PELI2_MOUSE
ID PELI2_MOUSE Reviewed; 419 AA.
AC Q8BST6; Q8C4F2; Q8CC65; Q8R2X4; Q9ERJ7;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase pellino homolog 2;
DE Short=Pellino-2;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase pellino homolog 2 {ECO:0000305};
GN Name=Peli2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=11306823; DOI=10.1159/000056895;
RA Resch K., Jockusch H., Schmitt-John T.;
RT "Assignment of homologous genes, Peli1/PELI1 and Peli2/PELI2, for the Pelle
RT adaptor protein Pellino to mouse chromosomes 11 and 14 and human
RT chromosomes 2p13.3 and 14q21, respectively, by physical and radiation
RT hybrid mapping.";
RL Cytogenet. Cell Genet. 92:172-174(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Epididymis, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH IRAK1.
RX PubMed=12370331; DOI=10.4049/jimmunol.169.8.4075;
RA Yu K.-Y., Kwon H.-J., Norman D.A.M., Vig E., Goebl M.G., Harrington M.A.;
RT "Mouse pellino-2 modulates IL-1 and lipopolysaccharide signaling.";
RL J. Immunol. 169:4075-4078(2002).
RN [5]
RP INTERACTION WITH BCL10.
RX PubMed=15213237; DOI=10.1074/jbc.m400241200;
RA Liu Y., Dong W., Chen L., Xiang R., Xiao H., De G., Wang Z., Qi Y.;
RT "BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through
RT interaction with Pellino2.";
RL J. Biol. Chem. 279:37436-37444(2004).
RN [6]
RP FUNCTION.
RX PubMed=22669975; DOI=10.1074/jbc.m112.352625;
RA Kim T.W., Yu M., Zhou H., Cui W., Wang J., DiCorleto P., Fox P., Xiao H.,
RA Li X.;
RT "Pellino 2 is critical for Toll-like receptor/interleukin-1 receptor
RT (TLR/IL-1R)-mediated post-transcriptional control.";
RL J. Biol. Chem. 287:25686-25695(2012).
CC -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-
CC 1 signaling pathways via interaction with the complex containing IRAK
CC kinases and TRAF6. Mediates IL1B-induced IRAK1 'Lys-63'-linked
CC polyubiquitination and possibly 'Lys-48'-linked ubiquitination. May be
CC important for LPS- and IL1B-induced MAP3K7-dependent, but not MAP3K3-
CC dependent, NF-kappa-B activation. Can activate the MAP (mitogen
CC activated protein) kinase pathway leading to activation of ELK1.
CC {ECO:0000269|PubMed:12370331, ECO:0000269|PubMed:22669975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TRAF6, IRAK4 and MAP3K7 (By similarity).
CC Interacts with IRAK1. Interacts with BCL10; this interaction is
CC impaired by SOCS3. {ECO:0000250, ECO:0000269|PubMed:12370331,
CC ECO:0000269|PubMed:15213237}.
CC -!- INTERACTION:
CC Q8BST6; Q62406: Irak1; NbExp=2; IntAct=EBI-448554, EBI-448533;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BST6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BST6-2; Sequence=VSP_008636;
CC Name=3;
CC IsoId=Q8BST6-3; Sequence=VSP_008637, VSP_008638;
CC -!- TISSUE SPECIFICITY: Widely expressed both in embryos and adult. Weakly
CC or not expressed in spleen and thymus. {ECO:0000269|PubMed:12370331}.
CC -!- DOMAIN: The atypical FHA domain contains a 'wing' insert and mediates
CC binding to threonine-phosphorylated IRAK1. {ECO:0000250}.
CC -!- PTM: Phosphorylated by IRAK1 and IRAK4 enhancing its E3 ligase
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pellino family. {ECO:0000305}.
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DR EMBL; AF302504; AAG15392.1; -; mRNA.
DR EMBL; AK030564; BAC27024.1; -; mRNA.
DR EMBL; AK033815; BAC28485.1; -; mRNA.
DR EMBL; AK082342; BAC38472.1; -; mRNA.
DR EMBL; BC027062; AAH27062.1; -; mRNA.
DR CCDS; CCDS36901.1; -. [Q8BST6-1]
DR RefSeq; NP_291080.2; NM_033602.2.
DR RefSeq; XP_006519804.1; XM_006519741.2. [Q8BST6-2]
DR AlphaFoldDB; Q8BST6; -.
DR SMR; Q8BST6; -.
DR BioGRID; 220309; 3.
DR IntAct; Q8BST6; 1.
DR STRING; 10090.ENSMUSP00000072894; -.
DR iPTMnet; Q8BST6; -.
DR PhosphoSitePlus; Q8BST6; -.
DR PaxDb; Q8BST6; -.
DR PRIDE; Q8BST6; -.
DR ProteomicsDB; 287672; -. [Q8BST6-1]
DR ProteomicsDB; 287673; -. [Q8BST6-2]
DR ProteomicsDB; 287674; -. [Q8BST6-3]
DR GeneID; 93834; -.
DR KEGG; mmu:93834; -.
DR UCSC; uc007tji.1; mouse. [Q8BST6-1]
DR CTD; 57161; -.
DR MGI; MGI:1891445; Peli2.
DR eggNOG; KOG3842; Eukaryota.
DR InParanoid; Q8BST6; -.
DR OrthoDB; 837213at2759; -.
DR PhylomeDB; Q8BST6; -.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
DR Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 93834; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Peli2; mouse.
DR PRO; PR:Q8BST6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BST6; protein.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0008592; P:regulation of Toll signaling pathway; IEA:InterPro.
DR InterPro; IPR006800; Pellino_fam.
DR PANTHER; PTHR12098; PTHR12098; 1.
DR Pfam; PF04710; Pellino; 1.
DR PIRSF; PIRSF038886; Pellino; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..419
FT /note="E3 ubiquitin-protein ligase pellino homolog 2"
FT /id="PRO_0000194175"
FT DOMAIN 15..202
FT /note="FHA; atypical"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008636"
FT VAR_SEQ 70..155
FT /note="AISSRGHHSISYTLSRSQTVVVEYTHDKDTDMFQVGRSTESPIDFVVTDTVS
FT GGQNEDAQITQSTISRFACRIVCDRNEPYTARIF -> LPAAKHYYNEADSESLSALTL
FT KVRDFLTGECSQRREYRDPAFSREGASGSAQLVAQAFLICPLSYTIVKQEQIRCLKKKI
FT FFSCWS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008637"
FT VAR_SEQ 156..419
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008638"
FT CONFLICT 7
FT /note="E -> K (in Ref. 2; BAC27024)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="A -> T (in Ref. 2; BAC27024)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="R -> G (in Ref. 2; BAC38472)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="RR -> KK (in Ref. 1; AAG15392)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="A -> T (in Ref. 1; AAG15392)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="S -> H (in Ref. 1; AAG15392)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> A (in Ref. 3; AAH27062)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="R -> M (in Ref. 1; AAG15392)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="A -> V (in Ref. 1; AAG15392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46272 MW; 786C92C28C38D0CB CRC64;
MFSPGQEEPS APNKEPVKYR ELVVLGYNGA LPNGDRGRRK SRFALYKRTY ASGVKPSTIH
MVSTPQASKA ISSRGHHSIS YTLSRSQTVV VEYTHDKDTD MFQVGRSTES PIDFVVTDTV
SGGQNEDAQI TQSTISRFAC RIVCDRNEPY TARIFAAGFD SSKNIFLGEK AAKWKNPDGH
MDGLTTNGVL VMHPQGGFTE ESQPGVWREI SVCGDVYTLR ETRSAQQRGK LVESETNVLQ
DGSLIDLCGA TLLWRTADGL FHAPTQKHIE ALRQEINAAR PQCPVGLNTL AFPSINRKEV
VEEKQPWAYL SCGHVHGYHS WGHRSDTEAN ERECPMCRTV GPYVPLWLGC EAGFYVDAGP
PTHAFTPCGH VCSEKSAKYW SQIPLPHGTH AFHAACPFCA TQLVGEQNCI KLIFQGPVD
