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P54819 (KAD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Adenylate kinase 2, mitochondrial

Short name=AK 2
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase 2
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Gene names
Name:AK2
Synonyms:ADK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. Ref.16

Catalytic activity

ATP + AMP = 2 ADP. HAMAP-Rule MF_03168

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03168

Subcellular location

Mitochondrion intermembrane space HAMAP-Rule MF_03168.

Tissue specificity

Present in most tissues. Present at high level in heart, liver and kidney, and at low level in brain, skeletal muscle and skin. Present in thrombocytes but not in erythrocytes, which lack mitochondria. Present in all nucleated cell populations from blood, while AK1 is mostly absent. In spleen and lymph nodes, mononuclear cells lack AK1, whereas AK2 is readily detectable. These results indicate that leukocytes may be susceptible to defects caused by the lack of AK2, as they do not express AK1 in sufficient amounts to compensate for the AK2 functional deficits (at protein level). Ref.15

Domain

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. HAMAP-Rule MF_03168

Involvement in disease

Reticular dysgenesis (RDYS) [MIM:267500]: Most severe form of inborn severe combined immunodeficiencies (SCID) and is characterized by absence of granulocytes and almost complete deficiency of lymphocytes in peripheral blood, hypoplasia of the thymus and secondary lymphoid organs, and lack of innate and adaptive humoral and cellular immune functions, leading to fatal septicemia within days after birth. In bone marrow of individuals with reticular dysgenesis, myeloid differentiation is blocked at the promyelocytic stage, whereas erythro- and megakaryocytic maturation is generally normal. In addition, affected newborns have bilateral sensorineural deafness. Defects may be due to its absence in leukocytes and inner ear, in which its absence can not be compensated by AK1.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16

Sequence similarities

Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processADP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

AMP metabolic process

Inferred from electronic annotation. Source: Ensembl

ATP metabolic process

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

dATP metabolic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleotide phosphorylation

Traceable author statement Ref.2. Source: GOC

oxidative phosphorylation

Inferred from electronic annotation. Source: Ensembl

response to thyroid hormone

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

sperm mitochondrial sheath

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54819-1)

Also known as: AK2A; AK2isoA;

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: P54819-2)

Also known as: AK2B; AK2isoB;

The sequence of this isoform differs from the canonical sequence as follows:
     232-239: CKDLVMFI → S
Isoform 3 (identifier: P54819-3)

Also known as: AK2C;

The sequence of this isoform differs from the canonical sequence as follows:
     178-239: DNEKALKIRL...ATCKDLVMFI → IGQAKRSFLRLAKISFDVLIKKALA
Isoform 4 (identifier: P54819-4)

Also known as: AK2D;

The sequence of this isoform differs from the canonical sequence as follows:
     2-48: Missing.
     177-178: DD → GL
     179-239: Missing.
Isoform 5 (identifier: P54819-5)

The sequence of this isoform differs from the canonical sequence as follows:
     135-142: Missing.
     232-239: CKDLVMFI → S
Note: No experimental confirmation available.
Isoform 6 (identifier: P54819-6)

The sequence of this isoform differs from the canonical sequence as follows:
     2-48: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239Adenylate kinase 2, mitochondrial HAMAP-Rule MF_03168
PRO_0000423212
Initiator methionine11Removed; alternate Ref.10
Chain2 – 239238Adenylate kinase 2, mitochondrial, N-terminally processed HAMAP-Rule MF_03168
PRO_0000158917

Regions

Nucleotide binding25 – 306ATP HAMAP-Rule MF_03168
Nucleotide binding72 – 743AMP By similarity
Nucleotide binding100 – 1034AMP By similarity
Nucleotide binding151 – 1522ATP HAMAP-Rule MF_03168
Region45 – 7430NMPbind HAMAP-Rule MF_03168
Region141 – 17838LID HAMAP-Rule MF_03168

Sites

Binding site461AMP By similarity
Binding site511AMP By similarity
Binding site1071AMP By similarity
Binding site1381ATP
Binding site1421ATP By similarity
Binding site1751AMP
Binding site1861AMP By similarity
Binding site2141ATP; via carbonyl oxygen

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.13
Modified residue621N6-succinyllysine By similarity
Modified residue931N6-succinyllysine By similarity
Modified residue1811N6-acetyllysine By similarity
Disulfide bond42 ↔ 92 Ref.14

Natural variations

Alternative sequence2 – 4847Missing in isoform 4 and isoform 6.
VSP_002792
Alternative sequence135 – 1428Missing in isoform 5.
VSP_036503
Alternative sequence177 – 1782DD → GL in isoform 4.
VSP_002793
Alternative sequence178 – 23962DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3.
VSP_002791
Alternative sequence179 – 23961Missing in isoform 4.
VSP_002794
Alternative sequence232 – 2398CKDLVMFI → S in isoform 2 and isoform 5.
VSP_002790
Natural variant1031R → W in RDYS. Ref.16
VAR_054630
Natural variant1651D → G in RDYS. Ref.16
VAR_054631
Natural variant2091A → T.
Corresponds to variant rs12116440 [ dbSNP | Ensembl ].
VAR_050032

Secondary structure

................................... 239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AK2A) (AK2isoA) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 86FA94F9EE33629F

FASTA23926,478
        10         20         30         40         50         60 
MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML RAMVASGSEL 

        70         80         90        100        110        120 
GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE 

       130        140        150        160        170        180 
KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE 

       190        200        210        220        230 
KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI 

« Hide

Isoform 2 (AK2B) (AK2isoB) [UniParc].

Checksum: 64AEE1A97D81D401
Show »

FASTA23225,615
Isoform 3 (AK2C) [UniParc].

Checksum: AE7593A8ADBD00CF
Show »

FASTA20222,265
Isoform 4 (AK2D) [UniParc].

Checksum: 99C780C24D0F7845
Show »

FASTA13114,840
Isoform 5 [UniParc].

Checksum: 1A769D71DDBB0B8A
Show »

FASTA22424,648
Isoform 6 [UniParc].

Checksum: 599AC964FCA56E89
Show »

FASTA19221,767

References

« Hide 'large scale' references
[1]"Cloning and characterization of cDNA for human adenylate kinase 2A."
Lee Y., Kim J.W., Lee I.A., Kang H.B., Choe Y.K., Lee H.G., Lim J.S., Kim H.J., Park C., Choe I.S.
Biochem. Mol. Biol. Int. 39:833-842(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Cloning and expression of human adenylate kinase 2 isozymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues."
Lee Y., Kim J.W., Lee S.M., Kim H.J., Lee K.S., Park C., Choe I.S.
J. Biochem. 123:47-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[3]"cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2."
Noma T., Song S., Yoon Y.-S., Tanaka S., Nakazawa A.
Biochim. Biophys. Acta 1395:34-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[4]"Novel isoforms of human adenylate kinase 2."
Guo J.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[5]"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 1; 5 AND 6).
Tissue: Brain, Placenta and Tongue.
[6]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Placenta and Uterus.
[10]Bienvenut W.V., Heiserich L., Gottlieb E.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14; 18-34; 73-85; 94-103; 107-117 AND 120-138, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[11]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of human adenylate kinase 2."
Bunkoczi G., Filippakopoulos P., Debreczeni J.E., Turnbull A., Papagrigoriou E., Savitsky P., Colebrook S., Von Delft F., Arrowsmith C., Edwards A., Sundstrom M., Weigelt J., Knapp S.
Submitted (JAN-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP4A, DISULFIDE BOND.
[15]"Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2."
Pannicke U., Hoenig M., Hess I., Friesen C., Holzmann K., Rump E.-M., Barth T.F., Rojewski M.T., Schulz A., Boehm T., Friedrich W., Schwarz K.
Nat. Genet. 41:101-105(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RDYS, TISSUE SPECIFICITY.
[16]"Human adenylate kinase 2 deficiency causes a profound hematopoietic defect associated with sensorineural deafness."
Lagresle-Peyrou C., Six E.M., Picard C., Rieux-Laucat F., Michel V., Ditadi A., Chappedelaine C.D., Morillon E., Valensi F., Simon-Stoos K.L., Mullikin J.C., Noroski L.M., Besse C., Wulffraat N.M., Ferster A., Abecasis M.M., Calvo F., Petit C. expand/collapse author list , Candotti F., Abel L., Fischer A., Cavazzana-Calvo M.
Nat. Genet. 41:106-111(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RDYS TRP-103 AND GLY-165, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39945 mRNA. Translation: AAC52061.1.
U84371 mRNA. Translation: AAB41790.1.
U54645 mRNA. Translation: AAC13881.1.
AB005621 mRNA. Translation: BAC16747.1.
AB005622 mRNA. Translation: BAC16748.1.
AY080899 mRNA. Translation: AAL87027.1.
AY080900 mRNA. Translation: AAL87028.1.
AK291676 mRNA. Translation: BAF84365.1.
AK295105 mRNA. Translation: BAG58139.1.
AK296863 mRNA. Translation: BAG59426.1.
AB451267 mRNA. Translation: BAG70081.1.
AB451394 mRNA. Translation: BAG70208.1.
AL020995 Genomic DNA. Translation: CAI19351.1.
AL020995 Genomic DNA. Translation: CAI19352.1.
CH471059 Genomic DNA. Translation: EAX07484.1.
CH471059 Genomic DNA. Translation: EAX07486.1.
BC009405 mRNA. Translation: AAH09405.1.
BC070127 mRNA. Translation: AAH70127.1.
BC090040 mRNA. Translation: AAH90040.1.
PIRG02248.
JC5893.
RefSeqNP_001186128.1. NM_001199199.1.
NP_001616.1. NM_001625.3.
NP_037543.1. NM_013411.4.
UniGeneHs.470907.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9YX-ray2.10A1-239[»]
ProteinModelPortalP54819.
SMRP54819. Positions 15-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106707. 16 interactions.
IntActP54819. 4 interactions.

Chemistry

BindingDBP54819.
ChEMBLCHEMBL4938.

PTM databases

PhosphoSiteP54819.

Polymorphism databases

DMDM1708596.

2D gel databases

OGPP54819.
REPRODUCTION-2DPAGEIPI00218988.
UCD-2DPAGEP54819.

Proteomic databases

PaxDbP54819.
PRIDEP54819.

Protocols and materials databases

DNASU204.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354858; ENSP00000346921; ENSG00000004455. [P54819-1]
ENST00000373449; ENSP00000362548; ENSG00000004455. [P54819-2]
GeneID204.
KEGGhsa:204.
UCSCuc001bwo.2. human. [P54819-2]
uc001bwp.2. human. [P54819-1]
uc010ohq.2. human. [P54819-5]

Organism-specific databases

CTD204.
GeneCardsGC01M033476.
HGNCHGNC:362. AK2.
HPAHPA018479.
MIM103020. gene.
267500. phenotype.
neXtProtNX_P54819.
Orphanet33355. Reticular dysgenesis.
PharmGKBPA24656.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0563.
HOVERGENHBG000458.
InParanoidP54819.
KOK00939.
OMALENNKAC.
OrthoDBEOG74TX0R.
PhylomeDBP54819.
TreeFamTF300896.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP54819.
BgeeP54819.
CleanExHS_AK2.
GenevestigatorP54819.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54819.
GeneWikiAK2.
GenomeRNAi204.
NextBio812.
PROP54819.
SOURCESearch...

Entry information

Entry nameKAD2_HUMAN
AccessionPrimary (citable) accession number: P54819
Secondary accession number(s): A8K6L1 expand/collapse secondary AC list , B4DHH7, B4DL64, Q16856, Q5EB54, Q5TIF7, Q8TCY2, Q8TCY3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 148 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM