Full text data of CKM
CKM
(CKMM)
[Confidence: low (only semi-automatic identification from reviews)]
Creatine kinase M-type; 2.7.3.2 (Creatine kinase M chain; M-CK; Creatine kinase M-type, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Creatine kinase M-type; 2.7.3.2 (Creatine kinase M chain; M-CK; Creatine kinase M-type, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P06732
ID KCRM_HUMAN Reviewed; 381 AA.
AC P06732; Q96QL9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Creatine kinase M-type;
DE EC=2.7.3.2;
DE AltName: Full=Creatine kinase M chain;
DE AltName: Full=M-CK;
DE Contains:
DE RecName: Full=Creatine kinase M-type, N-terminally processed;
GN Name=CKM; Synonyms=CKMM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT creatine kinase.";
RL Biochem. Biophys. Res. Commun. 140:981-989(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2903158;
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
RT 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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
RT project: 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;
RA Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D.,
RA Goodman C., 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
RT 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
RT creatine kinase.";
RL Acta Crystallogr. D 55:669-670(1999).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC the major form in skeletal muscle and myocardium, MB existing in
CC myocardium, and BB existing in many tissues, especially brain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry;
CC URL="http://en.wikipedia.org/wiki/Creatine_kinase";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ckm/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CKM entry;
CC URL="http://en.wikipedia.org/wiki/CKM_(gene)";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A31793; KIHUCM.
DR RefSeq; NP_001815.2; NM_001824.4.
DR UniGene; Hs.334347; -.
DR PDB; 1I0E; X-ray; 3.50 A; A/B/C/D=1-381.
DR PDBsum; 1I0E; -.
DR ProteinModelPortal; P06732; -.
DR SMR; P06732; 8-381.
DR IntAct; P06732; 2.
DR STRING; 9606.ENSP00000221476; -.
DR BindingDB; P06732; -.
DR ChEMBL; CHEMBL2656; -.
DR DrugBank; DB00148; Creatine.
DR PhosphoSite; P06732; -.
DR DMDM; 125305; -.
DR UCD-2DPAGE; P06732; -.
DR PaxDb; P06732; -.
DR PeptideAtlas; P06732; -.
DR PRIDE; P06732; -.
DR DNASU; 1158; -.
DR Ensembl; ENST00000221476; ENSP00000221476; ENSG00000104879.
DR GeneID; 1158; -.
DR KEGG; hsa:1158; -.
DR UCSC; uc002pbd.4; human.
DR CTD; 1158; -.
DR GeneCards; GC19M045809; -.
DR HGNC; HGNC:1994; CKM.
DR HPA; HPA047859; -.
DR MIM; 123310; gene.
DR neXtProt; NX_P06732; -.
DR PharmGKB; PA26532; -.
DR eggNOG; COG3869; -.
DR HOGENOM; HOG000232165; -.
DR HOVERGEN; HBG001339; -.
DR InParanoid; P06732; -.
DR KO; K00933; -.
DR OMA; MTQPGFL; -.
DR OrthoDB; EOG7XM2XW; -.
DR PhylomeDB; P06732; -.
DR BioCyc; MetaCyc:HS02640-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P06732; -.
DR ChiTaRS; CKM; human.
DR EvolutionaryTrace; P06732; -.
DR GeneWiki; CKM_(gene); -.
DR GenomeRNAi; 1158; -.
DR NextBio; 4804; -.
DR PRO; PR:P06732; -.
DR Bgee; P06732; -.
DR CleanEx; HS_CKM; -.
DR Genevestigator; P06732; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; TAS:ProtInc.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.10.135.10; -; 1.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 381 Creatine kinase M-type.
FT /FTId=PRO_0000211975.
FT INIT_MET 1 1 Removed; alternate (By similarity).
FT CHAIN 2 381 Creatine kinase M-type, N-terminally
FT processed.
FT /FTId=PRO_0000421788.
FT DOMAIN 11 98 Phosphagen kinase N-terminal.
FT DOMAIN 125 367 Phosphagen kinase C-terminal.
FT NP_BIND 128 132 ATP (By similarity).
FT NP_BIND 320 325 ATP (By similarity).
FT BINDING 191 191 ATP (By similarity).
FT BINDING 236 236 ATP (By similarity).
FT BINDING 292 292 ATP (By similarity).
FT BINDING 335 335 ATP (By similarity).
FT VARIANT 83 83 E -> G (in dbSNP:rs11559024).
FT /FTId=VAR_018680.
FT VARIANT 127 127 L -> V (in dbSNP:rs17875653).
FT /FTId=VAR_018681.
FT VARIANT 166 166 T -> M (in dbSNP:rs17357122).
FT /FTId=VAR_049675.
FT VARIANT 243 243 G -> A (in dbSNP:rs17875625).
FT /FTId=VAR_018682.
FT CONFLICT 47 47 T -> I (in Ref. 1; AAA52025).
FT CONFLICT 130 130 R -> P (in Ref. 1; AAA52025).
FT CONFLICT 193 193 L -> Q (in Ref. 1; AAA52025).
FT CONFLICT 210 210 D -> H (in Ref. 1; AAA52025).
FT CONFLICT 215 215 R -> P (in Ref. 1; AAA52025).
FT CONFLICT 225 225 F -> L (in Ref. 3; AAP35439 and 6;
FT AAH07462).
FT CONFLICT 324 324 G -> A (in Ref. 1; AAA52025).
FT HELIX 16 19
FT HELIX 29 33
FT HELIX 36 42
FT HELIX 53 62
FT STRAND 67 69
FT HELIX 80 84
FT HELIX 86 93
FT TURN 94 96
FT STRAND 97 99
FT TURN 123 125
FT STRAND 126 132
FT TURN 143 145
FT HELIX 148 164
FT HELIX 167 169
FT STRAND 171 176
FT TURN 181 183
FT HELIX 184 189
FT TURN 200 206
FT TURN 209 214
FT STRAND 216 220
FT STRAND 223 244
FT HELIX 246 266
FT TURN 275 277
FT HELIX 284 286
FT STRAND 292 298
FT TURN 300 304
FT HELIX 308 314
FT STRAND 333 338
FT STRAND 342 344
FT HELIX 346 368
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
//
ID KCRM_HUMAN Reviewed; 381 AA.
AC P06732; Q96QL9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1990, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Creatine kinase M-type;
DE EC=2.7.3.2;
DE AltName: Full=Creatine kinase M chain;
DE AltName: Full=M-CK;
DE Contains:
DE RecName: Full=Creatine kinase M-type, N-terminally processed;
GN Name=CKM; Synonyms=CKMM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT creatine kinase.";
RL Biochem. Biophys. Res. Commun. 140:981-989(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2903158;
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
RT 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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
RT project: 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;
RA Hamburg R.J., Friedman D.L., Olson E.N., Ma T.S., Cortez M.D.,
RA Goodman C., 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
RT 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
RT creatine kinase.";
RL Acta Crystallogr. D 55:669-670(1999).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC kinase isoenzymes play a central role in energy transduction in
CC tissues with large, fluctuating energy demands, such as skeletal
CC muscle, heart, brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC the major form in skeletal muscle and myocardium, MB existing in
CC myocardium, and BB existing in many tissues, especially brain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Creatine kinase entry;
CC URL="http://en.wikipedia.org/wiki/Creatine_kinase";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/ckm/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CKM entry;
CC URL="http://en.wikipedia.org/wiki/CKM_(gene)";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; A31793; KIHUCM.
DR RefSeq; NP_001815.2; NM_001824.4.
DR UniGene; Hs.334347; -.
DR PDB; 1I0E; X-ray; 3.50 A; A/B/C/D=1-381.
DR PDBsum; 1I0E; -.
DR ProteinModelPortal; P06732; -.
DR SMR; P06732; 8-381.
DR IntAct; P06732; 2.
DR STRING; 9606.ENSP00000221476; -.
DR BindingDB; P06732; -.
DR ChEMBL; CHEMBL2656; -.
DR DrugBank; DB00148; Creatine.
DR PhosphoSite; P06732; -.
DR DMDM; 125305; -.
DR UCD-2DPAGE; P06732; -.
DR PaxDb; P06732; -.
DR PeptideAtlas; P06732; -.
DR PRIDE; P06732; -.
DR DNASU; 1158; -.
DR Ensembl; ENST00000221476; ENSP00000221476; ENSG00000104879.
DR GeneID; 1158; -.
DR KEGG; hsa:1158; -.
DR UCSC; uc002pbd.4; human.
DR CTD; 1158; -.
DR GeneCards; GC19M045809; -.
DR HGNC; HGNC:1994; CKM.
DR HPA; HPA047859; -.
DR MIM; 123310; gene.
DR neXtProt; NX_P06732; -.
DR PharmGKB; PA26532; -.
DR eggNOG; COG3869; -.
DR HOGENOM; HOG000232165; -.
DR HOVERGEN; HBG001339; -.
DR InParanoid; P06732; -.
DR KO; K00933; -.
DR OMA; MTQPGFL; -.
DR OrthoDB; EOG7XM2XW; -.
DR PhylomeDB; P06732; -.
DR BioCyc; MetaCyc:HS02640-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P06732; -.
DR ChiTaRS; CKM; human.
DR EvolutionaryTrace; P06732; -.
DR GeneWiki; CKM_(gene); -.
DR GenomeRNAi; 1158; -.
DR NextBio; 4804; -.
DR PRO; PR:P06732; -.
DR Bgee; P06732; -.
DR CleanEx; HS_CKM; -.
DR Genevestigator; P06732; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; TAS:ProtInc.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.10.135.10; -; 1.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 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; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 381 Creatine kinase M-type.
FT /FTId=PRO_0000211975.
FT INIT_MET 1 1 Removed; alternate (By similarity).
FT CHAIN 2 381 Creatine kinase M-type, N-terminally
FT processed.
FT /FTId=PRO_0000421788.
FT DOMAIN 11 98 Phosphagen kinase N-terminal.
FT DOMAIN 125 367 Phosphagen kinase C-terminal.
FT NP_BIND 128 132 ATP (By similarity).
FT NP_BIND 320 325 ATP (By similarity).
FT BINDING 191 191 ATP (By similarity).
FT BINDING 236 236 ATP (By similarity).
FT BINDING 292 292 ATP (By similarity).
FT BINDING 335 335 ATP (By similarity).
FT VARIANT 83 83 E -> G (in dbSNP:rs11559024).
FT /FTId=VAR_018680.
FT VARIANT 127 127 L -> V (in dbSNP:rs17875653).
FT /FTId=VAR_018681.
FT VARIANT 166 166 T -> M (in dbSNP:rs17357122).
FT /FTId=VAR_049675.
FT VARIANT 243 243 G -> A (in dbSNP:rs17875625).
FT /FTId=VAR_018682.
FT CONFLICT 47 47 T -> I (in Ref. 1; AAA52025).
FT CONFLICT 130 130 R -> P (in Ref. 1; AAA52025).
FT CONFLICT 193 193 L -> Q (in Ref. 1; AAA52025).
FT CONFLICT 210 210 D -> H (in Ref. 1; AAA52025).
FT CONFLICT 215 215 R -> P (in Ref. 1; AAA52025).
FT CONFLICT 225 225 F -> L (in Ref. 3; AAP35439 and 6;
FT AAH07462).
FT CONFLICT 324 324 G -> A (in Ref. 1; AAA52025).
FT HELIX 16 19
FT HELIX 29 33
FT HELIX 36 42
FT HELIX 53 62
FT STRAND 67 69
FT HELIX 80 84
FT HELIX 86 93
FT TURN 94 96
FT STRAND 97 99
FT TURN 123 125
FT STRAND 126 132
FT TURN 143 145
FT HELIX 148 164
FT HELIX 167 169
FT STRAND 171 176
FT TURN 181 183
FT HELIX 184 189
FT TURN 200 206
FT TURN 209 214
FT STRAND 216 220
FT STRAND 223 244
FT HELIX 246 266
FT TURN 275 277
FT HELIX 284 286
FT STRAND 292 298
FT TURN 300 304
FT HELIX 308 314
FT STRAND 333 338
FT STRAND 342 344
FT HELIX 346 368
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
//
MIM
123310
*RECORD*
*FIELD* NO
123310
*FIELD* TI
*123310 CREATINE KINASE, MUSCLE TYPE; CKM
;;CKMM
*FIELD* TX
DESCRIPTION
Creatine kinase (CK; EC 2.7.3.2) catalyzes the reversible transfer of a
read morephosphate from phosphocreatine to adenosine diphosphate, generating
adenosine triphosphate in tissues such as brain and muscle that require
large amounts of an energy source. The active form of the cytosolic
enzyme is a dimer of 2 subunit types, CKM and CKB (123280), which can
combine to form 3 electrophoretically separable isozymes, CKMM, CKBB,
and CKMB (summary by Nigro et al., 1987). The dimeric creatine kinase
isozymes are involved in maintaining intracellular ATP levels,
particularly in tissues that have high energy demands. The creatine
kinase MM isozyme is found exclusively in striated muscle; the BB
isozyme is found in smooth muscle, brain, and nerve; CKMB is found in
human heart (summary by Perryman et al., 1986).
CLONING
Dawson et al. (1968) determined that creatine kinase exists as a dimer:
the muscle enzyme (MM) consists of 2 identical M subunits, and the brain
enzyme (BB) consists of 2 identical B subunits. Other tissues showed a
third, hybrid MB enzyme. Schweinfest et al. (1985) used a chicken CK-M
cDNA clone to isolate a human clone from a cDNA library constructed from
human heart mRNA. One clone showed greater than 90% homology to rabbit
CK-M and less than 50% homology to rabbit CK-B, indicating that it
represented the human CK-M gene.
MAPPING
By somatic cell hybrid analysis, Schweinfest et al. (1985) mapped the
human CKM gene to chromosome 19.
By in situ hybridization, Nigro et al. (1987) regionalized the
assignment of CKM to 19q13. On the basis of high-resolution g-banding,
the predominant labeling site was 19q13.2-q13.3.
By Southern analysis of hybrid cell DNA, Stallings et al. (1988)
confirmed the assignment of CKM to chromosome 19. Study of independent
hybrids that had portions of 19q missing indicated that APOC2 (608083)
is distal to CKM.
Studying DNAs from somatic cell hybrids with a rearranged 19q that
carries a breakpoint across the CKM gene, Smeets et al. (1990) localized
the CKM gene and the 2 DNA repair genes, ERCC1 (126380) and ERCC2
(126340), within the same 250 kb of DNA. The order appeared to be
cen--CKM--ERCC2--ERCC1--ter, with APOC2 (608083) being at a distance
more than 260 kb proximal to CKM. The transcriptional start sites of the
CKM and DNA-repair genes are all on the telomeric side of the genes.
MOLECULAR GENETICS
In 59 families with myotonic dystrophy (DM; 160900) from Italy and
Spain, Gennarelli et al. (1991) found very close linkage of the disease
to a polymorphism at the CKMM locus; maximum lod score = 21.26 at theta
= 0.00. Bailly et al. (1991) sequenced CKMM cDNA from a DM chromosome 19
and found 2 novel polymorphisms but no translationally significant
mutations. They concluded that this finding excludes the CKMM gene as
the site of mutation in DM.
ANIMAL MODEL
Steeghs et al. (1997) generated mice who had combined deficiency of
cytosolic CK (CKM) and mitochondrial CK (CKMT; 123290). This mutation
blocked creatine kinase-mediated phosphocreatine (PCr)-to-ATP
transphosphorylation in skeletal muscle. Contrary to expectation, the
PCr level was only marginally affected, but the compound was rendered
metabolically inert. Mutant muscles in vivo showed significantly
impaired tetanic force output, increased relaxation times, altered
mitochondrial volume and location, and conspicuous tubular aggregates of
sarcoplasmic reticulum membranes, as seen in myopathies with electrolyte
disturbances. In depolarized myotubes cultured in vitro, CK absence
influenced both the release and sequestration of calcium ion. The data
pointed to a direct link between the CK-PCr system and the regulation of
calcium ion flux during the excitation and relaxation phases of muscle
contraction.
*FIELD* SA
Roman et al. (1985); Rosenberg et al. (1982); Watts (1973)
*FIELD* RF
1. Bailly, J.; MacKenzie, A. E.; Leblond, S.; Korneluk, R. G.: Assessment
of a creatine kinase isoform M defect as a cause of myotonic dystrophy
and the characterization of two novel CKMM polymorphisms. Hum. Genet. 86:
457-462, 1991.
2. Dawson, D. M.; Eppenberger, H. M.; Eppenberger, M. E.: Multiple
molecular forms of creatine kinases. Ann. N.Y. Acad. Sci. 151: 616-626,
1968.
3. Gennarelli, M.; Novelli, G.; Cobo, A.; Baiget, M.; Dallapiccola,
B.: 3-Prime creatine kinase (M-type) polymorphisms linked to myotonic
dystrophy in Italian and Spanish populations. Hum. Genet. 87: 654-656,
1991.
4. 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.
5. 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.
6. Roman, D.; Billadello, J.; Gordon, J.; Grace, A.; Sobel, B.; Strauss,
A.: Complete nucleotide sequence of dog heart creatine kinase mRNA:
conservation of amino acid sequence within and among species. Proc.
Nat. Acad. Sci. 82: 8394-8398, 1985.
7. Rosenberg, U. B.; Kunz, G.; Frischauf, A.; Lehrach, H.; Mahr, R.;
Eppenberger, H. M.; Perriard, J.-C.: Molecular cloning and expression
during myogenesis of sequences coding for M-creatine kinase. Proc.
Nat. Acad. Sci. 79: 6589-6592, 1982.
8. Schweinfest, C. W.; Nigro, J. M.; Rajkovic, A.; Dottin, R. P.;
Hart, J. M.; Karmack, M. E.; Rae, P. M. M.: Localization of the human
creatine kinase-M gene to chromosome 19. (Abstract) Cytogenet. Cell
Genet. 40: 740-741, 1985.
9. Smeets, H.; Bachinski, L.; Coerwinkel, M.; Schepens, J.; Hoeijmakers,
J.; van Duin, M.; Grzeschik, K.-H.; Weber, C. A.; de Jong, P.; Siciliano,
M. J.; Wieringa, B.: A long-range restriction map of the human chromosome
19q13 region: close physical linkage between CKMM and the ERCC1 and
ERCC2 genes. Am. J. Hum. Genet. 46: 492-501, 1990.
10. Stallings, R. L.; Olson, E.; Strauss, A. W.; Thompson, L. H.;
Bachinski, L. L.; Siciliano, M. J.: Human creatine kinase genes on
chromosomes 15 and 19, and proximity of the gene for the muscle form
to the genes for apolipoprotein C2 and excision repair. Am. J. Hum.
Genet. 43: 144-151, 1988.
11. Steeghs, K.; Benders, A.; Oerlemans, F.; de Haan, A.; Heerschap,
A.; Ruitenbeek, W.; Jost, C.; van Deursen, J.; Perryman, B.; Pette,
D.; Bruckwilder, M.; Koudijs, J.; Jap, P.; Veerkamp, J.; Wieringa,
B.: Altered Ca(2+) responses in muscles with combined mitochondrial
and cytosolic creatine kinase deficiencies. Cell 89: 93-103, 1997.
12. Watts, D. C.: Creatine kinase (adenosine 5-prime-triphosphate-creatine
phosphotransferase).In: Boyer, P. D.: The Enzymes. New York: Academic
Press (pub.) (3rd ed.) 8: 1973. Pp. 384-455.
*FIELD* CN
Victor A. McKusick - updated: 5/13/1997
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/21/2013
alopez: 9/11/2012
ckniffin: 9/24/2003
carol: 11/3/2000
terry: 4/30/1999
terry: 6/5/1998
alopez: 5/14/1997
alopez: 5/13/1997
terry: 5/6/1997
davew: 8/1/1994
warfield: 2/15/1994
supermim: 3/16/1992
carol: 12/2/1991
carol: 11/25/1991
supermim: 10/26/1990
*RECORD*
*FIELD* NO
123310
*FIELD* TI
*123310 CREATINE KINASE, MUSCLE TYPE; CKM
;;CKMM
*FIELD* TX
DESCRIPTION
Creatine kinase (CK; EC 2.7.3.2) catalyzes the reversible transfer of a
read morephosphate from phosphocreatine to adenosine diphosphate, generating
adenosine triphosphate in tissues such as brain and muscle that require
large amounts of an energy source. The active form of the cytosolic
enzyme is a dimer of 2 subunit types, CKM and CKB (123280), which can
combine to form 3 electrophoretically separable isozymes, CKMM, CKBB,
and CKMB (summary by Nigro et al., 1987). The dimeric creatine kinase
isozymes are involved in maintaining intracellular ATP levels,
particularly in tissues that have high energy demands. The creatine
kinase MM isozyme is found exclusively in striated muscle; the BB
isozyme is found in smooth muscle, brain, and nerve; CKMB is found in
human heart (summary by Perryman et al., 1986).
CLONING
Dawson et al. (1968) determined that creatine kinase exists as a dimer:
the muscle enzyme (MM) consists of 2 identical M subunits, and the brain
enzyme (BB) consists of 2 identical B subunits. Other tissues showed a
third, hybrid MB enzyme. Schweinfest et al. (1985) used a chicken CK-M
cDNA clone to isolate a human clone from a cDNA library constructed from
human heart mRNA. One clone showed greater than 90% homology to rabbit
CK-M and less than 50% homology to rabbit CK-B, indicating that it
represented the human CK-M gene.
MAPPING
By somatic cell hybrid analysis, Schweinfest et al. (1985) mapped the
human CKM gene to chromosome 19.
By in situ hybridization, Nigro et al. (1987) regionalized the
assignment of CKM to 19q13. On the basis of high-resolution g-banding,
the predominant labeling site was 19q13.2-q13.3.
By Southern analysis of hybrid cell DNA, Stallings et al. (1988)
confirmed the assignment of CKM to chromosome 19. Study of independent
hybrids that had portions of 19q missing indicated that APOC2 (608083)
is distal to CKM.
Studying DNAs from somatic cell hybrids with a rearranged 19q that
carries a breakpoint across the CKM gene, Smeets et al. (1990) localized
the CKM gene and the 2 DNA repair genes, ERCC1 (126380) and ERCC2
(126340), within the same 250 kb of DNA. The order appeared to be
cen--CKM--ERCC2--ERCC1--ter, with APOC2 (608083) being at a distance
more than 260 kb proximal to CKM. The transcriptional start sites of the
CKM and DNA-repair genes are all on the telomeric side of the genes.
MOLECULAR GENETICS
In 59 families with myotonic dystrophy (DM; 160900) from Italy and
Spain, Gennarelli et al. (1991) found very close linkage of the disease
to a polymorphism at the CKMM locus; maximum lod score = 21.26 at theta
= 0.00. Bailly et al. (1991) sequenced CKMM cDNA from a DM chromosome 19
and found 2 novel polymorphisms but no translationally significant
mutations. They concluded that this finding excludes the CKMM gene as
the site of mutation in DM.
ANIMAL MODEL
Steeghs et al. (1997) generated mice who had combined deficiency of
cytosolic CK (CKM) and mitochondrial CK (CKMT; 123290). This mutation
blocked creatine kinase-mediated phosphocreatine (PCr)-to-ATP
transphosphorylation in skeletal muscle. Contrary to expectation, the
PCr level was only marginally affected, but the compound was rendered
metabolically inert. Mutant muscles in vivo showed significantly
impaired tetanic force output, increased relaxation times, altered
mitochondrial volume and location, and conspicuous tubular aggregates of
sarcoplasmic reticulum membranes, as seen in myopathies with electrolyte
disturbances. In depolarized myotubes cultured in vitro, CK absence
influenced both the release and sequestration of calcium ion. The data
pointed to a direct link between the CK-PCr system and the regulation of
calcium ion flux during the excitation and relaxation phases of muscle
contraction.
