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Serine/threonine-protein kinase ULK1 (EC 2.7.11.1) (Serine/threonine-protein kinase Unc51.1) (Unc-51-like kinase 1)

 ULK1_MOUSE              Reviewed;        1051 AA.
O70405; Q6PGB2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
23-MAY-2018, entry version 158.
RecName: Full=Serine/threonine-protein kinase ULK1;
EC=2.7.11.1;
AltName: Full=Serine/threonine-protein kinase Unc51.1;
AltName: Full=Unc-51-like kinase 1;
Name=Ulk1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9600096; DOI=10.1006/bbrc.1998.8546;
Yan J., Kuroyanagi H., Kuroiwa A., Matsuda Y., Tokumitsu H.,
Tomoda T., Shirasawa T., Muramatsu M.-A.;
"Identification of mouse ULK1, a novel protein kinase structurally
related to C. elegans UNC-51.";
Biochem. Biophys. Res. Commun. 246:222-227(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=10624947; DOI=10.1016/S0896-6273(00)81031-4;
Tomoda T., Bhatt R.S., Kuroyanagi H., Shirasawa T., Hatten M.E.;
"A mouse serine/threonine kinase homologous to C. elegans UNC51
functions in parallel fiber formation of cerebellar granule neurons.";
Neuron 24:833-846(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH ATG13 AND RB1CC1, PHOSPHORYLATION, AND
SUBCELLULAR LOCATION.
PubMed=19258318; DOI=10.1074/jbc.M900573200;
Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.;
"ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential
for autophagy.";
J. Biol. Chem. 284:12297-12305(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-521; THR-635;
SER-637; SER-638 AND SER-757, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
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).
[7]
FUNCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-317; SER-757 AND
SER-777, AND MUTAGENESIS OF LYS-46; SER-317; SER-494; SER-555;
THR-574; SER-622; THR-624; SER-693; SER-757; SER-777 AND SER-811.
PubMed=21258367; DOI=10.1038/ncb2152;
Kim J., Kundu M., Viollet B., Guan K.L.;
"AMPK and mTOR regulate autophagy through direct phosphorylation of
Ulk1.";
Nat. Cell Biol. 13:132-141(2011).
[8]
FUNCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-467; SER-555;
THR-574 AND SER-637, AND MUTAGENESIS OF LYS-46.
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).
[9]
FUNCTION, AND INTERACTION WITH SESN2 AND SQSTM1.
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).
-!- 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:10624947, ECO:0000269|PubMed:19258318,
ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367,
ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:25040165}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with GABARAP and GABARAPL2 (By similarity).
Interacts (via C-terminus) with ATG13 (PubMed:19258318). Part of a
complex consisting of ATG13, ATG101, ULK1 and RB1CC1
(PubMed:19258318). 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 (By similarity). Interacts with FEZ1; SCOC
interferes with FEZ1-binding (By similarity). Interacts with
TBC1D14 (By similarity). Interacts (phosphorylated form) with
TRIM5 (By similarity). When phosphorylated at Ser-317, interacts
with MEFV and BECN1 simultaneously. Interacts with TRIM21 and
IRF3, in the presence of TRIM21 (By similarity). Interacts with
SESN2 (PubMed:25040165). Interacts with SQSTM1 (PubMed:25040165).
Interacts with C9orf72 (By similarity).
{ECO:0000250|UniProtKB:O75385, ECO:0000269|PubMed:19258318,
ECO:0000269|PubMed:25040165}.
-!- INTERACTION:
Q8IVP5:FUNDC1 (xeno); NbExp=3; IntAct=EBI-8390771, EBI-3059266;
Q9DB70:Fundc1; NbExp=2; IntAct=EBI-8390771, EBI-10106464;
P42859:Htt; NbExp=4; IntAct=EBI-8390771, EBI-5327353;
Q9JLN9:Mtor; NbExp=3; IntAct=EBI-8390771, EBI-1571628;
P58004:SESN2 (xeno); NbExp=5; IntAct=EBI-8390771, EBI-3939642;
Q13501:SQSTM1 (xeno); NbExp=2; IntAct=EBI-8390771, EBI-307104;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:19258318}. Preautophagosomal structure
{ECO:0000269|PubMed:19258318}. 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.
-!- PTM: Autophosphorylated. Phosphorylated under nutrient-rich
conditions; dephosphorylated during starvation or following
treatment with rapamycin. In response to nutrient limitation,
phosphorylated and activated by AMPK, leading to activate
autophagy. Under nutrient sufficiency, phosphorylated by
MTOR/mTOR, disrupting the interaction with AMPK and preventing
activation of ULK1. {ECO:0000269|PubMed:19258318,
ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. APG1/unc-51/ULK1 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; AF053756; AAC40118.1; -; mRNA.
EMBL; AF072370; AAF23317.1; -; mRNA.
EMBL; BC057121; AAH57121.1; -; mRNA.
CCDS; CCDS19532.1; -.
PIR; JW0051; JW0051.
RefSeq; NP_033495.2; NM_009469.3.
UniGene; Mm.271898; -.
ProteinModelPortal; O70405; -.
SMR; O70405; -.
BioGrid; 204438; 6.
DIP; DIP-60541N; -.
IntAct; O70405; 16.
MINT; O70405; -.
STRING; 10090.ENSMUSP00000031490; -.
iPTMnet; O70405; -.
PhosphoSitePlus; O70405; -.
MaxQB; O70405; -.
PaxDb; O70405; -.
PeptideAtlas; O70405; -.
PRIDE; O70405; -.
GeneID; 22241; -.
KEGG; mmu:22241; -.
UCSC; uc008yrq.1; mouse.
CTD; 8408; -.
MGI; MGI:1270126; Ulk1.
eggNOG; KOG0595; Eukaryota.
eggNOG; ENOG410XR01; LUCA.
HOGENOM; HOG000044146; -.
HOVERGEN; HBG000342; -.
InParanoid; O70405; -.
KO; K21357; -.
PhylomeDB; O70405; -.
TreeFam; TF324551; -.
BRENDA; 2.7.11.1; 3474.
ChiTaRS; Ulk1; mouse.
PRO; PR:O70405; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ULK1; -.
GO; GO:1990316; C:Atg1/ULK1 kinase complex; IDA:MGI.
GO; GO:0005776; C:autophagosome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0097635; C:extrinsic component of autophagosome membrane; ISO:MGI.
GO; GO:0097629; C:extrinsic component of omegasome membrane; ISO:MGI.
GO; GO:0097632; C:extrinsic component of phagophore assembly site membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0051879; F:Hsp90 protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0075044; P:autophagy of host cells involved in interaction with symbiont; ISO:MGI.
GO; GO:0048675; P:axon extension; IMP:MGI.
GO; GO:0007409; P:axonogenesis; IDA:MGI.
GO; GO:0034198; P:cellular response to amino acid starvation; IGI:ParkinsonsUK-UCL.
GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB.
GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
GO; GO:0016236; P:macroautophagy; IMP:MGI.
GO; GO:0000423; P:mitophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:MGI.
GO; GO:0031333; P:negative regulation of protein complex assembly; ISO:MGI.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0008104; P:protein localization; ISS:UniProtKB.
GO; GO:0021933; P:radial glia guided migration of cerebellar granule cell; IMP:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
GO; GO:0031623; P:receptor internalization; IMP:MGI.
GO; GO:0010941; P:regulation of cell death; IGI:ParkinsonsUK-UCL.
GO; GO:0010468; P:regulation of gene expression; IGI:ParkinsonsUK-UCL.
GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; IMP:MGI.
GO; GO:0098780; P:response to mitochondrial depolarisation; IMP:BHF-UCL.
GO; GO:0042594; P:response to starvation; IDA:UniProtKB.
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;
ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 1051 Serine/threonine-protein kinase ULK1.
/FTId=PRO_0000086781.
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:0000250|UniProtKB:O75385}.
REGION 829 1051 C-terminal domain; mediates interaction
with SESN2.
{ECO:0000250|UniProtKB:O75385}.
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:0000305}.
MOD_RES 317 317 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:21258367}.
MOD_RES 403 403 Phosphoserine.
{ECO:0000250|UniProtKB:O75385}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 456 456 Phosphothreonine.
{ECO:0000250|UniProtKB:O75385}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000269|PubMed:21205641}.
MOD_RES 477 477 Phosphoserine.
{ECO:0000250|UniProtKB:O75385}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000250|UniProtKB:O75385}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 555 555 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:21205641}.
MOD_RES 574 574 Phosphothreonine.
{ECO:0000269|PubMed:21205641}.
MOD_RES 635 635 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 637 637 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:21205641}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 757 757 Phosphoserine; by MTOR.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:21258367}.
MOD_RES 774 774 Phosphoserine.
{ECO:0000250|UniProtKB:O75385}.
MOD_RES 777 777 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 46 46 K->R: Loss of kinase activity and
autophosphorylation.
{ECO:0000269|PubMed:21205641,
ECO:0000269|PubMed:21258367}.
MUTAGEN 317 317 S->A: Impairs phosphorylation by AMPK and
ability to promote autophagy; when
associated with A-777.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 494 494 S->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 555 555 S->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 574 574 T->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 622 622 S->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 624 624 T->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 693 693 S->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 757 757 S->A,D: Impairs interaction with AMPK and
subsequent phosphorylation by AMPK.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 777 777 S->A: Impairs phosphorylation by AMPK and
ability to promote autophagy; when
associated with A-317.
{ECO:0000269|PubMed:21258367}.
MUTAGEN 811 811 S->A: Does not affect phosphorylation by
AMPK in vitro.
{ECO:0000269|PubMed:21258367}.
CONFLICT 469 469 T -> S (in Ref. 3; AAH57121).
{ECO:0000305}.
SEQUENCE 1051 AA; 112463 MW; 99B021985FB4E8A0 CRC64;
MEPGRGGVET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK KNLAKSQTLL
GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL ADYLHTMRTL SEDTVRLFLQ
QIAGAMRLLH SKGIIHRDLK PQNILLSNPG GRRANPSNIR VKIADFGFAR YLQSNMMAAT
LCGSPMYMAP EVIMSQHYDG KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV
PAIPRETSAP LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA STPIKKSPPV PVPSYPSSGS
GSSSSSSSAS HLASPPSLGE MPQLQKTLTS PADAAGFLQG SRDSGGSSKD SCDTDDFVMV
PAQFPGDLVA EAASAKPPPD SLLCSGSSLV ASAGLESHGR TPSPSPTCSS SPSPSGRPGP
FSSNRYGASV PIPVPTQVHN YQRIEQNLQS PTQQQTARSS AIRRSGSTTP LGFGRASPSP
PSHTDGAMLA RKLSLGGGRP YTPSPQVGTI PERPSWSRVP SPQGADVRVG RSPRPGSSVP
EHSPRTTGLG CRLHSAPNLS DFHVVRPKLP KPPTDPLGAT FSPPQTSAPQ PCPGLQSCRP
LRGSPKLPDF LQRSPLPPIL GSPTKAGPSF DFPKTPSSQN LLTLLARQGV VMTPPRNRTL
PDLSEASPFH GQQLGSGLRP AEDTRGPFGR SFSTSRITDL LLKAAFGTQA SDSGSTDSLQ
EKPMEIAPSA GFGGTLHPGA RGGGASSPAP VVFTVGSPPS GATPPQSTRT RMFSVGSSSS
LGSTGSSSAR HLVPGACGEA PELSAPGHCC SLADPLAANL EGAVTFEAPD LPEETLMEQE
HTETLHSLRF TLAFAQQVLE IAALKGSASE AAGGPEYQLQ ESVVADQISQ LSREWGFAEQ
LVLYLKVAEL LSSGLQTAID QIRAGKLCLS STVKQVVRRL NELYKASVVS CQGLSLRLQR
FFLDKQRLLD GIHGVTAERL ILSHAVQMVQ SAALDEMFQH REGCVPRYHK ALLLLEGLQH
TLTDQADIEN IAKCKLCIER RLSALLSGVY A


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