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Protein

E3 ubiquitin-protein ligase pellino homolog 2

Gene

PELI2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 ELK1.5 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000139946-MONOMER.
ReactomeiR-HSA-446652. Interleukin-1 signaling.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SIGNORiQ9HAT8.
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:8828. PELI2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106R → A: Abolishes binding to IRAK1. 1 Publication1
Mutagenesisi187T → A: Abolishes binding to IRAK1; when associated with A-188. 1 Publication1
Mutagenesisi188N → A: Abolishes binding to IRAK1; when associated with A-187. 1 Publication1
Mutagenesisi397C → A: Loss of IRAK1-polyubiquitination. 1 Publication1
Mutagenesisi400C → A: Loss of IRAK1-polyubiquitination. 1 Publication1

Organism-specific databases

DisGeNETi57161.
OpenTargetsiENSG00000139946.
PharmGKBiPA33173.

Polymorphism and mutation databases

BioMutaiPELI2.
DMDMi37999785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001941741 – 420E3 ubiquitin-protein ligase pellino homolog 2Add BLAST420

Post-translational modificationi

Phosphorylated by IRAK1 and IRAK4 enhancing its E3 ligase activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HAT8.
MaxQBiQ9HAT8.
PaxDbiQ9HAT8.
PeptideAtlasiQ9HAT8.
PRIDEiQ9HAT8.

PTM databases

iPTMnetiQ9HAT8.
PhosphoSitePlusiQ9HAT8.

Expressioni

Gene expression databases

BgeeiENSG00000139946.
CleanExiHS_PELI2.
ExpressionAtlasiQ9HAT8. baseline and differential.
GenevisibleiQ9HAT8. HS.

Organism-specific databases

HPAiHPA053182.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
IRAK1P516173EBI-448407,EBI-358664
IRAK4Q9NWZ33EBI-448407,EBI-448378

Protein-protein interaction databases

BioGridi121417. 18 interactors.
DIPiDIP-31350N.
IntActiQ9HAT8. 28 interactors.
MINTiMINT-2845048.
STRINGi9606.ENSP00000267460.

Structurei

Secondary structure

1420
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 24Combined sources7
Beta strandi41 – 46Combined sources6
Beta strandi53 – 63Combined sources11
Beta strandi76 – 82Combined sources7
Beta strandi84 – 96Combined sources13
Beta strandi99 – 106Combined sources8
Beta strandi113 – 115Combined sources3
Beta strandi141 – 148Combined sources8
Beta strandi153 – 158Combined sources6
Beta strandi164 – 168Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi182 – 184Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi208 – 211Combined sources4
Beta strandi215 – 218Combined sources4
Beta strandi222 – 225Combined sources4
Beta strandi245 – 247Combined sources3
Beta strandi252 – 257Combined sources6
Helixi258 – 263Combined sources6
Helixi266 – 269Combined sources4
Helixi270 – 276Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EGAX-ray1.80A15-275[»]
3EGBX-ray3.25A/B7-289[»]
ProteinModelPortaliQ9HAT8.
SMRiQ9HAT8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HAT8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 202FHA; atypicalAdd BLAST188

Domaini

The atypical FHA domain contains a 'wing' insert and mediates binding to threonine-phosphorylated IRAK1.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3842. Eukaryota.
ENOG410XP3S. LUCA.
GeneTreeiENSGT00390000007680.
HOGENOMiHOG000234110.
HOVERGENiHBG053559.
InParanoidiQ9HAT8.
KOiK11964.
OMAiHAPTQKH.
OrthoDBiEOG091G0631.
PhylomeDBiQ9HAT8.
TreeFamiTF314338.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9HAT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSPGQEEHC APNKEPVKYG ELVVLGYNGA LPNGDRGRRK SRFALYKRPK
60 70 80 90 100
ANGVKPSTVH VISTPQASKA ISCKGQHSIS YTLSRNQTVV VEYTHDKDTD
110 120 130 140 150
MFQVGRSTES PIDFVVTDTI SGSQNTDEAQ ITQSTISRFA CRIVCDRNEP
160 170 180 190 200
YTARIFAAGF DSSKNIFLGE KAAKWKNPDG HMDGLTTNGV LVMHPRGGFT
210 220 230 240 250
EESQPGVWRE ISVCGDVYTL RETRSAQQRG KLVESETNVL QDGSLIDLCG
260 270 280 290 300
ATLLWRTADG LFHTPTQKHI EALRQEINAA RPQCPVGLNT LAFPSINRKE
310 320 330 340 350
VVEEKQPWAY LSCGHVHGYH NWGHRSDTEA NERECPMCRT VGPYVPLWLG
360 370 380 390 400
CEAGFYVDAG PPTHAFTPCG HVCSEKSAKY WSQIPLPHGT HAFHAACPFC
410 420
ATQLVGEQNC IKLIFQGPID
Length:420
Mass (Da):46,435
Last modified:March 1, 2001 - v1
Checksum:i2FC5E661C13BC11A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302502 mRNA. Translation: AAG15390.1.
AK315727 mRNA. Translation: BAG38082.1.
CH471061 Genomic DNA. Translation: EAW80689.1.
BC009476 mRNA. Translation: AAH09476.1.
CCDSiCCDS9726.1.
RefSeqiNP_067078.1. NM_021255.2.
UniGeneiHs.657926.

Genome annotation databases

EnsembliENST00000267460; ENSP00000267460; ENSG00000139946.
GeneIDi57161.
KEGGihsa:57161.
UCSCiuc001xch.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302502 mRNA. Translation: AAG15390.1.
AK315727 mRNA. Translation: BAG38082.1.
CH471061 Genomic DNA. Translation: EAW80689.1.
BC009476 mRNA. Translation: AAH09476.1.
CCDSiCCDS9726.1.
RefSeqiNP_067078.1. NM_021255.2.
UniGeneiHs.657926.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EGAX-ray1.80A15-275[»]
3EGBX-ray3.25A/B7-289[»]
ProteinModelPortaliQ9HAT8.
SMRiQ9HAT8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121417. 18 interactors.
DIPiDIP-31350N.
IntActiQ9HAT8. 28 interactors.
MINTiMINT-2845048.
STRINGi9606.ENSP00000267460.

PTM databases

iPTMnetiQ9HAT8.
PhosphoSitePlusiQ9HAT8.

Polymorphism and mutation databases

BioMutaiPELI2.
DMDMi37999785.

Proteomic databases

EPDiQ9HAT8.
MaxQBiQ9HAT8.
PaxDbiQ9HAT8.
PeptideAtlasiQ9HAT8.
PRIDEiQ9HAT8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267460; ENSP00000267460; ENSG00000139946.
GeneIDi57161.
KEGGihsa:57161.
UCSCiuc001xch.4. human.

Organism-specific databases

CTDi57161.
DisGeNETi57161.
GeneCardsiPELI2.
HGNCiHGNC:8828. PELI2.
HPAiHPA053182.
MIMi614798. gene.
neXtProtiNX_Q9HAT8.
OpenTargetsiENSG00000139946.
PharmGKBiPA33173.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3842. Eukaryota.
ENOG410XP3S. LUCA.
GeneTreeiENSGT00390000007680.
HOGENOMiHOG000234110.
HOVERGENiHBG053559.
InParanoidiQ9HAT8.
KOiK11964.
OMAiHAPTQKH.
OrthoDBiEOG091G0631.
PhylomeDBiQ9HAT8.
TreeFamiTF314338.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000139946-MONOMER.
ReactomeiR-HSA-446652. Interleukin-1 signaling.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SIGNORiQ9HAT8.

Miscellaneous databases

ChiTaRSiPELI2. human.
EvolutionaryTraceiQ9HAT8.
GeneWikiiPELI2.
GenomeRNAii57161.
PROiQ9HAT8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000139946.
CleanExiHS_PELI2.
ExpressionAtlasiQ9HAT8. baseline and differential.
GenevisibleiQ9HAT8. HS.

Family and domain databases

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

Entry informationi

Entry nameiPELI2_HUMAN
AccessioniPrimary (citable) accession number: Q9HAT8
Secondary accession number(s): B2RDY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.