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Protein

Tax1-binding protein 1

Gene

TAX1BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri725 – 75430UBZ-type 1Add
BLAST
Zinc fingeri755 – 78935UBZ-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tax1-binding protein 1
Alternative name(s):
TRAF6-binding protein
Gene namesi
Name:TAX1BP1
Synonyms:T6BP
ORF Names:PRO0105
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:11575. TAX1BP1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36339.

Polymorphism and mutation databases

BioMutaiTAX1BP1.
DMDMi97202549.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 789789Tax1-binding protein 1PRO_0000234554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei225 – 2251Phosphoserine1 Publication
Modified residuei593 – 5931Phosphoserine; by IKKA1 Publication
Modified residuei666 – 6661Phosphoserine; by IKKA1 Publication

Post-translational modificationi

Phosphorylated in the C-terminal region by CHUK/IKKA leading to NF-kappa-B signaling down-regulation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86VP1.
PaxDbiQ86VP1.
PRIDEiQ86VP1.

PTM databases

PhosphoSiteiQ86VP1.

Expressioni

Tissue specificityi

Expressed in all tissues tested.

Gene expression databases

BgeeiQ86VP1.
CleanExiHS_TAX1BP1.
ExpressionAtlasiQ86VP1. baseline and differential.
GenevestigatoriQ86VP1.

Organism-specific databases

HPAiHPA024432.

Interactioni

Subunit structurei

Homooligomer. Interacts with TRAF6 in a IL-1-dependent manner. Interacts with TNFAIP3. Interacts with STARD13. Interacts with the HTLV-1 protein Tax-1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8KAD63EBI-529518,EBI-10174974
Q8WU023EBI-529518,EBI-747182
CHUKO151112EBI-529518,EBI-81249
COG7P834363EBI-529518,EBI-389534
CXXC1Q9P0U43EBI-529518,EBI-949911
DAZAP2Q150383EBI-529518,EBI-724310
DSTNP609813EBI-529518,EBI-745191
EMILIN1Q9Y6C23EBI-529518,EBI-744586
FAM168AQ925673EBI-529518,EBI-7957930
FOXC2Q999583EBI-529518,EBI-3956892
HEL-S-61V9HW293EBI-529518,EBI-10330057
LGALS8O002143EBI-529518,EBI-740058
LMO3Q8TAP43EBI-529518,EBI-742259
MRPL11Q9Y3B73EBI-529518,EBI-5453723
MRPL53Q96EL33EBI-529518,EBI-2513715
NMRK1Q9NWW63EBI-529518,EBI-10315485
PLEKHN1Q494U13EBI-529518,EBI-10241513
RAB18Q9NP723EBI-529518,EBI-722247
RAD18Q9NS913EBI-529518,EBI-2339393
RALBP1Q153113EBI-529518,EBI-749285
RNF11Q9Y3C52EBI-529518,EBI-396669
SSX2BQ163853EBI-529518,EBI-2210673
STARD13Q9Y3M82EBI-529518,EBI-465487
TCEA2Q155603EBI-529518,EBI-710310
TNIP1Q150253EBI-529518,EBI-357849
TNIP3Q96KP63EBI-529518,EBI-2509913
TRAF6Q9Y4K38EBI-529518,EBI-359276
TSG101Q998163EBI-529518,EBI-346882
TSHZ3A1L0U73EBI-529518,EBI-10171826
UBCP0CG485EBI-529518,EBI-3390054

Protein-protein interaction databases

BioGridi114405. 58 interactions.
DIPiDIP-33010N.
IntActiQ86VP1. 47 interactions.
MINTiMINT-200894.
STRINGi9606.ENSP00000379612.

