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P55263 (ADK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Adenosine kinase

Short name=AK
EC=2.7.1.20
Alternative name(s):
Adenosine 5'-phosphotransferase
Gene names
Name:ADK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

ATP + adenosine = ADP + AMP.

Cofactor

Binds 3 magnesium ions per subunit.

Pathway

Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenosine: step 1/1.

Subunit structure

Monomer.

Subcellular location

Isoform 1: Nucleus Ref.9.

Isoform 2: Cytoplasm Ref.9.

Tissue specificity

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

Involvement in disease

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. Ref.14

Sequence similarities

Belongs to the carbohydrate kinase PfkB family.

Sequence caution

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

Ontologies

Keywords
   Biological processPurine salvage
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processAMP salvage

Inferred from electronic annotation. Source: UniProtKB-UniPathway

adenosine metabolic process

Inferred from electronic annotation. Source: Ensembl

circadian regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

dATP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside salvage

Inferred from electronic annotation. Source: UniProtKB-KW

purine-containing compound salvage

Traceable author statement. Source: Reactome

ribonucleoside monophosphate biosynthetic process

Traceable author statement Ref.3. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

type B pancreatic cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenosine kinase activity

Inferred from experiment. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphotransferase activity, alcohol group as acceptor

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55263-1)

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.
Isoform 2 (identifier: P55263-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MAAAEEEPKPKKLKVEAPQAL → MTSV
Isoform 3 (identifier: P55263-3)

The sequence of this isoform differs from the canonical sequence as follows:
     186-242: Missing.
Isoform 4 (identifier: P55263-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MAAAEEEPKP...ILAEDKHKEL → MTSVRENILFGMGNPLLDISAVVDKDFLDK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 362361Adenosine kinase
PRO_0000080053

Regions

Motif8 – 169Nuclear localization signal Ref.9

Sites

Active site3171
Metal binding491Magnesium 1
Metal binding1471Magnesium 2
Metal binding1481Magnesium 2

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11
Modified residue771Phosphotyrosine Ref.13

Natural variations

Alternative sequence1 – 6565MAAAE…KHKEL → MTSVRENILFGMGNPLLDIS AVVDKDFLDK in isoform 4.
VSP_004668
Alternative sequence1 – 2121MAAAE…APQAL → MTSV in isoform 2.
VSP_046713
Alternative sequence186 – 24257Missing in isoform 3.
VSP_043526
Natural variant301G → E in HMAKD; the mutant shows some residual activity. Ref.14
VAR_066640
Natural variant2351D → A in HMAKD; the mutant shows some residual activity. Ref.14
VAR_066641
Natural variant3181A → E in HMAKD; complete loss of activity. Ref.14
VAR_066642

Experimental info

Mutagenesis11 – 122KK → AA or AD: Abolishes nuclear localization. Ref.9
Sequence conflict981H → A AA sequence Ref.1
Sequence conflict1331N → D in AAB01689. Ref.2
Sequence conflict1711K → R in AAB01689. Ref.2
Sequence conflict1901T → H in AAA97893. Ref.1
Sequence conflict2191I → F in AAH03568. Ref.7
Sequence conflict2731S → V AA sequence Ref.1
Sequence conflict2891I → N AA sequence Ref.1
Sequence conflict3071K → R in AAB01689. Ref.2

Secondary structure

................................................................ 362
Helix Strand Turn

Details...

Sequences

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

Last modified May 30, 2000. Version 2.
Checksum: 48AA4925865BFE70

FASTA36240,545
        10         20         30         40         50         60 
MAAAEEEPKP KKLKVEAPQA LRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED 

        70         80         90        100        110        120 
KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA 

       130        140        150        160        170        180 
AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR 

       190        200        210        220        230        240 
VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN 

       250        260        270        280        290        300 
ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA 

       310        320        330        340        350        360 
VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD 


FH 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 7DC20F364E63D944
Show »

FASTA34538,703
Isoform 3 [UniParc].

Checksum: DC7E0245659B0F06
Show »

FASTA30534,084
Isoform 4 [UniParc].

Checksum: E5A9FDBDB77E7357
Show »

FASTA32736,580

References

« Hide 'large scale' references
[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]"Cloning and expression of the adenosine kinase gene from rat and human tissues."
McNally T., Helfrich R.J., Cowart M., Dorwin S.A., Meuth J.L., Idler K.B., Klute K.A., Simmer R.L., Kowaluk E.A., Halbert D.N.
Biochem. Biophys. Res. Commun. 231:645-650(1997) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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
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]"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].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC5363.
JC5364.
RefSeqNP_001114.2. NM_001123.3.
NP_001189378.1. NM_001202449.1.
NP_001189379.1. NM_001202450.1.
NP_006712.2. NM_006721.3.
UniGeneHs.656586.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX4X-ray1.50A22-362[»]
2I6AX-ray2.20A/B/C/D22-362[»]
2I6BX-ray2.30A/B22-362[»]
ProteinModelPortalP55263.
SMRP55263. Positions 20-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106644. 3 interactions.
IntActP55263. 3 interactions.
MINTMINT-5001097.
STRING9606.ENSP00000286621.

Chemistry

BindingDBP55263.
ChEMBLCHEMBL3589.
DrugBankDB00640. Adenosine.
DB00131. Adenosine monophosphate.
DB00171. Adenosine triphosphate.
DB00061. Pegademase bovine.
DB00811. Ribavirin.
GuidetoPHARMACOLOGY1231.

PTM databases

PhosphoSiteP55263.

Polymorphism databases

DMDM6840802.

2D gel databases

REPRODUCTION-2DPAGEIPI00234368.

Proteomic databases

PaxDbP55263.
PRIDEP55263.

Protocols and materials databases

DNASU132.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286621; ENSP00000286621; ENSG00000156110. [P55263-1]
ENST00000372734; ENSP00000361819; ENSG00000156110. [P55263-2]
ENST00000539909; ENSP00000443965; ENSG00000156110. [P55263-3]
ENST00000541550; ENSP00000438321; ENSG00000156110. [P55263-4]
GeneID132.
KEGGhsa:132.
UCSCuc001jwi.3. human. [P55263-1]
uc010qlb.2. human. [P55263-3]

Organism-specific databases

CTD132.
GeneCardsGC10P075910.
HGNCHGNC:257. ADK.
HPAHPA038409.
MIM102750. gene.
614300. phenotype.
neXtProtNX_P55263.
Orphanet289290. Hypermethioninemia encephalopathy due to adenosine kinase deficiency.
PharmGKBPA24579.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0524.
HOGENOMHOG000172419.
HOVERGENHBG002367.
InParanoidP55263.
KOK00856.
OMACITGGNR.
OrthoDBEOG7VMP5W.
PhylomeDBP55263.
TreeFamTF300745.

Enzyme and pathway databases

BioCycMetaCyc:HS08097-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP55263.
UniPathwayUPA00588; UER00659.

Gene expression databases

ArrayExpressP55263.
BgeeP55263.
CleanExHS_ADK.
GenevestigatorP55263.

Family and domain databases

InterProIPR001805. Adenokinase.
IPR002173. Carboh/pur_kinase_PfkB_CS.
IPR011611. PfkB_dom.
[Graphical view]
PANTHERPTHR10584:SF24. PTHR10584:SF24. 1 hit.
PfamPF00294. PfkB. 1 hit.
[Graphical view]
PRINTSPR00989. ADENOKINASE.
PROSITEPS00584. PFKB_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADK. human.
EvolutionaryTraceP55263.
GeneWikiADK_(gene).
GenomeRNAi132.
NextBio527.
PROP55263.
SOURCESearch...

Entry information

Entry nameADK_HUMAN
AccessionPrimary (citable) accession number: P55263
Secondary accession number(s): B7Z783 expand/collapse secondary AC list , B7Z800, O00741, O00742, Q16710, Q5JQ10, Q5JQ11, Q9BTN2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 154 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM