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Q9NYJ8 (TAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 2
Alternative name(s):
Mitogen-activated protein kinase kinase kinase 7-interacting protein 2
TAK1-binding protein 2
Short name=TAB-2
TGF-beta-activated kinase 1-binding protein 2
Gene names
Name:TAB2
Synonyms:KIAA0733, MAP3K7IP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter linking MAP3K7/TAK1 and TRAF6. Promotes MAP3K7 activation in the IL1 signaling pathway. The binding of 'Lys-63'-linked polyubiquitin chains to TAB2 promotes autophosphorylation of MAP3K7 at 'Thr-187'. Involved in heart development. Ref.1 Ref.11 Ref.18

Subunit structure

Interacts with MAP3K7 and TRAF6. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2. Binds 'Lys-63'-linked polyubiquitin chains. Interacts with NCOR1 and HDAC3 to form a ternary complex. Interacts (via C-terminal) with NUMBL (via PTB domain). Interacts (via the C-terminus) with WDR34 (via WD domains). Interacts with RBCK1. Interacts with TRIM5. Ref.1 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.21 Ref.23

Subcellular location

Membrane; Peripheral membrane protein. Cytoplasmcytosol. Note: Following IL1 stimulation, translocation occurs from the membrane to cytosol. Ref.1

Tissue specificity

Widely expressed. In the embryo, expressed in the ventricular trabeculae, endothelial cells of the conotruncal cushions of the outflow tract and in the endothelial cells lining the developing aortic valves. Ref.1 Ref.18

Domain

The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins By similarity.

Post-translational modification

Ubiquitinated; following IL1 stimulation or TRAF6 overexpression. Ubiquitination involves RBCK1 leading to proteasomal degradation. Ref.12 Ref.13

Phosphorylated Probable. Ref.1

Involvement in disease

Congenital heart defects, multiple types, 2 (CHTD2) [MIM:614980]: A disease characterized by congenital developmental abnormalities involving structures of the heart. CHTD2 patients have left ventricular outflow tract obstruction, subaortic stenosis, residual aortic regurgitation, atrial fibrillation, bicuspid aortic valve and aortic dilation.
Note: The disease is caused by mutations affecting the gene represented in this entry. A chromosomal aberration involving TAB2 has been found in a family with congenital heart disease. Translocation t(2;6)(q21;q25). Ref.18

Sequence similarities

Contains 1 CUE domain.

Contains 1 RanBP2-type zinc finger.

Sequence caution

The sequence BAA34453.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseDisease mutation
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

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

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

heart development

Inferred from mutant phenotype Ref.18. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Traceable author statement. Source: Reactome

positive regulation of protein kinase activity

Inferred from direct assay Ref.11. Source: UniProtKB

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 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

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 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_functionK63-linked polyubiquitin binding

Inferred from direct assay Ref.23. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYJ8-1)

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: Q9NYJ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     535-536: AL → DI
     537-693: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 693693TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
PRO_0000225695

Regions

Domain8 – 5144CUE
Zinc finger663 – 69331RanBP2-type
Region675 – 68511Interaction with polyubiquitin
Coiled coil532 – 61988 Potential

Amino acid modifications

Modified residue3721Phosphoserine Ref.15
Modified residue4501Phosphoserine Ref.19
Modified residue5241Phosphoserine Ref.19

Natural variations

Alternative sequence535 – 5362AL → DI in isoform 2.
VSP_017419
Alternative sequence537 – 693157Missing in isoform 2.
VSP_017420
Natural variant2081P → S in CHTD2. Ref.18
Corresponds to variant rs267607101 [ dbSNP | Ensembl ].
VAR_063774
Natural variant2301Q → K in CHTD2. Ref.18
Corresponds to variant rs267607100 [ dbSNP | Ensembl ].
VAR_063775

Experimental info

Mutagenesis6751F → A: Abolishes ubiquitin binding. Ref.23
Mutagenesis6781H → A: Abolishes ubiquitin binding. Ref.23
Mutagenesis6811L → A: Abolishes ubiquitin binding. Ref.23
Mutagenesis6851E → A: Abolishes ubiquitin binding. Ref.23
Sequence conflict1961H → R in CAG33668. Ref.5

Secondary structure

.............. 693
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 2000. Version 1.
Checksum: 47BB8709320084D7

FASTA69376,494
        10         20         30         40         50         60 
MAQGSHQIDF QVLHDLRQKF PEVPEVVVSR CMLQNNNNLD ACCAVLSQES TRYLYGEGDL 

        70         80         90        100        110        120 
NFSDDSGISG LRNHMTSLNL DLQSQNIYHH GREGSRMNGS RTLTHSISDG QLQGGQSNSE 

       130        140        150        160        170        180 
LFQQEPQTAP AQVPQGFNVF GMSSSSGASN SAPHLGFHLG SKGTSSLSQQ TPRFNPIMVT 

       190        200        210        220        230        240 
LAPNIQTGRN TPTSLHIHGV PPPVLNSPQG NSIYIRPYIT TPGGTTRQTQ QHSGWVSQFN 

       250        260        270        280        290        300 
PMNPQQVYQP SQPGPWTTCP ASNPLSHTSS QQPNQQGHQT SHVYMPISSP TTSQPPTIHS 

       310        320        330        340        350        360 
SGSSQSSAHS QYNIQNISTG PRKNQIEIKL EPPQRNNSSK LRSSGPRTSS TSSSVNSQTL 

       370        380        390        400        410        420 
NRNQPTVYIA ASPPNTDELM SRSQPKVYIS ANAATGDEQV MRNQPTLFIS TNSGASAASR 

       430        440        450        460        470        480 
NMSGQVSMGP AFIHHHPPKS RAIGNNSATS PRVVVTQPNT KYTFKITVSP NKPPAVSPGV 

       490        500        510        520        530        540 
VSPTFELTNL LNHPDHYVET ENIQHLTDPT LAHVDRISET RKLSMGSDDA AYTQALLVHQ 

       550        560        570        580        590        600 
KARMERLQRE LEIQKKKLDK LKSEVNEMEN NLTRRRLKRS NSISQIPSLE EMQQLRSCNR 

       610        620        630        640        650        660 
QLQIDIDCLT KEIDLFQARG PHFNPSAIHN FYDNIGFVGP VPPKPKDQRS IIKTPKTQDT 

       670        680        690 
EDDEGAQWNC TACTFLNHPA LIRCEQCEMP RHF 

« Hide

Isoform 2 [UniParc].

Checksum: D74074A216D23425
Show »

FASTA53658,131

References

« Hide 'large scale' references
[1]"TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway."
Takaesu G., Kishida S., Hiyama A., Yamaguchi K., Shibuya H., Irie K., Ninomiya-Tsuji J., Matsumoto K.
Mol. Cell 5:649-658(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH TAK1 AND TRAF6.
Tissue: Kidney.
[2]"Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Testis.
[5]"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] (ISOFORM 2).
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[7]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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).
Tissue: Eye.
[11]"TAK1 is a ubiquitin-dependent kinase of MKK and IKK."
Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.
Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN THE TRIKA2 COMPLEX.
[12]"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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
Tissue: Kidney.
[13]"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] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
[14]"NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-kappaB activation."
Ma Q., Zhou L., Shi H., Huo K.
Cell. Signal. 20:1044-1051(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUMBL.
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WDR34.
[17]"Direct activation of protein kinases by unanchored polyubiquitin chains."
Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W., Chen Z.J.
Nature 461:114-119(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLYUBIQUITIN.
[18]"Haploinsufficiency of TAB2 causes congenital heart defects in humans."
Thienpont B., Zhang L., Postma A.V., Breckpot J., Tranchevent L.C., Van Loo P., Mollgard K., Tommerup N., Bache I., Tumer Z., van Engelen K., Menten B., Mortier G., Waggoner D., Gewillig M., Moreau Y., Devriendt K., Larsen L.A.
Am. J. Hum. Genet. 86:839-849(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HEART DEVELOPMENT, TISSUE SPECIFICITY, VARIANTS CHTD2 SER-208 AND LYS-230, CHROMOSOMAL TRANSLOCATION.
[19]"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-450 AND SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"TRIM5 is an innate immune sensor for the retrovirus capsid lattice."
Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J., Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.
Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM5.
[22]"Solution structure of the N-terminal CUE domain in the human mitogen-activated protein kinase kinase kinase 7-interacting protein 2 (MAP3K7IP2)."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 5-70.
[23]"Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain."
Kulathu Y., Akutsu M., Bremm A., Hofmann K., Komander D.
Nat. Struct. Mol. Biol. 16:1328-1330(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 662-693 IN COMPLEX WITH POLYUBIQUITIN CHAINS, MUTAGENESIS OF PHE-675; HIS-678; LEU-681 AND GLU-685, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF241230 mRNA. Translation: AAF67176.1.
AB018276 mRNA. Translation: BAA34453.2. Different initiation.
AK315038 mRNA. Translation: BAG37521.1.
CR457387 mRNA. Translation: CAG33668.1.
DQ314877 Genomic DNA. Translation: ABC40736.1.
AL117407 mRNA. Translation: CAB55907.1.
AL031133, AL138727, AL139103 Genomic DNA. Translation: CAI20026.1.
AL139103, AL031133, AL138727 Genomic DNA. Translation: CAI20971.1.
AL138727, AL031133, AL139103 Genomic DNA. Translation: CAI19581.1.
CH471051 Genomic DNA. Translation: EAW47805.1.
CH471051 Genomic DNA. Translation: EAW47806.1.
CH471051 Genomic DNA. Translation: EAW47807.1.
BC035910 mRNA. Translation: AAH35910.1.
PIRT17217.
RefSeqNP_055908.1. NM_015093.4.
UniGeneHs.269775.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAENMR-A7-70[»]
2WWZX-ray1.40C662-693[»]
2WX0X-ray2.40C/G663-693[»]
2WX1X-ray3.00C663-693[»]
ProteinModelPortalQ9NYJ8.
SMRQ9NYJ8. Positions 5-70, 662-693.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116740. 71 interactions.
DIPDIP-27525N.
IntActQ9NYJ8. 30 interactions.
MINTMINT-1132340.

PTM databases

PhosphoSiteQ9NYJ8.

Polymorphism databases

DMDM74753070.

Proteomic databases

PaxDbQ9NYJ8.
PRIDEQ9NYJ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286332; ENSP00000286332; ENSG00000055208. [Q9NYJ8-1]
ENST00000367456; ENSP00000356426; ENSG00000055208. [Q9NYJ8-1]
ENST00000392282; ENSP00000376106; ENSG00000055208. [Q9NYJ8-2]
ENST00000470466; ENSP00000432709; ENSG00000055208. [Q9NYJ8-2]
ENST00000538427; ENSP00000445752; ENSG00000055208. [Q9NYJ8-1]
GeneID23118.
KEGGhsa:23118.
UCSCuc003qmj.3. human. [Q9NYJ8-1]

Organism-specific databases

CTD23118.
GeneCardsGC06P149543.
HGNCHGNC:17075. TAB2.
MIM605101. gene.
614980. phenotype.
neXtProtNX_Q9NYJ8.
PharmGKBPA30605.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47991.
HOVERGENHBG056952.
InParanoidQ9NYJ8.
KOK04404.
OMAVYHHGRE.
OrthoDBEOG776SPP.
PhylomeDBQ9NYJ8.
TreeFamTF332021.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SignaLinkQ9NYJ8.

Gene expression databases

ArrayExpressQ9NYJ8.
BgeeQ9NYJ8.
CleanExHS_MAP3K7IP2.
GenevestigatorQ9NYJ8.

Family and domain databases

InterProIPR003892. CUE.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF02845. CUE. 1 hit.
PF00641. zf-RanBP. 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

ChiTaRSTAB2. human.
EvolutionaryTraceQ9NYJ8.
GeneWikiMAP3K7IP2.
GenomeRNAi23118.
NextBio44335.
PROQ9NYJ8.
SOURCESearch...

Entry information

Entry nameTAB2_HUMAN
AccessionPrimary (citable) accession number: Q9NYJ8
Secondary accession number(s): B2RCC4 expand/collapse secondary AC list , E1P5A0, O94838, Q6I9W8, Q76N06, Q9UFP7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 125 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM