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Q9U9Y8

- NLK_CAEEL

UniProt

Q9U9Y8 - NLK_CAEEL

Protein

Serine/threonine kinase NLK

Gene

lit-1

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Has a role in the Wnt signaling pathway controlling the asymmetry of cell divisions during embryogenesis. Operates in the AB and EMS cell lineages influencing cell specification. Required for body wall muscle development, endoderm development, pop-1 asymmetry and T-cell division asymmetry. Lit-1/wrm-1 complex regulates pop-1 localization and is required for pop-1/par-5 interaction.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei269 – 2691ATPPROSITE-ProRule annotation
    Active sitei366 – 3661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 2549ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: WormBase
    6. protein N-terminus binding Source: UniProtKB
    7. protein serine/threonine kinase activity Source: WormBase

    GO - Biological processi

    1. anatomical structure morphogenesis Source: WormBase
    2. asymmetric cell division Source: WormBase
    3. asymmetric protein localization involved in cell fate determination Source: WormBase
    4. embryo development Source: WormBase
    5. endodermal cell fate specification Source: WormBase
    6. endoderm development Source: UniProtKB
    7. muscle cell fate specification Source: WormBase
    8. polarity specification of proximal/distal axis Source: WormBase
    9. protein phosphorylation Source: WormBase
    10. Wnt signaling pathway Source: WormBase

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_184336. Ca2+ pathway.
    SignaLinkiQ9U9Y8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine kinase NLKBy similarity (EC:2.7.11.24)
    Alternative name(s):
    Loss of intestine protein 1
    Nemo-like kinaseBy similarity
    Gene namesi
    Name:lit-1Imported
    Synonyms:nlkBy similarity
    ORF Names:W06F12.1
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome III

    Organism-specific databases

    WormBaseiW06F12.1a; CE29476; WBGene00003048; lit-1.
    W06F12.1b; CE29477; WBGene00003048; lit-1.
    W06F12.1c; CE29478; WBGene00003048; lit-1.
    W06F12.1d; CE37160; WBGene00003048; lit-1.
    W06F12.1e; CE37161; WBGene00003048; lit-1.

    Subcellular locationi

    Cytoplasmcell cortex 2 Publications. Nucleus 2 Publications
    Note: Located in the anterior cell cortex before and during asymmetric cell division. After division, located preferentially in the nucleus of the posterior daughter cell.2 Publications

    GO - Cellular componenti

    1. cell cortex Source: WormBase
    2. cytoplasm Source: WormBase
    3. nucleus Source: WormBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi357 – 3571L → S in t1512; intestine cells absent but have an excess of pharyngeal cells, symmetrical localization of pop-1 and symmetrical T-cell division. 2 Publications
    Mutagenesisi400 – 4001T → A: No detectable kinase activity. 1 Publication
    Mutagenesisi402 – 4021E → K in t1534; reduced body-wall muscle. 1 Publication
    Mutagenesisi541 – 5411C → Y in or131; loss of pop-1 asymmetry and protruding vulva phenotype and defects in gonadal migration and development. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 634634Serine/threonine kinase NLKPRO_0000372802Add
    BLAST

    Proteomic databases

    PaxDbiQ9U9Y8.
    PRIDEiQ9U9Y8.

    Expressioni

    Tissue specificityi

    Expressed in larval and adult pharynx and seam and vulval cells.1 Publication

    Interactioni

    Subunit structurei

    Interacts with wrm-1 (via N-terminus); activates lit-1 kinase activity and the lit-1/wrm-1 dimer phosphorylates pop-1 which promotes pop-1 interaction with par-5 and translocation of pop-1 from the nucleus to the cytoplasm. Interacts with pop-1 (phosphorylated on 'Ser-118' and 'Ser-127'); dependent on lit-1/wrm-1 complex.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CELE_R02D5.1Q216365EBI-318513,EBI-329142
    CELE_ZK1055.7O764493EBI-318513,EBI-313622
    spe-44Q181713EBI-318513,EBI-320157
    wrm-1Q109538EBI-318513,EBI-2530558

    Protein-protein interaction databases

    BioGridi41974. 64 interactions.
    DIPiDIP-25624N.
    IntActiQ9U9Y8. 23 interactions.
    MINTiMINT-1045592.
    STRINGi6239.W06F12.1a.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9U9Y8.
    SMRiQ9U9Y8. Positions 214-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini240 – 531292Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi80 – 216137Gln-richSequence AnalysisAdd
    BLAST
    Compositional biasi102 – 18887His-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110881.
    InParanoidiQ9U9Y8.
    KOiK04468.
    OMAiQHRYLEE.
    OrthoDBiEOG72RMZ3.
    PhylomeDBiQ9U9Y8.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform a1 Publication (identifier: Q9U9Y8-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVSWGRGKDA YYLYISREQE EDDDDSLSFY SSQKDTEDEF CGCLFPDPEI    50
    PGSSSSSGCS SSSTELYDLA AAHAALISRQ QQILSQAIPI IPEHQLAAVA 100
    AHHQHHQQLH PSVQYQLVAA ATHHNHHQPQ AAQPHYSAVV PRSDVIQQPP 150
    HFALHHHLQN LVQQQQQQQA HHHHQQLVGE MALVSHTHPA AVGSTTCYEK 200
    NQQKQQQVQQ IPTQPQVAHV SSNAILAAAQ PFYPPPVQDS QPDRPIGYGA 250
    FGVVWSVTDP RSGKRVALKK MPNVFQNLAS CKRVFREIKM LSSFRHDNVL 300
    SLLDILQPAN PSFFQELYVL TELMQSDLHK IIVSPQALTP DHVKVFVYQI 350
    LRGLKYLHTA NILHRDIKPG NLLVNSNCIL KICDFGLART WDQRDRLNMT 400
    HEVVTQYYRA PELLMGARRY TGAVDIWSVG CIFAELLQRK ILFQAAGPIE 450
    QLQMIIDLLG TPSQEAMKYA CEGAKNHVLR AGLRAPDTQR LYKIASPDDK 500
    NHEAVDLLQK LLHFDPDKRI SVEEALQHRY LEEGRLRFHS CMCSCCYTKP 550
    NMPSRLFAQD LDPRHESPFD PKWEKDMSRL SMFELREKMY QFVMDRPALY 600
    GVALCINPQS AAYKNFASSS VAQASELPPS PQAW 634
    Length:634
    Mass (Da):71,777
    Last modified:May 1, 2000 - v1
    Checksum:iA9F2EA7E3E2CE7F5
    GO
    Isoform b1 Publication (identifier: Q9U9Y8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-172: Missing.
         173-178: HHQQLV → MRDMIY

    Show »
    Length:462
    Mass (Da):52,603
    Checksum:iD030A48CA8F2968C
    GO
    Isoform c1 Publication (identifier: Q9U9Y8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-197: Missing.
         198-216: YEKNQQKQQQVQQIPTQPQ → MILIAIIESFIEYLRKIVW

    Note: No experimental confirmation available.Curated

    Show »
    Length:437
    Mass (Da):49,951
    Checksum:i21C9CF88553F20D3
    GO
    Isoform d1 Publication (identifier: Q9U9Y8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-33: Missing.
         34-51: KDTEDEFCGCLFPDPEIP → MGRNQEGQFNGAGNSESA

    Note: No experimental confirmation available.Curated

    Show »
    Length:601
    Mass (Da):67,652
    Checksum:i311EED6DED5AA170
    GO
    Isoform e1 Publication (identifier: Q9U9Y8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-180: Missing.

    Show »
    Length:454
    Mass (Da):51,607
    Checksum:iD951AB8C0CAC9394
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 197197Missing in isoform c. 1 PublicationVSP_052845Add
    BLAST
    Alternative sequencei1 – 180180Missing in isoform e. 1 PublicationVSP_052846Add
    BLAST
    Alternative sequencei1 – 172172Missing in isoform b. 1 PublicationVSP_052847Add
    BLAST
    Alternative sequencei1 – 3333Missing in isoform d. 1 PublicationVSP_052848Add
    BLAST
    Alternative sequencei34 – 5118KDTED…DPEIP → MGRNQEGQFNGAGNSESA in isoform d. 1 PublicationVSP_052849Add
    BLAST
    Alternative sequencei173 – 1786HHQQLV → MRDMIY in isoform b. 1 PublicationVSP_052850
    Alternative sequencei198 – 21619YEKNQ…PTQPQ → MILIAIIESFIEYLRKIVW in isoform c. 1 PublicationVSP_052851Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143243 mRNA. Translation: AAD37360.1.
    AF143244 mRNA. Translation: AAD37361.1.
    AF145376 mRNA. Translation: AAD39815.1.
    Z83244 Genomic DNA. Translation: CAB05827.2.
    Z83244 Genomic DNA. Translation: CAB60300.2.
    Z83244 Genomic DNA. Translation: CAD18878.1.
    Z83244 Genomic DNA. Translation: CAH10803.1.
    Z83244, Z92822 Genomic DNA. Translation: CAH10804.1.
    PIRiT26240.
    RefSeqiNP_001022805.1. NM_001027634.2. [Q9U9Y8-1]
    NP_001022806.1. NM_001027635.2. [Q9U9Y8-2]
    NP_001022807.1. NM_001027636.2. [Q9U9Y8-3]
    NP_001022808.1. NM_001027637.3. [Q9U9Y8-4]
    NP_001022809.1. NM_001027638.3. [Q9U9Y8-5]
    UniGeneiCel.6733.

    Genome annotation databases

    EnsemblMetazoaiW06F12.1a; W06F12.1a; WBGene00003048. [Q9U9Y8-1]
    GeneIDi176808.
    KEGGicel:CELE_W06F12.1.
    UCSCiW06F12.1d. c. elegans.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF143243 mRNA. Translation: AAD37360.1 .
    AF143244 mRNA. Translation: AAD37361.1 .
    AF145376 mRNA. Translation: AAD39815.1 .
    Z83244 Genomic DNA. Translation: CAB05827.2 .
    Z83244 Genomic DNA. Translation: CAB60300.2 .
    Z83244 Genomic DNA. Translation: CAD18878.1 .
    Z83244 Genomic DNA. Translation: CAH10803.1 .
    Z83244 , Z92822 Genomic DNA. Translation: CAH10804.1 .
    PIRi T26240.
    RefSeqi NP_001022805.1. NM_001027634.2. [Q9U9Y8-1 ]
    NP_001022806.1. NM_001027635.2. [Q9U9Y8-2 ]
    NP_001022807.1. NM_001027636.2. [Q9U9Y8-3 ]
    NP_001022808.1. NM_001027637.3. [Q9U9Y8-4 ]
    NP_001022809.1. NM_001027638.3. [Q9U9Y8-5 ]
    UniGenei Cel.6733.

    3D structure databases

    ProteinModelPortali Q9U9Y8.
    SMRi Q9U9Y8. Positions 214-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 41974. 64 interactions.
    DIPi DIP-25624N.
    IntActi Q9U9Y8. 23 interactions.
    MINTi MINT-1045592.
    STRINGi 6239.W06F12.1a.

    Proteomic databases

    PaxDbi Q9U9Y8.
    PRIDEi Q9U9Y8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai W06F12.1a ; W06F12.1a ; WBGene00003048 . [Q9U9Y8-1 ]
    GeneIDi 176808.
    KEGGi cel:CELE_W06F12.1.
    UCSCi W06F12.1d. c. elegans.

    Organism-specific databases

    CTDi 176808.
    WormBasei W06F12.1a ; CE29476 ; WBGene00003048 ; lit-1.
    W06F12.1b ; CE29477 ; WBGene00003048 ; lit-1.
    W06F12.1c ; CE29478 ; WBGene00003048 ; lit-1.
    W06F12.1d ; CE37160 ; WBGene00003048 ; lit-1.
    W06F12.1e ; CE37161 ; WBGene00003048 ; lit-1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110881.
    InParanoidi Q9U9Y8.
    KOi K04468.
    OMAi QHRYLEE.
    OrthoDBi EOG72RMZ3.
    PhylomeDBi Q9U9Y8.

    Enzyme and pathway databases

    Reactomei REACT_184336. Ca2+ pathway.
    SignaLinki Q9U9Y8.

    Miscellaneous databases

    NextBioi 894088.
    PROi Q9U9Y8.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "WRM-1 activates the LIT-1 protein kinase to transduce anterior/posterior polarity signals in C. elegans."
      Rocheleau C.E., Yasuda J., Shin T.H., Lin R., Sawa H., Okano H., Priess J.R., Davis R.J., Mello C.C.
      Cell 97:717-726(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND E), FUNCTION, INTERACTION WITH WRM-1, MUTAGENESIS OF LEU-357.
    2. "MAP kinase and Wnt pathways converge to downregulate an HMG-domain repressor in Caenorhabditis elegans."
      Meneghini M.D., Ishitani T., Carter J.C., Hisamoto N., Ninomiya-Tsuji J., Thorpe C.J., Hamill D.R., Matsumoto K., Bowerman B.
      Nature 399:793-797(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, MUTAGENESIS OF CYS-541.
    3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
      Strain: Bristol N2Imported.
    4. "Binary specification of the embryonic lineage in Caenorhabditis elegans."
      Kaletta T., Schnabel H., Schnabel R.
      Nature 390:294-298(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LEU-357 AND GLU-402.
    5. "MOM-4, a MAP kinase kinase kinase-related protein, activates WRM-1/LIT-1 kinase to transduce anterior/posterior polarity signals in C. elegans."
      Shin T.H., Yasuda J., Rocheleau C.E., Lin R., Soto M., Bei Y., Davis R.J., Mello C.C.
      Mol. Cell 4:275-280(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-400.
    6. "Left-right asymmetry in C. elegans intestine organogenesis involves a LIN-12/Notch signaling pathway."
      Hermann G.J., Leung B., Priess J.R.
      Development 127:3429-3440(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Phosphorylation by the beta-catenin/MAPK complex promotes 14-3-3-mediated nuclear export of TCF/POP-1 in signal-responsive cells in C. elegans."
      Lo M.-C., Gay F., Odom R., Shi Y., Lin R.
      Cell 117:95-106(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH POP-1.
    8. "Identification of C. elegans DAF-12-binding sites, response elements, and target genes."
      Shostak Y., Van Gilst M.R., Antebi A., Yamamoto K.R.
      Genes Dev. 18:2529-2544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF CYS-541.
    9. "Asymmetric cortical and nuclear localizations of WRM-1/beta-catenin during asymmetric cell division in C. elegans."
      Takeshita H., Sawa H.
      Genes Dev. 19:1743-1748(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiNLK_CAEEL
    AccessioniPrimary (citable) accession number: Q9U9Y8
    Secondary accession number(s): O62395
    , Q69YW9, Q8WQB7, Q9U343, Q9UA07, Q9Y198
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Miscellaneous

    Worms lacking nlk exhibit defects in body wall muscle, endoderm development and pop-1 asymmetry.3 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3