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Protein

Tax1-binding protein 3

Gene

TAX1BP3

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

Functioni

May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6.3 Publications

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

BRENDAi3.5.1.2. 2681.
ReactomeiREACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.

Names & Taxonomyi

Protein namesi
Recommended name:
Tax1-binding protein 3
Alternative name(s):
Glutaminase-interacting protein 3
Tax interaction protein 1
Short name:
TIP-1
Tax-interacting protein 1
Gene namesi
Name:TAX1BP3Imported
Synonyms:TIP1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:30684. TAX1BP3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201K → A: Abolishes interaction with KCNJ4. 1 Publication
Mutagenesisi90 – 901H → A: Abolishes interaction with KCNJ4. 1 Publication

Organism-specific databases

PharmGKBiPA134950693.

Polymorphism and mutation databases

BioMutaiTAX1BP3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 124123Tax1-binding protein 3PRO_0000233943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei61 – 611Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14907.
PaxDbiO14907.
PRIDEiO14907.

2D gel databases

UCD-2DPAGEO14907.

PTM databases

PhosphoSiteiO14907.

Expressioni

Tissue specificityi

Ubiquitous. Detected in brain, heart, kidney, lung, small intestine and skeletal muscle. Detected in various cell lines including HeLa. Weakly expressed in peripheral blood leukocytes.2 Publications

Gene expression databases

BgeeiO14907.
CleanExiHS_TAX1BP3.
ExpressionAtlasiO14907. baseline.
GenevestigatoriO14907.

Organism-specific databases

HPAiHPA063078.

Interactioni

Subunit structurei

Interacts (via its PDZ domain) with GLS2. Interacts (via its PDZ domain) with RTKN (via the C-terminal region); this interaction facilitates Rho-mediated activation of the FOS serum response element (SRE). Interacts (via its PDZ domain) with CTNNB1; this interaction inhibits the transcriptional activity of CTNNB1. Interacts with HTLV-1 TAX protein. Interacts (via PDZ domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via C-terminus). Competes with LIN7A for KCNJ4 binding.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E6P031262EBI-723259,EBI-1177242From a different organism.
RNF183Q96D593EBI-723259,EBI-743938

Protein-protein interaction databases

BioGridi119061. 18 interactions.
IntActiO14907. 11 interactions.
MINTiMINT-142501.
STRINGi9606.ENSP00000225525.

Structurei

Secondary structure

1
124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi12 – 198Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 356Combined sources
Beta strandi37 – 393Combined sources
Helixi41 – 433Combined sources
Turni45 – 473Combined sources
Beta strandi48 – 503Combined sources
Beta strandi54 – 607Combined sources
Beta strandi62 – 643Combined sources
Helixi65 – 695Combined sources
Beta strandi76 – 805Combined sources
Beta strandi83 – 853Combined sources
Helixi90 – 978Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi115 – 1184Combined sources
Turni121 – 1233Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KG2NMR-A2-124[»]
2L4SNMR-A1-124[»]
2L4TNMR-A1-124[»]
2VZ5X-ray1.74A13-113[»]
3GJ9X-ray2.80A/B1-124[»]
3SFJX-ray1.24A/C10-112[»]
4E3BX-ray1.50A/B11-112[»]
4NNLX-ray1.50A/B10-112[»]
4NNMX-ray1.60A/B10-120[»]
ProteinModelPortaliO14907.
SMRiO14907. Positions 9-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 11298PDZPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG236405.
GeneTreeiENSGT00390000002877.
HOGENOMiHOG000015753.
HOVERGENiHBG052814.
InParanoidiO14907.
OMAiDPTQNPF.
OrthoDBiEOG7S4X7S.
PhylomeDBiO14907.
TreeFamiTF318964.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR017268. Tax1-binding_p3.
[Graphical view]
PANTHERiPTHR23136. PTHR23136. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF037712. Tax1-binding_p3. 1 hit.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O14907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK
60 70 80 90 100
TDKGIYVTRV SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR
110 120
SEEVVRLLVT RQSLQKAVQQ SMLS
Length:124
Mass (Da):13,735
Last modified:March 1, 2001 - v2
Checksum:iFF0BCDF475F682CD
GO

Sequence cautioni

The sequence AAF43104.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028823 mRNA. Translation: AAB84248.2.
AF168787 Genomic DNA. Translation: AAF43104.1. Different initiation.
AF234997 mRNA. Translation: AAG44368.1.
AF277318 mRNA. Translation: AAK69111.1.
AK315408 mRNA. Translation: BAG37800.1.
CH471108 Genomic DNA. Translation: EAW90491.1.
CH471108 Genomic DNA. Translation: EAW90492.1.
BC023980 mRNA. Translation: AAH23980.1.
CCDSiCCDS11032.1.
RefSeqiNP_001191627.1. NM_001204698.1.
NP_055419.1. NM_014604.3.
UniGeneiHs.12956.
Hs.731607.

Genome annotation databases

EnsembliENST00000225525; ENSP00000225525; ENSG00000213977.
GeneIDi30851.
KEGGihsa:30851.
UCSCiuc002fwc.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF028823 mRNA. Translation: AAB84248.2.
AF168787 Genomic DNA. Translation: AAF43104.1. Different initiation.
AF234997 mRNA. Translation: AAG44368.1.
AF277318 mRNA. Translation: AAK69111.1.
AK315408 mRNA. Translation: BAG37800.1.
CH471108 Genomic DNA. Translation: EAW90491.1.
CH471108 Genomic DNA. Translation: EAW90492.1.
BC023980 mRNA. Translation: AAH23980.1.
CCDSiCCDS11032.1.
RefSeqiNP_001191627.1. NM_001204698.1.
NP_055419.1. NM_014604.3.
UniGeneiHs.12956.
Hs.731607.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KG2NMR-A2-124[»]
2L4SNMR-A1-124[»]
2L4TNMR-A1-124[»]
2VZ5X-ray1.74A13-113[»]
3GJ9X-ray2.80A/B1-124[»]
3SFJX-ray1.24A/C10-112[»]
4E3BX-ray1.50A/B11-112[»]
4NNLX-ray1.50A/B10-112[»]
4NNMX-ray1.60A/B10-120[»]
ProteinModelPortaliO14907.
SMRiO14907. Positions 9-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119061. 18 interactions.
IntActiO14907. 11 interactions.
MINTiMINT-142501.
STRINGi9606.ENSP00000225525.

PTM databases

PhosphoSiteiO14907.

Polymorphism and mutation databases

BioMutaiTAX1BP3.

2D gel databases

UCD-2DPAGEO14907.

Proteomic databases

MaxQBiO14907.
PaxDbiO14907.
PRIDEiO14907.

Protocols and materials databases

DNASUi30851.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225525; ENSP00000225525; ENSG00000213977.
GeneIDi30851.
KEGGihsa:30851.
UCSCiuc002fwc.3. human.

Organism-specific databases

CTDi30851.
GeneCardsiGC17M003566.
HGNCiHGNC:30684. TAX1BP3.
HPAiHPA063078.
neXtProtiNX_O14907.
PharmGKBiPA134950693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG236405.
GeneTreeiENSGT00390000002877.
HOGENOMiHOG000015753.
HOVERGENiHBG052814.
InParanoidiO14907.
OMAiDPTQNPF.
OrthoDBiEOG7S4X7S.
PhylomeDBiO14907.
TreeFamiTF318964.

Enzyme and pathway databases

BRENDAi3.5.1.2. 2681.
ReactomeiREACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.

Miscellaneous databases

ChiTaRSiTAX1BP3. human.
EvolutionaryTraceiO14907.
GeneWikiiTAX1BP3.
GenomeRNAii30851.
NextBioi52992.
PROiO14907.

Gene expression databases

BgeeiO14907.
CleanExiHS_TAX1BP3.
ExpressionAtlasiO14907. baseline.
GenevestigatoriO14907.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
IPR017268. Tax1-binding_p3.
[Graphical view]
PANTHERiPTHR23136. PTHR23136. 1 hit.
PfamiPF00595. PDZ. 1 hit.
[Graphical view]
PIRSFiPIRSF037712. Tax1-binding_p3. 1 hit.
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins."
    Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.
    Oncogene 16:643-654(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HTLV-1 TAX.
    Tissue: Peripheral blood lymphocyteImported.
  2. "The genomic region encompassing the nephropathic cystinosis gene (CTNS): complete sequencing of a 200-kb segment and discovery of a novel gene within the common cystinosis-causing deletion."
    Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G., Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A., Green E.D.
    Genome Res. 10:165-173(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The C-terminus of human glutaminase L mediates association with PDZ domain-containing proteins."
    Olalla L., Aledo J.C., Bannenberg G., Marquez J.
    FEBS Lett. 488:116-122(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GLS2.
    Tissue: BrainImported.
  4. "hPWP1-interacting proteins 2 and 11 (Tax-interacting protein 1)."
    Honore B.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: OvaryImported.
  5. "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: Tongue.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: KidneyImported.
  8. "The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element."
    Reynaud C., Fabre S., Jalinot P.
    J. Biol. Chem. 275:33962-33968(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RTKN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. Cited for: FUNCTION, INTERACTION WITH KCNJ4, MUTAGENESIS OF LYS-20 AND HIS-90, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which activates Cdc42."
    Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L., Hampson I.N.
    Br. J. Cancer 104:324-331(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARHGEF16.
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "Solution structure of the human Tax-interacting protein-1."
    Durney M.A., Birrane G., Anklin C., Soni A., Ladias J.A.
    J. Biomol. NMR 45:329-334(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, INTERACTION WITH KCNJ4.
  17. "Molecular mechanism of inward rectifier potassium channel 2.3 regulation by tax-interacting protein-1."
    Yan X., Zhou H., Zhang J., Shi C., Xie X., Wu Y., Tian C., Shen Y., Long J.
    J. Mol. Biol. 392:967-976(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), INTERACTION WITH KCNJ4.
  18. "The structure of the PDZ domain of TAX1BP."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 13-124.
  19. "Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L."
    Zoetewey D.L., Ovee M., Banerjee M., Bhaskaran R., Mohanty S.
    Biochemistry 50:3528-3539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH GLS2, INTERACTION WITH GLS2.

Entry informationi

Entry nameiTX1B3_HUMAN
AccessioniPrimary (citable) accession number: O14907
Secondary accession number(s): B2RD53, D3DTJ6, Q7LCQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2001
Last modified: May 27, 2015
This is version 121 of the entry and version 2 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.