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Reviewed, UniProtKB/Swiss-Prot Q9WTP7 (KAD3_MOUSE)

Last modified November 3, 2009. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: Ak3l, Ak3l1, Akl3l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 227226GTP:AMP phosphotransferase mitochondrial
PRO_0000158923

Regions

Nucleotide binding14 – 229GTP By similarity
Nucleotide binding91 – 988AMP By similarity

Sites

Binding site381AMP By similarity

Amino acid modifications

Modified residue341N6-acetyllysine Ref.4

Experimental info

Sequence conflict1711K → E in BAB23625. Ref.1
Sequence conflict2021N → D in BAB23876. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WTP7-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6601DF10971DE5AC

FASTA22725,426
        10         20         30         40         50         60 
MGASGRLLRA VIMGAPGSGK GTVSSRITKH FELKHLSSGD LLRQNMLQGT EIGVLAKTFI 

        70         80         90        100        110        120 
DQGKLIPDDV MTRLALHELK TLTQCSWLLD GFPRTLPQAE ALDKVYQIDT VINLNVPFEV 

       130        140        150        160        170        180 
IKQRLTARWI HPASGRVYNI EFNPPKTVGI DDLTGEPLIQ REDDKPETVI KRLKAYEAQT 

       190        200        210        220 
EPVLQYYQKK GVLETFSGTE TNKIWPHVYS FLQTKVPETT QKASVTP 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Amnion, Bone marrow, Cerebellum, Eye, Liver, Stomach, Testis and Thymus.
[2]"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: Colon and Mammary gland.
[3]Noma T.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-227.
[4]"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK004864 mRNA. Translation: BAB23625.1.
AK005194 mRNA. Translation: BAB23876.1.
AK008681 mRNA. Translation: BAB25829.1.
AK031631 mRNA. Translation: BAC27488.1.
AK053644 mRNA. Translation: BAC35459.1.
AK089027 mRNA. Translation: BAC40707.1.
AK147060 mRNA. Translation: BAE27644.1.
AK149996 mRNA. Translation: BAE29224.1.
BC016432 mRNA. Translation: AAH16432.1.
BC019174 mRNA. Translation: AAH19174.1.
BC024871 mRNA. Translation: AAH24871.1.
BC058191 mRNA. Translation: AAH58191.1.
AB020203 mRNA. Translation: BAA77360.1.
IPIIPI00221769.
RefSeqNP_067274.1.
UniGeneMm.196067

3D structure databases

HSSPHSSP built from PDB template 2AK3 based on UniProtKB P08760.
SMRQ9WTP7. Positions 2-227.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9WTP7.

PTM databases

PhosphoSiteQ9WTP7.

Proteomic databases

PRIDEQ9WTP7.

Genome annotation databases

EnsemblENSMUST00000025696; ENSMUSP00000025696; ENSMUSG00000024782; Mus musculus. [Genome view]
GeneID56248.
KEGGmmu:56248.
NMPDRfig|10090.3.peg.4905.
UCSCuc008hcx.1. mouse.

Organism-specific databases

CTD56248.
MGIMGI:1860835. Ak3.

Phylogenomic databases

HOGENOMQ9WTP7.
HOVERGENQ9WTP7.
OMANPPKTVG.

Enzyme and pathway databases

BRENDA2.7.4.10. 244.

Gene expression databases

ArrayExpressQ9WTP7.
BgeeQ9WTP7.
CleanExMM_AK3.
MM_AK3L1.
GenevestigatorQ9WTP7.
GermOnlineENSMUSG00000024782. Mus musculus.

Family and domain databases

InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_Znf_lid.
[Graphical view]
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
ProDomPD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01351. adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio312140.
SOURCESearch...

Entry information

Entry nameKAD3_MOUSE
AccessionPrimary (citable) accession number: Q9WTP7
Secondary accession number(s): Q3UDN7 expand/collapse secondary AC list , Q8BGX5, Q9D7Z1, Q9DB57, Q9DBM5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents