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Protein

Adenosine kinase

Gene

ADK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+Note: Binds 3 Mg2+ ions per subunit.

Pathway: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from adenosine.
Proteins known to be involved in this subpathway in this organism are:
  1. Adenosine kinase (ADK)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from adenosine, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

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

GO - Biological processi

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.
BRENDAi2.7.1.20. 2681.
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 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:257. ADK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hypermethioninemia due to adenosine kinase deficiency (HMAKD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614300
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.

Chemistry

DrugBankiDB01048. Abacavir.
DB00640. Adenosine.
DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.
DB00811. Ribavirin.

Polymorphism and mutation databases

BioMutaiADK.
DMDMi6840802.

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

BgeeiP55263.
CleanExiHS_ADK.
GenevisibleiP55263. HS.

Organism-specific databases

HPAiCAB032876.
HPA038391.
HPA038409.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi106644. 5 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 – 294Combined sources
Beta strandi33 – 397Combined sources
Helixi42 – 476Combined sources
Beta strandi52 – 576Combined sources
Helixi60 – 623Combined sources
Helixi63 – 7210Combined sources
Beta strandi76 – 805Combined sources
Helixi82 – 9413Combined sources
Beta strandi96 – 994Combined sources
Beta strandi101 – 11010Combined sources
Helixi111 – 12212Combined sources
Beta strandi126 – 13510Combined sources
Beta strandi139 – 1457Combined sources
Beta strandi148 – 1547Combined sources
Helixi156 – 1605Combined sources
Helixi163 – 1653Combined sources
Turni166 – 1683Combined sources
Helixi170 – 1789Combined sources
Beta strandi180 – 1856Combined sources
Helixi186 – 1905Combined sources
Helixi193 – 20513Combined sources
Beta strandi209 – 2135Combined sources
Helixi217 – 2226Combined sources
Helixi224 – 2307Combined sources
Helixi231 – 2333Combined sources
Beta strandi235 – 2406Combined sources
Helixi241 – 25010Combined sources
Helixi258 – 2669Combined sources
Beta strandi278 – 2836Combined sources
Beta strandi286 – 2916Combined sources
Beta strandi296 – 2994Combined sources
Helixi312 – 32716Combined sources
Turni328 – 3303Combined sources
Helixi333 – 34715Combined sources
Beta strandi350 – 3534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX4X-ray1.50A22-362[»]
2I6AX-ray2.20A/B/C/D22-362[»]
2I6BX-ray2.30A/B22-362[»]
4O1LX-ray2.50A/B17-362[»]
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.
GeneTreeiENSGT00390000014320.
HOGENOMiHOG000172419.
HOVERGENiHBG002367.
InParanoidiP55263.
KOiK00856.
OMAiREDTIMA.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAAEEEPKP KKLKVEAPQA LRENILFGMG NPLLDISAVV DKDFLDKYSL
60 70 80 90 100
KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA
110 120 130 140 150
ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS
160 170 180 190 200
LIANLAAANC YKKEKHLDLE KNWMLVEKAR VCYIAGFFLT VSPESVLKVA
210 220 230 240 250
HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE
260 270 280 290 300
QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA
310 320 330 340 350
VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR
360
TGCTFPEKPD FH
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. Curated

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:
EMBLi
GenBanki
DDBJi
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]
uc010qlc.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX4X-ray1.50A22-362[»]
2I6AX-ray2.20A/B/C/D22-362[»]
2I6BX-ray2.30A/B22-362[»]
4O1LX-ray2.50A/B17-362[»]
ProteinModelPortaliP55263.
SMRiP55263. Positions 20-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106644. 5 interactions.
IntActiP55263. 3 interactions.
MINTiMINT-5001097.
STRINGi9606.ENSP00000286621.

Chemistry

BindingDBiP55263.
ChEMBLiCHEMBL3589.
DrugBankiDB01048. Abacavir.
DB00640. Adenosine.
DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.
DB00811. Ribavirin.
GuidetoPHARMACOLOGYi1231.

PTM databases

PhosphoSiteiP55263.

Polymorphism and mutation databases

BioMutaiADK.
DMDMi6840802.

2D gel databases

REPRODUCTION-2DPAGEIPI00234368.

Proteomic databases

MaxQBiP55263.
PaxDbiP55263.
PRIDEiP55263.

Protocols and materials databases

DNASUi132.
Structural Biology KnowledgebaseSearch...

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]
uc010qlc.2. human.

Organism-specific databases

CTDi132.
GeneCardsiGC10P075910.
HGNCiHGNC:257. ADK.
HPAiCAB032876.
HPA038391.
HPA038409.
MIMi102750. gene.
614300. phenotype.
neXtProtiNX_P55263.
Orphaneti289290. Hypermethioninemia encephalopathy due to adenosine kinase deficiency.
PharmGKBiPA24579.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0524.
GeneTreeiENSGT00390000014320.
HOGENOMiHOG000172419.
HOVERGENiHBG002367.
InParanoidiP55263.
KOiK00856.
OMAiREDTIMA.
OrthoDBiEOG7VMP5W.
PhylomeDBiP55263.
TreeFamiTF300745.

Enzyme and pathway databases

UniPathwayiUPA00588; UER00659.
BioCyciMetaCyc:HS08097-MONOMER.
BRENDAi2.7.1.20. 2681.
ReactomeiREACT_1923. Purine salvage.
SABIO-RKP55263.

Miscellaneous databases

ChiTaRSiADK. human.
EvolutionaryTraceiP55263.
GeneWikiiADK_(gene).
GenomeRNAii132.
NextBioi527.
PROiP55263.
SOURCEiSearch...

Gene expression databases

BgeeiP55263.
CleanExiHS_ADK.
GenevisibleiP55263. HS.

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]
ProtoNetiSearch...

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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "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.
  14. "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.
  15. "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: June 24, 2015
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.