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O75385

- ULK1_HUMAN

UniProt

O75385 - ULK1_HUMAN

Protein

Serine/threonine-protein kinase ULK1

Gene

ULK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      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 negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity. May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences. Plays a role early in neuronal differentiation and is required for granule cell axon formation.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATPPROSITE-ProRule annotation
    Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 309ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein complex binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. Rab GTPase binding Source: BHF-UCL

    GO - Biological processi

    1. autophagic vacuole assembly Source: RefGenome
    2. axon extension Source: RefGenome
    3. cellular response to nutrient levels Source: UniProtKB
    4. cerebellar granule cell differentiation Source: Ensembl
    5. negative regulation of collateral sprouting Source: Ensembl
    6. neuron projection development Source: UniProtKB
    7. neuron projection regeneration Source: Ensembl
    8. positive regulation of autophagy Source: UniProtKB
    9. positive regulation of macroautophagy Source: BHF-UCL
    10. protein autophosphorylation Source: UniProtKB
    11. protein localization Source: UniProtKB
    12. protein phosphorylation Source: UniProtKB
    13. radial glia guided migration of cerebellar granule cell Source: Ensembl
    14. Ras protein signal transduction Source: Ensembl
    15. receptor internalization Source: Ensembl
    16. regulation of autophagy Source: UniProtKB
    17. regulation of neurotrophin TRK receptor signaling pathway Source: Ensembl
    18. response to starvation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Autophagy

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    SignaLinkiO75385.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase ULK1 (EC:2.7.11.1)
    Alternative name(s):
    Autophagy-related protein 1 homolog
    Short name:
    ATG1
    Short name:
    hATG1
    Unc-51-like kinase 1
    Gene namesi
    Name:ULK1
    Synonyms:KIAA0722
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12558. ULK1.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Preautophagosomal structure By similarity
    Note: Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of an autophagosome.By similarity

    GO - Cellular componenti

    1. ATG1/UKL1 signaling complex Source: RefGenome
    2. autophagic vacuole Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. cytoplasmic vesicle membrane Source: Ensembl
    5. cytosol Source: UniProtKB
    6. neuronal cell body Source: Ensembl
    7. neuron projection Source: Ensembl
    8. pre-autophagosomal structure membrane Source: UniProtKB
    9. ULK1-ATG13-FIP200 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37198.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10501050Serine/threonine-protein kinase ULK1PRO_0000086780Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei317 – 3171Phosphoserine; by AMPKBy similarity
    Modified residuei450 – 4501Phosphoserine5 Publications
    Modified residuei456 – 4561Phosphothreonine3 Publications
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei469 – 4691Phosphoserine2 Publications
    Modified residuei477 – 4771Phosphoserine2 Publications
    Modified residuei479 – 4791Phosphoserine2 Publications
    Modified residuei556 – 5561Phosphoserine3 Publications
    Modified residuei575 – 5751PhosphothreonineBy similarity
    Modified residuei638 – 6381Phosphoserine4 Publications
    Modified residuei758 – 7581Phosphoserine; by MTOR1 Publication

    Post-translational modificationi

    Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting the interaction with AMPK and preventing activation of ULK1 By similarity. In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy.By similarity6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75385.
    PaxDbiO75385.
    PRIDEiO75385.

    PTM databases

    PhosphoSiteiO75385.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Detected in the following adult tissues: skeletal muscle, heart, pancreas, brain, placenta, liver, kidney, and lung.

    Gene expression databases

    ArrayExpressiO75385.
    BgeeiO75385.
    CleanExiHS_ULK1.
    GenevestigatoriO75385.

    Organism-specific databases

    HPAiHPA054007.

    Interactioni

    Subunit structurei

    Interacts with GABARAP and GABARAPL2. Interacts (via C-terminus) with ATG13. Part of a complex consisting of ATG13, ATG101, ULK1 and RB1CC1. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR; the association depends on nutrient conditions and is reduced during starvation. Interacts with FEZ1; SCOC interferes with FEZ1-binding. Interacts with TBC1D14.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATG13O751433EBI-908831,EBI-2798775
    GABARAPL1Q9H0R82EBI-908831,EBI-746969
    GABARAPL2P605203EBI-908831,EBI-720116
    MAP1LC3BQ9GZQ82EBI-908831,EBI-373144
    MAP1LC3CQ9BXW42EBI-908831,EBI-2603996
    RB1CC1Q8TDY27EBI-908831,EBI-1047793
    TBC1D14Q9P2M44EBI-908831,EBI-2797718

    Protein-protein interaction databases

    BioGridi113996. 32 interactions.
    DIPiDIP-35196N.
    IntActiO75385. 27 interactions.
    MINTiMINT-1892187.
    STRINGi9606.ENSP00000324560.

