(data stored in SCRATCH zone)

SWISSPROT: KCRU_HUMAN

ID   KCRU_HUMAN              Reviewed;         417 AA.
AC   P12532; B4DIT8; B7ZA09; Q0VAM3; Q32NF6; Q53FC4;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   30-AUG-2017, entry version 186.
DE   RecName: Full=Creatine kinase U-type, mitochondrial;
DE            EC=2.7.3.2;
DE   AltName: Full=Acidic-type mitochondrial creatine kinase;
DE            Short=Mia-CK;
DE   AltName: Full=Ubiquitous mitochondrial creatine kinase;
DE            Short=U-MtCK;
DE   Flags: Precursor;
GN   Name=CKMT1A; Synonyms=CKMT;
GN   and
GN   Name=CKMT1B; Synonyms=CKMT;
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 [GENOMIC DNA].
RX   PubMed=2914937;
RA   Haas R.C., Korenfeld C., Zhang Z., Perryman B., Roman D.,
RA   Strauss A.W.;
RT   "Isolation and characterization of the gene and cDNA encoding human
RT   mitochondrial creatine kinase.";
RL   J. Biol. Chem. 264:2890-2897(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon, and Hippocampus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and PNS;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-417, AND SUBUNIT.
RX   PubMed=10737943;
RX   DOI=10.1002/(SICI)1097-0134(20000515)39:3<216::AID-PROT40>3.0.CO;2-#;
RA   Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., Schlattner U.;
RT   "Crystal structure of human ubiquitous mitochondrial creatine
RT   kinase.";
RL   Proteins 39:216-225(2000).
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       {ECO:0000255|PROSITE-ProRule:PRU10029}.
CC   -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC       {ECO:0000269|PubMed:10737943}.
CC   -!- INTERACTION:
CC       P0CE72:OCM; NbExp=8; IntAct=EBI-1050662, EBI-11955379;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P12532-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P12532-2; Sequence=VSP_038045;
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC       ProRule:PRU00843}.
DR   EMBL; J04469; AAA98744.1; -; Genomic_DNA.
DR   EMBL; BT006628; AAP35274.1; -; mRNA.
DR   EMBL; AK295776; BAG58600.1; -; mRNA.
DR   EMBL; AK223365; BAD97085.1; -; mRNA.
DR   EMBL; AK316124; BAH14495.1; -; mRNA.
DR   EMBL; AK316319; BAH14690.1; -; mRNA.
DR   EMBL; BC001926; AAH01926.1; -; mRNA.
DR   EMBL; BC006467; AAH06467.1; -; mRNA.
DR   EMBL; BC108652; AAI08653.1; -; mRNA.
DR   EMBL; BC121001; AAI21002.1; -; mRNA.
DR   EMBL; BC121002; AAI21003.1; -; mRNA.
DR   CCDS; CCDS10097.1; -. [P12532-1]
DR   CCDS; CCDS32217.1; -. [P12532-1]
DR   PIR; A31431; A30789.
DR   RefSeq; NP_001015001.1; NM_001015001.2. [P12532-1]
DR   RefSeq; NP_001308855.1; NM_001321926.1. [P12532-1]
DR   RefSeq; NP_001308856.1; NM_001321927.1. [P12532-2]
DR   RefSeq; NP_001308857.1; NM_001321928.1. [P12532-2]
DR   RefSeq; NP_066270.1; NM_020990.4. [P12532-1]
DR   RefSeq; XP_011519496.1; XM_011521194.1. [P12532-2]
DR   RefSeq; XP_011519497.1; XM_011521195.2. [P12532-2]
DR   RefSeq; XP_011519498.1; XM_011521196.1. [P12532-2]
DR   RefSeq; XP_011519499.1; XM_011521197.2. [P12532-1]
DR   RefSeq; XP_016877858.1; XM_017022369.1. [P12532-2]
DR   RefSeq; XP_016877859.1; XM_017022370.1. [P12532-2]
DR   UniGene; Hs.654988; -.
DR   UniGene; Hs.741420; -.
DR   PDB; 1QK1; X-ray; 2.70 A; A/B/C/D/E/F/G/H=39-417.
DR   PDBsum; 1QK1; -.
DR   ProteinModelPortal; P12532; -.
DR   SMR; P12532; -.
DR   BioGrid; 107579; 20.
DR   BioGrid; 139227; 17.
DR   IntAct; P12532; 13.
DR   MINT; MINT-3304503; -.
DR   STRING; 9606.ENSP00000406577; -.
DR   DrugBank; DB00148; Creatine.
DR   iPTMnet; P12532; -.
DR   PhosphoSitePlus; P12532; -.
DR   SwissPalm; P12532; -.
DR   BioMuta; CKMT1A; -.
DR   DMDM; 125315; -.
DR   UCD-2DPAGE; P12532; -.
DR   EPD; P12532; -.
DR   MaxQB; P12532; -.
DR   PaxDb; P12532; -.
DR   PeptideAtlas; P12532; -.
DR   PRIDE; P12532; -.
DR   DNASU; 1159; -.
DR   Ensembl; ENST00000300283; ENSP00000300283; ENSG00000237289. [P12532-1]
DR   Ensembl; ENST00000413453; ENSP00000406577; ENSG00000223572. [P12532-1]
DR   Ensembl; ENST00000434505; ENSP00000413165; ENSG00000223572. [P12532-1]
DR   Ensembl; ENST00000441322; ENSP00000413255; ENSG00000237289. [P12532-1]
DR   GeneID; 1159; -.
DR   GeneID; 548596; -.
DR   KEGG; hsa:1159; -.
DR   KEGG; hsa:548596; -.
DR   UCSC; uc001zsc.3; human. [P12532-1]
DR   CTD; 1159; -.
DR   CTD; 548596; -.
DR   DisGeNET; 1159; -.
DR   DisGeNET; 548596; -.
DR   GeneCards; CKMT1A; -.
DR   GeneCards; CKMT1B; -.
DR   HGNC; HGNC:31736; CKMT1A.
DR   HGNC; HGNC:1995; CKMT1B.
DR   HPA; HPA043491; -.
DR   MIM; 123290; gene.
DR   MIM; 613415; gene.
DR   neXtProt; NX_P12532; -.
DR   OpenTargets; ENSG00000223572; -.
DR   OpenTargets; ENSG00000237289; -.
DR   PharmGKB; PA142672108; -.
DR   eggNOG; KOG3581; Eukaryota.
DR   eggNOG; COG3869; LUCA.
DR   GeneTree; ENSGT00550000074561; -.
DR   HOGENOM; HOG000232165; -.
DR   HOVERGEN; HBG001339; -.
DR   InParanoid; P12532; -.
DR   KO; K00933; -.
DR   OMA; LCDKATP; -.
DR   OrthoDB; EOG091G0HZ0; -.
DR   PhylomeDB; P12532; -.
DR   TreeFam; TF314214; -.
DR   BioCyc; MetaCyc:HS09820-MONOMER; -.
DR   BRENDA; 2.7.3.2; 2681.
DR   Reactome; R-HSA-71288; Creatine metabolism.
DR   ChiTaRS; CKMT1B; human.
DR   EvolutionaryTrace; P12532; -.
DR   GeneWiki; CKMT1B; -.
DR   PRO; PR:P12532; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000223572; -.
DR   CleanEx; HS_CKMT1A; -.
DR   CleanEx; HS_CKMT1B; -.
DR   ExpressionAtlas; P12532; baseline and differential.
DR   Genevisible; P12532; HS.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; TAS:Reactome.
DR   GO; GO:0006600; P:creatine metabolic process; TAS:Reactome.
DR   Gene3D; 1.10.135.10; -; 1.
DR   Gene3D; 3.30.590.10; -; 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; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; PTHR11547; 1.
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;
DR   PRODOM; P12532.
DR   SWISS-2DPAGE; P12532.
KW   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    417       Creatine kinase U-type, mitochondrial.
FT                                /FTId=PRO_0000016590.
FT   DOMAIN       45    131       Phosphagen kinase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00842}.
FT   DOMAIN      158    400       Phosphagen kinase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00843}.
FT   NP_BIND     161    165       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     353    358       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   REGION       40     64       Cardiolipin-binding. {ECO:0000250}.
FT   BINDING     224    224       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     269    269       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     325    325       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     368    368       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   MOD_RES     151    151       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25809}.
FT   MOD_RES     196    196       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P25809}.
FT   MOD_RES     232    232       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P30275}.
FT   VAR_SEQ      50     50       S -> SQTWPTGQLPGNCTRSRRLCPPSMVTGYPLPS (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_038045.
FT   CONFLICT    176    176       P -> L (in Ref. 3; BAG58600).
FT                                {ECO:0000305}.
FT   CONFLICT    401    401       E -> G (in Ref. 4; BAD97085).
FT                                {ECO:0000305}.
FT   HELIX        49     52       {ECO:0000244|PDB:1QK1}.
FT   HELIX        62     66       {ECO:0000244|PDB:1QK1}.
FT   HELIX        69     75       {ECO:0000244|PDB:1QK1}.
FT   HELIX        86     95       {ECO:0000244|PDB:1QK1}.
FT   STRAND      100    102       {ECO:0000244|PDB:1QK1}.
FT   HELIX       114    117       {ECO:0000244|PDB:1QK1}.
FT   HELIX       119    129       {ECO:0000244|PDB:1QK1}.
FT   TURN        130    132       {ECO:0000244|PDB:1QK1}.
FT   TURN        135    137       {ECO:0000244|PDB:1QK1}.
FT   HELIX       146    148       {ECO:0000244|PDB:1QK1}.
FT   TURN        156    158       {ECO:0000244|PDB:1QK1}.
FT   STRAND      159    168       {ECO:0000244|PDB:1QK1}.
FT   TURN        176    178       {ECO:0000244|PDB:1QK1}.
FT   HELIX       181    195       {ECO:0000244|PDB:1QK1}.
FT   HELIX       200    202       {ECO:0000244|PDB:1QK1}.
FT   STRAND      204    208       {ECO:0000244|PDB:1QK1}.
FT   HELIX       209    211       {ECO:0000244|PDB:1QK1}.
FT   HELIX       214    222       {ECO:0000244|PDB:1QK1}.
FT   HELIX       233    236       {ECO:0000244|PDB:1QK1}.
FT   TURN        237    247       {ECO:0000244|PDB:1QK1}.
FT   STRAND      249    253       {ECO:0000244|PDB:1QK1}.
FT   STRAND      258    277       {ECO:0000244|PDB:1QK1}.
FT   HELIX       279    298       {ECO:0000244|PDB:1QK1}.
FT   TURN        299    301       {ECO:0000244|PDB:1QK1}.
FT   TURN        308    310       {ECO:0000244|PDB:1QK1}.
FT   HELIX       317    319       {ECO:0000244|PDB:1QK1}.
FT   STRAND      325    331       {ECO:0000244|PDB:1QK1}.
FT   HELIX       333    337       {ECO:0000244|PDB:1QK1}.
FT   HELIX       341    348       {ECO:0000244|PDB:1QK1}.
FT   STRAND      350    353       {ECO:0000244|PDB:1QK1}.
FT   TURN        359    361       {ECO:0000244|PDB:1QK1}.
FT   STRAND      364    372       {ECO:0000244|PDB:1QK1}.
FT   STRAND      375    377       {ECO:0000244|PDB:1QK1}.
FT   HELIX       379    400       {ECO:0000244|PDB:1QK1}.
FT   TURN        401    403       {ECO:0000244|PDB:1QK1}.
SQ   SEQUENCE   417 AA;  47037 MW;  274DAC2E9A8AD882 CRC64;
     MAGPFSRLLS ARPGLRLLAL AGAGSLAAGF LLRPEPVRAA SERRRLYPPS AEYPDLRKHN
     NCMASHLTPA VYARLCDKTT PTGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAD
     LFDPVIQERH NGYDPRTMKH TTDLDASKIR SGYFDERYVL SSRVRTGRSI RGLSLPPACT
     RAERREVERV VVDALSGLKG DLAGRYYRLS EMTEAEQQQL IDDHFLFDKP VSPLLTAAGM
     ARDWPDARGI WHNNEKSFLI WVNEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
     GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
     AATGGVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL ERGQDIRIPT PVIHTKH
//

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