Reviewed, UniProtKB/Swiss-Prot P54819 (KAD2_HUMAN)

Names and origin

Protein names

Recommended name:
    Adenylate kinase isoenzyme 2, mitochondrial
      Short name=AK 2
    EC=2.7.4.3
Alternative name(s):
    ATP-AMP transphosphorylase 2

Gene names

Name:	AK2
Synonyms:	ADK2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	This small ubiquitous enzyme is essential for maintenance and cell growth.
Catalytic activity	ATP + AMP = 2 ADP.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion intermembrane space.
Tissue specificity	Abundant in heart.
Sequence similarities	Belongs to the adenylate kinase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	mitochondrial intermembrane space Inferred from Experiment. Source: Reactome
Molecular function	adenylate kinase activity Ref.2 Traceable author statement. Source: ProtInc nucleoside kinase activity Inferred from Experiment. Source: Reactome
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P54819-1)

Also known as: AK2A;

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;

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:
     1-48: Missing.
     177-178: DD → GL
     179-239: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 239

238

Adenylate kinase isoenzyme 2, mitochondrial

Regions

Nucleotide binding

22 – 30

9

ATP By similarity

Amino acid modifications

Modified residue

93

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 48

48

Missing in isoform 4.

Alternative sequence

177 – 178

2

DD → GL in isoform 4.

Alternative sequence

178 – 239

62

DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3.

Alternative sequence

179 – 239

61

Missing in isoform 4.

Alternative sequence

232 – 239

8

CKDLVMFI → S in isoform 2.

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) [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) [UniParc]. Checksum: 64AEE1A97D81D401		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		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: C6FEB90B2BFF7845		130	14,709
	10 20 30 40 50 60 MLRAMVASGS ELGKKLKATM DAGKLVSDEM VVELIEKNLE TPLCKNGFLL DGFPRTVRQA 70 80 90 100 110 120 EMLDDLMEKR KEKLDSVIEF SIPDSLLIRR ITGRLIHPKS GRSYHEEFNP PKEPMKDDIT 130 GEPLIRRSGL

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: 8843353] [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: 9504408] [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: 9434148] [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]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta and Uterus.
[7]	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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
AL020995 Genomic DNA. Translation: CAI19352.1.
BC009405 mRNA. Translation: AAH09405.1.
BC070127 mRNA. Translation: AAH70127.1.

PIR

G02248.
JC5893.

RefSeq

NP_001616.1.

UniGene

Hs.470907

3D structure databases

PDBMSD

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

ModBase

Search...

2-D gel databases

OGP

P54819.

REPRODUCTION-2DPAGE

IPI00218988.

Genome annotation databases

Ensembl

ENSG00000004455. Homo sapiens. [Contig view]

GeneID

204.

KEGG

hsa:204.

Organism-specific databases

H-InvDB

HIX0000387.

HGNC

HGNC:362. AK2.

MIM

103020. gene.

PharmGKB

PA24656.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P54819.

HOVERGEN

P54819.

Enzyme and pathway databases

Reactome

REACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpress

P54819.

CleanEx

HS_AK2.

GermOnline

ENSG00000004455. Homo sapiens.

Family and domain databases

InterPro

IPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_Znf_lid.
[Graphical view]

PANTHER

PTHR23359. Adenylate_kin. 1 hit.

Pfam

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

PRINTS

PR00094. ADENYLTKNASE.

ProDom

PD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

LinkHub

P54819.

SOURCE

Search...

ProtoNet

Search...

Entry information

Entry name

KAD2_HUMAN

Accession

Primary (citable) accession number: P54819
Secondary accession number(s): Q16856 , Q5TIF7, Q8TCY2, Q8TCY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	September 23, 2008
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)