*FIELD* SA
Roman et al. (1985); Rosenberg et al. (1982); Watts (1973)
*FIELD* RF
1. Bailly, J.; MacKenzie, A. E.; Leblond, S.; Korneluk, R. G.: Assessment
of a creatine kinase isoform M defect as a cause of myotonic dystrophy
and the characterization of two novel CKMM polymorphisms. Hum. Genet. 86:
457-462, 1991.
2. Dawson, D. M.; Eppenberger, H. M.; Eppenberger, M. E.: Multiple
molecular forms of creatine kinases. Ann. N.Y. Acad. Sci. 151: 616-626,
1968.
3. Gennarelli, M.; Novelli, G.; Cobo, A.; Baiget, M.; Dallapiccola,
B.: 3-Prime creatine kinase (M-type) polymorphisms linked to myotonic
dystrophy in Italian and Spanish populations. Hum. Genet. 87: 654-656,
1991.
4. 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.
5. 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.
6. Roman, D.; Billadello, J.; Gordon, J.; Grace, A.; Sobel, B.; Strauss,
A.: Complete nucleotide sequence of dog heart creatine kinase mRNA:
conservation of amino acid sequence within and among species. Proc.
Nat. Acad. Sci. 82: 8394-8398, 1985.
7. Rosenberg, U. B.; Kunz, G.; Frischauf, A.; Lehrach, H.; Mahr, R.;
Eppenberger, H. M.; Perriard, J.-C.: Molecular cloning and expression
during myogenesis of sequences coding for M-creatine kinase. Proc.
Nat. Acad. Sci. 79: 6589-6592, 1982.
8. Schweinfest, C. W.; Nigro, J. M.; Rajkovic, A.; Dottin, R. P.;
Hart, J. M.; Karmack, M. E.; Rae, P. M. M.: Localization of the human
creatine kinase-M gene to chromosome 19. (Abstract) Cytogenet. Cell
Genet. 40: 740-741, 1985.
9. Smeets, H.; Bachinski, L.; Coerwinkel, M.; Schepens, J.; Hoeijmakers,
J.; van Duin, M.; Grzeschik, K.-H.; Weber, C. A.; de Jong, P.; Siciliano,
M. J.; Wieringa, B.: A long-range restriction map of the human chromosome
19q13 region: close physical linkage between CKMM and the ERCC1 and
ERCC2 genes. Am. J. Hum. Genet. 46: 492-501, 1990.
10. Stallings, R. L.; Olson, E.; Strauss, A. W.; Thompson, L. H.;
Bachinski, L. L.; Siciliano, M. J.: Human creatine kinase genes on
chromosomes 15 and 19, and proximity of the gene for the muscle form
to the genes for apolipoprotein C2 and excision repair. Am. J. Hum.
Genet. 43: 144-151, 1988.
11. Steeghs, K.; Benders, A.; Oerlemans, F.; de Haan, A.; Heerschap,
A.; Ruitenbeek, W.; Jost, C.; van Deursen, J.; Perryman, B.; Pette,
D.; Bruckwilder, M.; Koudijs, J.; Jap, P.; Veerkamp, J.; Wieringa,
B.: Altered Ca(2+) responses in muscles with combined mitochondrial
and cytosolic creatine kinase deficiencies. Cell 89: 93-103, 1997.
12. Watts, D. C.: Creatine kinase (adenosine 5-prime-triphosphate-creatine
phosphotransferase).In: Boyer, P. D.: The Enzymes. New York: Academic
Press (pub.) (3rd ed.) 8: 1973. Pp. 384-455.
*FIELD* CN
Victor A. McKusick - updated: 5/13/1997
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/21/2013
alopez: 9/11/2012
ckniffin: 9/24/2003
carol: 11/3/2000
terry: 4/30/1999
terry: 6/5/1998
alopez: 5/14/1997
alopez: 5/13/1997
terry: 5/6/1997
davew: 8/1/1994
warfield: 2/15/1994
supermim: 3/16/1992
carol: 12/2/1991
carol: 11/25/1991
supermim: 10/26/1990