Q9UIJ7 (KAD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTP:AMP phosphotransferase AK3, 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) [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	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)

Function	Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. Ref.1
Catalytic activity	NTP + AMP = NDP + ADP. Ref.1
Subunit structure	Monomer By similarity.
Subcellular location	Mitochondrion matrix Ref.1.
Tissue specificity	Highly expressed in heart, skeletal muscle and liver, moderately expressed in pancreas and kidney, and weakly expressed in placenta, brain and lung. Ref.1
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 GTP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis. HAMAP-Rule MF_03169
Sequence similarities	Belongs to the adenylate kinase family. AK3 subfamily.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	AMP metabolic process Inferred from direct assay Ref.1. Source: BHF-UCL GTP metabolic process Inferred from direct assay Ref.1. Source: BHF-UCL ITP metabolic process Inferred from direct assay Ref.1. Source: BHF-UCL UTP metabolic process Inferred from direct assay Ref.1. Source: BHF-UCL blood coagulation Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside triphosphate adenylate kinase activity Inferred from direct assay Ref.1. Source: BHF-UCL nucleotide kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UIJ7-1)

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: Q9UIJ7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-70: Missing.

Isoform 3 (identifier: Q9UIJ7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     51-90: 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 By similarity

Chain

2 – 227

226

GTP:AMP phosphotransferase AK3, mitochondrial HAMAP-Rule MF_03169

PRO_0000158922

Regions

Nucleotide binding

17 – 22

6

GTP By similarity

Nucleotide binding

64 – 66

3

AMP By similarity

Nucleotide binding

91 – 94

4

AMP By similarity

Nucleotide binding

137 – 138

2

GTP By similarity

Region

37 – 66

30

NMPbind HAMAP-Rule MF_03169

Region

127 – 164

38

LID HAMAP-Rule MF_03169

Sites

Binding site

38

1

AMP By similarity

Binding site

43

1

AMP By similarity

Binding site

98

1

AMP By similarity

Binding site

128

1

GTP By similarity

Binding site

161

1

AMP By similarity

Binding site

172

1

AMP By similarity

Binding site

201

1

GTP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

34

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

2 – 70

69

Missing in isoform 2.

VSP_043090

Alternative sequence

51 – 90

40

Missing in isoform 3.

VSP_044876

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

Sequence conflict

181

1

K → E in BAG60470. Ref.3

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)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: C7DA98633182FC79	FASTA	158	18,323
	10 20 30 40 50 60 MMTRLALHEL KNLTQYSWLL DGFPRTLPQA EALDRAYQID TVINLNVPFE VIKQRLTARW 70 80 90 100 110 120 IHPASGRVYN IEFNPPKTVG IDDLTGEPLI QREDDKPETV IKRLKAYEDQ TKPVLEYYQK 130 140 150 KGVLETFSGT ETNKIWPYVY AFLQTKVPQR SQKASVTP
	Isoform 3 [UniParc]. Checksum: 107B098298461090	FASTA	187	21,014
	10 20 30 40 50 60 MGASARLLRA VIMGAPGSGK GTVSSRITTH FELKHLSSGD LLRDNMLRGT GFPRTLPQAE 70 80 90 100 110 120 ALDRAYQIDT VINLNVPFEV IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ 130 140 150 160 170 180 REDDKPETVI KRLKAYEDQT KPVLEYYQKK GVLETFSGTE TNKIWPYVYA FLQTKVPQRS QKASVTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of human mitochondrial adenylate kinase targeted to the mitochondrial matrix." Noma T., Fujisawa K., Yamashiro Y., Shinohara M., Nakazawa A., Gondo T., Ishihara T., Yoshinobu K. Biochem. J. 358:225-232(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Liver.
[2]	"A novel gene expressed in human pheochromocytoma." Li Y., Peng Y., Jiang Z., Gu W., Han Z., Chen Z. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Pheochromocytoma.
[3]	"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; 2 AND 3). Tissue: Placenta.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[7]	"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].
[8]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB021870 mRNA. Translation: BAA87913.1.
AF183419 mRNA. Translation: AAG09688.1.
AK001553 mRNA. Translation: BAA91753.1.
AK001951 mRNA. Translation: BAA91996.1.
AK027534 mRNA. Translation: BAB55183.1.
AK098205 mRNA. Translation: BAG53592.1.
AK298200 mRNA. Translation: BAG60470.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41262.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72282.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41260.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72283.1.
CH471071 Genomic DNA. Translation: EAW58779.1.
CH471071 Genomic DNA. Translation: EAW58780.1.
CH471071 Genomic DNA. Translation: EAW58781.1.
BC013771 mRNA. Translation: AAH13771.1.

IPI

IPI00465256.
IPI00478236.
IPI00910240.

RefSeq

NP_001186781.1. NM_001199852.1.
NP_001186782.1. NM_001199853.1.
NP_001186784.1. NM_001199855.1.
NP_001186785.1. NM_001199856.1.
NP_057366.2. NM_016282.3.

UniGene

Hs.732022.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q9UIJ7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UIJ7. 1 interaction.

STRING

9606.ENSP00000371230.

PTM databases

PhosphoSite

Q9UIJ7.

Polymorphism databases

DMDM

23831297.

2D gel databases

OGP

Q9UIJ7.

REPRODUCTION-2DPAGE

IPI00465256.

UCD-2DPAGE

Q9UIJ7.

Proteomic databases

PaxDb

Q9UIJ7.

PRIDE

Q9UIJ7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359883; ENSP00000352948; ENSG00000147853.
ENST00000381809; ENSP00000371230; ENSG00000147853.
ENST00000447596; ENSP00000413933; ENSG00000147853.
ENST00000474822; ENSP00000439177; ENSG00000147853.

GeneID

50808.

KEGG

hsa:50808.

UCSC

uc003ziq.2. human.

Organism-specific databases

CTD

50808.

GeneCards

GC09M004703.

HGNC

HGNC:17376. AK3.

MIM

609290. gene.

neXtProt

NX_Q9UIJ7.

PharmGKB

PA164741184.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0563.

HOGENOM

HOG000238772.

HOVERGEN

HBG000458.

InParanoid

Q9UIJ7.

KO

K00944.

OMA

DKPETVT.

OrthoDB

EOG40VVQF.

PhylomeDB

Q9UIJ7.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9UIJ7.

Bgee

Q9UIJ7.

CleanEx

HS_AK3.
HS_AK3L1.

Genevestigator

Q9UIJ7.

GermOnline

ENSG00000147853. Homo sapiens.

Family and domain databases

HAMAP

MF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.

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.

SUPFAM

SSF57774. Adenylate_kinase_Znf_lid. 1 hit.

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AK3. human.

EvolutionaryTrace

Q9UIJ7.

GenomeRNAi

50808.

NextBio

53246.

SOURCE

Search...

Entry information

Entry name

KAD3_HUMAN

Accession

Primary (citable) accession number: Q9UIJ7
Secondary accession number(s): B4DP58 , D3DRI1, E7ET30, Q5VYW6, Q9H576, Q9HC01, Q9NPB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 125 of the entry and version 4 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.