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Q8BST6 (PELI2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase pellino homolog 2

Short name=Pellino-2
EC=6.3.2.-
Gene names
Name:Peli2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with TRAF6, IRAK4 and MAP3K7 By similarity. Interacts with IRAK1. Interacts with BCL10; this interaction is impaired by SOCS3. Ref.4 Ref.5

Tissue specificity

Widely expressed both in embryos and adult. Weakly or not expressed in spleen and thymus. Ref.4

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the pellino family.

Contains 1 FHA domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processToll signaling pathway

Inferred from electronic annotation. Source: InterPro

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytosol

Inferred from direct assay PubMed 16831874. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16831874. Source: UniProtKB

   Molecular_functionligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Irak1Q624062EBI-448554,EBI-448533

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BST6-1)

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.
Isoform 2 (identifier: Q8BST6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8BST6-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419E3 ubiquitin-protein ligase pellino homolog 2
PRO_0000194175

Regions

Domain15 – 202188FHA; atypical

Natural variations

Alternative sequence1 – 100100Missing in isoform 2.
VSP_008636
Alternative sequence70 – 15586AISSR…TARIF → LPAAKHYYNEADSESLSALT LKVRDFLTGECSQRREYRDP AFSREGASGSAQLVAQAFLI CPLSYTIVKQEQIRCLKKKI FFSCWS in isoform 3.
VSP_008637
Alternative sequence156 – 419264Missing in isoform 3.
VSP_008638

Experimental info

Sequence conflict71E → K in BAC27024. Ref.2
Sequence conflict111A → T in BAC27024. Ref.2
Sequence conflict201R → G in BAC38472. Ref.2
Sequence conflict38 – 392RR → KK in AAG15392. Ref.1
Sequence conflict441A → T in AAG15392. Ref.1
Sequence conflict3201S → H in AAG15392. Ref.1
Sequence conflict3271T → A in AAH27062. Ref.3
Sequence conflict3381R → M in AAG15392. Ref.1
Sequence conflict3641A → V in AAG15392. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: 786C92C28C38D0CB

FASTA41946,272
        10         20         30         40         50         60 
MFSPGQEEPS APNKEPVKYR ELVVLGYNGA LPNGDRGRRK SRFALYKRTY ASGVKPSTIH 

        70         80         90        100        110        120 
MVSTPQASKA ISSRGHHSIS YTLSRSQTVV VEYTHDKDTD MFQVGRSTES PIDFVVTDTV 

       130        140        150        160        170        180 
SGGQNEDAQI TQSTISRFAC RIVCDRNEPY TARIFAAGFD SSKNIFLGEK AAKWKNPDGH 

       190        200        210        220        230        240 
MDGLTTNGVL VMHPQGGFTE ESQPGVWREI SVCGDVYTLR ETRSAQQRGK LVESETNVLQ 

       250        260        270        280        290        300 
DGSLIDLCGA TLLWRTADGL FHAPTQKHIE ALRQEINAAR PQCPVGLNTL AFPSINRKEV 

       310        320        330        340        350        360 
VEEKQPWAYL SCGHVHGYHS WGHRSDTEAN ERECPMCRTV GPYVPLWLGC EAGFYVDAGP 

       370        380        390        400        410 
PTHAFTPCGH VCSEKSAKYW SQIPLPHGTH AFHAACPFCA TQLVGEQNCI KLIFQGPVD 

« Hide

Isoform 2 [UniParc].

Checksum: 7FFA0991F1FA0950
Show »

FASTA31935,165
Isoform 3 [UniParc].

Checksum: E443ACF3246FA349
Show »

FASTA15517,403

References

« Hide 'large scale' references
[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. 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] (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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_291080.2. NM_033602.2.
XP_006519804.1. XM_006519741.1.
UniGeneMm.296457.

3D structure databases

ProteinModelPortalQ8BST6.
SMRQ8BST6. Positions 15-257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220309. 3 interactions.
IntActQ8BST6. 1 interaction.

PTM databases

PhosphoSiteQ8BST6.

Proteomic databases

PaxDbQ8BST6.
PRIDEQ8BST6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID93834.
KEGGmmu:93834.
UCSCuc007tji.1. mouse. [Q8BST6-1]

Organism-specific databases

CTD57161.
MGIMGI:1891445. Peli2.

Phylogenomic databases

eggNOGNOG258040.
HOGENOMHOG000234110.
HOVERGENHBG053559.
InParanoidQ8BST6.
KOK11964.
PhylomeDBQ8BST6.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

CleanExMM_PELI2.
GenevestigatorQ8BST6.

Family and domain databases

InterProIPR006800. Pellino_fam.
[Graphical view]
PANTHERPTHR12098. PTHR12098. 1 hit.
PfamPF04710. Pellino. 1 hit.
[Graphical view]
PIRSFPIRSF038886. Pellino. 1 hit.
ProtoNetSearch...

Other

NextBio351677.
PROQ8BST6.
SOURCESearch...

Entry information

Entry namePELI2_MOUSE
AccessionPrimary (citable) accession number: Q8BST6
Secondary accession number(s): Q8C4F2 expand/collapse secondary AC list , Q8CC65, Q8R2X4, Q9ERJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: April 16, 2014
This is version 90 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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