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P23919 (KTHY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thymidylate kinase

EC=2.7.4.9
Alternative name(s):
dTMP kinase
Gene names
Name:DTYMK
Synonyms:CDC8, TMPK, TYMK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of dTMP to dTDP. HAMAP-Rule MF_00165

Catalytic activity

ATP + dTMP = ADP + dTDP. HAMAP-Rule MF_00165

Pathway

Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00165

Sequence similarities

Belongs to the thymidylate kinase family.

Ontologies

Keywords
   Biological processNucleotide biosynthesis
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Traceable author statement Ref.2. Source: ProtInc

cell proliferation

Traceable author statement Ref.2. Source: ProtInc

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

dTDP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

dTTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

myoblast differentiation

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleoside monophosphate phosphorylation

Inferred from experiment. Source: GOC

nucleotide phosphorylation

Inferred from direct assay PubMed 8845311. Source: GOC

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrial intermembrane space

Inferred from electronic annotation. Source: Ensembl

mitochondrial matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside phosphate kinase activity

Inferred from experiment. Source: Reactome

thymidylate kinase activity

Inferred from direct assay PubMed 8845311. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23919-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P23919-2)

The sequence of this isoform differs from the canonical sequence as follows:
     111-134: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 212211Thymidylate kinase HAMAP-Rule MF_00165
PRO_0000155210

Regions

Nucleotide binding13 – 208ATP Probable

Amino acid modifications

Modified residue21N-acetylalanine Ref.5
Modified residue1691N6-acetyllysine Ref.6

Natural variations

Alternative sequence111 – 13424Missing in isoform 2.
VSP_054164

Experimental info

Sequence conflict31A → P in CAG46783. Ref.3
Sequence conflict31 – 377CAAGHRA → SRGPPP in CAA38528. Ref.1
Sequence conflict581Q → K in AAA21719. Ref.2
Sequence conflict681V → A in CAG46783. Ref.3
Sequence conflict183 – 1842SI → RL in CAA38528. Ref.1
Sequence conflict190 – 1912DI → EL Ref.1
Sequence conflict190 – 1912DI → EL Ref.2

Secondary structure

..................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 7, 2004. Version 4.
Checksum: A52876625B3621B1

FASTA21223,819
        10         20         30         40         50         60 
MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK 

        70         80         90        100        110        120 
SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP 

       130        140        150        160        170        180 
DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA 

       190        200        210 
SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK 

« Hide

Isoform 2 [UniParc].

Checksum: 38FE4F99F6DDA886
Show »

FASTA18821,064

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast."
Su J.Y., Sclafani R.A.
Nucleic Acids Res. 19:823-827(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth."
Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C., Jong A.
DNA Cell Biol. 13:461-471(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Muscle.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds."
Ostermann N., Segura-Pena D., Meier C., Veit T., Monnerjahn C., Konrad M., Lavie A.
Biochemistry 42:2568-2577(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54729 mRNA. Translation: CAA38528.1.
L16991 mRNA. Translation: AAA21719.1.
CR541986 mRNA. Translation: CAG46783.1.
BC001827 mRNA. Translation: AAH01827.1.
BC171902 mRNA. Translation: AAI71902.1.
PIRS26845.
RefSeqNP_036277.2. NM_012145.3.
UniGeneHs.471873.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E2DX-ray1.65A1-212[»]
1E2EX-ray2.00A1-212[»]
1E2FX-ray1.60A1-212[»]
1E2GX-ray1.70A1-212[»]
1E2QX-ray1.70A1-212[»]
1E98X-ray1.90A1-212[»]
1E99X-ray1.80A1-212[»]
1E9AX-ray1.60A1-212[»]
1E9BX-ray1.70A1-212[»]
1E9CX-ray1.60A1-212[»]
1E9DX-ray1.70A1-212[»]
1E9EX-ray1.60A1-212[»]
1E9FX-ray1.90A1-212[»]
1NMXX-ray1.70A1-212[»]
1NMYX-ray1.60A4-212[»]
1NMZX-ray1.75A1-212[»]
1NN0X-ray1.60A1-212[»]
1NN1X-ray1.90A1-212[»]
1NN3X-ray1.55A1-212[»]
1NN5X-ray1.50A1-212[»]
2XX3X-ray2.00A1-212[»]
ProteinModelPortalP23919.
SMRP23919. Positions 4-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108174. 5 interactions.
IntActP23919. 2 interactions.
MINTMINT-3010142.
STRING9606.ENSP00000304802.

Chemistry

BindingDBP23919.
ChEMBLCHEMBL4388.

PTM databases

PhosphoSiteP23919.

Polymorphism databases

DMDM56405325.

Proteomic databases

PaxDbP23919.
PRIDEP23919.

Protocols and materials databases

DNASU1841.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305784; ENSP00000304802; ENSG00000168393.
GeneID1841.
KEGGhsa:1841.
UCSCuc002wbz.2. human.

Organism-specific databases

CTD1841.
GeneCardsGC02M242634.
H-InvDBHIX0161852.
HGNCHGNC:3061. DTYMK.
HPAHPA042593.
HPA042719.
MIM188345. gene.
neXtProtNX_P23919.
PharmGKBPA150.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0125.
HOGENOMHOG000229079.
HOVERGENHBG051418.
InParanoidP23919.
KOK00943.
OMAGKMIDSY.
OrthoDBEOG7WQ7T8.
PhylomeDBP23919.
TreeFamTF324638.

Enzyme and pathway databases

BioCycMetaCyc:HS11384-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP23919.
UniPathwayUPA00575.

Gene expression databases

ArrayExpressP23919.
BgeeP23919.
CleanExHS_DTYMK.
GenevestigatorP23919.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00165. Thymidylate_kinase.
InterProIPR027417. P-loop_NTPase.
IPR018095. Thymidylate_kin_CS.
IPR018094. Thymidylate_kinase.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00041. DTMP_kinase. 1 hit.
PROSITEPS01331. THYMIDYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23919.
GeneWikiDTYMK.
GenomeRNAi1841.
NextBio7537.
PROP23919.
SOURCESearch...

Entry information

Entry nameKTHY_HUMAN
AccessionPrimary (citable) accession number: P23919
Secondary accession number(s): B7ZW70, Q6FGX1, Q9BUX4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 7, 2004
Last modified: April 16, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM