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Q9QY01

- ULK2_MOUSE

UniProt

Q9QY01 - ULK2_MOUSE

Protein

Serine/threonine-protein kinase ULK2

Gene

Ulk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy: acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391ATPCurated
    Active sitei131 – 1311Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. autophagic vacuole assembly Source: RefGenome
    2. axon extension Source: MGI
    3. negative regulation of collateral sprouting Source: MGI
    4. protein autophosphorylation Source: RefGenome
    5. regulation of autophagy Source: UniProtKB
    6. response to starvation Source: UniProtKB
    7. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Autophagy, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase ULK2 (EC:2.7.11.1)
    Alternative name(s):
    Serine/threonine-protein kinase Unc51.2
    Unc-51-like kinase 2
    Gene namesi
    Name:Ulk2
    Synonyms:Kiaa0623
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1352758. Ulk2.

    Subcellular locationi

    Cytoplasmic vesicle membrane 1 Publication; Peripheral membrane protein 1 Publication
    Note: Localizes to pre-autophagosomal membrane.

    GO - Cellular componenti

    1. ATG1/UKL1 signaling complex Source: RefGenome
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. cytosol Source: RefGenome
    4. pre-autophagosomal structure membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi39 – 391K → T: Decreased kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10371037Serine/threonine-protein kinase ULK2PRO_0000086783Add
    BLAST

    Post-translational modificationi

    Autophosphorylated. In response to nutrient limitation, probably phosphorylated and activated by AMPK, leading to activate autophagy.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9QY01.

    PTM databases

    PhosphoSiteiQ9QY01.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    BgeeiQ9QY01.
    CleanExiMM_ULK2.
    GenevestigatoriQ9QY01.

    Interactioni

    Subunit structurei

    Component of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR By similarity. Interacts with SYNGAP1.By similarity2 Publications

    Protein-protein interaction databases

    DIPiDIP-60901N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QY01.
    SMRiQ9QY01. Positions 9-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 271263Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni813 – 1037225CTD-like regionBy similarityAdd
    BLAST

    Domaini

    The CTD-like region mediates membrane-binding and incorporation into large protein complexes.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117559.
    HOGENOMiHOG000044146.
    HOVERGENiHBG000342.
    InParanoidiQ9QY01.
    KOiK08269.
    OMAiGTIPEQF.
    OrthoDBiEOG7K0ZBF.
    PhylomeDBiQ9QY01.
    TreeFamiTF324551.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR016237. Ser/Thr_kin_STPK_Ulk-1/2.
    IPR008271. Ser/Thr_kinase_AS.
    IPR022708. Ser/Thr_kinase_C.
    [Graphical view]
    PfamiPF12063. DUF3543. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QY01-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ     50
    ILLGKEIKIL KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK 100
    GTLSEDTIRV FLHQIAAAMR ILHSKGIIHR DLKPQNILLS YANRRKSNVS 150
    GIRIKIADFG FARYLHSNTM AATLCGSPMY MAPEVIMSQH YDAKADLWSI 200
    GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET SPYLANLLLG 250
    LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP 300
    SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT 350
    DDFVLVPHNI SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP 400
    IPVPTQVRNY QRIEQNLIST ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG 450
    SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL VGTIPEQFSQ CCCGHPQGHE 500
    ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ KLRKQHSDPV 550
    CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS 600
    PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG 650
    SERHRSEQQQ SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD 700
    VAPAGACGVM LALPAGTAAS ARAVLFTVGS PPHSATAPTC THMVLRTRTT 750
    SVGSSSSGGS LCSASGRVCV GSPPGPGLGS SPPGAEGAPS LRYVPYGASP 800
    PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC VLDLTAVRGG 850
    NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL 900
    HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK 950
    QRFIDEINSV TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL 1000
    EGLSKILQDP TDVENVHKYK CSIERRLSAL CCSTATV 1037
    Length:1,037
    Mass (Da):112,877
    Last modified:May 1, 2000 - v1
    Checksum:i2E7DC3B0B87E9607
    GO

    Sequence cautioni

    The sequence BAC65613.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti998 – 9981L → V in BAA77341. (PubMed:10557072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF145922 mRNA. Translation: AAF18325.1.
    AB019577 mRNA. Translation: BAA77341.1.
    AK146620 mRNA. Translation: BAE27309.1.
    AK122331 mRNA. Translation: BAC65613.2. Different initiation.
    BC046778 mRNA. Translation: AAH46778.1.
    BC053029 mRNA. Translation: AAH53029.1.
    CCDSiCCDS24820.1.
    RefSeqiNP_038909.3. NM_013881.4.
    UniGeneiMm.162025.

    Genome annotation databases

    EnsembliENSMUST00000004920; ENSMUSP00000004920; ENSMUSG00000004798.
    GeneIDi29869.
    KEGGimmu:29869.
    UCSCiuc007jih.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF145922 mRNA. Translation: AAF18325.1 .
    AB019577 mRNA. Translation: BAA77341.1 .
    AK146620 mRNA. Translation: BAE27309.1 .
    AK122331 mRNA. Translation: BAC65613.2 . Different initiation.
    BC046778 mRNA. Translation: AAH46778.1 .
    BC053029 mRNA. Translation: AAH53029.1 .
    CCDSi CCDS24820.1.
    RefSeqi NP_038909.3. NM_013881.4.
    UniGenei Mm.162025.

    3D structure databases

    ProteinModelPortali Q9QY01.
    SMRi Q9QY01. Positions 9-317.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60901N.

    PTM databases

    PhosphoSitei Q9QY01.

    Proteomic databases

    PRIDEi Q9QY01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004920 ; ENSMUSP00000004920 ; ENSMUSG00000004798 .
    GeneIDi 29869.
    KEGGi mmu:29869.
    UCSCi uc007jih.2. mouse.

    Organism-specific databases

    CTDi 9706.
    MGIi MGI:1352758. Ulk2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117559.
    HOGENOMi HOG000044146.
    HOVERGENi HBG000342.
    InParanoidi Q9QY01.
    KOi K08269.
    OMAi GTIPEQF.
    OrthoDBi EOG7K0ZBF.
    PhylomeDBi Q9QY01.
    TreeFami TF324551.

    Miscellaneous databases

    NextBioi 307094.
    PROi Q9QY01.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9QY01.
    CleanExi MM_ULK2.
    Genevestigatori Q9QY01.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR016237. Ser/Thr_kin_STPK_Ulk-1/2.
    IPR008271. Ser/Thr_kinase_AS.
    IPR022708. Ser/Thr_kinase_C.
    [Graphical view ]
    Pfami PF12063. DUF3543. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A mouse serine/threonine kinase homologous to C. elegans UNC51 functions in parallel fiber formation of cerebellar granule neurons."
      Tomoda T., Bhatt R.S., Kuroyanagi H., Shirasawa T., Hatten M.E.
      Neuron 24:833-846(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Strain: C57BL/6J.
      Tissue: Brain.
    2. "Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains."
      Yan J., Kuroyanagi H., Tomemori T., Okazaki N., Asato K., Matsuda Y., Suzuki Y., Ohshima Y., Mitani S., Masuho Y., Shirasawa T., Muramatsu M.
      Oncogene 18:5850-5859(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
    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].
      Strain: C57BL/6J.
      Tissue: Kidney.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    6. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    7. "Role of Unc51.1 and its binding partners in CNS axon outgrowth."
      Tomoda T., Kim J.H., Zhan C., Hatten M.E.
      Genes Dev. 18:541-558(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYNGAP1.
    8. "UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3."
      Avery A.W., Figueroa C., Vojtek A.B.
      Cell. Signal. 19:177-184(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2 AND FRS3.
    9. "FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells."
      Hara T., Takamura A., Kishi C., Iemura S., Natsume T., Guan J.L., Mizushima N.
      J. Cell Biol. 181:497-510(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RB1CC1, MUTAGENESIS OF LYS-39.
    10. "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
      Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.
      Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF AMPK.
    11. "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
      Kim J., Kundu M., Viollet B., Guan K.L.
      Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY AMPK.

    Entry informationi

    Entry nameiULK2_MOUSE
    AccessioniPrimary (citable) accession number: Q9QY01
    Secondary accession number(s): Q80TV7, Q9WTP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 113 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3