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O75385 (ULK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ULK1
Synonyms:KIAA0722
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1050 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.16 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

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. Ref.5 Ref.9 Ref.10 Ref.11 Ref.12 Ref.17 Ref.20 Ref.21

Subcellular location

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.

Tissue specificity

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

Post-translational modification

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. Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. APG1/unc-51/ULK1 subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAutophagy
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from electronic annotation. Source: Ensembl

autophagic vacuole assembly

Inferred from electronic annotation. Source: Ensembl

axon extension

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from sequence or structural similarity. Source: UniProtKB

cerebellar granule cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of collateral sprouting

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from mutant phenotype PubMed 18007665. Source: UniProtKB

neuron projection regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of macroautophagy

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.12. Source: UniProtKB

protein localization

Inferred from mutant phenotype PubMed 16940348. Source: UniProtKB

protein phosphorylation

Non-traceable author statement Ref.1. Source: UniProtKB

radial glia guided migration of cerebellar granule cell

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of autophagy

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of neurotrophin TRK receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentULK1-ATG13-FIP200 complex

Inferred from physical interaction Ref.11. Source: UniProtKB

autophagic vacuole

Inferred from direct assay PubMed 17595159. Source: UniProtKB

cytoplasm

Non-traceable author statement Ref.1. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay Ref.5. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

pre-autophagosomal structure membrane

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Rab GTPase binding

Inferred from physical interaction Ref.21. Source: BHF-UCL

protein complex binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10501050Serine/threonine-protein kinase ULK1
PRO_0000086780

Regions

Domain16 – 278263Protein kinase
Nucleotide binding22 – 309ATP By similarity
Region287 – 416130Interaction with GABARAP and GABARAPL2
Compositional bias297 – 31014Poly-Ser

Sites

Active site1381Proton acceptor By similarity
Binding site461ATP By similarity

Amino acid modifications

Modified residue3171Phosphoserine; by AMPK By similarity
Modified residue4501Phosphoserine Ref.7 Ref.14 Ref.15 Ref.18
Modified residue4561Phosphothreonine Ref.7 Ref.15
Modified residue4671Phosphoserine By similarity
Modified residue4691Phosphoserine Ref.18
Modified residue4771Phosphoserine Ref.6
Modified residue4791Phosphoserine Ref.6
Modified residue5561Phosphoserine Ref.7 Ref.18
Modified residue5751Phosphothreonine By similarity
Modified residue6381Phosphoserine Ref.14 Ref.15 Ref.18
Modified residue7581Phosphoserine; by MTOR Probable

Natural variations

Natural variant2901V → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.22
VAR_041274
Natural variant2981S → L. Ref.22
Corresponds to variant rs56364352 [ dbSNP | Ensembl ].
VAR_041275
Natural variant4781P → L. Ref.22
Corresponds to variant rs12827141 [ dbSNP | Ensembl ].
VAR_041276
Natural variant5031T → M. Ref.22
Corresponds to variant rs55824543 [ dbSNP | Ensembl ].
VAR_041277
Natural variant6651S → L. Ref.22
Corresponds to variant rs55815560 [ dbSNP | Ensembl ].
VAR_041278
Natural variant7141P → L. Ref.22
Corresponds to variant rs11546871 [ dbSNP | Ensembl ].
VAR_041279
Natural variant7841S → C in a lung adenocarcinoma sample; somatic mutation. Ref.22
VAR_041280
Natural variant8161T → A. Ref.1 Ref.2
Corresponds to variant rs11609348 [ dbSNP | Ensembl ].
VAR_054892

Sequences

Sequence LengthMass (Da)Tools
O75385 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: AED9BD5139F2DB92

FASTA1,050112,631
        10         20         30         40         50         60 
MEPGRGGTET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK KNLAKSQTLL 

        70         80         90        100        110        120 
GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL ADYLHAMRTL SEDTIRLFLQ 

       130        140        150        160        170        180 
QIAGAMRLLH SKGIIHRDLK PQNILLSNPA GRRANPNSIR VKIADFGFAR YLQSNMMAAT 

       190        200        210        220        230        240 
LCGSPMYMAP EVIMSQHYDG KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV 

       250        260        270        280        290        300 
PTIPRETSAP LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA SPSVRKSPPV PVPSYPSSGS 

       310        320        330        340        350        360 
GSSSSSSSTS HLASPPSLGE MQQLQKTLAS PADTAGFLHS SRDSGGSKDS SCDTDDFVMV 

       370        380        390        400        410        420 
PAQFPGDLVA EAPSAKPPPD SLMCSGSSLV ASAGLESHGR TPSPSPPCSS SPSPSGRAGP 

       430        440        450        460        470        480 
FSSSRCGASV PIPVPTQVQN YQRIERNLQS PTQFQTPRSS AIRRSGSTSP LGFARASPSP 

       490        500        510        520        530        540 
PAHAEHGGVL ARKMSLGGGR PYTPSPQVGT IPERPGWSGT PSPQGAEMRG GRSPRPGSSA 

       550        560        570        580        590        600 
PEHSPRTSGL GCRLHSAPNL SDLHVVRPKL PKPPTDPLGA VFSPPQASPP QPSHGLQSCR 

       610        620        630        640        650        660 
NLRGSPKLPD FLQRNPLPPI LGSPTKAVPS FDFPKTPSSQ NLLALLARQG VVMTPPRNRT 

       670        680        690        700        710        720 
LPDLSEVGPF HGQPLGPGLR PGEDPKGPFG RSFSTSRLTD LLLKAAFGTQ APDPGSTESL 

       730        740        750        760        770        780 
QEKPMEIAPS AGFGGSLHPG ARAGGTSSPS PVVFTVGSPP SGSTPPQGPR TRMFSAGPTG 

       790        800        810        820        830        840 
SASSSARHLV PGPCSEAPAP ELPAPGHGCS FADPITANLE GAVTFEAPDL PEETLMEQEH 

       850        860        870        880        890        900 
TEILRGLRFT LLFVQHVLEI AALKGSASEA AGGPEYQLQE SVVADQISLL SREWGFAEQL 

       910        920        930        940        950        960 
VLYLKVAELL SSGLQSAIDQ IRAGKLCLSS TVKQVVRRLN ELYKASVVSC QGLSLRLQRF 

       970        980        990       1000       1010       1020 
FLDKQRLLDR IHSITAERLI FSHAVQMVQS AALDEMFQHR EGCVPRYHKA LLLLEGLQHM 

      1030       1040       1050 
LSDQADIENV TKCKLCIERR LSALLTGICA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy."
Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A., Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M., Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.
Science 331:456-461(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF045458 mRNA. Translation: AAC32326.1.
AB018265 mRNA. Translation: BAA34442.2. Different initiation.
AC131009 Genomic DNA. No translation available.
RefSeqNP_003556.1. NM_003565.2.
UniGeneHs.47061.

3D structure databases

ProteinModelPortalO75385.
SMRO75385. Positions 15-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113996. 30 interactions.
IntActO75385. 27 interactions.
MINTMINT-1892187.
STRING9606.ENSP00000324560.

Chemistry

BindingDBO75385.
ChEMBLCHEMBL6006.
GuidetoPHARMACOLOGY2271.

PTM databases

PhosphoSiteO75385.

Proteomic databases

PaxDbO75385.
PRIDEO75385.

Protocols and materials databases

DNASU8408.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000321867; ENSP00000324560; ENSG00000177169.
GeneID8408.
KEGGhsa:8408.
UCSCuc001uje.3. human.

Organism-specific databases

CTD8408.
GeneCardsGC12P132379.
HGNCHGNC:12558. ULK1.
HPAHPA054007.
MIM603168. gene.
neXtProtNX_O75385.
PharmGKBPA37198.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000044146.
HOVERGENHBG000342.
InParanoidO75385.
KOK08269.
OMADTDDFVM.
OrthoDBEOG7K0ZBF.
PhylomeDBO75385.
TreeFamTF324551.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
SignaLinkO75385.

Gene expression databases

ArrayExpressO75385.
BgeeO75385.
CleanExHS_ULK1.
GenevestigatorO75385.

Family and domain databases

InterProIPR011009. 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]
PfamPF12063. DUF3543. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSULK1. human.
GeneWikiULK1.
GenomeRNAi8408.
NextBio31476.
PROO75385.
SOURCESearch...

Entry information

Entry nameULK1_HUMAN
AccessionPrimary (citable) accession number: O75385
Secondary accession number(s): Q9UQ28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM