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Q8BST6

- PELI2_MOUSE

UniProt

Q8BST6 - PELI2_MOUSE

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Protein

E3 ubiquitin-protein ligase pellino homolog 2

Gene

Peli2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

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

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
Complete GO annotation...

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

        10         20         30         40         50
MFSPGQEEPS APNKEPVKYR ELVVLGYNGA LPNGDRGRRK SRFALYKRTY
60 70 80 90 100
ASGVKPSTIH MVSTPQASKA ISSRGHHSIS YTLSRSQTVV VEYTHDKDTD
110 120 130 140 150
MFQVGRSTES PIDFVVTDTV SGGQNEDAQI TQSTISRFAC RIVCDRNEPY
160 170 180 190 200
TARIFAAGFD SSKNIFLGEK AAKWKNPDGH MDGLTTNGVL VMHPQGGFTE
210 220 230 240 250
ESQPGVWREI SVCGDVYTLR ETRSAQQRGK LVESETNVLQ DGSLIDLCGA
260 270 280 290 300
TLLWRTADGL FHAPTQKHIE ALRQEINAAR PQCPVGLNTL AFPSINRKEV
310 320 330 340 350
VEEKQPWAYL SCGHVHGYHS WGHRSDTEAN ERECPMCRTV GPYVPLWLGC
360 370 380 390 400
EAGFYVDAGP PTHAFTPCGH VCSEKSAKYW SQIPLPHGTH AFHAACPFCA
410
TQLVGEQNCI KLIFQGPVD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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 29, 2014
This is version 95 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