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Thymidine kinase 2, mitochondrial (EC 2.7.1.21) (Mt-TK)

 KITM_HUMAN              Reviewed;         265 AA.
O00142; B4DGJ7; B4DZK7; B7ZAB1; E5KNQ5; E9PH08; O15238;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 4.
07-JUN-2017, entry version 163.
RecName: Full=Thymidine kinase 2, mitochondrial;
EC=2.7.1.21;
AltName: Full=Mt-TK;
Flags: Precursor;
Name=TK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=9079672; DOI=10.1074/jbc.272.13.8454;
Johansson M., Karlsson A.;
"Cloning of the cDNA and chromosome localization of the gene for human
thymidine kinase 2.";
J. Biol. Chem. 272:8454-8458(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 34-61
(ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=9989599; DOI=10.1016/S0014-5793(98)01711-6;
Wang L., Munch-Petersen B., Herrstroem Sjoeberg A., Hellman U.,
Bergman T., Joernvall H., Eriksson S.;
"Human thymidine kinase 2: molecular cloning and characterisation of
the enzyme activity with antiviral and cytostatic nucleoside
substrates.";
FEBS Lett. 443:170-174(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 6), AND SUBUNIT.
PubMed=20843780; DOI=10.1093/nar/gkq750;
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W.,
Mindrinos M., Speed T.P., Scharfe C.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
[4]
SEQUENCE REVISION.
Wang L.;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
TISSUE=Brain, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[9]
VARIANTS MTDPS2 ASN-121 AND ASN-212, FUNCTION, AND CHARACTERIZATION OF
VARIANTS MTDPS2 ASN-121 AND ASN-212.
PubMed=11687801; DOI=10.1038/ng751;
Saada A., Shaag A., Mandel H., Nevo Y., Eriksson S., Elpeleg O.;
"Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion
myopathy.";
Nat. Genet. 29:342-344(2001).
[10]
VARIANTS MTDPS2 MET-53; MET-108 AND ASN-121.
PubMed=12391347; DOI=10.1212/01.WNL.0000028689.93049.9A;
Mancuso M., Salviati L., Sacconi S., Otaegui D., Camano P., Marina A.,
Bacman S., Moraes C.T., Carlo J.R., Garcia M., Garcia-Alvarez M.,
Monzon L., Naini A.B., Hirano M., Bonilla E., Taratuto A.L.,
DiMauro S., Vu T.H.;
"Mitochondrial DNA depletion: mutations in thymidine kinase gene with
myopathy and SMA.";
Neurology 59:1197-1202(2002).
[11]
VARIANTS MTDPS2 MET-108 AND LYS-192, AND CHARACTERIZATION OF VARIANTS
MTDPS2 MET-108 AND LYS-192.
PubMed=15639197; DOI=10.1016/j.ymgme.2004.09.005;
Wang L., Limongelli A., Vila M.R., Carrara F., Zeviani M.,
Eriksson S.;
"Molecular insight into mitochondrial DNA depletion syndrome in two
patients with novel mutations in the deoxyguanosine kinase and
thymidine kinase 2 genes.";
Mol. Genet. Metab. 84:75-82(2005).
[12]
VARIANTS MTDPS2 MET-64 AND TRP-183.
PubMed=15907288; DOI=10.1016/j.nmd.2005.03.010;
Tulinius M., Moslemi A.-R., Darin N., Holme E., Oldfors A.;
"Novel mutations in the thymidine kinase 2 gene (TK2) associated with
fatal mitochondrial myopathy and mitochondrial DNA depletion.";
Neuromuscul. Disord. 15:412-415(2005).
[13]
INVOLVEMENT IN PEOB3, VARIANTS PEOB3 TRP-183 AND ALA-188,
CHARACTERIZATION OF VARIANTS PEOB3 TRP-183 AND ALA-188, AND SUBUNIT.
PubMed=21937588; DOI=10.1093/hmg/ddr438;
Tyynismaa H., Sun R., Ahola-Erkkilae S., Almusa H., Poeyhoenen R.,
Korpela M., Honkaniemi J., Isohanni P., Paetau A., Wang L.,
Suomalainen A.;
"Thymidine kinase 2 mutations in autosomal recessive progressive
external ophthalmoplegia with multiple mitochondrial DNA deletions.";
Hum. Mol. Genet. 21:66-75(2012).
[14]
VARIANTS MTDPS2 VAL-117 AND VAL-139.
PubMed=25446393; DOI=10.1016/j.mito.2014.10.007;
Knierim E., Seelow D., Gill E., von Moers A., Schuelke M.;
"Clinical application of whole exome sequencing reveals a novel
compound heterozygous TK2-mutation in two brothers with rapidly
progressive combined muscle-brain atrophy, axonal neuropathy, and
status epilepticus.";
Mitochondrion 20:1-6(2015).
-!- FUNCTION: Phosphorylates thymidine, deoxycytidine, and
deoxyuridine in the mitochondrial matrix. In non-replicating
cells, where cytosolic dNTP synthesis is down-regulated, mtDNA
synthesis depends solely on TK2 and DGUOK. Widely used as target
of antiviral and chemotherapeutic agents.
{ECO:0000269|PubMed:11687801}.
-!- CATALYTIC ACTIVITY: ATP + thymidine = ADP + thymidine 5'-
phosphate.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20843780,
ECO:0000269|PubMed:21937588}.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O00142-1; Sequence=Displayed;
Name=2;
IsoId=O00142-2; Sequence=VSP_003028;
Note=No experimental confirmation available.;
Name=3;
IsoId=O00142-3; Sequence=VSP_043503;
Note=No experimental confirmation available.;
Name=4;
IsoId=O00142-4; Sequence=VSP_044459;
Note=No experimental confirmation available.;
Name=5;
IsoId=O00142-5; Sequence=VSP_054606;
Note=No experimental confirmation available.;
Name=6;
IsoId=O00142-6; Sequence=VSP_058694;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver, pancreas,
muscle, and brain.
-!- DISEASE: Mitochondrial DNA depletion syndrome 2 (MTDPS2)
[MIM:609560]: A disorder due to mitochondrial dysfunction
characterized by childhood onset of muscle weakness associated
with depletion of mtDNA in skeletal muscle. There is wide clinical
variability; some patients have onset in infancy and show a
rapidly progressive course with early death due to respiratory
failure, whereas others have later onset of a slowly progressive
myopathy. {ECO:0000269|PubMed:11687801,
ECO:0000269|PubMed:12391347, ECO:0000269|PubMed:15639197,
ECO:0000269|PubMed:15907288, ECO:0000269|PubMed:25446393}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Progressive external ophthalmoplegia with mitochondrial
DNA deletions, autosomal recessive 3 (PEOB3) [MIM:617069]: A form
of progressive external ophthalmoplegia, a mitochondrial myopathy
characterized by progressive paralysis of the levator palpebrae,
orbicularis oculi, and extraocular muscles. PEOB3 patients
manifest adult-onset progressive external ophthalmoplegia and
progressive proximal muscle weakness associated with muscle
atrophy. {ECO:0000269|PubMed:21937588}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the DCK/DGK family.
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EMBL; U77088; AAC51167.1; -; mRNA.
EMBL; Y10498; CAA71523.3; -; mRNA.
EMBL; AK294627; BAG57808.1; -; mRNA.
EMBL; AK302976; BAG64119.1; -; mRNA.
EMBL; AK316226; BAH14597.1; -; mRNA.
EMBL; AC010542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83013.1; -; Genomic_DNA.
EMBL; CH471092; EAW83015.1; -; Genomic_DNA.
EMBL; CH471092; EAW83017.1; -; Genomic_DNA.
EMBL; HQ205385; ADP90853.1; -; Genomic_DNA.
EMBL; HQ205382; ADP90850.1; -; Genomic_DNA.
EMBL; HQ205383; ADP90851.1; -; Genomic_DNA.
EMBL; HQ205384; ADP90852.1; -; Genomic_DNA.
EMBL; HQ205381; ADP90849.1; -; Genomic_DNA.
EMBL; HQ205380; ADP90848.1; -; Genomic_DNA.
EMBL; HQ205379; ADP90847.1; -; Genomic_DNA.
EMBL; HQ205378; ADP90846.1; -; Genomic_DNA.
EMBL; HQ205377; ADP90845.1; -; Genomic_DNA.
EMBL; HQ205376; ADP90844.1; -; Genomic_DNA.
EMBL; HQ205375; ADP90843.1; -; Genomic_DNA.
EMBL; HQ205374; ADP90842.1; -; Genomic_DNA.
EMBL; HQ205373; ADP90841.1; -; Genomic_DNA.
EMBL; HQ205372; ADP90840.1; -; Genomic_DNA.
EMBL; HQ205371; ADP90839.1; -; Genomic_DNA.
EMBL; HQ205370; ADP90838.1; -; Genomic_DNA.
EMBL; HQ205362; ADP90830.1; -; Genomic_DNA.
EMBL; HQ205363; ADP90831.1; -; Genomic_DNA.
EMBL; HQ205364; ADP90832.1; -; Genomic_DNA.
EMBL; HQ205365; ADP90833.1; -; Genomic_DNA.
EMBL; HQ205366; ADP90834.1; -; Genomic_DNA.
EMBL; HQ205367; ADP90835.1; -; Genomic_DNA.
EMBL; HQ205368; ADP90836.1; -; Genomic_DNA.
EMBL; HQ205369; ADP90837.1; -; Genomic_DNA.
EMBL; HQ205346; ADP90814.1; -; Genomic_DNA.
EMBL; HQ205347; ADP90815.1; -; Genomic_DNA.
EMBL; HQ205348; ADP90816.1; -; Genomic_DNA.
EMBL; HQ205349; ADP90817.1; -; Genomic_DNA.
EMBL; HQ205350; ADP90818.1; -; Genomic_DNA.
EMBL; HQ205351; ADP90819.1; -; Genomic_DNA.
EMBL; HQ205352; ADP90820.1; -; Genomic_DNA.
EMBL; HQ205353; ADP90821.1; -; Genomic_DNA.
EMBL; HQ205354; ADP90822.1; -; Genomic_DNA.
EMBL; HQ205355; ADP90823.1; -; Genomic_DNA.
EMBL; HQ205356; ADP90824.1; -; Genomic_DNA.
EMBL; HQ205357; ADP90825.1; -; Genomic_DNA.
EMBL; HQ205358; ADP90826.1; -; Genomic_DNA.
EMBL; HQ205359; ADP90827.1; -; Genomic_DNA.
EMBL; HQ205360; ADP90828.1; -; Genomic_DNA.
EMBL; HQ205361; ADP90829.1; -; Genomic_DNA.
CCDS; CCDS10805.2; -. [O00142-1]
CCDS; CCDS54016.1; -. [O00142-3]
CCDS; CCDS54017.1; -. [O00142-4]
CCDS; CCDS54018.1; -. [O00142-2]
CCDS; CCDS61955.1; -. [O00142-5]
RefSeq; NP_001166114.1; NM_001172643.1. [O00142-2]
RefSeq; NP_001166115.1; NM_001172644.1. [O00142-3]
RefSeq; NP_001258864.1; NM_001271935.1.
RefSeq; NP_001258979.1; NM_001272050.1. [O00142-5]
RefSeq; NP_004605.4; NM_004614.4. [O00142-1]
UniGene; Hs.512619; -.
ProteinModelPortal; O00142; -.
SMR; O00142; -.
BioGrid; 112939; 8.
STRING; 9606.ENSP00000414334; -.
BindingDB; O00142; -.
ChEMBL; CHEMBL4580; -.
DrugBank; DB02594; 2'-Deoxycytidine.
DrugBank; DB04485; Deoxythymidine.
DrugBank; DB02452; Thymidine-5'-Triphosphate.
iPTMnet; O00142; -.
PhosphoSitePlus; O00142; -.
BioMuta; TK2; -.
MaxQB; O00142; -.
PaxDb; O00142; -.
PeptideAtlas; O00142; -.
PRIDE; O00142; -.
Ensembl; ENST00000299697; ENSP00000299697; ENSG00000166548. [O00142-1]
Ensembl; ENST00000451102; ENSP00000414334; ENSG00000166548. [O00142-6]
Ensembl; ENST00000525974; ENSP00000434594; ENSG00000166548. [O00142-5]
Ensembl; ENST00000527284; ENSP00000435312; ENSG00000166548. [O00142-2]
Ensembl; ENST00000527800; ENSP00000433770; ENSG00000166548. [O00142-5]
Ensembl; ENST00000544898; ENSP00000440898; ENSG00000166548. [O00142-1]
Ensembl; ENST00000545043; ENSP00000438143; ENSG00000166548. [O00142-3]
Ensembl; ENST00000563369; ENSP00000463560; ENSG00000166548. [O00142-5]
Ensembl; ENST00000620035; ENSP00000483833; ENSG00000166548. [O00142-4]
GeneID; 7084; -.
KEGG; hsa:7084; -.
UCSC; uc002eor.4; human. [O00142-1]
CTD; 7084; -.
DisGeNET; 7084; -.
GeneCards; TK2; -.
GeneReviews; TK2; -.
H-InvDB; HIX0021286; -.
HGNC; HGNC:11831; TK2.
HPA; HPA041162; -.
MalaCards; TK2; -.
MIM; 188250; gene.
MIM; 609560; phenotype.
MIM; 617069; phenotype.
neXtProt; NX_O00142; -.
OpenTargets; ENSG00000166548; -.
Orphanet; 254886; Autosomal recessive progressive external ophthalmoplegia.
Orphanet; 254875; Mitochondrial DNA depletion syndrome, myopathic form.
PharmGKB; PA36535; -.
eggNOG; KOG4235; Eukaryota.
eggNOG; COG1428; LUCA.
GeneTree; ENSGT00510000046588; -.
HOGENOM; HOG000006872; -.
HOVERGEN; HBG006216; -.
InParanoid; O00142; -.
KO; K00857; -.
OMA; RDACRWG; -.
OrthoDB; EOG091G0PXX; -.
PhylomeDB; O00142; -.
TreeFam; TF324413; -.
BioCyc; MetaCyc:HS09420-MONOMER; -.
BRENDA; 2.7.1.21; 2681.
Reactome; R-HSA-73614; Pyrimidine salvage.
SABIO-RK; O00142; -.
GenomeRNAi; 7084; -.
PRO; PR:O00142; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000166548; -.
CleanEx; HS_TK2; -.
ExpressionAtlas; O00142; baseline and differential.
Genevisible; O00142; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004137; F:deoxycytidine kinase activity; IEA:Ensembl.
GO; GO:0019206; F:nucleoside kinase activity; TAS:Reactome.
GO; GO:0004797; F:thymidine kinase activity; TAS:ProtInc.
GO; GO:0046092; P:deoxycytidine metabolic process; IEA:Ensembl.
GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
GO; GO:0043097; P:pyrimidine nucleoside salvage; TAS:Reactome.
GO; GO:0046104; P:thymidine metabolic process; IEA:Ensembl.
InterPro; IPR002624; DCK/DGK.
InterPro; IPR031314; DNK_dom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01712; dNK; 1.
PIRSF; PIRSF000705; DNK; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Disease mutation; DNA synthesis; Kinase;
Mitochondrion; Nucleotide-binding; Primary mitochondrial disease;
Progressive external ophthalmoplegia; Reference proteome; Transferase;
Transit peptide.
TRANSIT 1 33 Mitochondrion.
CHAIN 34 265 Thymidine kinase 2, mitochondrial.
/FTId=PRO_0000016842.
NP_BIND 57 65 ATP. {ECO:0000250}.
ACT_SITE 133 133 Proton acceptor. {ECO:0000255}.
BINDING 81 81 Substrate. {ECO:0000250}.
BINDING 99 99 Substrate. {ECO:0000250}.
BINDING 110 110 Substrate. {ECO:0000250}.
BINDING 134 134 Substrate. {ECO:0000250}.
BINDING 201 201 Substrate. {ECO:0000250}.
VAR_SEQ 1 97 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054606.
VAR_SEQ 1 41 MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPP
-> MGAFCQRPSS (in isoform 2).
{ECO:0000303|PubMed:9079672}.
/FTId=VSP_003028.
VAR_SEQ 1 1 M -> MRPGLFKGQAPGSRRRPTAGLAVVRADSHKKEPRAS
GSARPAM (in isoform 6).
{ECO:0000303|PubMed:20843780}.
/FTId=VSP_058694.
VAR_SEQ 53 77 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043503.
VAR_SEQ 78 95 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044459.
VARIANT 53 53 I -> M (in MTDPS2; dbSNP:rs137854432).
{ECO:0000269|PubMed:12391347}.
/FTId=VAR_019419.
VARIANT 64 64 T -> M (in MTDPS2; dbSNP:rs281865487).
{ECO:0000269|PubMed:15907288}.
/FTId=VAR_023790.
VARIANT 108 108 T -> M (in MTDPS2; reduction of activity;
dbSNP:rs137854431).
{ECO:0000269|PubMed:12391347,
ECO:0000269|PubMed:15639197}.
/FTId=VAR_019420.
VARIANT 117 117 M -> V (in MTDPS2; severe form of
combined brain and muscular atrophy;
depletion of mtDNA in skeletal muscle;
normal residual mtDNA in blood and
fibroblasts).
{ECO:0000269|PubMed:25446393}.
/FTId=VAR_072789.
VARIANT 121 121 H -> N (in MTDPS2; reduction of activity
in muscles; dbSNP:rs137854429).
{ECO:0000269|PubMed:11687801,
ECO:0000269|PubMed:12391347}.
/FTId=VAR_019421.
VARIANT 139 139 A -> V (in MTDPS2; severe form of
combined brain and muscular atrophy;
depletion of mtDNA in skeletal muscle;
normal residual mtDNA in blood and
fibroblasts; dbSNP:rs281865494).
{ECO:0000269|PubMed:25446393}.
/FTId=VAR_072790.
VARIANT 183 183 R -> W (in MTDPS2 and PEOB3; reduction of
activity; reduced affinity for ATP;
dbSNP:rs137886900).
{ECO:0000269|PubMed:15907288,
ECO:0000269|PubMed:21937588}.
/FTId=VAR_023791.
VARIANT 188 188 T -> A (in PEOB3; reduction of activity;
reduced affinity for ATP;
dbSNP:rs281865495).
{ECO:0000269|PubMed:21937588}.
/FTId=VAR_076984.
VARIANT 192 192 R -> K (in MTDPS2; reduction of activity;
dbSNP:rs281865496).
{ECO:0000269|PubMed:15639197}.
/FTId=VAR_023792.
VARIANT 212 212 I -> N (in MTDPS2; reduction of activity
in muscles; dbSNP:rs137854430).
{ECO:0000269|PubMed:11687801}.
/FTId=VAR_019422.
CONFLICT 37 37 R -> Y (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 49 49 K -> E (in Ref. 5; BAG57808).
{ECO:0000305}.
CONFLICT 61 61 S -> G (in Ref. 1; AAC51167).
{ECO:0000305}.
CONFLICT 206 206 L -> P (in Ref. 5; BAG57808).
{ECO:0000305}.
CONFLICT 238 238 D -> DH (in Ref. 2; CAA71523).
{ECO:0000305}.
CONFLICT 241 241 Missing (in Ref. 1; AAC51167).
{ECO:0000305}.
CONFLICT 251 251 N -> S (in Ref. 5; BAG57808).
{ECO:0000305}.
SEQUENCE 265 AA; 31005 MW; 1E9CB62D0321A992 CRC64;
MLLWPLRGWA ARALRCFGPG SRGSPASGPG PRRVQRRAWP PDKEQEKEKK SVICVEGNIA
SGKTTCLEFF SNATDVEVLT EPVSKWRNVR GHNPLGLMYH DASRWGLTLQ TYVQLTMLDR
HTRPQVSSVR LMERSIHSAR YIFVENLYRS GKMPEVDYVV LSEWFDWILR NMDVSVDLIV
YLRTNPETCY QRLKKRCREE EKVIPLEYLE AIHHLHEEWL IKGSLFPMAA PVLVIEADHH
MERMLELFEQ NRDRILTPEN RKHCP


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