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Q9HAT8

- PELI2_HUMAN

UniProt

Q9HAT8 - PELI2_HUMAN

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Protein

E3 ubiquitin-protein ligase pellino homolog 2

Gene

PELI2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW

GO - Biological processi

  1. innate immune response Source: Reactome
  2. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Reactome
  4. positive regulation of MAPK cascade Source: MGI
  5. positive regulation of protein phosphorylation Source: MGI
  6. protein ubiquitination Source: UniProtKB-UniPathway
  7. toll-like receptor 10 signaling pathway Source: Reactome
  8. toll-like receptor 2 signaling pathway Source: Reactome
  9. toll-like receptor 4 signaling pathway Source: Reactome
  10. toll-like receptor 5 signaling pathway Source: Reactome
  11. toll-like receptor 9 signaling pathway Source: Reactome
  12. toll-like receptor signaling pathway Source: Reactome
  13. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  14. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  15. Toll signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:8828. PELI2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061R → A: Abolishes binding to IRAK1. 1 Publication
Mutagenesisi187 – 1871T → A: Abolishes binding to IRAK1; when associated with A-188. 1 Publication
Mutagenesisi188 – 1881N → A: Abolishes binding to IRAK1; when associated with A-187. 1 Publication
Mutagenesisi397 – 3971C → A: Loss of IRAK1-polyubiquitination. 1 Publication
Mutagenesisi400 – 4001C → A: Loss of IRAK1-polyubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA33173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 420420E3 ubiquitin-protein ligase pellino homolog 2PRO_0000194174Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HAT8.
PaxDbiQ9HAT8.
PRIDEiQ9HAT8.

PTM databases

PhosphoSiteiQ9HAT8.

Expressioni

Gene expression databases

BgeeiQ9HAT8.
CleanExiHS_PELI2.
ExpressionAtlasiQ9HAT8. baseline and differential.
GenevestigatoriQ9HAT8.

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 interactions.
DIPiDIP-31350N.
IntActiQ9HAT8. 14 interactions.
MINTiMINT-2845048.
STRINGi9606.ENSP00000267460.

Structurei

Secondary structure

1
420
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247
Beta strandi41 – 466
Beta strandi53 – 6311
Beta strandi76 – 827
Beta strandi84 – 9613
Beta strandi99 – 1068
Beta strandi113 – 1153
Beta strandi141 – 1488
Beta strandi153 – 1586
Beta strandi164 – 1685
Beta strandi174 – 1763
Beta strandi182 – 1843
Beta strandi190 – 1934
Beta strandi208 – 2114
Beta strandi215 – 2184
Beta strandi222 – 2254
Beta strandi245 – 2473
Beta strandi252 – 2576
Helixi258 – 2636
Helixi266 – 2694
Helixi270 – 2767

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EGAX-ray1.80A15-275[»]
3EGBX-ray3.25A/B7-289[»]
ProteinModelPortaliQ9HAT8.
SMRiQ9HAT8. Positions 15-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HAT8.

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 IRAK1.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG258040.
GeneTreeiENSGT00390000007680.
HOGENOMiHOG000234110.
HOVERGENiHBG053559.
InParanoidiQ9HAT8.
KOiK11964.
OMAiHAPTQKH.
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:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi37999785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF302502 mRNA. Translation: AAG15390.1 .
AK315727 mRNA. Translation: BAG38082.1 .
CH471061 Genomic DNA. Translation: EAW80689.1 .
BC009476 mRNA. Translation: AAH09476.1 .
CCDSi CCDS9726.1.
RefSeqi NP_067078.1. NM_021255.2.
UniGenei Hs.657926.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3EGA X-ray 1.80 A 15-275 [» ]
3EGB X-ray 3.25 A/B 7-289 [» ]
ProteinModelPortali Q9HAT8.
SMRi Q9HAT8. Positions 15-258.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121417. 18 interactions.
DIPi DIP-31350N.
IntActi Q9HAT8. 14 interactions.
MINTi MINT-2845048.
STRINGi 9606.ENSP00000267460.

PTM databases

PhosphoSitei Q9HAT8.

Polymorphism databases

DMDMi 37999785.

Proteomic databases

MaxQBi Q9HAT8.
PaxDbi Q9HAT8.
PRIDEi Q9HAT8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000267460 ; ENSP00000267460 ; ENSG00000139946 .
GeneIDi 57161.
KEGGi hsa:57161.
UCSCi uc001xch.3. human.

Organism-specific databases

CTDi 57161.
GeneCardsi GC14P056585.
HGNCi HGNC:8828. PELI2.
MIMi 614798. gene.
neXtProti NX_Q9HAT8.
PharmGKBi PA33173.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258040.
GeneTreei ENSGT00390000007680.
HOGENOMi HOG000234110.
HOVERGENi HBG053559.
InParanoidi Q9HAT8.
KOi K11964.
OMAi HAPTQKH.
PhylomeDBi Q9HAT8.
TreeFami TF314338.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_22442. Interleukin-1 signaling.
REACT_24918. IRAK1 recruits IKK complex.
REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.

Miscellaneous databases

EvolutionaryTracei Q9HAT8.
GeneWikii PELI2.
GenomeRNAii 57161.
NextBioi 63165.
PROi Q9HAT8.
SOURCEi Search...

Gene expression databases

Bgeei Q9HAT8.
CleanExi HS_PELI2.
ExpressionAtlasi Q9HAT8. baseline and differential.
Genevestigatori Q9HAT8.

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].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Lung.
  5. "Pellino2 activates the mitogen activated protein kinase pathway."
    Jensen L.E., Whitehead A.S.
    FEBS Lett. 545:199-202(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRAF6 AND MAP3K7.
  6. "Characterization of Pellino2, a substrate of IRAK1 and IRAK4."
    Strelow A., Kollewe C., Wesche H.
    FEBS Lett. 547:157-161(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH IRAK1 AND IRAK4.
  7. "Kinase-active interleukin-1 receptor-associated kinases promote polyubiquitination and degradation of the Pellino family: direct evidence for PELLINO proteins being ubiquitin-protein isopeptide ligases."
    Butler M.P., Hanly J.A., Moynagh P.N.
    J. Biol. Chem. 282:29729-29737(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS E3 UBIQUITIN LIGASE.
  8. "The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1."
    Ordureau A., Smith H., Windheim M., Peggie M., Carrick E., Morrice N., Cohen P.
    Biochem. J. 409:43-52(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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, MUTAGENESIS OF CYS-397 AND CYS-400.
  10. "Pellino proteins contain a cryptic FHA domain that mediates interaction with phosphorylated IRAK1."
    Lin C.C., Huoh Y.S., Schmitz K.R., Jensen L.E., Ferguson K.M.
    Structure 16:1806-1816(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 15-275, DOMAIN FHA, MUTAGENESIS OF ARG-106; THR-187 AND ASN-188.

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: October 29, 2014
This is version 102 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

External Data

Dasty 3