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Q9R0Y5 (KAD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Adenylate kinase isoenzyme 1

Short name=AK 1
EC=2.7.4.3
EC=2.7.4.6
Alternative name(s):
ATP-AMP transphosphorylase 1
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Myokinase
Gene names
Name:Ak1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also possesses broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism By similarity. May provide a mechanism to buffer the adenylate energy charge for sperm motility. Ref.2

Catalytic activity

ATP + AMP = 2 ADP. HAMAP-Rule MF_03171

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. HAMAP-Rule MF_03171

Subunit structure

Monomer By similarity. HAMAP-Rule MF_03171

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03171.

Developmental stage

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

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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis By similarity. HAMAP-Rule MF_03171

Sequence similarities

Belongs to the adenylate kinase family. AK1 subfamily.

Sequence caution

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

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 HAMAP-Rule MF_03171
PRO_0000158911

Regions

Nucleotide binding18 – 236ATP By similarity
Nucleotide binding65 – 673AMP By similarity
Nucleotide binding94 – 974AMP By similarity
Region38 – 6730NMPbind By similarity
Region131 – 14111LID By similarity

Sites

Binding site391AMP By similarity
Binding site441AMP By similarity
Binding site1011AMP By similarity
Binding site1321ATP By similarity
Binding site1381AMP By similarity
Binding site1491AMP By similarity
Binding site1771ATP; via carbonyl oxygen 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) [UniParc].

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[7]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001185719.1. NM_001198790.1.
NP_001185720.1. NM_001198791.1.
NP_001185721.1. NM_001198792.1.
NP_067490.1. NM_021515.3.
XP_006497687.1. XM_006497624.1.
UniGeneMm.29189.

3D structure databases

ProteinModelPortalQ9R0Y5.
SMRQ9R0Y5. Positions 1-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198045. 1 interaction.
IntActQ9R0Y5. 3 interactions.
MINTMINT-4130855.

PTM databases

PhosphoSiteQ9R0Y5.

2D gel databases

REPRODUCTION-2DPAGEIPI00128209.
Q9R0Y5.

Proteomic databases

PaxDbQ9R0Y5.
PRIDEQ9R0Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817. [Q9R0Y5-2]
ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817. [Q9R0Y5-1]
ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817. [Q9R0Y5-1]
GeneID11636.
KEGGmmu:11636.
UCSCuc008jgh.2. mouse. [Q9R0Y5-1]
uc008jgj.2. mouse. [Q9R0Y5-2]

Organism-specific databases

CTD203.
MGIMGI:87977. Ak1.

Phylogenomic databases

eggNOGCOG0563.
GeneTreeENSGT00390000016215.
HOGENOMHOG000238771.
HOVERGENHBG108060.
KOK00939.
OMAVDYYESK.
OrthoDBEOG7060S3.
PhylomeDBQ9R0Y5.
TreeFamTF354283.

Enzyme and pathway databases

BRENDA2.7.4.3. 3474.

Gene expression databases

BgeeQ9R0Y5.
CleanExMM_AK1.
GenevestigatorQ9R0Y5.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
HAMAPMF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01360. aden_kin_iso1. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279205.
PROQ9R0Y5.
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: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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