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Q9R0Y5

- KAD1_MOUSE

UniProt

Q9R0Y5 - KAD1_MOUSE

Protein

Adenylate kinase isoenzyme 1

Gene

Ak1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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.By similarity1 Publication

    Catalytic activityi

    ATP + AMP = 2 ADP.UniRule annotation
    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391AMPUniRule annotation
    Binding sitei44 – 441AMPUniRule annotation
    Binding sitei101 – 1011AMPUniRule annotation
    Binding sitei132 – 1321ATPUniRule annotation
    Binding sitei138 – 1381AMPUniRule annotation
    Binding sitei149 – 1491AMPUniRule annotation
    Binding sitei177 – 1771ATP; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 236ATPUniRule annotation
    Nucleotide bindingi65 – 673AMPUniRule annotation
    Nucleotide bindingi94 – 974AMPUniRule annotation

    GO - Molecular functioni

    1. adenylate kinase activity Source: MGI
    2. ATP binding Source: UniProtKB-KW
    3. nucleoside diphosphate kinase activity Source: UniProtKB

    GO - Biological processi

    1. ADP biosynthetic process Source: UniProtKB-HAMAP
    2. AMP metabolic process Source: UniProtKB-HAMAP
    3. ATP metabolic process Source: UniProtKB-HAMAP
    4. cell cycle arrest Source: MGI
    5. nucleoside diphosphate phosphorylation Source: UniProtKB
    6. nucleoside triphosphate biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.4.3. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinase isoenzyme 1UniRule annotation (EC:2.7.4.3UniRule annotation, EC:2.7.4.6UniRule annotation)
    Short name:
    AK 1UniRule annotation
    Alternative name(s):
    ATP-AMP transphosphorylase 1UniRule annotation
    ATP:AMP phosphotransferaseUniRule annotation
    Adenylate monophosphate kinaseUniRule annotation
    MyokinaseUniRule annotation
    Gene namesi
    Name:Ak1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:87977. Ak1.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. outer dense fiber Source: MGI
    3. plasma membrane Source: MGI
    4. sperm flagellum Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194Adenylate kinase isoenzyme 1PRO_0000158911Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R0Y5.
    PaxDbiQ9R0Y5.
    PRIDEiQ9R0Y5.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00128209.
    Q9R0Y5.

    PTM databases

    PhosphoSiteiQ9R0Y5.

    Expressioni

    Developmental stagei

    Up-regulated during late spermiogenesis, when the flagellum is being assembled.1 Publication

    Gene expression databases

    BgeeiQ9R0Y5.
    CleanExiMM_AK1.
    GenevestigatoriQ9R0Y5.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    BioGridi198045. 1 interaction.
    IntActiQ9R0Y5. 3 interactions.
    MINTiMINT-4130855.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0Y5.
    SMRiQ9R0Y5. Positions 1-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 6730NMPbindUniRule annotationAdd
    BLAST
    Regioni131 – 14111LIDUniRule annotationAdd
    BLAST

    Domaini

    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.UniRule annotation

    Sequence similaritiesi

    Belongs to the adenylate kinase family. AK1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    GeneTreeiENSGT00390000016215.
    HOGENOMiHOG000238771.
    HOVERGENiHBG108060.
    KOiK00939.
    OMAiYKTINGE.
    OrthoDBiEOG7060S3.
    PhylomeDBiQ9R0Y5.
    TreeFamiTF354283.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    MF_03171. Adenylate_kinase_AK1.
    InterProiIPR000850. Adenylat/UMP-CMP_kin.
    IPR028582. AK1.
    IPR006267. AK1/5.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9R0Y5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG    50
    SERGKKLSAI MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK 100
    QGEEFEQKIG QPTLLLYVDA GAETMTQRLL KRGETSGRVD DNEETIKKRL 150
    ETYYNATEPV ISFYDKRGIV RKVNAEGTVD TVFSEVCTYL DSLK 194
    Length:194
    Mass (Da):21,540
    Last modified:May 1, 2000 - v1
    Checksum:i88E7862522967D14
    GO
    Isoform 2 (identifier: Q9R0Y5-2) [UniParc]FASTAAdd to Basket

    Also known as: Ak1b

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

    Show »
    Length:210
    Mass (Da):23,116
    Checksum:i5295189A6E7CB6D8
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 22ME → MGCCVSSEPQEEGGRKTG in isoform 2. 2 PublicationsVSP_024843

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS15924.1. [Q9R0Y5-2]
    CCDS57167.1. [Q9R0Y5-1]
    RefSeqiNP_001185719.1. NM_001198790.1. [Q9R0Y5-1]
    NP_001185720.1. NM_001198791.1. [Q9R0Y5-1]
    NP_001185721.1. NM_001198792.1. [Q9R0Y5-1]
    NP_067490.1. NM_021515.3. [Q9R0Y5-2]
    XP_006497687.1. XM_006497624.1. [Q9R0Y5-1]
    UniGeneiMm.29189.

    Genome annotation databases

    EnsembliENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817. [Q9R0Y5-2]
    ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817. [Q9R0Y5-1]
    ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817. [Q9R0Y5-1]
    GeneIDi11636.
    KEGGimmu:11636.
    UCSCiuc008jgh.2. mouse. [Q9R0Y5-1]
    uc008jgj.2. mouse. [Q9R0Y5-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS15924.1. [Q9R0Y5-2 ]
    CCDS57167.1. [Q9R0Y5-1 ]
    RefSeqi NP_001185719.1. NM_001198790.1. [Q9R0Y5-1 ]
    NP_001185720.1. NM_001198791.1. [Q9R0Y5-1 ]
    NP_001185721.1. NM_001198792.1. [Q9R0Y5-1 ]
    NP_067490.1. NM_021515.3. [Q9R0Y5-2 ]
    XP_006497687.1. XM_006497624.1. [Q9R0Y5-1 ]
    UniGenei Mm.29189.

    3D structure databases

    ProteinModelPortali Q9R0Y5.
    SMRi Q9R0Y5. Positions 1-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198045. 1 interaction.
    IntActi Q9R0Y5. 3 interactions.
    MINTi MINT-4130855.

    PTM databases

    PhosphoSitei Q9R0Y5.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00128209.
    Q9R0Y5.

    Proteomic databases

    MaxQBi Q9R0Y5.
    PaxDbi Q9R0Y5.
    PRIDEi Q9R0Y5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000068271 ; ENSMUSP00000068479 ; ENSMUSG00000026817 . [Q9R0Y5-2 ]
    ENSMUST00000113277 ; ENSMUSP00000108902 ; ENSMUSG00000026817 . [Q9R0Y5-1 ]
    ENSMUST00000113278 ; ENSMUSP00000108903 ; ENSMUSG00000026817 . [Q9R0Y5-1 ]
    GeneIDi 11636.
    KEGGi mmu:11636.
    UCSCi uc008jgh.2. mouse. [Q9R0Y5-1 ]
    uc008jgj.2. mouse. [Q9R0Y5-2 ]

    Organism-specific databases

    CTDi 203.
    MGIi MGI:87977. Ak1.

    Phylogenomic databases

    eggNOGi COG0563.
    GeneTreei ENSGT00390000016215.
    HOGENOMi HOG000238771.
    HOVERGENi HBG108060.
    KOi K00939.
    OMAi YKTINGE.
    OrthoDBi EOG7060S3.
    PhylomeDBi Q9R0Y5.
    TreeFami TF354283.

    Enzyme and pathway databases

    BRENDAi 2.7.4.3. 3474.

    Miscellaneous databases

    NextBioi 279205.
    PROi Q9R0Y5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R0Y5.
    CleanExi MM_AK1.
    Genevestigatori Q9R0Y5.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    MF_03171. Adenylate_kinase_AK1.
    InterProi IPR000850. Adenylat/UMP-CMP_kin.
    IPR028582. AK1.
    IPR006267. AK1/5.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR23359. PTHR23359. 1 hit.
    PRINTSi PR00094. ADENYLTKNASE.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01360. aden_kin_iso1. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiKAD1_MOUSE
    AccessioniPrimary (citable) accession number: Q9R0Y5
    Secondary accession number(s): A2AK80, Q542C5, Q9R0Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3