O75385 (ULK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ULK1
Synonyms:	KIAA0722

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1050 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14 Ref.17 Ref.18
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with GABARAP and GABARAPL2. Interacts (via C-terminus) with ATG13/KIAA0652. Part of a complex consisting of ATG13/KIAA0652, 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. Ref.5 Ref.12 Ref.13 Ref.14 Ref.18
Subcellular location	Cytoplasm › cytosol 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.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.15 Ref.16 Ref.17 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 process	Autophagy
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of autophagy Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.14. Source: UniProtKB protein localization Inferred from mutant phenotype. Source: UniProtKB
Cellular component	ULK1-ATG13-FIP200 complex Inferred from physical interaction Ref.13. Source: UniProtKB autophagic vacuole Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay Ref.5. Source: UniProtKB pre-autophagosomal structure membrane Inferred from direct assay Ref.14. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein complex binding Inferred from physical interaction Ref.13. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL1	Q9H0R8	2	EBI-908831,EBI-746969
GABARAPL2	P60520	3	EBI-908831,EBI-720116
MAP1LC3B	Q9GZQ8	2	EBI-908831,EBI-373144
MAP1LC3C	Q9BXW4	2	EBI-908831,EBI-2603996
RB1CC1	Q8TDY2	4	EBI-908831,EBI-1047793

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1050	1050	Serine/threonine-protein kinase ULK1		PRO_0000086780
Regions
	Domain	16 – 278	263	Protein kinase
	Nucleotide binding	22 – 30	9	ATP By similarity
	Region	287 – 416	130	Interaction with GABARAP and GABARAPL2
	Compositional bias	297 – 310	14	Poly-Ser
Sites
	Active site	138	1	Proton acceptor By similarity
	Binding site	46	1	ATP By similarity
Amino acid modifications
	Modified residue	317	1	Phosphoserine; by AMPK By similarity
	Modified residue	450	1	Phosphoserine Ref.9 Ref.10 Ref.15 Ref.16
	Modified residue	456	1	Phosphothreonine Ref.10
	Modified residue	467	1	Phosphoserine By similarity
	Modified residue	469	1	Phosphoserine Ref.16
	Modified residue	477	1	Phosphoserine Ref.9
	Modified residue	479	1	Phosphoserine Ref.9
	Modified residue	556	1	Phosphoserine; by AMPK Probable
	Modified residue	575	1	Phosphothreonine By similarity
	Modified residue	623	1	Phosphoserine Ref.16
	Modified residue	625	1	Phosphothreonine By similarity
	Modified residue	638	1	Phosphoserine; by AMPK By similarity
	Modified residue	717	1	Phosphothreonine Ref.11
	Modified residue	758	1	Phosphoserine; by MTOR Probable
Natural variations
	Natural variant	290	1	V → M in an ovarian mucinous carcinoma sample; somatic mutation. Ref.20		VAR_041274
	Natural variant	298	1	S → L. Ref.20 Corresponds to variant rs56364352 [ dbSNP | Ensembl ].		VAR_041275
	Natural variant	478	1	P → L. Ref.20 Corresponds to variant rs12827141 [ dbSNP | Ensembl ].		VAR_041276
	Natural variant	503	1	T → M. Ref.20 Corresponds to variant rs55824543 [ dbSNP | Ensembl ].		VAR_041277
	Natural variant	665	1	S → L. Ref.20 Corresponds to variant rs55815560 [ dbSNP | Ensembl ].		VAR_041278
	Natural variant	714	1	P → L. Ref.20 Corresponds to variant rs11546871 [ dbSNP | Ensembl ].		VAR_041279
	Natural variant	784	1	S → C in a lung adenocarcinoma sample; somatic mutation. Ref.20		VAR_041280
	Natural variant	816	1	T → A. Ref.1 Ref.2 Corresponds to variant rs11609348 [ dbSNP | Ensembl ].		VAR_054892

Sequences

	Sequence		Length	Mass (Da)
	O75385 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: AED9BD5139F2DB92	FASTA	1,050	112,631
	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

References

	« Hide 'large scale' referencesShow '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: 9693035] [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: 9872452] [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: 12168954] [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: 16541075] [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: 11146101] [Abstract] Cited for: INTERACTION WITH GABARAP AND GABARAPL2.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-477 AND SER-479, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; THR-456 AND SER-556, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-717, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"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: 19597335] [Abstract] Cited for: SUBUNIT.
[13]	"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: 19211835] [Abstract] Cited for: SUBUNIT, INTERACTION WITH RPTOR AND TORC1 COMPLEX.
[14]	"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: 18936157] [Abstract] Cited for: FUNCTION, INTERACTION WITH ATG13.
[15]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, MASS SPECTROMETRY.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-469; SER-623; SER-638 AND SER-758, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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: 21460634] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF AMPK.
[18]	"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: 21795849] [Abstract] Cited for: FUNCTION, INTERACTION WITH RPTOR.
[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: 21205641] [Abstract] Cited for: PHOSPHORYLATION BY AMPK.
[20]	"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: 17344846] [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.
IPI	IPI00289357.
RefSeq	NP_003556.1. NM_003565.2.
UniGene	Hs.47061.
3D structure databases
ProteinModelPortal	O75385.
SMR	O75385. Positions 15-281.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75385. 21 interactions.
MINT	MINT-1892187.
STRING	O75385.
PTM databases
PhosphoSite	O75385.
Proteomic databases
PRIDE	O75385.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000321867; ENSP00000324560; ENSG00000177169.
GeneID	8408.
KEGG	hsa:8408.
UCSC	uc001uje.1. human.
Organism-specific databases
CTD	8408.
GeneCards	GC12P132379.
H-InvDB	HIX0019606.
HGNC	HGNC:12558. ULK1.
MIM	603168. gene.
neXtProt	NX_O75385.
PharmGKB	PA37198.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07636.
GeneTree	ENSGT00570000078909.
HOGENOM	HBG446996.
HOVERGEN	HBG000342.
InParanoid	O75385.
OMA	LHSLRFT.
OrthoDB	EOG4NS39T.
PhylomeDB	O75385.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Gene expression databases
ArrayExpress	O75385.
Bgee	O75385.
CleanEx	HS_ULK1.
Genevestigator	O75385.
GermOnline	ENSG00000177169. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR016237. Ser/Thr_kin_STPK_Ulk-1/2. IPR008271. Ser/Thr_kinase_AS. IPR022708. Ser/Thr_kinase_C. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K08269.
Pfam	PF12063. DUF3543. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view]
PIRSF	PIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	31476.
SOURCE	Search...

Entry information

Entry name

ULK1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.