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TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 2) (TAK1-binding protein 2) (TAB-2) (TGF-beta-activated kinase 1-binding protein 2)

 TAB2_MOUSE              Reviewed;         693 AA.
Q99K90; Q3UGP1; Q8BTP4; Q8CHD3; Q99KP4;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
08-MAY-2019, entry version 136.
RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 2;
AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 2;
AltName: Full=TAK1-binding protein 2;
Short=TAB-2;
AltName: Full=TGF-beta-activated kinase 1-binding protein 2;
Name=Tab2; Synonyms=Kiaa0733, Map3k7ip2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, PHOSPHORYLATION,
SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=Brain;
PubMed=12150997; DOI=10.1016/S0092-8674(02)00809-7;
Baek S.H., Ohgi K.A., Rose D.W., Koo E.H., Glass C.K., Rosenfeld M.G.;
"Exchange of N-CoR corepressor and Tip60 coactivator complexes links
gene expression by NF-kappaB and beta-amyloid precursor protein.";
Cell 110:55-67(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-595.
STRAIN=C57BL/6J, and NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-693.
TISSUE=Embryonic tail;
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-173, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[9]
X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 665-693 IN COMPLEX WITH ZINC
IONS AND 'LYS-63'-LINKED UBIQUITIN, FUNCTION, LINKAGE-SPECIFIC
INTERACTION WITH UBIQUITIN, NZF DOMAIN, SUBUNIT, AND MUTAGENESIS OF
THR-674; PHE-675; HIS-678; LEU-681; GLU-685 AND GLN-686.
PubMed=19927120; DOI=10.1038/emboj.2009.345;
Sato Y., Yoshikawa A., Yamashita M., Yamagata A., Fukai S.;
"Structural basis for specific recognition of Lys 63-linked
polyubiquitin chains by NZF domains of TAB2 and TAB3.";
EMBO J. 28:3903-3909(2009).
-!- 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' (By similarity). Regulates the IL1-mediated
translocation of NCOR1 out of the nucleus. Involved in heart
development (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12150997, ECO:0000269|PubMed:19927120}.
-!- SUBUNIT: 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 (By similarity). Interacts with
TRIM5 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Q62073:Map3k7; NbExp=8; IntAct=EBI-1775124, EBI-1775345;
P62991:Ubc; NbExp=9; IntAct=EBI-1775124, EBI-413074;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12150997}.
Cytoplasm, cytosol {ECO:0000269|PubMed:12150997}. Note=Cytoplasmic
when activated. Following IL1 stimulation, localized in the to
cytosol.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12150997}.
-!- DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two
consecutive 'Lys-63'-linked ubiquitins.
-!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6
overexpression. Ubiquitination involves RBCK1 leading to7
proteasomal degradation (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000305|PubMed:12150997}.
-!- SEQUENCE CAUTION:
Sequence=BAC40772.1; Type=Frameshift; Positions=62, 72, 152, 275; Evidence={ECO:0000305};
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EMBL; AY093701; AAM10487.1; -; mRNA.
EMBL; BC004072; AAH04072.1; -; mRNA.
EMBL; BC004813; AAH04813.1; -; mRNA.
EMBL; AK089164; BAC40772.1; ALT_FRAME; mRNA.
EMBL; AK147830; BAE28166.1; -; mRNA.
EMBL; AB093262; BAC41446.1; -; mRNA.
CCDS; CCDS23691.1; -.
RefSeq; NP_619608.1; NM_138667.3.
RefSeq; XP_017169562.1; XM_017314073.1.
PDB; 3A9J; X-ray; 1.18 A; C=665-693.
PDBsum; 3A9J; -.
SMR; Q99K90; -.
BioGrid; 212973; 9.
IntAct; Q99K90; 4.
MINT; Q99K90; -.
STRING; 10090.ENSMUSP00000121266; -.
iPTMnet; Q99K90; -.
PhosphoSitePlus; Q99K90; -.
EPD; Q99K90; -.
MaxQB; Q99K90; -.
PaxDb; Q99K90; -.
PRIDE; Q99K90; -.
Ensembl; ENSMUST00000146444; ENSMUSP00000121266; ENSMUSG00000015755.
GeneID; 68652; -.
KEGG; mmu:68652; -.
UCSC; uc007eir.2; mouse.
CTD; 23118; -.
MGI; MGI:1915902; Tab2.
eggNOG; ENOG410IK8E; Eukaryota.
eggNOG; ENOG410XPAC; LUCA.
GeneTree; ENSGT00940000158473; -.
HOGENOM; HOG000261646; -.
InParanoid; Q99K90; -.
KO; K04404; -.
OMA; MHPQQVY; -.
OrthoDB; 324984at2759; -.
PhylomeDB; Q99K90; -.
TreeFam; TF332021; -.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
Reactome; R-MMU-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
ChiTaRS; Tab2; mouse.
EvolutionaryTrace; Q99K90; -.
PRO; PR:Q99K90; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000015755; Expressed in 311 organ(s), highest expression level in quadriceps femoris.
ExpressionAtlas; Q99K90; baseline and differential.
Genevisible; Q99K90; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
CDD; cd14362; CUE_TAB2_TAB3; 1.
InterPro; IPR003892; CUE.
InterPro; IPR041911; TAB2/3_CUE.
InterPro; IPR001876; Znf_RanBP2.
InterPro; IPR036443; Znf_RanBP2_sf.
Pfam; PF02845; CUE; 1.
SMART; SM00546; CUE; 1.
SMART; SM00547; ZnF_RBZ; 1.
SUPFAM; SSF90209; SSF90209; 1.
PROSITE; PS51140; CUE; 1.
PROSITE; PS01358; ZF_RANBP2_1; 1.
PROSITE; PS50199; ZF_RANBP2_2; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Cytoplasm;
Metal-binding; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 693 TGF-beta-activated kinase 1 and MAP3K7-
binding protein 2.
/FTId=PRO_0000225696.
DOMAIN 8 51 CUE. {ECO:0000255|PROSITE-
ProRule:PRU00468}.
ZN_FING 663 693 RanBP2-type. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
REGION 675 685 Interaction with polyubiquitin.
COILED 532 619 {ECO:0000255}.
MOD_RES 173 173 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYJ8}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYJ8}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYJ8}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NYJ8}.
MUTAGEN 674 674 T->A: Loss of interaction with 'Lys-63'-
linked ubiquitin.
{ECO:0000269|PubMed:19927120}.
MUTAGEN 675 675 F->A: Loss of interaction with 'Lys-63'-
linked ubiquitin.
{ECO:0000269|PubMed:19927120}.
MUTAGEN 678 678 H->Q: Loss of interaction with 'Lys-63'-
linked ubiquitin.
{ECO:0000269|PubMed:19927120}.
MUTAGEN 681 681 L->T: Loss of interaction with 'Lys-63'-
linked ubiquitin.
{ECO:0000269|PubMed:19927120}.
MUTAGEN 685 685 E->V: Loss of interaction with 'Lys-63'-
linked ubiquitin.
{ECO:0000269|PubMed:19927120}.
MUTAGEN 686 686 Q->I,M: Confers ability to bind
monoubiquitin and polyubiquitin,
irrespective of the type of linkage.
{ECO:0000269|PubMed:19927120}.
CONFLICT 183 183 P -> T (in Ref. 3; BAE28166).
{ECO:0000305}.
CONFLICT 476 476 V -> F (in Ref. 3; BAC40772).
{ECO:0000305}.
CONFLICT 580 580 S -> L (in Ref. 3; BAE28166).
{ECO:0000305}.
TURN 671 673 {ECO:0000244|PDB:3A9J}.
TURN 685 687 {ECO:0000244|PDB:3A9J}.
SEQUENCE 693 AA; 76442 MW; 810F17CBE6F80BA8 CRC64;
MAQGSHQIDF QVLHDLRQKF PEVPEVVVSR CMLQNNNNLD ACCAVLSQES TRYLYGEGDL
NFSDESGISG LRNHMTSLNL DLQSQNVYHH GREGSRVNGS RTLTHSVSDG QLHGGQSNNE
LFQQEPQTAP AQVPQGFNVF GMPSTSGASN STPHLGFHLG SKGTSNLSQQ TPRFNPIMVT
LAPNIQTGRS TPTSLHIHGV PPPVLNSPQG NSIYIRPYIT TPSGTARQTQ QHSGWVSQFN
PMNPQQAYQP SQPGPWTTYP ASNPLPHTST QQPNQQGHQT SHVYMPISSP TTPQPPTIHS
SGSSQSSAHS QYNIQNISTG PRKNQIEIKL EPPQRNSSSK LRSSGPRTAS TSSLVNSQTL
NRNQPTVYIA ASPPNTDEMI SRSQPKVYIS ANATAGDEQG MRNQPTLFIS TNSGPSAASR
NMSGQVSMGP AFIHHHPPKS RVLGGNSATS PRVVVTQPNT KYTFKITVSP NKPPAVSPGV
VSPTFELTNL LNHPDHYVET ENIQHLTDPA LAHVDRISEA RKLSMGSDDA AYTQALLVHQ
KARMERLQRE LEMQKKKLDK LKSEVNEMEN NLTRRRLKRS NSISQIPSLE EMQQLRSCNR
QLQIDIDCLT KEIDLFQARG PHFNPSAIHN FYDNIGFVGP VPPKPKDQRS TIKAPKTQDA
EDEEGAQWNC TACTFLNHPA LIRCEQCEMP RHF


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