Structurei

Secondary structure

1
789
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 216Combined sources
Beta strandi24 – 263Combined sources
Beta strandi32 – 387Combined sources
Beta strandi49 – 546Combined sources
Helixi60 – 623Combined sources
Beta strandi63 – 686Combined sources
Beta strandi81 – 877Combined sources
Helixi89 – 913Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi727 – 7293Combined sources
Beta strandi731 – 7344Combined sources
Helixi743 – 7519Combined sources
Beta strandi754 – 7563Combined sources
Turni758 – 7603Combined sources
Helixi770 – 78213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M7QNMR-A725-789[»]
4BMJX-ray2.75A/B/C/D/E/F/G/H/I/J/K725-789[»]
4NLHX-ray1.90A/B15-147[»]
ProteinModelPortaliQ86VP1.
SMRiQ86VP1. Positions 15-124, 150-239, 725-789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili144 – 599456Sequence AnalysisAdd
BLAST

Domaini

The C-terminal UBZ-type zinc fingers function as ubiquitin-binding domains.1 Publication

Sequence similaritiesi

Contains 2 UBZ-type zinc fingers.Sequence Analysis

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri725 – 75430UBZ-type 1Add
BLAST
Zinc fingeri755 – 78935UBZ-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG135564.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000271638.
HOVERGENiHBG053034.
InParanoidiQ86VP1.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ86VP1.
TreeFamiTF329501.

Family and domain databases

InterProiIPR012852. CoCoA.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86VP1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSFQEVPLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHPKDWV
60 70 80 90 100
GIFKVGWSTA RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY
110 120 130 140 150
QFCYVTHKGE IRGASTPFQF RASSPVEELL TMEDEGNSDM LVVTTKAGLL
160 170 180 190 200
ELKIEKTMKE KEELLKLIAV LEKETAQLRE QVGRMERELN HEKERCDQLQ
210 220 230 240 250
AEQKGLTEVT QSLKMENEEF KKRFSDATSK AHQLEEDIVS VTHKAIEKET
260 270 280 290 300
ELDSLKDKLK KAQHEREQLE CQLKTEKDEK ELYKVHLKNT EIENTKLMSE
310 320 330 340 350
VQTLKNLDGN KESVITHFKE EIGRLQLCLA EKENLQRTFL LTTSSKEDTC
360 370 380 390 400
FLKEQLRKAE EQVQATRQEV VFLAKELSDA VNVRDRTMAD LHTARLENEK
410 420 430 440 450
VKKQLADAVA ELKLNAMKKD QDKTDTLEHE LRREVEDLKL RLQMAADHYK
460 470 480 490 500
EKFKECQRLQ KQINKLSDQS ANNNNVFTKK TGNQQKVNDA SVNTDPATSA
510 520 530 540 550
STVDVKPSPS AAEADFDIVT KGQVCEMTKE IADKTEKYNK CKQLLQDEKA
560 570 580 590 600
KCNKYADELA KMELKWKEQV KIAENVKLEL AEVQDNYKEL KRSLENPAER
610 620 630 640 650
KMEGQNSQSP QCFKTCSEQN GYVLTLSNAQ PVLQYGNPYA SQETRDGADG
660 670 680 690 700
AFYPDEIQRP PVRVPSWGLE DNVVCSQPAR NFSRPDGLED SEDSKEDENV
710 720 730 740 750
PTAPDPPSQH LRGHGTGFCF DSSFDVHKKC PLCELMFPPN YDQSKFEEHV
760 770 780
ESHWKVCPMC SEQFPPDYDQ QVFERHVQTH FDQNVLNFD
Length:789
Mass (Da):90,877
Last modified:May 16, 2006 - v2
Checksum:iDE8460DAA6712125
GO
Isoform 2 (identifier: Q86VP1-2) [UniParc]FASTAAdd to basket

Also known as: TXBP151-L

The sequence of this isoform differs from the canonical sequence as follows:
     604-645: Missing.

Show »
Length:747
Mass (Da):86,257
Checksum:i93EEDFF29106CE1C
GO
Isoform 3 (identifier: Q86VP1-3) [UniParc]FASTAAdd to basket

Also known as: TXBP151-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-184: Missing.
     604-645: Missing.

Show »
Length:563
Mass (Da):65,112
Checksum:iEFA52B16B4408B9C
GO
Isoform 4 (identifier: Q86VP1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-157: Missing.
     604-645: Missing.

Note: No experimental confirmation available.

Show »
Length:590
Mass (Da):68,277
Checksum:iF65F3BC653A80234
GO

Sequence cautioni

The sequence AAC13359.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991L → P in BAG59309 (PubMed:14702039).Curated
Sequence conflicti233 – 2342QL → HV in AAA75595 (PubMed:10435631).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581S → N.
Corresponds to variant rs7809260 [ dbSNP | Ensembl ].
VAR_051415
Natural varianti307 – 3071L → I.1 Publication
Corresponds to variant rs11540483 [ dbSNP | Ensembl ].
VAR_026286
Natural varianti457 – 4571Q → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035665

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 184184Missing in isoform 3. CuratedVSP_018354Add
BLAST
Alternative sequencei1 – 157157Missing in isoform 4. 1 PublicationVSP_045921Add
BLAST
Alternative sequencei604 – 64542Missing in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_018355Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33821 mRNA. Translation: AAA75595.2.
AF268075 mRNA. Translation: AAG03025.1.
AL136586 mRNA. Translation: CAB66521.1.
AF090891 mRNA. Translation: AAF24016.1.
CR457056 mRNA. Translation: CAG33337.1.
AK296720 mRNA. Translation: BAG59309.1.
AK314292 mRNA. Translation: BAG36949.1.
CR533556 mRNA. Translation: CAG38587.1.
AC004549 Genomic DNA. Translation: AAC13359.2. Sequence problems.
AC005091 Genomic DNA. Translation: AAD15412.1.
CH236948 Genomic DNA. Translation: EAL24213.1.
CH471073 Genomic DNA. Translation: EAW93901.1.
CH471073 Genomic DNA. Translation: EAW93904.1.
BC050358 mRNA. Translation: AAH50358.1.
CCDSiCCDS43561.1. [Q86VP1-2]
CCDS5415.1. [Q86VP1-1]
CCDS56471.1. [Q86VP1-4]
PIRiG02043.
RefSeqiNP_001073333.1. NM_001079864.2. [Q86VP1-2]
NP_001193830.1. NM_001206901.1. [Q86VP1-2]
NP_001193831.1. NM_001206902.1. [Q86VP1-4]
NP_006015.4. NM_006024.6. [Q86VP1-1]
UniGeneiHs.34576.

Genome annotation databases

EnsembliENST00000265393; ENSP00000265393; ENSG00000106052. [Q86VP1-2]
ENST00000396319; ENSP00000379612; ENSG00000106052. [Q86VP1-1]
ENST00000433216; ENSP00000391907; ENSG00000106052. [Q86VP1-4]
ENST00000543117; ENSP00000444811; ENSG00000106052. [Q86VP1-2]
GeneIDi8887.
KEGGihsa:8887.
UCSCiuc003szk.3. human. [Q86VP1-2]
uc003szl.3. human. [Q86VP1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33821 mRNA. Translation: AAA75595.2.
AF268075 mRNA. Translation: AAG03025.1.
AL136586 mRNA. Translation: CAB66521.1.
AF090891 mRNA. Translation: AAF24016.1.
CR457056 mRNA. Translation: CAG33337.1.
AK296720 mRNA. Translation: BAG59309.1.
AK314292 mRNA. Translation: BAG36949.1.
CR533556 mRNA. Translation: CAG38587.1.
AC004549 Genomic DNA. Translation: AAC13359.2. Sequence problems.
AC005091 Genomic DNA. Translation: AAD15412.1.
CH236948 Genomic DNA. Translation: EAL24213.1.
CH471073 Genomic DNA. Translation: EAW93901.1.
CH471073 Genomic DNA. Translation: EAW93904.1.
BC050358 mRNA. Translation: AAH50358.1.
CCDSiCCDS43561.1. [Q86VP1-2]
CCDS5415.1. [Q86VP1-1]
CCDS56471.1. [Q86VP1-4]
PIRiG02043.
RefSeqiNP_001073333.1. NM_001079864.2. [Q86VP1-2]
NP_001193830.1. NM_001206901.1. [Q86VP1-2]
NP_001193831.1. NM_001206902.1. [Q86VP1-4]
NP_006015.4. NM_006024.6. [Q86VP1-1]
UniGeneiHs.34576.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M7QNMR-A725-789[»]
4BMJX-ray2.75A/B/C/D/E/F/G/H/I/J/K725-789[»]
4NLHX-ray1.90A/B15-147[»]
ProteinModelPortaliQ86VP1.
SMRiQ86VP1. Positions 15-124, 150-239, 725-789.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114405. 58 interactions.
DIPiDIP-33010N.
IntActiQ86VP1. 47 interactions.
MINTiMINT-200894.
STRINGi9606.ENSP00000379612.