    Structurei

    3D structure databases

    ProteinModelPortaliO75385.
    SMRiO75385. Positions 8-383.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 278263Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 416130Interaction with GABARAP and GABARAPL2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi297 – 31014Poly-SerAdd
    BLAST

    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.
    HOGENOMiHOG000044146.
    HOVERGENiHBG000342.
    InParanoidiO75385.
    KOiK08269.
    OMAiDTDDFVM.
    OrthoDBiEOG7K0ZBF.
    PhylomeDBiO75385.
    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.

    O75385-1 [UniParc]FASTAAdd to Basket

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    MEPGRGGTET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK     50
    KNLAKSQTLL GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL 100
    ADYLHAMRTL SEDTIRLFLQ QIAGAMRLLH SKGIIHRDLK PQNILLSNPA 150
    GRRANPNSIR VKIADFGFAR YLQSNMMAAT LCGSPMYMAP EVIMSQHYDG 200
    KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV PTIPRETSAP 250
    LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA SPSVRKSPPV PVPSYPSSGS 300
    GSSSSSSSTS HLASPPSLGE MQQLQKTLAS PADTAGFLHS SRDSGGSKDS 350
    SCDTDDFVMV PAQFPGDLVA EAPSAKPPPD SLMCSGSSLV ASAGLESHGR 400
    TPSPSPPCSS SPSPSGRAGP FSSSRCGASV PIPVPTQVQN YQRIERNLQS 450
    PTQFQTPRSS AIRRSGSTSP LGFARASPSP PAHAEHGGVL ARKMSLGGGR 500
    PYTPSPQVGT IPERPGWSGT PSPQGAEMRG GRSPRPGSSA PEHSPRTSGL 550
    GCRLHSAPNL SDLHVVRPKL PKPPTDPLGA VFSPPQASPP QPSHGLQSCR 600
    NLRGSPKLPD FLQRNPLPPI LGSPTKAVPS FDFPKTPSSQ NLLALLARQG 650
    VVMTPPRNRT LPDLSEVGPF HGQPLGPGLR PGEDPKGPFG RSFSTSRLTD 700
    LLLKAAFGTQ APDPGSTESL QEKPMEIAPS AGFGGSLHPG ARAGGTSSPS 750
    PVVFTVGSPP SGSTPPQGPR TRMFSAGPTG SASSSARHLV PGPCSEAPAP 800
    ELPAPGHGCS FADPITANLE GAVTFEAPDL PEETLMEQEH TEILRGLRFT 850
    LLFVQHVLEI AALKGSASEA AGGPEYQLQE SVVADQISLL SREWGFAEQL 900
    VLYLKVAELL SSGLQSAIDQ IRAGKLCLSS TVKQVVRRLN ELYKASVVSC 950
    QGLSLRLQRF FLDKQRLLDR IHSITAERLI FSHAVQMVQS AALDEMFQHR 1000
    EGCVPRYHKA LLLLEGLQHM LSDQADIENV TKCKLCIERR LSALLTGICA 1050
    Length:1,050
    Mass (Da):112,631
    Last modified:January 11, 2011 - v2
    Checksum:iAED9BD5139F2DB92
    GO

    Sequence cautioni

    The sequence BAA34442.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti290 – 2901V → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_041274
    Natural varianti298 – 2981S → L.1 Publication
    Corresponds to variant rs56364352 [ dbSNP | Ensembl ].
    VAR_041275
    Natural varianti478 – 4781P → L.1 Publication
    Corresponds to variant rs12827141 [ dbSNP | Ensembl ].
    VAR_041276
    Natural varianti503 – 5031T → M.1 Publication
    Corresponds to variant rs55824543 [ dbSNP | Ensembl ].
    VAR_041277
    Natural varianti665 – 6651S → L.1 Publication
    Corresponds to variant rs55815560 [ dbSNP | Ensembl ].
    VAR_041278
    Natural varianti714 – 7141P → L.1 Publication
    Corresponds to variant rs11546871 [ dbSNP | Ensembl ].
    VAR_041279
    Natural varianti784 – 7841S → C in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041280
    Natural varianti816 – 8161T → A.2 Publications
    Corresponds to variant rs11609348 [ dbSNP | Ensembl ].
    VAR_054892

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045458 mRNA. Translation: AAC32326.1.
    AB018265 mRNA. Translation: BAA34442.2. Different initiation.
    AC131009 Genomic DNA. No translation available.
    CCDSiCCDS9274.1.
    RefSeqiNP_003556.1. NM_003565.2.
    UniGeneiHs.47061.

    Genome annotation databases

    EnsembliENST00000321867; ENSP00000324560; ENSG00000177169.
    GeneIDi8408.
    KEGGihsa:8408.
    UCSCiuc001uje.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF045458 mRNA. Translation: AAC32326.1 .
    AB018265 mRNA. Translation: BAA34442.2 . Different initiation.
    AC131009 Genomic DNA. No translation available.
    CCDSi CCDS9274.1.
    RefSeqi NP_003556.1. NM_003565.2.
    UniGenei Hs.47061.

    3D structure databases

    ProteinModelPortali O75385.
    SMRi O75385. Positions 8-383.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113996. 32 interactions.
    DIPi DIP-35196N.
    IntActi O75385. 27 interactions.
    MINTi MINT-1892187.
    STRINGi 9606.ENSP00000324560.

    Chemistry

    BindingDBi O75385.
    ChEMBLi CHEMBL6006.
    GuidetoPHARMACOLOGYi 2271.

    PTM databases

    PhosphoSitei O75385.

    Proteomic databases

    MaxQBi O75385.
    PaxDbi O75385.
    PRIDEi O75385.

    Protocols and materials databases

    DNASUi 8408.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321867 ; ENSP00000324560 ; ENSG00000177169 .
    GeneIDi 8408.
    KEGGi hsa:8408.
    UCSCi uc001uje.3. human.

    Organism-specific databases

    CTDi 8408.
    GeneCardsi GC12P132379.
    HGNCi HGNC:12558. ULK1.
    HPAi HPA054007.
    MIMi 603168. gene.
    neXtProti NX_O75385.
    PharmGKBi PA37198.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000044146.
    HOVERGENi HBG000342.
    InParanoidi O75385.
    KOi K08269.
    OMAi DTDDFVM.
    OrthoDBi EOG7K0ZBF.
    PhylomeDBi O75385.
    TreeFami TF324551.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    SignaLinki O75385.

    Miscellaneous databases

    ChiTaRSi ULK1. human.
    GeneWikii ULK1.
    GenomeRNAii 8408.
    NextBioi 31476.
    PROi O75385.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75385.
    Bgeei O75385.
    CleanExi HS_ULK1.
    Genevestigatori O75385.

    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. "Human ULK1, a novel serine/threonine kinase related to UNC-51 kinase of Caenorhabditis elegans: cDNA cloning, expression, and chromosomal assignment."
      Kuroyanagi H., Yan J., Seki N., Yamanouchi Y., Suzuki Y., Takano T., Muramatsu M., Shirasawa T.
      Genomics 51:76-85(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-816.
    2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-816.
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Interaction of the Unc-51-like kinase and microtubule-associated protein light chain 3 related proteins in the brain: possible role of vesicular transport in axonal elongation."
      Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y., Koga H., Muramatsu M.-A.
      Brain Res. Mol. Brain Res. 85:1-12(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABARAP AND GABARAPL2.
    6. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; THR-456 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and is essential for macroautophagy."
      Mercer C.A., Kaliappan A., Dennis P.B.
      Autophagy 5:649-662(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, COMPLEX FORMATION WITH ATG13; ATG101 AND RB1CC1.
    10. "Atg101, a novel mammalian autophagy protein interacting with Atg13."
      Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T., Mizushima N.
      Autophagy 5:973-979(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
      Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., Mizushima N.
      Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH RPTOR AND TORC1 COMPLEX.
    12. "Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13-independent mechanism."
      Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.
      Mol. Cell. Biol. 29:157-171(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ATG13.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; THR-456 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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.
    17. "ULK1 inhibits the kinase activity of mTORC1 and cell proliferation."
      Jung C.H., Seo M., Otto N.M., Kim D.H.
      Autophagy 7:1212-1221(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPTOR.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-469; SER-556 AND SER-638, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: PHOSPHORYLATION BY AMPK.
    20. "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC."
      McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M., Johansen T., Tooze S.A.
      EMBO J. 31:1931-1946(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FEZ1.
    21. "TBC1D14 regulates autophagosome formation via Rab11- and ULK1-positive recycling endosomes."
      Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.
      J. Cell Biol. 197:659-675(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TBC1D14.
    22. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-290; LEU-298; LEU-478; MET-503; LEU-665; LEU-714 AND CYS-784.

    Entry informationi

    Entry nameiULK1_HUMAN
    AccessioniPrimary (citable) accession number: O75385
    Secondary accession number(s): Q9UQ28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3