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Q9ESW4

- AGK_MOUSE

UniProt

Q9ESW4 - AGK_MOUSE

Protein

Acylglycerol kinase, mitochondrial

Gene

Agk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth.1 Publication

    Catalytic activityi

    ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate.
    ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.

    Cofactori

    Magnesium.By similarity

    Kineticsi

    1. KM=45 µM for diacylglycerol1 Publication

    Vmax=159 nmol/min/mg enzyme with dioeoylglycerol as substrate1 Publication

    Pathwayi

    GO - Molecular functioni

    1. acylglycerol kinase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. ceramide kinase activity Source: MGI
    4. diacylglycerol kinase activity Source: UniProtKB-EC
    5. lipid kinase activity Source: MGI
    6. NAD+ kinase activity Source: InterPro

    GO - Biological processi

    1. ceramide biosynthetic process Source: MGI
    2. glycerolipid metabolic process Source: UniProtKB-UniPathway
    3. lipid phosphorylation Source: MGI
    4. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ9ESW4.
    UniPathwayiUPA00230.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acylglycerol kinase, mitochondrial (EC:2.7.1.107, EC:2.7.1.94)
    Alternative name(s):
    Multiple substrate lipid kinase
    Short name:
    MuLK
    Short name:
    Multi-substrate lipid kinase
    Gene namesi
    Name:Agk
    Synonyms:Mulk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1917173. Agk.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: MGI
    2. mitochondrial membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3131MitochondrionSequence AnalysisAdd
    BLAST
    Chaini32 – 421390Acylglycerol kinase, mitochondrialPRO_0000252381Add
    BLAST

    Proteomic databases

    MaxQBiQ9ESW4.
    PaxDbiQ9ESW4.
    PRIDEiQ9ESW4.

    PTM databases

    PhosphoSiteiQ9ESW4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiQ9ESW4.
    CleanExiMM_AGK.
    GenevestigatoriQ9ESW4.

    Interactioni

    Protein-protein interaction databases

    BioGridi213759. 1 interaction.
    IntActiQ9ESW4. 2 interactions.
    MINTiMINT-4129364.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ESW4.
    SMRiQ9ESW4. Positions 59-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 199142DAGKcPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 DAGKc domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1597.
    GeneTreeiENSGT00690000101761.
    HOGENOMiHOG000252977.
    HOVERGENiHBG080751.
    InParanoidiQ9ESW4.
    KOiK09881.
    OMAiTKAAHFF.
    OrthoDBiEOG7P2XS5.
    PhylomeDBiQ9ESW4.
    TreeFamiTF320485.

    Family and domain databases

    InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [Graphical view]
    PfamiPF00781. DAGK_cat. 1 hit.
    [Graphical view]
    SMARTiSM00046. DAGKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 2 hits.
    PROSITEiPS50146. DAGK. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ESW4-1) [UniParc]FASTAAdd to Basket

    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

    MTAFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG    50
    NQLIPPNAQV KKATVFLNPA ACKGKARTLF EKNAAPILHL SGMDVTVVKT 100
    DYEGQAKKLL ELMESTDVII VAGGDGTLQE VVTGVLRRTD EATFSKIPIG 150
    FIPLGQTSSL SHTLFAESGN KVQHITDATL AIVKGETVPL DVLQIKGEKE 200
    QPVYAMTGLR WGSFRDAGVK VSKYWYLGPL KTKAAHFFST LQEWPQTHQA 250
    SISYTGPRER PPIEPEETPP RPSLYRRILR RLASFWAQPQ DASSREVSPE 300
    VWKDVQLSTI ELSITTRNTQ LDLMSKEDFM NICIEPDTVS KGDFIIIGSK 350
    KVRDPGLRAA GTECLQASHC TLVLPEGTEG SFSIDSEEYE AMPVEVKLLP 400
    RKLRFFCDPR KREQMLPSTS Q 421
    Length:421
    Mass (Da):46,976
    Last modified:March 1, 2001 - v1
    Checksum:iDBBC48C9EB3206FD
    GO
    Isoform 2 (identifier: Q9ESW4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-421: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:173
    Mass (Da):18,899
    Checksum:i54E2CB009875A90B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei174 – 421248Missing in isoform 2. 1 PublicationVSP_020927Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY772469 mRNA. Translation: AAV38106.1.
    AJ401619 mRNA. Translation: CAC06108.1.
    AK011715 mRNA. Translation: BAB27796.1.
    AK076224 mRNA. Translation: BAC36260.1.
    BC019145 mRNA. Translation: AAH19145.1.
    BC093525 mRNA. Translation: AAH93525.1.
    CCDSiCCDS20027.1. [Q9ESW4-1]
    RefSeqiNP_076027.1. NM_023538.2. [Q9ESW4-1]
    UniGeneiMm.32840.

    Genome annotation databases

    EnsembliENSMUST00000031977; ENSMUSP00000031977; ENSMUSG00000029916. [Q9ESW4-1]
    GeneIDi69923.
    KEGGimmu:69923.
    UCSCiuc009bmm.2. mouse. [Q9ESW4-2]
    uc009bmn.2. mouse. [Q9ESW4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY772469 mRNA. Translation: AAV38106.1 .
    AJ401619 mRNA. Translation: CAC06108.1 .
    AK011715 mRNA. Translation: BAB27796.1 .
    AK076224 mRNA. Translation: BAC36260.1 .
    BC019145 mRNA. Translation: AAH19145.1 .
    BC093525 mRNA. Translation: AAH93525.1 .
    CCDSi CCDS20027.1. [Q9ESW4-1 ]
    RefSeqi NP_076027.1. NM_023538.2. [Q9ESW4-1 ]
    UniGenei Mm.32840.

    3D structure databases

    ProteinModelPortali Q9ESW4.
    SMRi Q9ESW4. Positions 59-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213759. 1 interaction.
    IntActi Q9ESW4. 2 interactions.
    MINTi MINT-4129364.

    PTM databases

    PhosphoSitei Q9ESW4.

    Proteomic databases

    MaxQBi Q9ESW4.
    PaxDbi Q9ESW4.
    PRIDEi Q9ESW4.

    Protocols and materials databases

    DNASUi 69923.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031977 ; ENSMUSP00000031977 ; ENSMUSG00000029916 . [Q9ESW4-1 ]
    GeneIDi 69923.
    KEGGi mmu:69923.
    UCSCi uc009bmm.2. mouse. [Q9ESW4-2 ]
    uc009bmn.2. mouse. [Q9ESW4-1 ]

    Organism-specific databases

    CTDi 55750.
    MGIi MGI:1917173. Agk.

    Phylogenomic databases

    eggNOGi COG1597.
    GeneTreei ENSGT00690000101761.
    HOGENOMi HOG000252977.
    HOVERGENi HBG080751.
    InParanoidi Q9ESW4.
    KOi K09881.
    OMAi TKAAHFF.
    OrthoDBi EOG7P2XS5.
    PhylomeDBi Q9ESW4.
    TreeFami TF320485.

    Enzyme and pathway databases

    UniPathwayi UPA00230 .
    SABIO-RK Q9ESW4.

    Miscellaneous databases

    ChiTaRSi AGK. mouse.
    NextBioi 330619.
    PROi Q9ESW4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9ESW4.
    CleanExi MM_AGK.
    Genevestigatori Q9ESW4.

    Family and domain databases

    InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR001206. Diacylglycerol_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00781. DAGK_cat. 1 hit.
    [Graphical view ]
    SMARTi SM00046. DAGKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 2 hits.
    PROSITEi PS50146. DAGK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Strain: FVB/N.
      Tissue: Carcinoma.
    2. "Further characterization of mammalian ceramide kinase: substrate delivery and (stereo)specificity, tissue distribution, and subcellular localization studies."
      Van Overloop H., Gijsbers S., Van Veldhoven P.P.
      J. Lipid Res. 47:268-283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Head.
    4. "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).
      Strain: FVB/N.
      Tissue: Liver and Mammary tumor.

    Entry informationi

    Entry nameiAGK_MOUSE
    AccessioniPrimary (citable) accession number: Q9ESW4
    Secondary accession number(s): Q9D087
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 104 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, Reference proteome

    Documents

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

    External Data

    Dasty 3