Q9NYJ8 (TAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytosol. 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 disease, 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 component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Disease mutation
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-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 T cell receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent 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 heart development Inferred from mutant phenotype Ref.18. Source: UniProtKB innate immune response 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 cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity 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_component	cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	K63-linked polyubiquitin binding Inferred from direct assay Ref.23. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAP3K7	O43318	2	EBI-358708,EBI-358684
ZBTB16	Q05516	3	EBI-358708,EBI-711925

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 693

693

TGF-beta-activated kinase 1 and MAP3K7-binding protein 2

PRO_0000225695

Regions

Domain

8 – 51

44

CUE

Zinc finger

663 – 693

31

RanBP2-type

Region

675 – 685

11

Interaction with polyubiquitin

Coiled coil

532 – 619

88

Potential

Amino acid modifications

Modified residue

372

1

Phosphoserine Ref.15

Modified residue

450

1

Phosphoserine Ref.19

Modified residue

524

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

535 – 536

2

AL → DI in isoform 2.

VSP_017419

Alternative sequence

537 – 693

157

Missing in isoform 2.

VSP_017420

Natural variant

208

1

P → S in CHTD2. Ref.18
Corresponds to variant rs267607101 [ dbSNP | Ensembl ].

VAR_063774

Natural variant

230

1

Q → K in CHTD2. Ref.18
Corresponds to variant rs267607100 [ dbSNP | Ensembl ].

VAR_063775

Experimental info

Mutagenesis

675

1

F → A: Abolishes ubiquitin binding. Ref.23

Mutagenesis

678

1

H → A: Abolishes ubiquitin binding. Ref.23

Mutagenesis

681

1

L → A: Abolishes ubiquitin binding. Ref.23

Mutagenesis

685

1

E → A: Abolishes ubiquitin binding. Ref.23

Sequence conflict

196

1

H → R in CAG33668. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

693

Helix Strand Turn

Details...

Helix

10 – 19

10

Beta strand

20 – 23

4

Helix

25 – 32

8

Turn

33 – 36

4

Helix

40 – 53

14

Turn

54 – 56

3

Turn

671 – 673

3

Turn

685 – 687

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 47BB8709320084D7	FASTA	693	76,494
	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
	Isoform 2 [UniParc]. Checksum: D74074A216D23425	FASTA	536	58,131
	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 VSPTFELTNL LNHPDHYVET ENIQHLTDPT LAHVDRISET RKLSMGSDDA AYTQDI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

IPI

IPI00157561.
IPI00419504.

PIR

T17217.

RefSeq

NP_055908.1. NM_015093.4.

UniGene

Hs.269775.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DAE	NMR	-	A	7-70	[»]
2WWZ	X-ray	1.40	C	662-693	[»]
2WX0	X-ray	2.40	C/G	663-693	[»]
2WX1	X-ray	3.00	C	663-693	[»]

ProteinModelPortal

Q9NYJ8.

ModBase

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Protein-protein interaction databases

DIP

DIP-27525N.

IntAct

Q9NYJ8. 25 interactions.

MINT

MINT-1132340.

PTM databases

PhosphoSite

Q9NYJ8.

Polymorphism databases

DMDM

74753070.

Proteomic databases

PaxDb

Q9NYJ8.

PRIDE

Q9NYJ8.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000286332; ENSP00000286332; ENSG00000055208.
ENST00000367456; ENSP00000356426; ENSG00000055208.
ENST00000392282; ENSP00000376106; ENSG00000055208.
ENST00000470466; ENSP00000432709; ENSG00000055208.
ENST00000538427; ENSP00000445752; ENSG00000055208.

GeneID

23118.

KEGG

hsa:23118.

UCSC

uc003qmj.3. human.

Organism-specific databases

CTD

23118.

GeneCards

GC06P149540.

HGNC

HGNC:17075. TAB2.

MIM

605101. gene.
614980. phenotype.

neXtProt

NX_Q9NYJ8.

PharmGKB

PA30605.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

NOG47991.

HOVERGEN

HBG056952.

InParanoid

Q9NYJ8.

KO

K04404.

OMA

VYHHGRE.

OrthoDB

EOG41JZBR.

PhylomeDB

Q9NYJ8.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
il1pathway. IL1-mediated signaling events.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
tgfbrpathway. TGF-beta receptor signaling.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9NYJ8.

Bgee

Q9NYJ8.

CleanEx

HS_MAP3K7IP2.

Genevestigator

Q9NYJ8.

Family and domain databases

InterPro

IPR003892. CUE.
IPR001876. Znf_RanBP2.
[Graphical view]

Pfam

PF02845. CUE. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]

SMART

SM00546. CUE. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS51140. CUE. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

TAB2. human.

EvolutionaryTrace

Q9NYJ8.

GenomeRNAi

23118.

NextBio

44335.

SOURCE

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Entry information

Entry name

TAB2_HUMAN

Accession

Primary (citable) accession number: Q9NYJ8
Secondary accession number(s): B2RCC4 , E1P5A0, O94838, Q6I9W8, Q76N06, Q9UFP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.