS02640-MON; -.
DR BRENDA; 2.7.3.2; 2681.
DR PathwayCommons; P06732; -.
DR Reactome; R-HSA-71288; Creatine metabolism.
DR SABIO-RK; P06732; -.
DR SignaLink; P06732; -.
DR SIGNOR; P06732; -.
DR BioGRID-ORCS; 1158; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; CKM; human.
DR EvolutionaryTrace; P06732; -.
DR GeneWiki; CKM_(gene); -.
DR GenomeRNAi; 1158; -.
DR Pharos; P06732; Tbio.
DR PRO; PR:P06732; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P06732; protein.
DR Bgee; ENSG00000104879; Expressed in skeletal muscle tissue of rectus abdominis and 118 other tissues.
DR Genevisible; P06732; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Creatine kinase M-type"
FT /id="PRO_0000211975"
FT DOMAIN 11..98
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 125..367
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 320..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 166
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00564"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07310"
FT VARIANT 83
FT /note="E -> G (in dbSNP:rs11559024)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018680"
FT VARIANT 127
FT /note="L -> V (in dbSNP:rs17875653)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018681"
FT VARIANT 166
FT /note="T -> M (in dbSNP:rs17357122)"
FT /id="VAR_049675"
FT VARIANT 243
FT /note="G -> A (in dbSNP:rs17875625)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018682"
FT CONFLICT 47
FT /note="T -> I (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="R -> P (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="L -> Q (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="D -> H (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="R -> P (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="F -> L (in Ref. 3; AAP35439 and 6; AAH07462)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> A (in Ref. 1; AAA52025)"
FT /evidence="ECO:0000305"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 200..206
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 209..214
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 223..244
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 246..266
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:1I0E"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1I0E"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:1I0E"
FT HELIX 346..368
FT /evidence="ECO:0007829|PDB:1I0E"
SQ 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
