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Protein

Tax1-binding protein 1 homolog

Gene

Tax1bp1

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

Functioni

Inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. Degraded by caspase-3-like family proteins upon TNF-induced apoptosis. May also play a role in the pro-inflammatory cytokine IL-1 signaling cascade (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri750 – 77930UBZ-type 1Add
BLAST
Zinc fingeri780 – 81435UBZ-type 2Add
BLAST

GO - Molecular functioni

  • kinase binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • ubiquitin binding Source: BHF-UCL

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tax1-binding protein 1 homolog
Gene namesi
Name:Tax1bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1289308. Tax1bp1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 814814Tax1-binding protein 1 homologPRO_0000234555Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineBy similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei619 – 6191Phosphoserine; by IKKACurated
Modified residuei632 – 6321PhosphoserineCombined sources
Modified residuei693 – 6931Phosphoserine; by IKKACombined sources

Post-translational modificationi

Phosphorylated in the C-terminal region by CHUK/IKKA leading to NF-kappa-B signaling down-regulation.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UKC1.
MaxQBiQ3UKC1.
PaxDbiQ3UKC1.
PeptideAtlasiQ3UKC1.
PRIDEiQ3UKC1.

PTM databases

iPTMnetiQ3UKC1.
PhosphoSiteiQ3UKC1.

Expressioni

Developmental stagei

Expressed at E11.5 and E12.5 in distal limb and genital bud.1 Publication

Gene expression databases

BgeeiQ3UKC1.
ExpressionAtlasiQ3UKC1. baseline and differential.
GenevisibleiQ3UKC1. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts with TRAF6 in a IL-1-dependent manner. Interacts with STARD13 (By similarity). Interacts with TNFAIP3.By similarity1 Publication

GO - Molecular functioni

  • kinase binding Source: BHF-UCL
  • ubiquitin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi206586. 10 interactions.
IntActiQ3UKC1. 5 interactions.
MINTiMINT-1651528.
STRINGi10090.ENSMUSP00000079548.

Structurei

3D structure databases

ProteinModelPortaliQ3UKC1.
SMRiQ3UKC1. Positions 15-124, 750-814.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 420101OligomerizationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili144 – 623480Sequence analysisAdd
BLAST

Domaini

The C-terminal UBZ-type zinc fingers function as ubiquitin-binding domains.By similarity

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri750 – 77930UBZ-type 1Add
BLAST
Zinc fingeri780 – 81435UBZ-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGMS. Eukaryota.
ENOG410XQDF. LUCA.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000252947.
HOVERGENiHBG053034.
InParanoidiQ3UKC1.
OMAiRKMEGQN.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ3UKC1.
TreeFamiTF329501.

Family and domain databases

InterProiIPR012852. CALCOCO1-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UKC1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSFQEVQLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHSKDWV
60 70 80 90 100
GIFKVGWSTA RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY
110 120 130 140 150
QFCYVTHKGE IRGASTPFQF RAASPVEELL TMEDEGNSDM LVVTTKAGLL
160 170 180 190 200
ELKIEKTLKE KEELLKLIAV LEKETAQLRE QVGRMERELS QEKGRCEQLQ
210 220 230 240 250
AEQKGLLEVS QSLRVENEEF MKRYSDATAK VQQLEEDIVS VTHKAIEKET
260 270 280 290 300
DLDSLKDKLR KAQHEREQLE CQLQTEKDEK ELYKVHLKNT EIENTKLVSE
310 320 330 340 350
IQTLKNLDGN KESMITHFKE EISKLQSCLA DKENLYRALL LTTSNKEDTL
360 370 380 390 400
FLKEQLRKAE EQVQATRQEL IFLTKELSDA VNVRDKTMAD LHTARLENER
410 420 430 440 450
VKKQLADTLA ELQLHAVKKD QEKTDTLEHE LRREVEDLKL RLQMAADHYR
460 470 480 490 500
EKFKECQRLQ KQINKLSDQA ASTNSVFTKK MGSQQKVNDA SINTDPAAST
510 520 530 540 550
SASAVDVKPA ASCAETGFDM STKDHVCEMT KEIAEKIEKY NKCKQLLQDE
560 570 580 590 600
KTKCNKYAEE LAKMELKWKE QVKIAENVKL ELAEVEDNYK VQLAEKEKEI
610 620 630 640 650
NGLASYLENL SREKELTKSL EDQKGRKLEG QSPQQVSRCL NTCSEQNGLL
660 670 680 690 700
PPLSSAQPVL QYGNPYSAQE TRDGADGAFY PDEIQRPPVR VPSWEDNVVC
710 720 730 740 750
SQPARNLSRP DGLEDPEDSR EDENVPIPPD PANQHLRSHG AGFCFDSSFD
760 770 780 790 800
VHKKCPLCEL MFPPNYDQTK FEEHVESHWK VCPMCSEQFP PDYDQQGFER
810
HVQTHFDQNV LNFD
Length:814
Mass (Da):93,630
Last modified:May 16, 2006 - v2
Checksum:i828A1FC7D61A06B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti328 – 3281C → S in BAB23383 (PubMed:16141072).Curated
Sequence conflicti368 – 3681Q → P in BAB23383 (PubMed:16141072).Curated
Sequence conflicti429 – 4291H → Y in BAE26880 (PubMed:16141072).Curated
Sequence conflicti658 – 6581P → T in BAB23383 (PubMed:16141072).Curated
Sequence conflicti751 – 7511V → A in AAH14798 (PubMed:15489334).Curated
Sequence conflicti764 – 7641P → H in BAB25721 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004574 mRNA. Translation: BAB23383.1.
AK008528 mRNA. Translation: BAB25721.1.
AK146076 mRNA. Translation: BAE26880.1.
BC014798 mRNA. Translation: AAH14798.1.
CCDSiCCDS39490.1.
RefSeqiNP_080092.2. NM_025816.3.
XP_006506432.1. XM_006506369.2.
UniGeneiMm.389757.

Genome annotation databases

EnsembliENSMUST00000080723; ENSMUSP00000079548; ENSMUSG00000004535.
GeneIDi52440.
KEGGimmu:52440.
UCSCiuc009byz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004574 mRNA. Translation: BAB23383.1.
AK008528 mRNA. Translation: BAB25721.1.
AK146076 mRNA. Translation: BAE26880.1.
BC014798 mRNA. Translation: AAH14798.1.
CCDSiCCDS39490.1.
RefSeqiNP_080092.2. NM_025816.3.
XP_006506432.1. XM_006506369.2.
UniGeneiMm.389757.

3D structure databases

ProteinModelPortaliQ3UKC1.
SMRiQ3UKC1. Positions 15-124, 750-814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206586. 10 interactions.
IntActiQ3UKC1. 5 interactions.
MINTiMINT-1651528.
STRINGi10090.ENSMUSP00000079548.

PTM databases

iPTMnetiQ3UKC1.
PhosphoSiteiQ3UKC1.

Proteomic databases

EPDiQ3UKC1.
MaxQBiQ3UKC1.
PaxDbiQ3UKC1.
PeptideAtlasiQ3UKC1.
PRIDEiQ3UKC1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080723; ENSMUSP00000079548; ENSMUSG00000004535.
GeneIDi52440.
KEGGimmu:52440.
UCSCiuc009byz.2. mouse.

Organism-specific databases

CTDi8887.
MGIiMGI:1289308. Tax1bp1.

Phylogenomic databases

eggNOGiENOG410IGMS. Eukaryota.
ENOG410XQDF. LUCA.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000252947.
HOVERGENiHBG053034.
InParanoidiQ3UKC1.
OMAiRKMEGQN.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ3UKC1.
TreeFamiTF329501.

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiTax1bp1. mouse.
PROiQ3UKC1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UKC1.
ExpressionAtlasiQ3UKC1. baseline and differential.
GenevisibleiQ3UKC1. MM.

Family and domain databases

InterProiIPR012852. CALCOCO1-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Lung, Placenta and Small intestine.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases."
    de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R., Fiers W., Jeang K.-T., Beyaert R.
    Oncogene 18:4182-4190(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFAIP3.
  4. "Conserved expression domains for genes upstream and within the HoxA and HoxD clusters suggests a long-range enhancer existed before cluster duplication."
    Lehoczky J.A., Williams M.E., Innis J.W.
    Evol. Dev. 6:423-430(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-632 AND SER-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTAXB1_MOUSE
AccessioniPrimary (citable) accession number: Q3UKC1
Secondary accession number(s): Q91YT6, Q9CVF0, Q9DC45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: July 6, 2016
This is version 90 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. 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.