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Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Autophagy-related protein 1 homolog) (ATG1) (hATG1) (Unc-51-like kinase 1)

 ULK1_HUMAN              Reviewed;        1050 AA.
O75385; Q9UQ28;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 173.
RecName: Full=Serine/threonine-protein kinase ULK1;
EC=2.7.11.1;
AltName: Full=Autophagy-related protein 1 homolog;
Short=ATG1;
Short=hATG1;
AltName: Full=Unc-51-like kinase 1;
Name=ULK1; Synonyms=KIAA0722;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-816.
PubMed=9693035; DOI=10.1006/geno.1998.5340;
Kuroyanagi H., Yan J., Seki N., Yamanouchi Y., Suzuki Y., Takano T.,
Muramatsu M., Shirasawa T.;
"Human ULK1, a novel serine/threonine kinase related to UNC-51 kinase
of Caenorhabditis elegans: cDNA cloning, expression, and chromosomal
assignment.";
Genomics 51:76-85(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-816.
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"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.";
DNA Res. 5:277-286(1998).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
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.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
INTERACTION WITH GABARAP AND GABARAPL2, AND REGION.
PubMed=11146101; DOI=10.1016/S0169-328X(00)00218-7;
Okazaki N., Yan J., Yuasa S., Ueno T., Kominami E., Masuho Y.,
Koga H., Muramatsu M.-A.;
"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.";
Brain Res. Mol. Brain Res. 85:1-12(2000).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-479, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; THR-456 AND
SER-556, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
SUBUNIT, AND COMPLEX FORMATION WITH ATG13; ATG101 AND RB1CC1.
PubMed=19287211; DOI=10.4161/auto.5.5.8249;
Mercer C.A., Kaliappan A., Dennis P.B.;
"A novel, human Atg13 binding protein, Atg101, interacts with ULK1 and
is essential for macroautophagy.";
Autophagy 5:649-662(2009).
[10]
SUBUNIT.
PubMed=19597335; DOI=10.4161/auto.5.7.9296;
Hosokawa N., Sasaki T., Iemura S.I., Natsume T., Hara T.,
Mizushima N.;
"Atg101, a novel mammalian autophagy protein interacting with Atg13.";
Autophagy 5:973-979(2009).
[11]
SUBUNIT, AND INTERACTION WITH RPTOR AND TORC1 COMPLEX.
PubMed=19211835; DOI=10.1091/mbc.E08-12-1248;
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.;
"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
complex required for autophagy.";
Mol. Biol. Cell 20:1981-1991(2009).
[12]
FUNCTION, AND INTERACTION WITH ATG13.
PubMed=18936157; DOI=10.1128/MCB.01082-08;
Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
"Kinase-inactivated ULK proteins inhibit autophagy via their conserved
C-terminal domains using an Atg13-independent mechanism.";
Mol. Cell. Biol. 29:157-171(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-638, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; THR-456 AND
SER-638, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
FUNCTION IN PHOSPHORYLATION OF AMPK.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
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.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[17]
FUNCTION, AND INTERACTION WITH RPTOR.
PubMed=21795849; DOI=10.4161/auto.7.10.16660;
Jung C.H., Seo M., Otto N.M., Kim D.H.;
"ULK1 inhibits the kinase activity of mTORC1 and cell proliferation.";
Autophagy 7:1212-1221(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-469; SER-556
AND SER-638, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION BY AMPK.
PubMed=21205641; DOI=10.1126/science.1196371;
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.;
"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase
connects energy sensing to mitophagy.";
Science 331:456-461(2011).
[20]
INTERACTION WITH FEZ1.
PubMed=22354037; DOI=10.1038/emboj.2012.36;
McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
Johansen T., Tooze S.A.;
"Genome-wide siRNA screen reveals amino acid starvation-induced
autophagy requires SCOC and WAC.";
EMBO J. 31:1931-1946(2012).
[21]
INTERACTION WITH TBC1D14.
PubMed=22613832; DOI=10.1083/jcb.201111079;
Longatti A., Lamb C.A., Razi M., Yoshimura S., Barr F.A., Tooze S.A.;
"TBC1D14 regulates autophagosome formation via Rab11- and ULK1-
positive recycling endosomes.";
J. Cell Biol. 197:659-675(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-450; SER-467;
SER-469; SER-477; SER-479; SER-556; SER-638; SER-758 AND SER-775, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
FUNCTION, INTERACTION WITH SESN2 AND SQSTM1, AND REGION.
PubMed=25040165; DOI=10.1111/febs.12905;
Ro S.H., Semple I.A., Park H., Park H., Park H.W., Kim M., Kim J.S.,
Lee J.H.;
"Sestrin2 promotes Unc-51-like kinase 1 mediated phosphorylation of
p62/sequestosome-1.";
FEBS J. 281:3816-3827(2014).
[24]
INTERACTION WITH TRIM5.
PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013;
Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T.,
Dinkins C., Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y.,
Levine B., Johansen T., Deretic V.;
"TRIM proteins regulate autophagy and can target autophagic substrates
by direct recognition.";
Dev. Cell 30:394-409(2014).
[25]
INTERACTION WITH BECN1; IRF3; MEFV AND TRIM21.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
[26]
VARIANTS [LARGE SCALE ANALYSIS] MET-290; LEU-298; LEU-478; MET-503;
LEU-665; LEU-714 AND CYS-784.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. May also phosphorylate SESN2 and SQSTM1 to
regulate autophagy (PubMed:25040165).
{ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:21460634,
ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:25040165}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: 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. Interacts (phosphorylated form)
with TRIM5 (PubMed:25127057). When phosphorylated at Ser-317,
interacts with MEFV and BECN1 simultaneously. Interacts with
TRIM21 and IRF3, in the presence of TRIM21 (PubMed:26347139).
Interacts with SESN2 (PubMed:25040165). Interacts with SQSTM1
(PubMed:25040165). {ECO:0000269|PubMed:11146101,
ECO:0000269|PubMed:18936157, ECO:0000269|PubMed:19211835,
ECO:0000269|PubMed:19287211, ECO:0000269|PubMed:19597335,
ECO:0000269|PubMed:21795849, ECO:0000269|PubMed:22354037,
ECO:0000269|PubMed:22613832, ECO:0000269|PubMed:25040165,
ECO:0000269|PubMed:25127057, ECO:0000269|PubMed:26347139}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-908831, EBI-908831;
Q9C0C7:AMBRA1; NbExp=3; IntAct=EBI-908831, EBI-2512975;
Q9C0C7-3:AMBRA1; NbExp=4; IntAct=EBI-908831, EBI-16042318;
O75143:ATG13; NbExp=10; IntAct=EBI-908831, EBI-2798775;
Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-908831, EBI-746969;
P60520:GABARAPL2; NbExp=3; IntAct=EBI-908831, EBI-720116;
P42858:HTT; NbExp=8; IntAct=EBI-908831, EBI-466029;
Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-908831, EBI-373144;
Q9BXW4:MAP1LC3C; NbExp=3; IntAct=EBI-908831, EBI-2603996;
P42345:MTOR; NbExp=7; IntAct=EBI-908831, EBI-359260;
P04629:NTRK1; NbExp=2; IntAct=EBI-908831, EBI-1028226;
Q8TDY2:RB1CC1; NbExp=9; IntAct=EBI-908831, EBI-1047793;
Q8N122:RPTOR; NbExp=3; IntAct=EBI-908831, EBI-1567928;
Q9P2M4:TBC1D14; NbExp=4; IntAct=EBI-908831, EBI-2797718;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-908831, EBI-359276;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
Preautophagosomal structure {ECO:0000250}. 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.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Detected in the
following adult tissues: skeletal muscle, heart, pancreas, brain,
placenta, liver, kidney, and lung.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:21205641}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. APG1/unc-51/ULK1 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAA34442.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF045458; AAC32326.1; -; mRNA.
EMBL; AB018265; BAA34442.2; ALT_INIT; mRNA.
EMBL; AC131009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS9274.1; -.
RefSeq; NP_003556.1; NM_003565.2.
UniGene; Hs.47061; -.
PDB; 4WNO; X-ray; 1.56 A; A=1-283.
PDB; 4WNP; X-ray; 1.88 A; A/B/C/D=1-283.
PDB; 5CI7; X-ray; 1.74 A; A=1-283.
PDBsum; 4WNO; -.
PDBsum; 4WNP; -.
PDBsum; 5CI7; -.
ProteinModelPortal; O75385; -.
SMR; O75385; -.
BioGrid; 113996; 50.
CORUM; O75385; -.
DIP; DIP-35196N; -.
IntAct; O75385; 40.
MINT; MINT-1892187; -.
STRING; 9606.ENSP00000324560; -.
