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P55263

- ADK_HUMAN

UniProt

P55263 - ADK_HUMAN

Protein

Adenosine kinase

Gene

ADK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides.

    Catalytic activityi

    ATP + adenosine = ADP + AMP.

    Cofactori

    Binds 3 magnesium ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi49 – 491Magnesium 1
    Metal bindingi147 – 1471Magnesium 2
    Metal bindingi148 – 1481Magnesium 2
    Active sitei317 – 3171

    GO - Molecular functioni

    1. adenosine kinase activity Source: Reactome
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. phosphotransferase activity, alcohol group as acceptor Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. adenosine metabolic process Source: Ensembl
    2. AMP salvage Source: UniProtKB-UniPathway
    3. circadian regulation of gene expression Source: Ensembl
    4. dATP biosynthetic process Source: Ensembl
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. positive regulation of cardiac muscle hypertrophy Source: Ensembl
    7. positive regulation of T cell proliferation Source: Ensembl
    8. purine-containing compound salvage Source: Reactome
    9. purine nucleobase metabolic process Source: Reactome
    10. purine ribonucleoside salvage Source: UniProtKB-KW
    11. ribonucleoside monophosphate biosynthetic process Source: ProtInc
    12. small molecule metabolic process Source: Reactome
    13. type B pancreatic cell proliferation Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Purine salvage

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08097-MONOMER.
    ReactomeiREACT_1923. Purine salvage.
    SABIO-RKP55263.
    UniPathwayiUPA00588; UER00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosine kinase (EC:2.7.1.20)
    Short name:
    AK
    Alternative name(s):
    Adenosine 5'-phosphotransferase
    Gene namesi
    Name:ADK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:257. ADK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Hypermethioninemia due to adenosine kinase deficiency (HMAKD) [MIM:614300]: A metabolic disorder characterized by global developmental delay, early-onset seizures, mild dysmorphic features, and characteristic biochemical anomalies, including persistent hypermethioninemia with increased levels of S-adenosylmethionine and S-adenosylhomocysteine. Homocysteine levels are typically normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301G → E in HMAKD; the mutant shows some residual activity. 1 Publication
    VAR_066640
    Natural varianti235 – 2351D → A in HMAKD; the mutant shows some residual activity. 1 Publication
    VAR_066641
    Natural varianti318 – 3181A → E in HMAKD; complete loss of activity. 1 Publication
    VAR_066642

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 122KK → AA or AD: Abolishes nuclear localization. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614300. phenotype.
    Orphaneti289290. Hypermethioninemia encephalopathy due to adenosine kinase deficiency.
    PharmGKBiPA24579.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 362361Adenosine kinasePRO_0000080053Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei77 – 771Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP55263.
    PaxDbiP55263.
    PRIDEiP55263.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00234368.

    PTM databases

    PhosphoSiteiP55263.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest level in placenta, liver, muscle and kidney.

    Gene expression databases

    ArrayExpressiP55263.
    BgeeiP55263.
    CleanExiHS_ADK.
    GenevestigatoriP55263.

    Organism-specific databases

    HPAiHPA038409.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi106644. 3 interactions.
    IntActiP55263. 3 interactions.
    MINTiMINT-5001097.
    STRINGi9606.ENSP00000286621.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 294
    Beta strandi33 – 397
    Helixi42 – 476
    Beta strandi52 – 576
    Helixi60 – 623
    Helixi63 – 7210
    Beta strandi76 – 805
    Helixi82 – 9413
    Beta strandi96 – 994
    Beta strandi101 – 11010
    Helixi111 – 12212
    Beta strandi126 – 13510
    Beta strandi139 – 1457
    Beta strandi148 – 1547
    Helixi156 – 1605
    Helixi163 – 1653
    Turni166 – 1683
    Helixi170 – 1789
    Beta strandi180 – 1856
    Helixi186 – 1905
    Helixi193 – 20513
    Beta strandi209 – 2135
    Helixi217 – 2226
    Helixi224 – 2307
    Helixi231 – 2333
    Beta strandi235 – 2406
    Helixi241 – 25010
    Helixi258 – 2669
    Beta strandi278 – 2836
    Beta strandi286 – 2916
    Beta strandi296 – 2994
    Helixi312 – 32716
    Turni328 – 3303
    Helixi333 – 34715
    Beta strandi350 – 3534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BX4X-ray1.50A22-362[»]
    2I6AX-ray2.20A/B/C/D22-362[»]
    2I6BX-ray2.30A/B22-362[»]
    ProteinModelPortaliP55263.
    SMRiP55263. Positions 20-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55263.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi8 – 169Nuclear localization signal1 Publication

    Sequence similaritiesi

    Belongs to the carbohydrate kinase PfkB family.Curated

    Phylogenomic databases

    eggNOGiCOG0524.
    HOGENOMiHOG000172419.
    HOVERGENiHBG002367.
    InParanoidiP55263.
    KOiK00856.
    OMAiCITGGNR.
    OrthoDBiEOG7VMP5W.
    PhylomeDBiP55263.
    TreeFamiTF300745.

    Family and domain databases

    Gene3Di3.40.1190.20. 1 hit.
    InterProiIPR001805. Adenokinase.
    IPR002173. Carboh/pur_kinase_PfkB_CS.
    IPR011611. PfkB_dom.
    IPR029056. Ribokinase-like.
    [Graphical view]
    PANTHERiPTHR10584:SF24. PTHR10584:SF24. 1 hit.
    PfamiPF00294. PfkB. 1 hit.
    [Graphical view]
    PRINTSiPR00989. ADENOKINASE.
    SUPFAMiSSF53613. SSF53613. 1 hit.
    PROSITEiPS00584. PFKB_KINASES_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55263-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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.

    « Hide

    MAAAEEEPKP KKLKVEAPQA LRENILFGMG NPLLDISAVV DKDFLDKYSL    50
    KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA 100
    ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS 150
    LIANLAAANC YKKEKHLDLE KNWMLVEKAR VCYIAGFFLT VSPESVLKVA 200
    HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE 250
    QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA 300
    VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR 350
    TGCTFPEKPD FH 362
    Length:362
    Mass (Da):40,545
    Last modified:May 30, 2000 - v2
    Checksum:i48AA4925865BFE70
    GO
    Isoform 2 (identifier: P55263-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MAAAEEEPKPKKLKVEAPQAL → MTSV

    Show »
    Length:345
    Mass (Da):38,703
    Checksum:i7DC20F364E63D944
    GO
    Isoform 3 (identifier: P55263-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         186-242: Missing.

    Show »
    Length:305
    Mass (Da):34,084
    Checksum:iDC7E0245659B0F06
    GO
    Isoform 4 (identifier: P55263-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-65: MAAAEEEPKP...ILAEDKHKEL → MTSVRENILFGMGNPLLDISAVVDKDFLDK

    Note: No experimental confirmation available.

    Show »
    Length:327
    Mass (Da):36,580
    Checksum:iE5A9FDBDB77E7357
    GO

    Sequence cautioni

    The sequence AAB01689.1 differs from that shown. Reason: Frameshift at position 17.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981H → A AA sequence (PubMed:8577746)Curated
    Sequence conflicti133 – 1331N → D in AAB01689. (PubMed:8917457)Curated
    Sequence conflicti171 – 1711K → R in AAB01689. (PubMed:8917457)Curated
    Sequence conflicti190 – 1901T → H in AAA97893. (PubMed:8577746)Curated
    Sequence conflicti219 – 2191I → F in AAH03568. (PubMed:15489334)Curated
    Sequence conflicti273 – 2731S → V AA sequence (PubMed:8577746)Curated
    Sequence conflicti289 – 2891I → N AA sequence (PubMed:8577746)Curated
    Sequence conflicti307 – 3071K → R in AAB01689. (PubMed:8917457)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301G → E in HMAKD; the mutant shows some residual activity. 1 Publication
    VAR_066640
    Natural varianti235 – 2351D → A in HMAKD; the mutant shows some residual activity. 1 Publication
    VAR_066641
    Natural varianti318 – 3181A → E in HMAKD; complete loss of activity. 1 Publication
    VAR_066642

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6565MAAAE…KHKEL → MTSVRENILFGMGNPLLDIS AVVDKDFLDK in isoform 4. 1 PublicationVSP_004668Add
    BLAST
    Alternative sequencei1 – 2121MAAAE…APQAL → MTSV in isoform 2. 4 PublicationsVSP_046713Add
    BLAST
    Alternative sequencei186 – 24257Missing in isoform 3. 1 PublicationVSP_043526Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50196 mRNA. Translation: AAA97893.1.
    U33936 mRNA. Translation: AAB01689.1. Frameshift.
    U90338 mRNA. Translation: AAB50234.1.
    U90339 mRNA. Translation: AAB50235.1.
    AK290633 mRNA. Translation: BAF83322.1.
    AK301590 mRNA. Translation: BAH13519.1.
    AK302706 mRNA. Translation: BAH13786.1.
    AC012046 Genomic DNA. No translation available.
    AC022026 Genomic DNA. No translation available.
    AC022540 Genomic DNA. No translation available.
    AC091699 Genomic DNA. No translation available.
    AL357037 Genomic DNA. No translation available.
    AL731576 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54555.1.
    CH471083 Genomic DNA. Translation: EAW54556.1.
    BC003568 mRNA. Translation: AAH03568.1.
    CCDSiCCDS55716.1. [P55263-3]
    CCDS55717.1. [P55263-4]
    CCDS7343.1. [P55263-1]
    CCDS7344.1. [P55263-2]
    PIRiJC5363.
    JC5364.
    RefSeqiNP_001114.2. NM_001123.3. [P55263-2]
    NP_001189378.1. NM_001202449.1. [P55263-4]
    NP_001189379.1. NM_001202450.1. [P55263-3]
    NP_006712.2. NM_006721.3. [P55263-1]
    UniGeneiHs.656586.

    Genome annotation databases

    EnsembliENST00000286621; ENSP00000286621; ENSG00000156110. [P55263-1]
    ENST00000372734; ENSP00000361819; ENSG00000156110. [P55263-2]
    ENST00000539909; ENSP00000443965; ENSG00000156110. [P55263-3]
    ENST00000541550; ENSP00000438321; ENSG00000156110. [P55263-4]
    GeneIDi132.
    KEGGihsa:132.
    UCSCiuc001jwi.3. human. [P55263-1]
    uc001jwj.3. human.
    uc010qlb.2. human. [P55263-3]

    Polymorphism databases

    DMDMi6840802.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U50196 mRNA. Translation: AAA97893.1 .
    U33936 mRNA. Translation: AAB01689.1 . Frameshift.
    U90338 mRNA. Translation: AAB50234.1 .
    U90339 mRNA. Translation: AAB50235.1 .
    AK290633 mRNA. Translation: BAF83322.1 .
    AK301590 mRNA. Translation: BAH13519.1 .
    AK302706 mRNA. Translation: BAH13786.1 .
    AC012046 Genomic DNA. No translation available.
    AC022026 Genomic DNA. No translation available.
    AC022540 Genomic DNA. No translation available.
    AC091699 Genomic DNA. No translation available.
    AL357037 Genomic DNA. No translation available.
    AL731576 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54555.1 .
    CH471083 Genomic DNA. Translation: EAW54556.1 .
    BC003568 mRNA. Translation: AAH03568.1 .
    CCDSi CCDS55716.1. [P55263-3 ]
    CCDS55717.1. [P55263-4 ]
    CCDS7343.1. [P55263-1 ]
    CCDS7344.1. [P55263-2 ]
    PIRi JC5363.
    JC5364.
    RefSeqi NP_001114.2. NM_001123.3. [P55263-2 ]
    NP_001189378.1. NM_001202449.1. [P55263-4 ]
    NP_001189379.1. NM_001202450.1. [P55263-3 ]
    NP_006712.2. NM_006721.3. [P55263-1 ]
    UniGenei Hs.656586.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BX4 X-ray 1.50 A 22-362 [» ]
    2I6A X-ray 2.20 A/B/C/D 22-362 [» ]
    2I6B X-ray 2.30 A/B 22-362 [» ]
    ProteinModelPortali P55263.
    SMRi P55263. Positions 20-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106644. 3 interactions.
    IntActi P55263. 3 interactions.
    MINTi MINT-5001097.
    STRINGi 9606.ENSP00000286621.

    Chemistry

    BindingDBi P55263.
    ChEMBLi CHEMBL3589.
    DrugBanki DB00640. Adenosine.
    DB00131. Adenosine monophosphate.
    DB00171. Adenosine triphosphate.
    DB00061. Pegademase bovine.
    DB00811. Ribavirin.
    GuidetoPHARMACOLOGYi 1231.

    PTM databases

    PhosphoSitei P55263.

    Polymorphism databases

    DMDMi 6840802.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00234368.

    Proteomic databases

    MaxQBi P55263.
    PaxDbi P55263.
    PRIDEi P55263.

    Protocols and materials databases

    DNASUi 132.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286621 ; ENSP00000286621 ; ENSG00000156110 . [P55263-1 ]
    ENST00000372734 ; ENSP00000361819 ; ENSG00000156110 . [P55263-2 ]
    ENST00000539909 ; ENSP00000443965 ; ENSG00000156110 . [P55263-3 ]
    ENST00000541550 ; ENSP00000438321 ; ENSG00000156110 . [P55263-4 ]
    GeneIDi 132.
    KEGGi hsa:132.
    UCSCi uc001jwi.3. human. [P55263-1 ]
    uc001jwj.3. human.
    uc010qlb.2. human. [P55263-3 ]

    Organism-specific databases

    CTDi 132.
    GeneCardsi GC10P075910.
    HGNCi HGNC:257. ADK.
    HPAi HPA038409.
    MIMi 102750. gene.
    614300. phenotype.
    neXtProti NX_P55263.
    Orphaneti 289290. Hypermethioninemia encephalopathy due to adenosine kinase deficiency.
    PharmGKBi PA24579.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0524.
    HOGENOMi HOG000172419.
    HOVERGENi HBG002367.
    InParanoidi P55263.
    KOi K00856.
    OMAi CITGGNR.
    OrthoDBi EOG7VMP5W.
    PhylomeDBi P55263.
    TreeFami TF300745.

    Enzyme and pathway databases

    UniPathwayi UPA00588 ; UER00659 .
    BioCyci MetaCyc:HS08097-MONOMER.
    Reactomei REACT_1923. Purine salvage.
    SABIO-RK P55263.

    Miscellaneous databases

    ChiTaRSi ADK. human.
    EvolutionaryTracei P55263.
    GeneWikii ADK_(gene).
    GenomeRNAii 132.
    NextBioi 527.
    PROi P55263.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55263.
    Bgeei P55263.
    CleanExi HS_ADK.
    Genevestigatori P55263.

    Family and domain databases

    Gene3Di 3.40.1190.20. 1 hit.
    InterProi IPR001805. Adenokinase.
    IPR002173. Carboh/pur_kinase_PfkB_CS.
    IPR011611. PfkB_dom.
    IPR029056. Ribokinase-like.
    [Graphical view ]
    PANTHERi PTHR10584:SF24. PTHR10584:SF24. 1 hit.
    Pfami PF00294. PfkB. 1 hit.
    [Graphical view ]
    PRINTSi PR00989. ADENOKINASE.
    SUPFAMi SSF53613. SSF53613. 1 hit.
    PROSITEi PS00584. PFKB_KINASES_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of human adenosine kinase cDNA: sequence similarity to microbial ribokinases and fructokinases."
      Spychala J., Datta N.S., Takabayashi K., Datta M., Fox I.H., Gribbin T., Mitchell B.S.
      Proc. Natl. Acad. Sci. U.S.A. 93:1232-1237(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 94-133; 175-200 AND 272-289.
      Tissue: Liver.
    2. "Cloning and characterization of cDNA for adenosine kinase from mammalian (Chinese hamster, mouse, human and rat) species. High frequency mutants of Chinese hamster ovary cells involve structural alterations in the gene."
      Singh B., Hao W., Wu Z.-C., Eigl B., Gupta R.S.
      Eur. J. Biochem. 241:564-571(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
      Tissue: Mammary gland and Testis.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 2).
      Tissue: Skin.
    8. "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].
    9. "Subcellular localization of adenosine kinase in mammalian cells: The long isoform of AdK is localized in the nucleus."
      Cui X.A., Singh B., Park J., Gupta R.S.
      Biochem. Biophys. Res. Commun. 388:46-50(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 11-LYS-LYS-12.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Structure of human adenosine kinase at 1.5-A resolution."
      Mathews I.I., Erion M.D., Ealick S.E.
      Biochemistry 37:15607-15620(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ISOFORM 2.
    13. "Identification of the phosphotyrosine proteome from thrombin activated platelets."
      Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
      Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-77.
    14. "Adenosine kinase deficiency disrupts the methionine cycle and causes hypermethioninemia, encephalopathy, and abnormal liver function."
      Bjursell M.K., Blom H.J., Cayuela J.A., Engvall M.L., Lesko N., Balasubramaniam S., Brandberg G., Halldin M., Falkenberg M., Jakobs C., Smith D., Struys E., von Dobeln U., Gustafsson C.M., Lundeberg J., Wedell A.
      Am. J. Hum. Genet. 89:507-515(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HMAKD GLU-30; ALA-235 AND GLU-318, CHARACTERIZATION OF VARIANTS HMAKD GLU-30; ALA-235 AND GLU-318.

    Entry informationi

    Entry nameiADK_HUMAN
    AccessioniPrimary (citable) accession number: P55263
    Secondary accession number(s): B7Z783
    , B7Z800, O00741, O00742, Q16710, Q5JQ10, Q5JQ11, Q9BTN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3