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P55263

- ADK_HUMAN

UniProt

P55263 - ADK_HUMAN

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Protein
Adenosine kinase
Gene
ADK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. ATP binding Source: UniProtKB-KW
  2. adenosine kinase activity Source: Reactome
  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. AMP salvage Source: UniProtKB-UniPathway
  2. adenosine metabolic process Source: Ensembl
  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 T cell proliferation Source: Ensembl
  7. positive regulation of cardiac muscle hypertrophy Source: Ensembl
  8. purine nucleobase metabolic process Source: Reactome
  9. purine ribonucleoside salvage Source: UniProtKB-KW
  10. purine-containing compound salvage Source: Reactome
  11. ribonucleoside monophosphate biosynthetic process Source: ProtInc
  12. small molecule metabolic process Source: Reactome
  13. type B pancreatic cell proliferation Source: Ensembl
Complete GO annotation...

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

Isoform 1 : Nucleus 1 Publication
Isoform 2 : Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 11Removed1 Publication
Chaini2 – 362361Adenosine kinase
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiP55263.

Family & Domainsi

Motif

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

Sequence similaritiesi

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.

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.
VSP_004668Add
BLAST
Alternative sequencei1 – 2121MAAAE…APQAL → MTSV in isoform 2.
VSP_046713Add
BLAST
Alternative sequencei186 – 24257Missing in isoform 3.
VSP_043526Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981H → A AA sequence 1 Publication
Sequence conflicti133 – 1331N → D in AAB01689. 1 Publication
Sequence conflicti171 – 1711K → R in AAB01689. 1 Publication
Sequence conflicti190 – 1901T → H in AAA97893. 1 Publication
Sequence conflicti219 – 2191I → F in AAH03568. 1 Publication
Sequence conflicti273 – 2731S → V AA sequence 1 Publication
Sequence conflicti289 – 2891I → N AA sequence 1 Publication
Sequence conflicti307 – 3071K → R in AAB01689. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 158 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

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