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Q9QY01 (ULK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase ULK2

EC=2.7.11.1
Alternative name(s):
Serine/threonine-protein kinase Unc51.2
Unc-51-like kinase 2
Gene names
Name:Ulk2
Synonyms:Kiaa0623
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1037 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 a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and RPTOR; however such data need additional evidences. Not involved in ammonia-induced autophagy or in autophagic response of cerebellar granule neurons (CGN) to low potassium concentration. Plays a role early in neuronal differentiation and is required for granule cell axon formation: may govern axon formation via Ras-like GTPase signaling and through regulation of the Rab5-mediated endocytic pathways within developing axons. Ref.1 Ref.8 Ref.9 Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Component of a complex consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-terminus) with ATG13/KIAA0652. Associates with the mammalian target of rapamycin complex 1 (mTORC1) through an interaction with RPTOR By similarity. Interacts with SYNGAP1. Ref.7 Ref.9

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein. Note: Localizes to pre-autophagosomal membrane. Ref.9

Tissue specificity

Widely expressed. Ref.2

Domain

The CTD-like region mediates membrane-binding and incorporation into large protein complexes By similarity.

Post-translational modification

Autophosphorylated. In response to nutrient limitation, probably phosphorylated and activated by AMPK, leading to activate autophagy. Ref.2 Ref.11

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 BAC65613.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10371037Serine/threonine-protein kinase ULK2
PRO_0000086783

Regions

Domain9 – 271263Protein kinase
Nucleotide binding15 – 239ATP By similarity
Region813 – 1037225CTD-like region By similarity

Sites

Active site1311Proton acceptor By similarity
Binding site391ATP Probable

Experimental info

Mutagenesis391K → T: Decreased kinase activity. Ref.9
Sequence conflict9981L → V in BAA77341. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QY01 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2E7DC3B0B87E9607

FASTA1,037112,877
        10         20         30         40         50         60 
MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ ILLGKEIKIL 

        70         80         90        100        110        120 
KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK GTLSEDTIRV FLHQIAAAMR 

       130        140        150        160        170        180 
ILHSKGIIHR DLKPQNILLS YANRRKSNVS GIRIKIADFG FARYLHSNTM AATLCGSPMY 

       190        200        210        220        230        240 
MAPEVIMSQH YDAKADLWSI GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET 

       250        260        270        280        290        300 
SPYLANLLLG LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP 

       310        320        330        340        350        360 
SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT DDFVLVPHNI 

       370        380        390        400        410        420 
SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP IPVPTQVRNY QRIEQNLIST 

       430        440        450        460        470        480 
ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL 

       490        500        510        520        530        540 
VGTIPEQFSQ CCCGHPQGHE ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ 

       550        560        570        580        590        600 
KLRKQHSDPV CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS 

       610        620        630        640        650        660 
PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG SERHRSEQQQ 

       670        680        690        700        710        720 
SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD VAPAGACGVM LALPAGTAAS 

       730        740        750        760        770        780 
ARAVLFTVGS PPHSATAPTC THMVLRTRTT SVGSSSSGGS LCSASGRVCV GSPPGPGLGS 

       790        800        810        820        830        840 
SPPGAEGAPS LRYVPYGASP PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC 

       850        860        870        880        890        900 
VLDLTAVRGG NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL 

       910        920        930        940        950        960 
HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK QRFIDEINSV 

       970        980        990       1000       1010       1020 
TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL EGLSKILQDP TDVENVHKYK 

      1030 
CSIERRLSAL CCSTATV 

« Hide

References

« Hide 'large scale' references
[1]"A mouse serine/threonine kinase homologous to C. elegans UNC51 functions in parallel fiber formation of cerebellar granule neurons."
Tomoda T., Bhatt R.S., Kuroyanagi H., Shirasawa T., Hatten M.E.
Neuron 24:833-846(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: C57BL/6J.
Tissue: Brain.
[2]"Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains."
Yan J., Kuroyanagi H., Tomemori T., Okazaki N., Asato K., Matsuda Y., Suzuki Y., Ohshima Y., Mitani S., Masuho Y., Shirasawa T., Muramatsu M.
Oncogene 18:5850-5859(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[7]"Role of Unc51.1 and its binding partners in CNS axon outgrowth."
Tomoda T., Kim J.H., Zhan C., Hatten M.E.
Genes Dev. 18:541-558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNGAP1.
[8]"UNC-51-like kinase regulation of fibroblast growth factor receptor substrate 2/3."
Avery A.W., Figueroa C., Vojtek A.B.
Cell. Signal. 19:177-184(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2 AND FRS3.
[9]"FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells."
Hara T., Takamura A., Kishi C., Iemura S., Natsume T., Guan J.L., Mizushima N.
J. Cell Biol. 181:497-510(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RB1CC1, MUTAGENESIS OF LYS-39.
[10]"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.
[11]"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
Kim J., Kundu M., Viollet B., Guan K.L.
Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY AMPK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF145922 mRNA. Translation: AAF18325.1.
AB019577 mRNA. Translation: BAA77341.1.
AK146620 mRNA. Translation: BAE27309.1.
AK122331 mRNA. Translation: BAC65613.2. Different initiation.
BC046778 mRNA. Translation: AAH46778.1.
BC053029 mRNA. Translation: AAH53029.1.
CCDSCCDS24820.1.
RefSeqNP_038909.3. NM_013881.4.
UniGeneMm.162025.

3D structure databases

ProteinModelPortalQ9QY01.
SMRQ9QY01. Positions 9-317.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QY01.

Proteomic databases

PRIDEQ9QY01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004920; ENSMUSP00000004920; ENSMUSG00000004798.
GeneID29869.
KEGGmmu:29869.
UCSCuc007jih.2. mouse.

Organism-specific databases

CTD9706.
MGIMGI:1352758. Ulk2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117559.
HOGENOMHOG000044146.
HOVERGENHBG000342.
InParanoidQ9QY01.
KOK08269.
OMAGTIPEQF.
OrthoDBEOG7K0ZBF.
PhylomeDBQ9QY01.
TreeFamTF324551.

Gene expression databases

BgeeQ9QY01.
CleanExMM_ULK2.
GenevestigatorQ9QY01.

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

NextBio307094.
PROQ9QY01.
SOURCESearch...

Entry information

Entry nameULK2_MOUSE
AccessionPrimary (citable) accession number: Q9QY01
Secondary accession number(s): Q80TV7, Q9WTP4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot