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Q9UIJ7 (KAD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. HAMAP-Rule MF_03169

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 227226GTP:AMP phosphotransferase AK3, mitochondrial HAMAP-Rule MF_03169
PRO_0000158922

Regions

Nucleotide binding17 – 226GTP By similarity
Nucleotide binding64 – 663AMP By similarity
Nucleotide binding91 – 944AMP By similarity
Nucleotide binding137 – 1382GTP By similarity
Region37 – 6630NMPbind HAMAP-Rule MF_03169
Region127 – 16438LID HAMAP-Rule MF_03169

Sites

Binding site381AMP By similarity
Binding site431AMP By similarity
Binding site981AMP By similarity
Binding site1281GTP By similarity
Binding site1611AMP By similarity
Binding site1721AMP By similarity
Binding site2011GTP; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue201N6-succinyllysine By similarity
Modified residue341N6-acetyllysine By similarity
Modified residue571N6-succinyllysine By similarity
Modified residue641N6-acetyllysine; alternate By similarity
Modified residue641N6-succinyllysine; alternate By similarity
Modified residue801N6-acetyllysine; alternate By similarity
Modified residue801N6-succinyllysine; alternate By similarity
Modified residue1741N6-acetyllysine; alternate By similarity
Modified residue1741N6-succinyllysine; alternate By similarity
Modified residue1891N6-acetyllysine; alternate By similarity
Modified residue1891N6-succinyllysine; alternate By similarity
Modified residue2031N6-acetyllysine By similarity

Natural variations

Alternative sequence2 – 7069Missing in isoform 2.
VSP_043090
Alternative sequence51 – 9040Missing in isoform 3.
VSP_044876

Experimental info

Sequence conflict51A → G in BAA87913. Ref.1
Sequence conflict381S → R in BAA87913. Ref.1
Sequence conflict571K → Q in BAA87913. Ref.1
Sequence conflict69 – 713DVM → YVT in BAA87913. Ref.1
Sequence conflict1811K → E in BAG60470. Ref.3

Secondary structure

.................................... 227
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 98A0EDF4FD9C9CEF

FASTA22725,565
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C7DA98633182FC79
Show »

FASTA15818,323
Isoform 3 [UniParc].

Checksum: 107B098298461090
Show »

FASTA18721,014

References

« Hide '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. 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; 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. expand/collapse author list , 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. 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].
[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.
RefSeqNP_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.
UniGeneHs.732022.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZD8X-ray1.48A1-227[»]
ProteinModelPortalQ9UIJ7.
SMRQ9UIJ7. Positions 7-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119127. 4 interactions.
IntActQ9UIJ7. 1 interaction.
STRING9606.ENSP00000371230.

PTM databases

PhosphoSiteQ9UIJ7.

Polymorphism databases

DMDM23831297.

2D gel databases

OGPQ9UIJ7.
REPRODUCTION-2DPAGEIPI00465256.
UCD-2DPAGEQ9UIJ7.

Proteomic databases

PaxDbQ9UIJ7.
PRIDEQ9UIJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359883; ENSP00000352948; ENSG00000147853.
ENST00000381809; ENSP00000371230; ENSG00000147853. [Q9UIJ7-1]
ENST00000447596; ENSP00000413933; ENSG00000147853. [Q9UIJ7-3]
GeneID50808.
KEGGhsa:50808.
UCSCuc003ziq.2. human. [Q9UIJ7-1]

Organism-specific databases

CTD50808.
GeneCardsGC09M004703.
HGNCHGNC:17376. AK3.
MIM609290. gene.
neXtProtNX_Q9UIJ7.
PharmGKBPA164741184.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0563.
HOGENOMHOG000238772.
HOVERGENHBG000458.
InParanoidQ9UIJ7.
KOK00944.
OMANVPFQTI.
OrthoDBEOG74TX0R.
PhylomeDBQ9UIJ7.
TreeFamTF312916.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

BgeeQ9UIJ7.
CleanExHS_AK3.
HS_AK3L1.
GenevestigatorQ9UIJ7.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAK3. human.
EvolutionaryTraceQ9UIJ7.
GenomeRNAi50808.
NextBio53246.
PROQ9UIJ7.
SOURCESearch...

Entry information

Entry nameKAD3_HUMAN
AccessionPrimary (citable) accession number: Q9UIJ7
Secondary accession number(s): B4DP58 expand/collapse secondary AC list , D3DRI1, E7ET30, Q5VYW6, Q9H576, Q9HC01, Q9NPB4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 134 of the entry and version 4 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 chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM