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Q8N5C8 (TAB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
Alternative name(s):
Mitogen-activated protein kinase kinase kinase 7-interacting protein 3
NF-kappa-B-activating protein 1
TAK1-binding protein 3
Short name=TAB-3
TGF-beta-activated kinase 1-binding protein 3
Gene names
Name:TAB3
Synonyms:MAP3K7IP3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length712 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator of MAP3K7 activation, respectively in the IL1 and TNF signaling pathways. Plays a role in activation of NF-kappa-B and AP1 transcription factor. Isoform 2 may be an oncogenic factor. Ref.1 Ref.3

Subunit structure

Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6. The minimal TAB3-containing complex (TAB1-MAP3K7-TAB3) appears not to contain TAB2. However, it seems sensible to consider that TAB2 may also join this complex and may act in a cooperative manner with TAB3. Interacts with WDR34 (via the WD domains). Interacts with RBCK1. Ref.1 Ref.2 Ref.3 Ref.6 Ref.9

Tissue specificity

Widely expressed. Constitutively overexpressed in certain tumor tissues. Isoform 1 is a major transcript while isoform 2 is a minor transcript. Ref.2 Ref.3

Post-translational modification

Ubiquitinated; following IL1 stimulation or TRAF6 overexpression. Ref.1

Phosphorylated at ser-506 by MAPKAPK2 and MAPKAPK3 following IL1 treatment. Ref.1 Ref.2 Ref.7 Ref.8

Sequence similarities

Contains 1 CUE domain.

Contains 1 RanBP2-type zinc finger.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processI-kappaB kinase/NF-kappaB cascade

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Toll signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 1 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

   Cellular componentcytosol

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

   Molecular functionprotein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Map3k7Q620732EBI-359964,EBI-1775345From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N5C8-1)

Also known as: Tab3a;

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.
Isoform 2 (identifier: Q8N5C8-2)

Also known as: Tab3b;

The sequence of this isoform differs from the canonical sequence as follows:
     602-629: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 712712TGF-beta-activated kinase 1 and MAP3K7-binding protein 3
PRO_0000226972

Regions

Domain8 – 5144CUE
Zinc finger682 – 71231RanBP2-type
Coiled coil517 – 55943 Potential
Compositional bias152 – 451300Pro-rich
Compositional bias504 – 5096Poly-Ser
Compositional bias659 – 6624Poly-Ala

Amino acid modifications

Modified residue601Phosphoserine Ref.8
Modified residue4041Phosphothreonine Ref.8
Modified residue4081Phosphoserine Ref.8
Modified residue4921Phosphoserine Ref.8
Modified residue5061Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.7

Natural variations

Alternative sequence602 – 62928Missing in isoform 2.
VSP_017516
Natural variant3941W → R. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs5927629 [ dbSNP | Ensembl ].
VAR_055294

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Tab3a) [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 591DAC3E74CE9294

FASTA71278,683
        10         20         30         40         50         60 
MAQSSPQLDI QVLHDLRQRF PEIPEGVVSQ CMLQNNNNLE ACCRALSQES SKYLYMEYHS 

        70         80         90        100        110        120 
PDDNRMNRNR LLHINLGIHS PSSYHPGDGA QLNGGRTLVH SSSDGHIDPQ HAAGKQLICL 

       130        140        150        160        170        180 
VQEPHSAPAV VAATPNYNPF FMNEQNRSAA TPPSQPPQQP SSMQTGMNPS AMQGPSPPPP 

       190        200        210        220        230        240 
PPSYMHIPRY STNPITVTVS QNLPSGQTVP RALQILPQIP SNLYGSPGSI YIRQTSQSSS 

       250        260        270        280        290        300 
GRQTPQSTPW QSSPQGPVPH YSQRPLPVYP HQQNYQPSQY SPKQQQIPQS AYHSPPPSQC 

       310        320        330        340        350        360 
PSPFSSPQHQ VQPSQLGHIF MPPSPSTTPP HPYQQGPPSY QKQGSHSVAY LPYTASSLSK 

       370        380        390        400        410        420 
GSMKKIEITV EPSQRPGTAI NRSPSPISNQ PSPWNQHSLY TATTPPSSSP SRGISSQPKP 

       430        440        450        460        470        480 
PFSVNPVYIT YTQPTGPSCT PSPSPRVIPN PTTVFKITVG RATTENLLNL VDQEERSAAP 

       490        500        510        520        530        540 
EPIQPISVIP GSGGEKGSHK YQRSSSSGSD DYAYTQALLL HQRARMERLA KQLKLEKEEL 

       550        560        570        580        590        600 
ERLKSEVNGM EHDLMQRRLR RVSCTTAIPT PEEMTRLRSM NRQLQINVDC TLKEVDLLQS 

       610        620        630        640        650        660 
RGNFDPKAMN NFYDNIEPGP VVPPKPSKKD SSDPCTIERK ARRISVTSKV QADIHDTQAA 

       670        680        690        700        710 
AADEHRTGST QSPRTQPRDE DYEGAPWNCD SCTFLNHPAL NRCEQCEMPR YT 

« Hide

Isoform 2 (Tab3b) [UniParc].

Checksum: 56FD54E4E2082928
Show »

FASTA68475,599

References

« Hide 'large scale' references
[1]"Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling."
Ishitani T., Takaesu G., Ninomiya-Tsuji J., Shibuya H., Gaynor R.B., Matsumoto K.
EMBO J. 22:6277-6288(2003) [PubMed: 14633987] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP3K7; TRAF2 AND TRAF6, UBIQUITINATION, PHOSPHORYLATION, FUNCTION, VARIANT ARG-394.
Tissue: Kidney.
[2]"TAB3, a new binding partner of the protein kinase TAK1."
Cheung P.C., Nebreda A.R., Cohen P.
Biochem. J. 378:27-34(2004) [PubMed: 14670075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH TAB1; TAB2 AND MAP3K7, VARIANT ARG-394.
[3]"Identification of a human NF-kappaB-activating protein, TAB3."
Jin G., Klika A., Callahan M., Faga B., Danzig J., Jiang Z., Li X., Stark G.R., Harrington J., Sherf B.
Proc. Natl. Acad. Sci. U.S.A. 101:2028-2033(2004) [PubMed: 14766965] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH MAP3K7 AND TRAF6, TISSUE SPECIFICITY, FUNCTION, VARIANT ARG-394.
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-394.
Tissue: Eye.
[6]"RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
J. Biol. Chem. 282:16776-16782(2007) [PubMed: 17449468] [Abstract]
Cited for: INTERACTION WITH RBCK1.
[7]"Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex."
Mendoza H., Campbell D.G., Burness K., Hastie J., Ronkina N., Shim J.H., Arthur J.S., Davis R.J., Gaestel M., Johnson G.L., Ghosh S., Cohen P.
Biochem. J. 409:711-722(2008) [PubMed: 18021073] [Abstract]
Cited for: PHOSPHORYLATION AT SER-506.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-404; SER-408 AND SER-492, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced NF-kappaB activation pathway."
Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.
Cell. Mol. Life Sci. 66:2573-2584(2009) [PubMed: 19521662] [Abstract]
Cited for: INTERACTION WITH WDR34.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY437560 mRNA. Translation: AAR06179.1.
AY371491 mRNA. Translation: AAQ88279.1.
AY331591 mRNA. Translation: AAQ92938.1.
AY331592 mRNA. Translation: AAQ92939.1.
AC108359 Genomic DNA. No translation available.
BC032526 mRNA. Translation: AAH32526.1.
IPIIPI00166840.
IPI00397561.
RefSeqNP_690000.2. NM_152787.3.
UniGeneHs.188256.

3D structure databases

ProteinModelPortalQ8N5C8.
SMRQ8N5C8. Positions 4-57, 684-712.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8N5C8. 4 interactions.
MINTMINT-1145071.
STRINGQ8N5C8.

PTM databases

PhosphoSiteQ8N5C8.

Polymorphism databases

DMDM229462756.

Proteomic databases

PRIDEQ8N5C8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000288422; ENSP00000288422; ENSG00000157625.
ENST00000378930; ENSP00000368212; ENSG00000157625.
ENST00000378933; ENSP00000368215; ENSG00000157625.
GeneID257397.
KEGGhsa:257397.
UCSCuc010ngl.1. human.

Organism-specific databases

CTD257397.
GeneCardsGC0XM030845.
H-InvDBHIX0016717.
HGNCHGNC:30681. TAB3.
HPAHPA034980.
MIM300480. gene.
neXtProtNX_Q8N5C8.
PharmGKBPA145148470.
PA165757406.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00530000063642.
HOGENOMHBG714653.
HOVERGENHBG056952.
InParanoidQ8N5C8.
OMAQGPVPHY.
OrthoDBEOG4XD3QR.
PhylomeDBQ8N5C8.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ8N5C8.
BgeeQ8N5C8.
CleanExHS_MAP3K7IP3.
GenevestigatorQ8N5C8.
GermOnlineENSG00000157625. Homo sapiens.

Family and domain databases

InterProIPR003892. CUE.
IPR001876. Znf_RanBP2.
[Graphical view]
KOK12793.
PfamPF02845. CUE. 1 hit.
[Graphical view]
SMARTSM00546. CUE. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS51140. CUE. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio93003.
SOURCESearch...

Entry information

Entry nameTAB3_HUMAN
AccessionPrimary (citable) accession number: Q8N5C8
Secondary accession number(s): A6NDD9, Q6VQR0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 5, 2009
Last modified: January 25, 2012
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

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Human chromosome X: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families