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O75385

- ULK1_HUMAN

UniProt

O75385 - ULK1_HUMAN

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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

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 complex binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. 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
Complete GO annotation...

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. extrinsic component of autophagic vacuole membrane Source: UniProtKB
  7. extrinsic component of omegasome membrane Source: UniProtKB
  8. extrinsic component of pre-autophagosomal structure membrane Source: UniProtKB
  9. neuronal cell body Source: Ensembl
  10. neuron projection Source: Ensembl
  11. pre-autophagosomal structure membrane Source: UniProtKB
  12. ULK1-ATG13-FIP200 complex Source: UniProtKB
Complete GO annotation...

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 – 4501Phosphoserine4 Publications
Modified residuei456 – 4561Phosphothreonine2 Publications
Modified residuei467 – 4671PhosphoserineBy similarity
Modified residuei469 – 4691Phosphoserine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei479 – 4791Phosphoserine1 Publication
Modified residuei556 – 5561Phosphoserine2 Publications
Modified residuei575 – 5751PhosphothreonineBy similarity
Modified residuei638 – 6381Phosphoserine3 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

BgeeiO75385.
CleanExiHS_ULK1.
ExpressionAtlasiO75385. baseline and differential.
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. 35 interactions.
DIPiDIP-35196N.
IntActiO75385. 28 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.
GeneTreeiENSGT00770000120504.
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.
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

« Hide

        10         20         30         40         50
MEPGRGGTET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK
60 70 80 90 100
KNLAKSQTLL GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL
110 120 130 140 150
ADYLHAMRTL SEDTIRLFLQ QIAGAMRLLH SKGIIHRDLK PQNILLSNPA
160 170 180 190 200
GRRANPNSIR VKIADFGFAR YLQSNMMAAT LCGSPMYMAP EVIMSQHYDG
210 220 230 240 250
KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV PTIPRETSAP
260 270 280 290 300
LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA SPSVRKSPPV PVPSYPSSGS
310 320 330 340 350
GSSSSSSSTS HLASPPSLGE MQQLQKTLAS PADTAGFLHS SRDSGGSKDS
360 370 380 390 400
SCDTDDFVMV PAQFPGDLVA EAPSAKPPPD SLMCSGSSLV ASAGLESHGR
410 420 430 440 450
TPSPSPPCSS SPSPSGRAGP FSSSRCGASV PIPVPTQVQN YQRIERNLQS
460 470 480 490 500
PTQFQTPRSS AIRRSGSTSP LGFARASPSP PAHAEHGGVL ARKMSLGGGR
510 520 530 540 550
PYTPSPQVGT IPERPGWSGT PSPQGAEMRG GRSPRPGSSA PEHSPRTSGL
560 570 580 590 600
GCRLHSAPNL SDLHVVRPKL PKPPTDPLGA VFSPPQASPP QPSHGLQSCR
610 620 630 640 650
NLRGSPKLPD FLQRNPLPPI LGSPTKAVPS FDFPKTPSSQ NLLALLARQG
660 670 680 690 700
VVMTPPRNRT LPDLSEVGPF HGQPLGPGLR PGEDPKGPFG RSFSTSRLTD
710 720 730 740 750
LLLKAAFGTQ APDPGSTESL QEKPMEIAPS AGFGGSLHPG ARAGGTSSPS
760 770 780 790 800
PVVFTVGSPP SGSTPPQGPR TRMFSAGPTG SASSSARHLV PGPCSEAPAP
810 820 830 840 850
ELPAPGHGCS FADPITANLE GAVTFEAPDL PEETLMEQEH TEILRGLRFT
860 870 880 890 900
LLFVQHVLEI AALKGSASEA AGGPEYQLQE SVVADQISLL SREWGFAEQL
910 920 930 940 950
VLYLKVAELL SSGLQSAIDQ IRAGKLCLSS TVKQVVRRLN ELYKASVVSC
960 970 980 990 1000
QGLSLRLQRF FLDKQRLLDR IHSITAERLI FSHAVQMVQS AALDEMFQHR
1010 1020 1030 1040 1050
EGCVPRYHKA LLLLEGLQHM LSDQADIENV TKCKLCIERR LSALLTGICA
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 35 interactions.
DIPi DIP-35196N.
IntActi O75385. 28 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.
GeneTreei ENSGT00770000120504.
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

Bgeei O75385.
CleanExi HS_ULK1.
ExpressionAtlasi O75385. baseline and differential.
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.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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