BindingDB; O75385; -.
ChEMBL; CHEMBL6006; -.
GuidetoPHARMACOLOGY; 2271; -.
iPTMnet; O75385; -.
PhosphoSitePlus; O75385; -.
SwissPalm; O75385; -.
BioMuta; ULK1; -.
EPD; O75385; -.
MaxQB; O75385; -.
PaxDb; O75385; -.
PeptideAtlas; O75385; -.
PRIDE; O75385; -.
DNASU; 8408; -.
Ensembl; ENST00000321867; ENSP00000324560; ENSG00000177169.
GeneID; 8408; -.
KEGG; hsa:8408; -.
UCSC; uc001uje.4; human.
CTD; 8408; -.
DisGeNET; 8408; -.
EuPathDB; HostDB:ENSG00000177169.9; -.
GeneCards; ULK1; -.
HGNC; HGNC:12558; ULK1.
HPA; HPA063990; -.
MIM; 603168; gene.
neXtProt; NX_O75385; -.
OpenTargets; ENSG00000177169; -.
PharmGKB; PA37198; -.
eggNOG; KOG0595; Eukaryota.
eggNOG; ENOG410XR01; LUCA.
GeneTree; ENSGT00900000140878; -.
HOGENOM; HOG000044146; -.
HOVERGEN; HBG000342; -.
InParanoid; O75385; -.
KO; K21357; -.
OMA; DTDDFVM; -.
OrthoDB; EOG091G14RD; -.
PhylomeDB; O75385; -.
TreeFam; TF324551; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-8854214; TBC/RABGAPs.
Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
SignaLink; O75385; -.
SIGNOR; O75385; -.
ChiTaRS; ULK1; human.
GeneWiki; ULK1; -.
GenomeRNAi; 8408; -.
PRO; PR:O75385; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000177169; -.
CleanEx; HS_ULK1; -.
Genevisible; O75385; HS.
GO; GO:1990316; C:ATG1/ULK1 kinase complex; IPI:UniProtKB.
GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0097635; C:extrinsic component of autophagosome membrane; IDA:UniProtKB.
GO; GO:0097629; C:extrinsic component of omegasome membrane; IDA:UniProtKB.
GO; GO:0097632; C:extrinsic component of pre-autophagosomal structure membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0034045; C:pre-autophagosomal structure membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IPI:BHF-UCL.
GO; GO:0006914; P:autophagy; IDA:UniProtKB.
GO; GO:0075044; P:autophagy of host cells involved in interaction with symbiont; IGI:UniProtKB.
GO; GO:0048675; P:axon extension; IBA:GO_Central.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; IMP:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0031333; P:negative regulation of protein complex assembly; IDA:ParkinsonsUK-UCL.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0031102; P:neuron projection regeneration; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:HGNC.
GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0008104; P:protein localization; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016237; Ser/Thr_kin_STPK_Ulk-1/2.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR022708; Ser/Thr_kinase_C.
Pfam; PF12063; DUF3543; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000580; Ser/Thr_PK_STPK_ULK-1/2; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autophagy; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 1050 Serine/threonine-protein kinase ULK1.
/FTId=PRO_0000086780.
DOMAIN 16 278 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 22 30 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 287 416 Interaction with GABARAP and GABARAPL2.
{ECO:0000269|PubMed:11146101}.
REGION 828 1050 C-terminal domain; mediates interaction
with SESN2.
{ECO:0000269|PubMed:25040165}.
COMPBIAS 297 310 Poly-Ser.
ACT_SITE 138 138 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 46 46 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 317 317 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O70405}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 456 456 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000250|UniProtKB:O70405}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 575 575 Phosphothreonine.
{ECO:0000250|UniProtKB:O70405}.
MOD_RES 636 636 Phosphothreonine.
{ECO:0000250|UniProtKB:O70405}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000250|UniProtKB:O70405}.
MOD_RES 758 758 Phosphoserine; by MTOR.
{ECO:0000244|PubMed:23186163,
ECO:0000305|PubMed:21205641}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 290 290 V -> M (in an ovarian mucinous carcinoma
sample; somatic mutation;
dbSNP:rs370624303).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041274.
VARIANT 298 298 S -> L (in dbSNP:rs56364352).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041275.
VARIANT 478 478 P -> L (in dbSNP:rs12827141).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041276.
VARIANT 503 503 T -> M (in dbSNP:rs55824543).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041277.
VARIANT 665 665 S -> L (in dbSNP:rs55815560).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041278.
VARIANT 714 714 P -> L (in dbSNP:rs11546871).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041279.
VARIANT 784 784 S -> C (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041280.
VARIANT 816 816 T -> A (in dbSNP:rs11609348).
{ECO:0000269|PubMed:9693035,
ECO:0000269|PubMed:9872452}.
/FTId=VAR_054892.
STRAND 9 11 {ECO:0000244|PDB:4WNO}.
STRAND 14 24 {ECO:0000244|PDB:4WNO}.
STRAND 29 37 {ECO:0000244|PDB:4WNO}.
STRAND 42 47 {ECO:0000244|PDB:4WNO}.
HELIX 50 52 {ECO:0000244|PDB:4WNO}.
HELIX 53 67 {ECO:0000244|PDB:4WNO}.
STRAND 78 83 {ECO:0000244|PDB:4WNO}.
STRAND 88 93 {ECO:0000244|PDB:4WNO}.
HELIX 100 106 {ECO:0000244|PDB:4WNO}.
HELIX 112 132 {ECO:0000244|PDB:4WNO}.
HELIX 141 143 {ECO:0000244|PDB:4WNO}.
STRAND 144 147 {ECO:0000244|PDB:4WNO}.
HELIX 151 153 {ECO:0000244|PDB:4WNP}.
HELIX 156 158 {ECO:0000244|PDB:4WNO}.
STRAND 160 163 {ECO:0000244|PDB:4WNO}.
TURN 185 187 {ECO:0000244|PDB:4WNO}.
HELIX 190 193 {ECO:0000244|PDB:4WNO}.
HELIX 201 216 {ECO:0000244|PDB:4WNO}.
HELIX 226 235 {ECO:0000244|PDB:4WNO}.
HELIX 249 258 {ECO:0000244|PDB:4WNO}.
TURN 263 265 {ECO:0000244|PDB:4WNO}.
HELIX 269 273 {ECO:0000244|PDB:4WNO}.
HELIX 276 278 {ECO:0000244|PDB:4WNO}.
SEQUENCE 1050 AA; 112631 MW; AED9BD5139F2DB92 CRC64;
MEPGRGGTET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK KNLAKSQTLL
GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL ADYLHAMRTL SEDTIRLFLQ
QIAGAMRLLH SKGIIHRDLK PQNILLSNPA GRRANPNSIR VKIADFGFAR YLQSNMMAAT
LCGSPMYMAP EVIMSQHYDG KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV
PTIPRETSAP LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA SPSVRKSPPV PVPSYPSSGS
GSSSSSSSTS HLASPPSLGE MQQLQKTLAS PADTAGFLHS SRDSGGSKDS SCDTDDFVMV
PAQFPGDLVA EAPSAKPPPD SLMCSGSSLV ASAGLESHGR TPSPSPPCSS SPSPSGRAGP
FSSSRCGASV PIPVPTQVQN YQRIERNLQS PTQFQTPRSS AIRRSGSTSP LGFARASPSP
PAHAEHGGVL ARKMSLGGGR PYTPSPQVGT IPERPGWSGT PSPQGAEMRG GRSPRPGSSA
PEHSPRTSGL GCRLHSAPNL SDLHVVRPKL PKPPTDPLGA VFSPPQASPP QPSHGLQSCR
NLRGSPKLPD FLQRNPLPPI LGSPTKAVPS FDFPKTPSSQ NLLALLARQG VVMTPPRNRT
LPDLSEVGPF HGQPLGPGLR PGEDPKGPFG RSFSTSRLTD LLLKAAFGTQ APDPGSTESL
QEKPMEIAPS AGFGGSLHPG ARAGGTSSPS PVVFTVGSPP SGSTPPQGPR TRMFSAGPTG
SASSSARHLV PGPCSEAPAP ELPAPGHGCS FADPITANLE GAVTFEAPDL PEETLMEQEH
TEILRGLRFT LLFVQHVLEI AALKGSASEA AGGPEYQLQE SVVADQISLL SREWGFAEQL
VLYLKVAELL SSGLQSAIDQ IRAGKLCLSS TVKQVVRRLN ELYKASVVSC QGLSLRLQRF
FLDKQRLLDR IHSITAERLI FSHAVQMVQS AALDEMFQHR EGCVPRYHKA LLLLEGLQHM
LSDQADIENV TKCKLCIERR LSALLTGICA


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