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Q9H0E2

- TOLIP_HUMAN

UniProt

Q9H0E2 - TOLIP_HUMAN

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Protein
Toll-interacting protein
Gene
TOLLIP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity.1 Publication

GO - Molecular functioni

  1. Toll-like receptor binding Source: UniProtKB
  2. kinase binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. signal transducer activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. epithelial cell differentiation Source: UniProt
  3. inflammatory response Source: UniProtKB
  4. innate immune response Source: UniProtKB-KW
  5. intracellular signal transduction Source: UniProtKB
  6. leukocyte activation Source: UniProtKB
  7. phosphorylation Source: UniProtKB
  8. positive regulation of protein sumoylation Source: Ensembl
  9. protein localization to endosome Source: UniProt
  10. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_22442. Interleukin-1 signaling.
SignaLinkiQ9H0E2.

Names & Taxonomyi

Protein namesi
Recommended name:
Toll-interacting protein
Gene namesi
Name:TOLLIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16476. TOLLIP.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. interleukin-1 receptor complex Source: UniProtKB
  5. interleukin-18 receptor complex Source: UniProtKB
  6. nuclear body Source: Ensembl
  7. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134876213.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 274273Toll-interacting protein
PRO_0000072625Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Post-translational modificationi

Phosphorylated by IRAK1 upon stimulation by IL-1 or microbial products.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0E2.
PaxDbiQ9H0E2.
PRIDEiQ9H0E2.

PTM databases

PhosphoSiteiQ9H0E2.

Expressioni

Gene expression databases

ArrayExpressiQ9H0E2.
BgeeiQ9H0E2.
CleanExiHS_TOLLIP.
GenevestigatoriQ9H0E2.

Organism-specific databases

HPAiHPA038621.
HPA038622.

Interactioni

Subunit structurei

Oligomerizes. Binds to TLR2 and the TLR4-MD2 complex via its C-terminus. Exists as complex with IRAK1 in unstimulated cells. Upon IL-1 signaling, Tollip binds to the activated IL-1 receptor complex containing IL-1RI, IL-1RacP and the adapter protein MyD88, where it interacts with the TIR domain of IL-1RacP. MyD88 then triggers IRAK1 autophosphorylation, which in turn leads to the dissociation of IRAK1 from Tollip and IL-1RAcP. Interacts with TOM1L2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSTF1Q050482EBI-74615,EBI-1789619
DAZAP2Q150383EBI-74615,EBI-724310
DZIP3Q86Y132EBI-74615,EBI-948630
EIF2AK2P195252EBI-74615,EBI-640775
IRAK2O431872EBI-74615,EBI-447733
PEG10Q86TG72EBI-74615,EBI-2858265
TOM1L1O756743EBI-74615,EBI-712991
WRNIP1Q96S552EBI-74615,EBI-2513471

Protein-protein interaction databases

BioGridi119978. 71 interactions.
IntActiQ9H0E2. 43 interactions.
MINTiMINT-4539075.
STRINGi9606.ENSP00000314733.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi231 – 24010
Beta strandi242 – 2443
Helixi246 – 2538
Turni254 – 2585
Helixi260 – 26910

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGLNMR-A229-274[»]
ProteinModelPortaliQ9H0E2.
SMRiQ9H0E2. Positions 48-174, 231-274.

Miscellaneous databases

EvolutionaryTraceiQ9H0E2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 13596C2
Add
BLAST
Domaini229 – 27244CUE
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 4417Gln-rich
Add
BLAST

Sequence similaritiesi

Belongs to the tollip family.
Contains 1 C2 domain.
Contains 1 CUE domain.

Phylogenomic databases

eggNOGiNOG85357.
HOGENOMiHOG000293427.
HOVERGENiHBG054213.
KOiK05402.
OMAiHVTIPES.
PhylomeDBiQ9H0E2.
TreeFamiTF324180.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR003892. CUE.
IPR009060. UBA-like.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00546. CUE. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF49562. SSF49562. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H0E2-1 [UniParc]FASTAAdd to Basket

« Hide

MATTVSTQRG PVYIGELPQD FLRITPTQQQ RQVQLDAQAA QQLQYGGAVG    50
TVGRLNITVV QAKLAKNYGM TRMDPYCRLR LGYAVYETPT AHNGAKNPRW 100
NKVIHCTVPP GVDSFYLEIF DERAFSMDDR IAWTHITIPE SLRQGKVEDK 150
WYSLSGRQGD DKEGMINLVM SYALLPAAMV MPPQPVVLMP TVYQQGVGYV 200
PITGMPAVCS PGMVPVALPP AAVNAQPRCS EEDLKAIQDM FPNMDQEVIR 250
SVLEAQRGNK DAAINSLLQM GEEP 274
Length:274
Mass (Da):30,282
Last modified:March 1, 2001 - v1
Checksum:i386E0F284D3837DA
GO

Sequence cautioni

The sequence BAB14283.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti222 – 2221A → S.
Corresponds to variant rs5744015 [ dbSNP | Ensembl ].
VAR_034557

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401Missing in CAB58118. 1 Publication
Sequence conflicti150 – 1501K → E in BAB14283. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242972 mRNA. Translation: CAB58118.1.
AL136835 mRNA. Translation: CAB66769.1.
BC004420 mRNA. Translation: AAH04420.1.
BC012057 mRNA. Translation: AAH12057.1.
BC018272 mRNA. Translation: AAH18272.1.
AK022871 mRNA. Translation: BAB14283.1. Different initiation.
CCDSiCCDS7723.1.
RefSeqiNP_061882.2. NM_019009.3.
UniGeneiHs.368527.

Genome annotation databases

EnsembliENST00000317204; ENSP00000314733; ENSG00000078902.
GeneIDi54472.
KEGGihsa:54472.
UCSCiuc001ltd.3. human.

Polymorphism databases

DMDMi20140803.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ242972 mRNA. Translation: CAB58118.1 .
AL136835 mRNA. Translation: CAB66769.1 .
BC004420 mRNA. Translation: AAH04420.1 .
BC012057 mRNA. Translation: AAH12057.1 .
BC018272 mRNA. Translation: AAH18272.1 .
AK022871 mRNA. Translation: BAB14283.1 . Different initiation.
CCDSi CCDS7723.1.
RefSeqi NP_061882.2. NM_019009.3.
UniGenei Hs.368527.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WGL NMR - A 229-274 [» ]
ProteinModelPortali Q9H0E2.
SMRi Q9H0E2. Positions 48-174, 231-274.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119978. 71 interactions.
IntActi Q9H0E2. 43 interactions.
MINTi MINT-4539075.
STRINGi 9606.ENSP00000314733.

PTM databases

PhosphoSitei Q9H0E2.

Polymorphism databases

DMDMi 20140803.

Proteomic databases

MaxQBi Q9H0E2.
PaxDbi Q9H0E2.
PRIDEi Q9H0E2.

Protocols and materials databases

DNASUi 54472.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317204 ; ENSP00000314733 ; ENSG00000078902 .
GeneIDi 54472.
KEGGi hsa:54472.
UCSCi uc001ltd.3. human.

Organism-specific databases

CTDi 54472.
GeneCardsi GC11M001295.
HGNCi HGNC:16476. TOLLIP.
HPAi HPA038621.
HPA038622.
MIMi 606277. gene.
neXtProti NX_Q9H0E2.
PharmGKBi PA134876213.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG85357.
HOGENOMi HOG000293427.
HOVERGENi HBG054213.
KOi K05402.
OMAi HVTIPES.
PhylomeDBi Q9H0E2.
TreeFami TF324180.

Enzyme and pathway databases

Reactomei REACT_22442. Interleukin-1 signaling.
SignaLinki Q9H0E2.

Miscellaneous databases

EvolutionaryTracei Q9H0E2.
GeneWikii TOLLIP.
GenomeRNAii 54472.
NextBioi 56772.
PROi Q9H0E2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H0E2.
Bgeei Q9H0E2.
CleanExi HS_TOLLIP.
Genevestigatori Q9H0E2.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR003892. CUE.
IPR009060. UBA-like.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF02845. CUE. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00546. CUE. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF49562. SSF49562. 1 hit.
PROSITEi PS51140. CUE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Tollip, a new component of the IL-1R1 pathway, links IRAK to the IL-1 receptor."
    Burns K., Clatworthy J., Martin L., Martinon F., Plumpton C., Maschera B., Lewis A., Ray K., Tschopp J., Volpe F.
    Nat. Cell Biol. 2:346-351(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  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].
    Tissue: Eye and Placenta.
  4. "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] OF 34-274.
  5. "Negative regulation of Toll-like receptor-mediated signaling by Tollip."
    Zhang G., Ghosh S.
    J. Biol. Chem. 277:7059-7065(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLR2 AND TLR4, FUNCTION.
  6. "Recruitment of clathrin onto endosomes by the Tom1-Tollip complex."
    Katoh Y., Imakagura H., Futatsumori M., Nakayama K.
    Biochem. Biophys. Res. Commun. 341:143-149(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOM1L2.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "Solution structure of CUE domain in the C-terminal of human Toll-interacting protein (TOLLIP)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 229-274.

Entry informationi

Entry nameiTOLIP_HUMAN
AccessioniPrimary (citable) accession number: Q9H0E2
Secondary accession number(s): Q9H9E6, Q9UJ69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 124 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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