Reviewed, UniProtKB/Swiss-Prot Q9UIJ7 (KAD3_HUMAN)

Names and origin

Protein names

Recommended name:
    GTP:AMP phosphotransferase mitochondrial
    EC=2.7.4.10
Alternative name(s):
    Adenylate kinase 3
      Short name=AK 3
    Adenylate kinase 3 alpha-like 1

Gene names

Name:	AK3
Synonyms:	AK3L1, AK6, AKL3L

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	227 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)

Catalytic activity	NTP + AMP = NDP + ADP.
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the adenylate kinase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	GTP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from electronic annotation. Source: InterPro nucleoside triphosphate adenylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 227

226

GTP:AMP phosphotransferase mitochondrial

PRO_0000158922

Regions

Nucleotide binding

14 – 22

9

GTP By similarity

Nucleotide binding

91 – 98

8

AMP By similarity

Sites

Binding site

38

1

AMP By similarity

Amino acid modifications

Modified residue

34

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

5

1

A → G in BAA87913. Ref.1

Sequence conflict

38

1

S → R in BAA87913. Ref.1

Sequence conflict

57

1

K → Q in BAA87913. Ref.1

Sequence conflict

69 – 71

3

DVM → YVT in BAA87913. Ref.1

Secondary structure

1

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227

Helix Strand Turn

Details...

Beta strand

9 – 14

6

Helix

20 – 30

11

Beta strand

31 – 37

7

Helix

38 – 48

11

Helix

51 – 60

10

Turn

61 – 63

3

Helix

68 – 80

13

Beta strand

87 – 91

5

Helix

96 – 103

8

Beta strand

110 – 115

6

Helix

118 – 125

8

Beta strand

128 – 131

4

Turn

132 – 135

4

Beta strand

136 – 139

4

Turn

140 – 142

3

Turn

152 – 154

3

Helix

162 – 164

3

Helix

166 – 189

24

Beta strand

193 – 197

5

Helix

201 – 212

12

Turn

213 – 215

3

Sequences

	Sequence		Length	Mass (Da)
	Q9UIJ7-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 98A0EDF4FD9C9CEF	FASTA	227	25,565
	10 20 30 40 50 60 MGASARLLRA VIMGAPGSGK GTVSSRITTH FELKHLSSGD LLRDNMLRGT EIGVLAKAFI 70 80 90 100 110 120 DQGKLIPDDV MTRLALHELK NLTQYSWLLD GFPRTLPQAE ALDRAYQIDT VINLNVPFEV 130 140 150 160 170 180 IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ REDDKPETVI KRLKAYEDQT 190 200 210 220 KPVLEYYQKK GVLETFSGTE TNKIWPYVYA FLQTKVPQRS QKASVTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Noma T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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]. Tissue: Lymph.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Structure of human adenylate kinase 3-like 1." Structural genomics consortium (SGC) Submitted (MAY-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AB021870 mRNA. Translation: BAA87913.1.
AK001553 mRNA. Translation: BAA91753.1.
AK001951 mRNA. Translation: BAA91996.1.
AK027534 mRNA. Translation: BAB55183.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41262.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72283.1.
BC013771 mRNA. Translation: AAH13771.1.

IPI

IPI00465256.

RefSeq

NP_057366.2.

UniGene

Hs.493362

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZD8	X-ray	1.48	A	1-227	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9UIJ7.

2-D gel databases

OGP

Q9UIJ7.

REPRODUCTION-2DPAGE

IPI00465256.

Proteomic databases

PRIDE

Q9UIJ7.

Genome annotation databases

Ensembl

ENSG00000147853. Homo sapiens. [Contig view]

GeneID

50808.

KEGG

hsa:50808.

NMPDR

fig|9606.3.peg.30995.

Organism-specific databases

GeneCards

GC09M004703.

HGNC

HGNC:17376. AK3.

MIM

609290. gene.

PharmGKB

PA24657.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9UIJ7.

HOVERGEN

Q9UIJ7.

OMA

Q9UIJ7. NPPKTVG.

Enzyme and pathway databases

BRENDA

2.7.4.10. 247.

Gene expression databases

ArrayExpress

Q9UIJ7.

Bgee

Q9UIJ7.

CleanEx

HS_AK3.
HS_AK3L1.

GermOnline

ENSG00000147853. 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]

ProtoNet

Search...

Other Resources

NextBio

53246.

SOURCE

Search...

Entry information

Entry name

KAD3_HUMAN

Accession

Primary (citable) accession number: Q9UIJ7
Secondary accession number(s): Q5VYW6, Q9H576, Q9NPB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 85 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)