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Q9QY01

- ULK2_MOUSE

UniProt

Q9QY01 - ULK2_MOUSE

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Protein
Serine/threonine-protein kinase ULK2
Gene
Ulk2, Kiaa0623
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391ATP Inferred
Active sitei131 – 1311Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. axon extension Source: MGI
  3. negative regulation of collateral sprouting Source: MGI
  4. protein autophosphorylation Source: Ensembl
  5. regulation of autophagy Source: UniProtKB
  6. response to starvation Source: UniProtKB
  7. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Autophagy, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ulk2
Synonyms:Kiaa0623
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1352758. Ulk2.

Subcellular locationi

Cytoplasmic vesicle membrane; Peripheral membrane protein
Note: Localizes to pre-autophagosomal membrane.1 Publication

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. pre-autophagosomal structure membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391K → T: Decreased kinase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10371037Serine/threonine-protein kinase ULK2
PRO_0000086783Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9QY01.

PTM databases

PhosphoSiteiQ9QY01.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9QY01.
CleanExiMM_ULK2.
GenevestigatoriQ9QY01.

Interactioni

Subunit structurei

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 SYNGAP1.2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ9QY01.
SMRiQ9QY01. Positions 9-317.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 271263Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni813 – 1037225CTD-like region By similarity
Add
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117559.
HOGENOMiHOG000044146.
HOVERGENiHBG000342.
InParanoidiQ9QY01.
KOiK08269.
OMAiGTIPEQF.
OrthoDBiEOG7K0ZBF.
PhylomeDBiQ9QY01.
TreeFamiTF324551.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF12063. DUF3543. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QY01-1 [UniParc]FASTAAdd to Basket

« Hide

MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ     50
ILLGKEIKIL KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK 100
GTLSEDTIRV FLHQIAAAMR ILHSKGIIHR DLKPQNILLS YANRRKSNVS 150
GIRIKIADFG FARYLHSNTM AATLCGSPMY MAPEVIMSQH YDAKADLWSI 200
GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET SPYLANLLLG 250
LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP 300
SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT 350
DDFVLVPHNI SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP 400
IPVPTQVRNY QRIEQNLIST ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG 450
SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL VGTIPEQFSQ CCCGHPQGHE 500
ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ KLRKQHSDPV 550
CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS 600
PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG 650
SERHRSEQQQ SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD 700
VAPAGACGVM LALPAGTAAS ARAVLFTVGS PPHSATAPTC THMVLRTRTT 750
SVGSSSSGGS LCSASGRVCV GSPPGPGLGS SPPGAEGAPS LRYVPYGASP 800
PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC VLDLTAVRGG 850
NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL 900
HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK 950
QRFIDEINSV TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL 1000
EGLSKILQDP TDVENVHKYK CSIERRLSAL CCSTATV 1037
Length:1,037
Mass (Da):112,877
Last modified:May 1, 2000 - v1
Checksum:i2E7DC3B0B87E9607
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti998 – 9981L → V in BAA77341. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24820.1.
RefSeqiNP_038909.3. NM_013881.4.
UniGeneiMm.162025.

Genome annotation databases

EnsembliENSMUST00000004920; ENSMUSP00000004920; ENSMUSG00000004798.
GeneIDi29869.
KEGGimmu:29869.
UCSCiuc007jih.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24820.1.
RefSeqi NP_038909.3. NM_013881.4.
UniGenei Mm.162025.

3D structure databases

ProteinModelPortali Q9QY01.
SMRi Q9QY01. Positions 9-317.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9QY01.

Proteomic databases

PRIDEi Q9QY01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004920 ; ENSMUSP00000004920 ; ENSMUSG00000004798 .
GeneIDi 29869.
KEGGi mmu:29869.
UCSCi uc007jih.2. mouse.

Organism-specific databases

CTDi 9706.
MGIi MGI:1352758. Ulk2.
Rougei Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117559.
HOGENOMi HOG000044146.
HOVERGENi HBG000342.
InParanoidi Q9QY01.
KOi K08269.
OMAi GTIPEQF.
OrthoDBi EOG7K0ZBF.
PhylomeDBi Q9QY01.
TreeFami TF324551.

Miscellaneous databases

NextBioi 307094.
PROi Q9QY01.
SOURCEi Search...

Gene expression databases

Bgeei Q9QY01.
CleanExi MM_ULK2.
Genevestigatori Q9QY01.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF12063. DUF3543. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000580. Ser/Thr_PK_STPK_ULK-1/2. 1 hit.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiULK2_MOUSE
AccessioniPrimary (citable) accession number: Q9QY01
Secondary accession number(s): Q80TV7, Q9WTP4
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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