PTM databases

PhosphoSiteiQ86VP1.

Polymorphism and mutation databases

BioMutaiTAX1BP1.
DMDMi97202549.

Proteomic databases

MaxQBiQ86VP1.
PaxDbiQ86VP1.
PRIDEiQ86VP1.

Protocols and materials databases

DNASUi8887.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265393; ENSP00000265393; ENSG00000106052. [Q86VP1-2]
ENST00000396319; ENSP00000379612; ENSG00000106052. [Q86VP1-1]
ENST00000433216; ENSP00000391907; ENSG00000106052. [Q86VP1-4]
ENST00000543117; ENSP00000444811; ENSG00000106052. [Q86VP1-2]
GeneIDi8887.
KEGGihsa:8887.
UCSCiuc003szk.3. human. [Q86VP1-2]
uc003szl.3. human. [Q86VP1-1]

Organism-specific databases

CTDi8887.
GeneCardsiGC07P027746.
HGNCiHGNC:11575. TAX1BP1.
HPAiHPA024432.
MIMi605326. gene.
neXtProtiNX_Q86VP1.
PharmGKBiPA36339.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG135564.
GeneTreeiENSGT00530000063216.
HOGENOMiHOG000271638.
HOVERGENiHBG053034.
InParanoidiQ86VP1.
OrthoDBiEOG7RRF8H.
PhylomeDBiQ86VP1.
TreeFamiTF329501.

Enzyme and pathway databases

ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiTAX1BP1. human.
GeneWikiiTAX1BP1.
GenomeRNAii8887.
NextBioi33373.
PROiQ86VP1.
SOURCEiSearch...

Gene expression databases

BgeeiQ86VP1.
CleanExiHS_TAX1BP1.
ExpressionAtlasiQ86VP1. baseline and differential.
GenevestigatoriQ86VP1.

Family and domain databases

InterProiIPR012852. CoCoA.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF07888. CALCOCO1. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TNFAIP3 AND HTLV-1 PROTEIN TAX-1, ALTERNATIVE SPLICING (ISOFORM 3).
    Tissue: Cervix carcinoma.
  2. "T6BP, a TRAF6-interacting protein involved in IL-1 signaling."
    Ling L., Goeddel D.V.
    Proc. Natl. Acad. Sci. U.S.A. 97:9567-9572(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH TRAF6, SUBUNIT.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  4. "Functional prediction of the coding sequences of 50 new genes deduced by analysis of cDNA clones from human fetal liver."
    Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S., Liu M., He F.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  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] (ISOFORMS 1 AND 4).
    Tissue: Testis and Tongue.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  7. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 1), VARIANT ILE-307.
    Tissue: Skin.
  11. "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins."
    Nagaraja G.M., Kandpal R.P.
    Biochem. Biophys. Res. Commun. 313:654-665(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STARD13.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HTLV-1 PROTEIN TAX-1.
  13. "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-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "The structure of TAX1BP1 UBZ1+2 provides insight into target specificity and adaptability."
    Ceregido M.A., Spinola Amilibia M., Buts L., Rivera-Torres J., Garcia-Pino A., Bravo J., van Nuland N.A.
    J. Mol. Biol. 426:674-690(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 725-789, X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 725-789, UBZ-TYPE ZINC FINGERS.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-457.
  17. "The kinase IKKalpha inhibits activation of the transcription factor NF-kappaB by phosphorylating the regulatory molecule TAX1BP1."
    Shembade N., Pujari R., Harhaj N.S., Abbott D.W., Harhaj E.W.
    Nat. Immunol. 12:834-843(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-593 AND SER-666 BY CHUK/IKKA.

Entry informationi

Entry nameiTAXB1_HUMAN
AccessioniPrimary (citable) accession number: Q86VP1
Secondary accession number(s): A4D196
, B4DKU7, E7ENV2, O60398, O95770, Q13311, Q9BQG5, Q9UI88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: May 27, 2015
This is version 104 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 7
    Human chromosome 7: 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

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.