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Reviewed, UniProtKB/Swiss-Prot Q9R0Y5 (KAD1_MOUSE)

Last modified November 3, 2009. Version 78. 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adenylate kinase isoenzyme 1
      Short name=AK 1
    EC=2.7.4.3
Alternative name(s):
    ATP-AMP transphosphorylase 1
    Myokinase
Gene names
Name: Ak1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth By similarity. May provide a mechanism to buffer the adenylate energy charge for sperm motility.

Catalytic activity

ATP + AMP = 2 ADP.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Developmental stage

Up-regulated during late spermiogenesis, when the flagellum is being assembled. Ref.2

Sequence similarities

Belongs to the adenylate kinase family.

Sequence caution

The sequence CAM16612.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processATP metabolic process

Inferred from electronic annotation. Source: InterPro

cell cycle arrest Ref.1

Inferred from direct assay. Source: MGI

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

plasma membrane Ref.1

Inferred from direct assay. Source: MGI

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R0Y5-1)

Also known as: Ak1a;

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: Q9R0Y5-2)

Also known as: Ak1b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ME → MGCCVSSEPQEEGGRKTG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Adenylate kinase isoenzyme 1
PRO_0000158911

Regions

Nucleotide binding15 – 239ATP By similarity
Nucleotide binding94 – 1018AMP By similarity

Sites

Binding site391AMP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Natural variations

Alternative sequence1 – 22ME → MGCCVSSEPQEEGGRKTG in isoform 2.
VSP_024843

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Ak1a) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 88E7862522967D14

FASTA19421,540
        10         20         30         40         50         60 
MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SERGKKLSAI 

        70         80         90        100        110        120 
MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK QGEEFEQKIG QPTLLLYVDA 

       130        140        150        160        170        180 
GAETMTQRLL KRGETSGRVD DNEETIKKRL ETYYNATEPV ISFYDKRGIV RKVNAEGTVD 

       190 
TVFSEVCTYL DSLK 

« Hide

Isoform 2 (Ak1b).

Checksum: 5295189A6E7CB6D8
Show »

FASTA21023,116

References

« Hide 'large scale' references
[1]"wt p53 dependent expression of a membrane-associated isoform of adenylate kinase."
Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M., Schneider C.
Oncogene 18:5879-5888(1999) [PubMed: 10557075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Adenylate kinases 1 and 2 are part of the accessory structures in the mouse sperm flagellum."
Cao W., Haig-Ladewig L., Gerton G.L., Moss S.B.
Biol. Reprod. 75:492-500(2006) [PubMed: 16790685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE.
Strain: CD-1.
[3]"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] (ISOFORM 1).
Strain: C57BL/6J and NOD.
Tissue: Adipose tissue.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6 and FVB/N.
Tissue: Mammary tumor and Retina.
[6]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 32-44; 64-77; 84-97 AND 150-166, MASS SPECTROMETRY.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ010108 mRNA. Translation: CAB52407.1.
AJ010109 mRNA. Translation: CAB52408.1.
DQ486026 mRNA. Translation: ABF46940.1.
AK046613 mRNA. Translation: BAC32808.1.
AK089270 mRNA. Translation: BAC40822.1.
AL772271 Genomic DNA. Translation: CAM16612.1. Sequence problems.
AL772271 Genomic DNA. Translation: CAM16613.1.
AL772271 Genomic DNA. Translation: CAM16614.1.
BC014802 mRNA. Translation: AAH14802.1.
BC054366 mRNA. Translation: AAH54366.1.
IPIIPI00128209.
IPI00750256.
RefSeqNP_067490.1.
UniGeneMm.29189

3D structure databases

HSSPHSSP built from PDB template 3ADK based on UniProtKB P00571.
SMRQ9R0Y5. Positions 1-193.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9R0Y5.

2-D gel databases

REPRODUCTION-2DPAGEQ9R0Y5.

Proteomic databases

PRIDEQ9R0Y5.

Genome annotation databases

EnsemblENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817; Mus musculus. [Genome view]
ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817; Mus musculus. [Genome view]
ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817; Mus musculus. [Genome view]
GeneID11636.
KEGGmmu:11636.
NMPDRfig|10090.3.peg.5814.
UCSCuc008jgh.1. mouse.
uc008jgj.1. mouse.

Organism-specific databases

MGIMGI:87977. Ak1.

Phylogenomic databases

HOGENOMQ9R0Y5.
HOVERGENQ9R0Y5.
OMAGPETMTQ.

Enzyme and pathway databases

BRENDA2.7.4.3. 244.

Gene expression databases

ArrayExpressQ9R0Y5.
BgeeQ9R0Y5.
CleanExMM_AK1.
GenevestigatorQ9R0Y5.
GermOnlineENSMUSG00000026817. Mus musculus.

Family and domain databases

InterProIPR000850. Adenylate_kin.
IPR006267. Adenylate_kin1.
[Graphical view]
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
ProDomPD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01360. aden_kin_iso1. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameKAD1_MOUSE
AccessionPrimary (citable) accession number: Q9R0Y5
Secondary accession number(s): A2AK80, Q542C5, Q9R0Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 1, 2000
Last modified: November 3, 2009
This is version 78 of the entry and version 1 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents