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Q8BST6

- PELI2_MOUSE

UniProt

Q8BST6 - PELI2_MOUSE

Protein

E3 ubiquitin-protein ligase pellino homolog 2

Gene

Peli2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (24 Oct 2003)
      Previous versions | rss
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    Functioni

    E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. May be important for LPS- and IL1B-induced MAP3K7-dependent, but not MAP3K3-dependent, NF-kappa-B activation. Can activate the MAP (mitogen activated protein) kinase pathway leading to activation of ELK1.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. protein ubiquitination Source: UniProtKB-UniPathway
    2. Toll signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase pellino homolog 2 (EC:6.3.2.-)
    Short name:
    Pellino-2
    Gene namesi
    Name:Peli2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1891445. Peli2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 419419E3 ubiquitin-protein ligase pellino homolog 2PRO_0000194175Add
    BLAST

    Post-translational modificationi

    Phosphorylated by IRAK1 and IRAK4 enhancing its E3 ligase activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8BST6.
    PRIDEiQ8BST6.

    PTM databases

    PhosphoSiteiQ8BST6.

    Expressioni

    Tissue specificityi

    Widely expressed both in embryos and adult. Weakly or not expressed in spleen and thymus.1 Publication

    Gene expression databases

    CleanExiMM_PELI2.
    GenevestigatoriQ8BST6.

    Interactioni

    Subunit structurei

    Interacts with TRAF6, IRAK4 and MAP3K7 By similarity. Interacts with IRAK1. Interacts with BCL10; this interaction is impaired by SOCS3.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Irak1Q624062EBI-448554,EBI-448533

    Protein-protein interaction databases

    BioGridi220309. 3 interactions.
    IntActiQ8BST6. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BST6.
    SMRiQ8BST6. Positions 15-257.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 202188FHA; atypicalAdd
    BLAST

    Domaini

    The atypical FHA domain contains a 'wing' insert and mediates binding to threonine-phosphorylated IRAK1.By similarity

    Sequence similaritiesi

    Belongs to the pellino family.Curated
    Contains 1 FHA domain.Curated

    Phylogenomic databases

    eggNOGiNOG258040.
    HOGENOMiHOG000234110.
    HOVERGENiHBG053559.
    InParanoidiQ8BST6.
    KOiK11964.
    PhylomeDBiQ8BST6.

    Family and domain databases

    InterProiIPR006800. Pellino_fam.
    [Graphical view]
    PANTHERiPTHR12098. PTHR12098. 1 hit.
    PfamiPF04710. Pellino. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038886. Pellino. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BST6-1) [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

    MFSPGQEEPS APNKEPVKYR ELVVLGYNGA LPNGDRGRRK SRFALYKRTY    50
    ASGVKPSTIH MVSTPQASKA ISSRGHHSIS YTLSRSQTVV VEYTHDKDTD 100
    MFQVGRSTES PIDFVVTDTV SGGQNEDAQI TQSTISRFAC RIVCDRNEPY 150
    TARIFAAGFD SSKNIFLGEK AAKWKNPDGH MDGLTTNGVL VMHPQGGFTE 200
    ESQPGVWREI SVCGDVYTLR ETRSAQQRGK LVESETNVLQ DGSLIDLCGA 250
    TLLWRTADGL FHAPTQKHIE ALRQEINAAR PQCPVGLNTL AFPSINRKEV 300
    VEEKQPWAYL SCGHVHGYHS WGHRSDTEAN ERECPMCRTV GPYVPLWLGC 350
    EAGFYVDAGP PTHAFTPCGH VCSEKSAKYW SQIPLPHGTH AFHAACPFCA 400
    TQLVGEQNCI KLIFQGPVD 419
    Length:419
    Mass (Da):46,272
    Last modified:October 24, 2003 - v2
    Checksum:i786C92C28C38D0CB
    GO
    Isoform 2 (identifier: Q8BST6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-100: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:319
    Mass (Da):35,165
    Checksum:i7FFA0991F1FA0950
    GO
    Isoform 3 (identifier: Q8BST6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         70-155: AISSRGHHSI...RNEPYTARIF → LPAAKHYYNE...KKKIFFSCWS
         156-419: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:155
    Mass (Da):17,403
    Checksum:iE443ACF3246FA349
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71E → K in BAC27024. (PubMed:16141072)Curated
    Sequence conflicti11 – 111A → T in BAC27024. (PubMed:16141072)Curated
    Sequence conflicti20 – 201R → G in BAC38472. (PubMed:16141072)Curated
    Sequence conflicti38 – 392RR → KK in AAG15392. (PubMed:11306823)Curated
    Sequence conflicti44 – 441A → T in AAG15392. (PubMed:11306823)Curated
    Sequence conflicti320 – 3201S → H in AAG15392. (PubMed:11306823)Curated
    Sequence conflicti327 – 3271T → A in AAH27062. (PubMed:15489334)Curated
    Sequence conflicti338 – 3381R → M in AAG15392. (PubMed:11306823)Curated
    Sequence conflicti364 – 3641A → V in AAG15392. (PubMed:11306823)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_008636Add
    BLAST
    Alternative sequencei70 – 15586AISSR…TARIF → LPAAKHYYNEADSESLSALT LKVRDFLTGECSQRREYRDP AFSREGASGSAQLVAQAFLI CPLSYTIVKQEQIRCLKKKI FFSCWS in isoform 3. 1 PublicationVSP_008637Add
    BLAST
    Alternative sequencei156 – 419264Missing in isoform 3. 1 PublicationVSP_008638Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302504 mRNA. Translation: AAG15392.1.
    AK030564 mRNA. Translation: BAC27024.1.
    AK033815 mRNA. Translation: BAC28485.1.
    AK082342 mRNA. Translation: BAC38472.1.
    BC027062 mRNA. Translation: AAH27062.1.
    CCDSiCCDS36901.1. [Q8BST6-1]
    RefSeqiNP_291080.2. NM_033602.2.
    XP_006519804.1. XM_006519741.1. [Q8BST6-2]
    UniGeneiMm.296457.

    Genome annotation databases

    GeneIDi93834.
    KEGGimmu:93834.
    UCSCiuc007tji.1. mouse. [Q8BST6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF302504 mRNA. Translation: AAG15392.1 .
    AK030564 mRNA. Translation: BAC27024.1 .
    AK033815 mRNA. Translation: BAC28485.1 .
    AK082342 mRNA. Translation: BAC38472.1 .
    BC027062 mRNA. Translation: AAH27062.1 .
    CCDSi CCDS36901.1. [Q8BST6-1 ]
    RefSeqi NP_291080.2. NM_033602.2.
    XP_006519804.1. XM_006519741.1. [Q8BST6-2 ]
    UniGenei Mm.296457.

    3D structure databases

    ProteinModelPortali Q8BST6.
    SMRi Q8BST6. Positions 15-257.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 220309. 3 interactions.
    IntActi Q8BST6. 1 interaction.

    PTM databases

    PhosphoSitei Q8BST6.

    Proteomic databases

    PaxDbi Q8BST6.
    PRIDEi Q8BST6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 93834.
    KEGGi mmu:93834.
    UCSCi uc007tji.1. mouse. [Q8BST6-1 ]

    Organism-specific databases

    CTDi 57161.
    MGIi MGI:1891445. Peli2.

    Phylogenomic databases

    eggNOGi NOG258040.
    HOGENOMi HOG000234110.
    HOVERGENi HBG053559.
    InParanoidi Q8BST6.
    KOi K11964.
    PhylomeDBi Q8BST6.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 351677.
    PROi Q8BST6.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PELI2.
    Genevestigatori Q8BST6.

    Family and domain databases

    InterProi IPR006800. Pellino_fam.
    [Graphical view ]
    PANTHERi PTHR12098. PTHR12098. 1 hit.
    Pfami PF04710. Pellino. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038886. Pellino. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Assignment of homologous genes, Peli1/PELI1 and Peli2/PELI2, for the Pelle adaptor protein Pellino to mouse chromosomes 11 and 14 and human chromosomes 2p13.3 and 14q21, respectively, by physical and radiation hybrid mapping."
      Resch K., Jockusch H., Schmitt-John T.
      Cytogenet. Cell Genet. 92:172-174(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
    2. "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] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Cerebellum, Epididymis and Pituitary.
    3. "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] (ISOFORM 2).
      Tissue: Mammary tumor.
    4. "Mouse pellino-2 modulates IL-1 and lipopolysaccharide signaling."
      Yu K.-Y., Kwon H.-J., Norman D.A.M., Vig E., Goebl M.G., Harrington M.A.
      J. Immunol. 169:4075-4078(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH IRAK1.
    5. "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through interaction with Pellino2."
      Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.
      J. Biol. Chem. 279:37436-37444(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCL10.
    6. "Pellino 2 is critical for Toll-like receptor/interleukin-1 receptor (TLR/IL-1R)-mediated post-transcriptional control."
      Kim T.W., Yu M., Zhou H., Cui W., Wang J., DiCorleto P., Fox P., Xiao H., Li X.
      J. Biol. Chem. 287:25686-25695(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiPELI2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BST6
    Secondary accession number(s): Q8C4F2
    , Q8CC65, Q8R2X4, Q9ERJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: October 24, 2003
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3