P54819 (KAD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	239 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14
Catalytic activity	ATP + AMP = 2 ADP. HAMAP-Rule MF_03168
Subunit structure	Monomer By similarity.
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.13
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.13 Ref.14
Sequence similarities	Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ADP biosynthetic process Inferred from electronic annotation. Source: Compara AMP metabolic process Inferred from electronic annotation. Source: Compara ATP metabolic process Inferred from electronic annotation. Source: Compara brain development Inferred from electronic annotation. Source: Compara dATP metabolic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara nucleobase-containing small molecule interconversion Traceable author statement. Source: Reactome oxidative phosphorylation Inferred from electronic annotation. Source: Compara response to thyroid hormone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial intermembrane space Traceable author statement. Source: Reactome sperm mitochondrial sheath Inferred from electronic annotation. Source: Compara
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.10

Chain

2 – 239

238

Adenylate kinase 2, mitochondrial HAMAP-Rule MF_03168

PRO_0000158917

Regions

Nucleotide binding

25 – 30

6

ATP HAMAP-Rule MF_03168

Nucleotide binding

72 – 74

3

AMP By similarity

Nucleotide binding

100 – 103

4

AMP By similarity

Nucleotide binding

151 – 152

2

ATP HAMAP-Rule MF_03168

Region

45 – 74

30

NMPbind HAMAP-Rule MF_03168

Region

141 – 178

38

LID HAMAP-Rule MF_03168

Sites

Binding site

46

1

AMP By similarity

Binding site

51

1

AMP By similarity

Binding site

107

1

AMP By similarity

Binding site

138

1

ATP

Binding site

142

1

ATP By similarity

Binding site

175

1

AMP

Binding site

186

1

AMP By similarity

Binding site

214

1

ATP; via carbonyl oxygen

Amino acid modifications

Modified residue

93

1

N6-acetyllysine By similarity

Disulfide bond

42 ↔ 92

Ref.12

Natural variations

Alternative sequence

2 – 48

47

Missing in isoform 4 and isoform 6.

VSP_002792

Alternative sequence

135 – 142

8

Missing in isoform 5.

VSP_036503

Alternative sequence

177 – 178

2

DD → GL in isoform 4.

VSP_002793

Alternative sequence

178 – 239

62

DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3.

VSP_002791

Alternative sequence

179 – 239

61

Missing in isoform 4.

VSP_002794

Alternative sequence

232 – 239

8

CKDLVMFI → S in isoform 2 and isoform 5.

VSP_002790

Natural variant

103

1

R → W in RDYS. Ref.14

VAR_054630

Natural variant

165

1

D → G in RDYS. Ref.14

VAR_054631

Natural variant

209

1

A → T.
Corresponds to variant rs12116440 [ dbSNP | Ensembl ].

VAR_050032

Secondary structure

1

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239

Helix Strand Turn

Details...

Beta strand

16 – 21

6

Helix

28 – 39

12

Beta strand

42 – 45

4

Helix

46 – 56

11

Helix

59 – 69

11

Helix

76 – 87

12

Helix

90 – 92

3

Beta strand

95 – 100

6

Helix

105 – 117

13

Beta strand

124 – 129

6

Helix

132 – 140

9

Turn

146 – 148

3

Beta strand

151 – 153

3

Turn

154 – 156

3

Beta strand

166 – 168

3

Helix

180 – 203

24

Beta strand

207 – 211

5

Helix

216 – 230

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (AK2A) (AK2isoA) [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 86FA94F9EE33629F	FASTA	239	26,478
	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
	Isoform 2 (AK2B) (AK2isoB) [UniParc]. Checksum: 64AEE1A97D81D401	FASTA	232	25,615
	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 TS
	Isoform 3 (AK2C) [UniParc]. Checksum: AE7593A8ADBD00CF	FASTA	202	22,265
	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 PLIRRSDIGQ 190 200 AKRSFLRLAK ISFDVLIKKA LA
	Isoform 4 (AK2D) [UniParc]. Checksum: 99C780C24D0F7845	FASTA	131	14,840
	10 20 30 40 50 60 MMLRAMVASG SELGKKLKAT MDAGKLVSDE MVVELIEKNL ETPLCKNGFL LDGFPRTVRQ 70 80 90 100 110 120 AEMLDDLMEK RKEKLDSVIE FSIPDSLLIR RITGRLIHPK SGRSYHEEFN PPKEPMKDDI 130 TGEPLIRRSG L
	Isoform 5 [UniParc]. Checksum: 1A769D71DDBB0B8A	FASTA	224	24,648
	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 PDSLLIHPKS GRSYHEEFNP PKEPMKDDIT GEPLIRRSDD NEKALKIRLQ 190 200 210 220 AYHTQTTPLI EYYRKRGIHS AIDASQTPDV VFASILAAFS KATS
	Isoform 6 [UniParc]. Checksum: 599AC964FCA56E89	FASTA	192	21,767
	10 20 30 40 50 60 MMLRAMVASG SELGKKLKAT MDAGKLVSDE MVVELIEKNL ETPLCKNGFL LDGFPRTVRQ 70 80 90 100 110 120 AEMLDDLMEK RKEKLDSVIE FSIPDSLLIR RITGRLIHPK SGRSYHEEFN PPKEPMKDDI 130 140 150 160 170 180 TGEPLIRRSD DNEKALKIRL QAYHTQTTPL IEYYRKRGIH SAIDASQTPD VVFASILAAF 190 SKATCKDLVM FI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[11]	"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].
[12]	"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.
[13]	"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.
[14]	"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. , 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.

IPI

IPI00172460.
IPI00215901.
IPI00218988.
IPI00218989.
IPI00921960.
IPI00922165.

PIR

G02248.
JC5893.

RefSeq

NP_001186128.1. NM_001199199.1.
NP_001616.1. NM_001625.3.
NP_037543.1. NM_013411.4.

UniGene

Hs.470907.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C9Y	X-ray	2.10	A	1-239	[»]

ProteinModelPortal

P54819.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54819. 4 interactions.

PTM databases

PhosphoSite

P54819.

Polymorphism databases

DMDM

1708596.

2D gel databases

OGP

P54819.

REPRODUCTION-2DPAGE

IPI00218988.

UCD-2DPAGE

P54819.

Proteomic databases

PaxDb

P54819.

PRIDE

P54819.

Protocols and materials databases

DNASU

204.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354858; ENSP00000346921; ENSG00000004455.
ENST00000373449; ENSP00000362548; ENSG00000004455.

GeneID

204.

KEGG

hsa:204.

UCSC

uc001bwo.2. human.
uc001bwp.2. human.
uc010ohq.2. human.

Organism-specific databases

CTD

204.

GeneCards

GC01M033474.

HGNC

HGNC:362. AK2.

HPA

HPA018479.

MIM

103020. gene.
267500. phenotype.

neXtProt

NX_P54819.

PharmGKB

PA24656.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0563.

HOVERGEN

HBG000458.

InParanoid

P54819.

KO

K00939.

OMA

QADAMKD.

PhylomeDB

P54819.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P54819.

Bgee

P54819.

CleanEx

HS_AK2.

Genevestigator

P54819.

GermOnline

ENSG00000004455. Homo sapiens.

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.

InterPro

IPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]

PANTHER

PTHR23359. PTHR23359. 1 hit.

Pfam

PF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P54819.

ChEMBL

CHEMBL4938.

EvolutionaryTrace

P54819.

GenomeRNAi

204.

NextBio

812.

SOURCE

Search...

Entry information

Entry name

KAD2_HUMAN

Accession

Primary (citable) accession number: P54819
Secondary accession number(s): A8K6L1 , 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:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.