TAB2_HUMAN
ID TAB2_HUMAN Reviewed; 693 AA.
AC Q9NYJ8; B2RCC4; E1P5A0; O94838; Q6I9W8; Q76N06; Q9UFP7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 {ECO:0000305};
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 2;
DE AltName: Full=TAK1-binding protein 2 {ECO:0000303|PubMed:10882101};
DE Short=TAB-2 {ECO:0000303|PubMed:10882101};
DE AltName: Full=TGF-beta-activated kinase 1-binding protein 2 {ECO:0000303|PubMed:10882101};
GN Name=TAB2 {ECO:0000303|PubMed:10882101, ECO:0000312|HGNC:HGNC:17075};
GN Synonyms=KIAA0733 {ECO:0000303|PubMed:9872452}, MAP3K7IP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH TAK1 AND TRAF6.
RC TISSUE=Kidney;
RX PubMed=10882101; DOI=10.1016/s1097-2765(00)80244-0;
RA Takaesu G., Kishida S., Hiyama A., Yamaguchi K., Shibuya H., Irie K.,
RA Ninomiya-Tsuji J., Matsumoto K.;
RT "TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by
RT linking TAK1 to TRAF6 in the IL-1 signal transduction pathway.";
RL Mol. Cell 5:649-658(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION IN THE TRIKA2 COMPLEX.
RX PubMed=11460167; DOI=10.1038/35085597;
RA Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J.;
RT "TAK1 is a ubiquitin-dependent kinase of MKK and IKK.";
RL Nature 412:346-351(2001).
RN [12]
RP UBIQUITINATION.
RC TISSUE=Kidney;
RX PubMed=14633987; DOI=10.1093/emboj/cdg605;
RA Ishitani T., Takaesu G., Ninomiya-Tsuji J., Shibuya H., Gaynor R.B.,
RA Matsumoto K.;
RT "Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling.";
RL EMBO J. 22:6277-6288(2003).
RN [13]
RP FUNCTION.
RX PubMed=15327770; DOI=10.1016/j.molcel.2004.08.008;
RA Kanayama A., Seth R.B., Sun L., Ea C.K., Hong M., Shaito A., Chiu Y.H.,
RA Deng L., Chen Z.J.;
RT "TAB2 and TAB3 activate the NF-kappaB pathway through binding to
RT polyubiquitin chains.";
RL Mol. Cell 15:535-548(2004).
RN [14]
RP UBIQUITINATION, AND INTERACTION WITH RBCK1.
RX PubMed=17449468; DOI=10.1074/jbc.m701913200;
RA Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M.,
RA Chen D.Y., Zhai Z.H., Shu H.B.;
RT "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-
RT triggered NF-kappaB activation by targeting TAB2/3 for degradation.";
RL J. Biol. Chem. 282:16776-16782(2007).
RN [15]
RP INTERACTION WITH NUMBL.
RX PubMed=18299187; DOI=10.1016/j.cellsig.2008.01.015;
RA Ma Q., Zhou L., Shi H., Huo K.;
RT "NUMBL interacts with TAB2 and inhibits TNFalpha and IL-1beta-induced NF-
RT kappaB activation.";
RL Cell. Signal. 20:1044-1051(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP INTERACTION WITH DYNC2I2.
RX PubMed=19521662; DOI=10.1007/s00018-009-0059-6;
RA Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.;
RT "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced
RT NF-kappaB activation pathway.";
RL Cell. Mol. Life Sci. 66:2573-2584(2009).
RN [18]
RP INTERACTION WITH POLYUBIQUITIN.
RX PubMed=19675569; DOI=10.1038/nature08247;
RA Xia Z.-P., Sun L., Chen X., Pineda G., Jiang X., Adhikari A., Zeng W.,
RA Chen Z.J.;
RT "Direct activation of protein kinases by unanchored polyubiquitin chains.";
RL Nature 461:114-119(2009).
RN [19]
RP FUNCTION IN HEART DEVELOPMENT, TISSUE SPECIFICITY, VARIANTS CHTD2 SER-208
RP AND LYS-230, AND CHROMOSOMAL TRANSLOCATION.
RX PubMed=20493459; DOI=10.1016/j.ajhg.2010.04.011;
RA Thienpont B., Zhang L., Postma A.V., Breckpot J., Tranchevent L.C.,
RA Van Loo P., Mollgard K., Tommerup N., Bache I., Tumer Z., van Engelen K.,
RA Menten B., Mortier G., Waggoner D., Gewillig M., Moreau Y., Devriendt K.,
RA Larsen L.A.;
RT "Haploinsufficiency of TAB2 causes congenital heart defects in humans.";
RL Am. J. Hum. Genet. 86:839-849(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-524, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP FUNCTION, DOMAIN, METHYLATION AT CYS-673 (MICROBIAL INFECTION), AND
RP MUTAGENESIS OF CYS-670; CYS-673; CYS-684 AND CYS-687.
RX PubMed=22158122; DOI=10.1038/nature10690;
RA Zhang L., Ding X., Cui J., Xu H., Chen J., Gong Y.N., Hu L., Zhou Y.,
RA Ge J., Lu Q., Liu L., Chen S., Shao F.;
RT "Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB
RT activation.";
RL Nature 481:204-208(2011).
RN [23]
RP INTERACTION WITH TRIM5.
RX PubMed=21512573; DOI=10.1038/nature09976;
RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J.,
RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L.,
RA Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.;
RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice.";
RL Nature 472:361-365(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-582, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [27]
RP METHYLATION AT CYS-673 (MICROBIAL INFECTION).
RX PubMed=25412445; DOI=10.1371/journal.ppat.1004522;
RA Yao Q., Zhang L., Wan X., Chen J., Hu L., Ding X., Li L., Karar J.,
RA Peng H., Chen S., Huang N., Rauscher F.J. III, Shao F.;
RT "Structure and specificity of the bacterial cysteine methyltransferase
RT effector NleE suggests a novel substrate in human DNA repair pathway.";
RL PLoS Pathog. 10:e1004522-e1004522(2014).
RN [28]
RP SUBCELLULAR LOCATION, DEGRADATION, AND INTERACTION WITH TRIM38.
RX PubMed=24434549; DOI=10.1073/pnas.1318227111;
RA Hu M.M., Yang Q., Zhang J., Liu S.M., Zhang Y., Lin H., Huang Z.F.,
RA Wang Y.Y., Zhang X.D., Zhong B., Shu H.B.;
RT "TRIM38 inhibits TNFalpha- and IL-1beta-triggered NF-kappaB activation by
RT mediating lysosome-dependent degradation of TAB2/3.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1509-1514(2014).
RN [29]
RP METHYLATION (MICROBIAL INFECTION).
RX PubMed=27445336; DOI=10.1074/jbc.m116.734079;
RA Zhang Y., Muehlen S., Oates C.V., Pearson J.S., Hartland E.L.;
RT "Identification of a distinct substrate-binding domain in the bacterial
RT cysteine methyltransferase effectors NleE and OspZ.";
RL J. Biol. Chem. 291:20149-20162(2016).
RN [30]
RP STRUCTURE BY NMR OF 5-70.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal CUE domain in the human mitogen-
RT activated protein kinase kinase kinase 7-interacting protein 2
RT (MAP3K7IP2).";
RL Submitted (FEB-2007) to the PDB data bank.
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 662-693 IN COMPLEX WITH
RP POLYUBIQUITIN CHAINS, MUTAGENESIS OF PHE-675; HIS-678; LEU-681 AND GLU-685,
RP AND SUBUNIT.
RX PubMed=19935683; DOI=10.1038/nsmb.1731;
RA Kulathu Y., Akutsu M., Bremm A., Hofmann K., Komander D.;
RT "Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain.";
RL Nat. Struct. Mol. Biol. 16:1328-1330(2009).
RN [32]
RP VARIANT LYS-569.
RX PubMed=27426733; DOI=10.1016/j.ajhg.2016.05.024;
RA Wade E.M., Daniel P.B., Jenkins Z.A., McInerney-Leo A., Leo P., Morgan T.,
RA Addor M.C., Ades L.C., Bertola D., Bohring A., Carter E., Cho T.J.,
RA Duba H.C., Fletcher E., Kim C.A., Krakow D., Morava E., Neuhann T.,
RA Superti-Furga A., Veenstra-Knol I., Wieczorek D., Wilson L.C.,
RA Hennekam R.C., Sutherland-Smith A.J., Strom T.M., Wilkie A.O., Brown M.A.,
RA Duncan E.L., Markie D.M., Robertson S.P.;
RT "Mutations in MAP3K7 that alter the activity of the TAK1 signaling complex
RT cause frontometaphyseal dysplasia.";
RL Am. J. Hum. Genet. 99:392-406(2016).
CC -!- FUNCTION: Adapter required to activate the JNK and NF-kappa-B signaling
CC pathways through the specific recognition of 'Lys-63'-linked
CC polyubiquitin chains by its RanBP2-type zinc finger (NZF)
CC (PubMed:10882101, PubMed:11460167, PubMed:15327770, PubMed:22158122).
CC Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked
CC polyubiquitin chains (PubMed:10882101, PubMed:11460167,
CC PubMed:15327770, PubMed:22158122). The RanBP2-type zinc finger (NZF)
CC specifically recognizes Lys-63'-linked polyubiquitin chains unanchored
CC or anchored to the substrate proteins such as RIPK1/RIP1: this acts as
CC a scaffold to organize a large signaling complex to promote
CC autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-
CC kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (PubMed:15327770,
CC PubMed:22158122). Regulates the IL1-mediated translocation of NCOR1 out
CC of the nucleus (By similarity). Involved in heart development
CC (PubMed:20493459). {ECO:0000250|UniProtKB:Q99K90,
CC ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:11460167,
CC ECO:0000269|PubMed:15327770, ECO:0000269|PubMed:20493459,
CC ECO:0000269|PubMed:22158122}.
CC -!- SUBUNIT: Interacts with MAP3K7 and TRAF6 (PubMed:10882101). Identified
CC in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2
CC (PubMed:11460167). Binds 'Lys-63'-linked polyubiquitin chains
CC (PubMed:19675569, PubMed:19935683). Interacts with NCOR1 and HDAC3 to
CC form a ternary complex (By similarity). Interacts (via C-terminal) with
CC NUMBL (via PTB domain) (PubMed:18299187). Interacts (via the C-
CC terminus) with DYNC2I2 (via WD domains) (PubMed:19521662). Interacts
CC with RBCK1 (PubMed:17449468). Interacts with TRIM5 (PubMed:21512573).
CC Interacts with TRIM38 (via B30.2/SPRY domain), leading to its
CC translocation to lysosomes and degradation (PubMed:24434549).
CC {ECO:0000250|UniProtKB:Q99K90, ECO:0000269|PubMed:10882101,
CC ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:17449468,
CC ECO:0000269|PubMed:18299187, ECO:0000269|PubMed:19521662,
CC ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:19935683,
CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:24434549}.
CC -!- INTERACTION:
CC Q9NYJ8; Q14457: BECN1; NbExp=11; IntAct=EBI-358708, EBI-949378;
CC Q9NYJ8; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-358708, EBI-1383687;
CC Q9NYJ8; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-358708, EBI-11748557;
CC Q9NYJ8; P15407: FOSL1; NbExp=4; IntAct=EBI-358708, EBI-744510;
CC Q9NYJ8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-358708, EBI-618309;
CC Q9NYJ8; O75031: HSF2BP; NbExp=3; IntAct=EBI-358708, EBI-7116203;
CC Q9NYJ8; P78386: KRT85; NbExp=3; IntAct=EBI-358708, EBI-1049371;
CC Q9NYJ8; O43318: MAP3K7; NbExp=7; IntAct=EBI-358708, EBI-358684;
CC Q9NYJ8; O43318-2: MAP3K7; NbExp=2; IntAct=EBI-358708, EBI-358700;
CC Q9NYJ8; Q15750: TAB1; NbExp=6; IntAct=EBI-358708, EBI-358643;
CC Q9NYJ8; Q9UKE5: TNIK; NbExp=3; IntAct=EBI-358708, EBI-1051794;
CC Q9NYJ8; P06753: TPM3; NbExp=3; IntAct=EBI-358708, EBI-355607;
CC Q9NYJ8; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-358708, EBI-359276;
CC Q9NYJ8; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-358708, EBI-2799833;
CC Q9NYJ8; Q05516: ZBTB16; NbExp=3; IntAct=EBI-358708, EBI-711925;
CC Q9NYJ8; Q9NTW7-5: ZFP64; NbExp=3; IntAct=EBI-358708, EBI-23201521;
CC Q9NYJ8; P52747: ZNF143; NbExp=3; IntAct=EBI-358708, EBI-2849334;
CC Q9NYJ8; Q62073: Map3k7; Xeno; NbExp=2; IntAct=EBI-358708, EBI-1775345;
CC Q9NYJ8; B7UI22: nleE; Xeno; NbExp=5; IntAct=EBI-358708, EBI-15957770;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10882101,
CC ECO:0000269|PubMed:24434549}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10882101}. Endosome membrane
CC {ECO:0000269|PubMed:24434549}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10882101}. Lysosome membrane
CC {ECO:0000269|PubMed:24434549}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10882101}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:24434549}.
CC Note=Following IL1 stimulation, translocation occurs from the membrane
CC to cytosol (PubMed:10882101). Interaction with TRIM38 promotes
CC translocation from cytosol to endosome and lysosome (PubMed:24434549).
CC {ECO:0000269|PubMed:10882101, ECO:0000269|PubMed:24434549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYJ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYJ8-2; Sequence=VSP_017419, VSP_017420;
CC -!- TISSUE SPECIFICITY: Widely expressed. In the embryo, expressed in the
CC ventricular trabeculae, endothelial cells of the conotruncal cushions
CC of the outflow tract and in the endothelial cells lining the developing
CC aortic valves. {ECO:0000269|PubMed:10882101,
CC ECO:0000269|PubMed:20493459}.
CC -!- DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two
CC consecutive 'Lys-63'-linked ubiquitins. {ECO:0000269|PubMed:19935683,
CC ECO:0000269|PubMed:22158122}.
CC -!- PTM: Degraded in a lysosome-dependent manner following interactiuon
CC with TRIM38. {ECO:0000269|PubMed:24434549}.
CC -!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression.
CC Ubiquitination involves RBCK1 leading to proteasomal degradation.
CC {ECO:0000269|PubMed:14633987, ECO:0000269|PubMed:17449468}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:10882101}.
CC -!- PTM: (Microbial infection) Methylated at Cys-673 by enteropathogenic
CC E.coli protein NleE or S.flexneri protein OspZ: methylation disrupts
CC zinc-binding and ability to bind 'Lys-63'-linked ubiquitin, leading to
CC NF-kappa-B inactivation. {ECO:0000269|PubMed:22158122,
CC ECO:0000269|PubMed:25412445, ECO:0000269|PubMed:27445336}.
CC -!- DISEASE: Congenital heart defects, multiple types, 2 (CHTD2)
CC [MIM:614980]: A disease characterized by congenital developmental
CC abnormalities involving structures of the heart. CHTD2 patients have
CC left ventricular outflow tract obstruction, subaortic stenosis,
CC residual aortic regurgitation, atrial fibrillation, bicuspid aortic
CC valve and aortic dilation. {ECO:0000269|PubMed:20493459}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. A chromosomal aberration involving TAB2 has been found in a
CC family with congenital heart disease. Translocation t(2;6)(q21;q25).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34453.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AF241230; AAF67176.1; -; mRNA.
DR EMBL; AB018276; BAA34453.2; ALT_INIT; mRNA.
DR EMBL; AK315038; BAG37521.1; -; mRNA.
DR EMBL; CR457387; CAG33668.1; -; mRNA.
DR EMBL; DQ314877; ABC40736.1; -; Genomic_DNA.
DR EMBL; AL117407; CAB55907.1; -; mRNA.
DR EMBL; AL031133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47805.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47806.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47807.1; -; Genomic_DNA.
DR EMBL; BC035910; AAH35910.1; -; mRNA.
DR CCDS; CCDS5214.1; -. [Q9NYJ8-1]
DR PIR; T17217; T17217.
DR RefSeq; NP_001278963.1; NM_001292034.2. [Q9NYJ8-1]
DR RefSeq; NP_001278964.1; NM_001292035.2.
DR RefSeq; NP_055908.1; NM_015093.5. [Q9NYJ8-1]
DR RefSeq; XP_011533935.1; XM_011535633.2. [Q9NYJ8-1]
DR RefSeq; XP_016866080.1; XM_017010591.1.
DR RefSeq; XP_016866081.1; XM_017010592.1. [Q9NYJ8-1]
DR PDB; 2DAE; NMR; -; A=7-68.
DR PDB; 2WWZ; X-ray; 1.40 A; C=662-693.
DR PDB; 2WX0; X-ray; 2.40 A; C/G=663-693.
DR PDB; 2WX1; X-ray; 3.00 A; C=663-693.
DR PDBsum; 2DAE; -.
DR PDBsum; 2WWZ; -.
DR PDBsum; 2WX0; -.
DR PDBsum; 2WX1; -.
DR AlphaFoldDB; Q9NYJ8; -.
DR BMRB; Q9NYJ8; -.
DR SMR; Q9NYJ8; -.
DR BioGRID; 116740; 154.
DR CORUM; Q9NYJ8; -.
DR DIP; DIP-27525N; -.
DR IntAct; Q9NYJ8; 64.
DR MINT; Q9NYJ8; -.
DR STRING; 9606.ENSP00000356426; -.
DR ChEMBL; CHEMBL4295965; -.
DR GlyGen; Q9NYJ8; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q9NYJ8; -.
DR PhosphoSitePlus; Q9NYJ8; -.
DR BioMuta; TAB2; -.
DR DMDM; 74753070; -.
DR CPTAC; CPTAC-1054; -.
DR CPTAC; CPTAC-909; -.
DR EPD; Q9NYJ8; -.
DR jPOST; Q9NYJ8; -.
DR MassIVE; Q9NYJ8; -.
DR MaxQB; Q9NYJ8; -.
DR PaxDb; Q9NYJ8; -.
DR PeptideAtlas; Q9NYJ8; -.
DR PRIDE; Q9NYJ8; -.
DR ProteomicsDB; 83238; -. [Q9NYJ8-1]
DR ProteomicsDB; 83239; -. [Q9NYJ8-2]
DR Antibodypedia; 19871; 237 antibodies from 36 providers.
DR DNASU; 23118; -.
DR Ensembl; ENST00000367456.5; ENSP00000356426.1; ENSG00000055208.19. [Q9NYJ8-1]
DR Ensembl; ENST00000470466.5; ENSP00000432709.1; ENSG00000055208.19. [Q9NYJ8-2]
DR Ensembl; ENST00000538427.5; ENSP00000445752.1; ENSG00000055208.19. [Q9NYJ8-1]
DR Ensembl; ENST00000637181.2; ENSP00000490618.1; ENSG00000055208.19. [Q9NYJ8-1]
DR GeneID; 23118; -.
DR KEGG; hsa:23118; -.
DR MANE-Select; ENST00000637181.2; ENSP00000490618.1; NM_001292034.3; NP_001278963.1.
DR UCSC; uc063sdy.1; human. [Q9NYJ8-1]
DR CTD; 23118; -.
DR DisGeNET; 23118; -.
DR GeneCards; TAB2; -.
DR HGNC; HGNC:17075; TAB2.
DR HPA; ENSG00000055208; Low tissue specificity.
DR MalaCards; TAB2; -.
DR MIM; 605101; gene.
DR MIM; 614980; phenotype.
DR neXtProt; NX_Q9NYJ8; -.
DR OpenTargets; ENSG00000055208; -.
DR Orphanet; 228410; Polyvalvular heart disease syndrome.
DR PharmGKB; PA30605; -.
DR VEuPathDB; HostDB:ENSG00000055208; -.
DR eggNOG; ENOG502QRAY; Eukaryota.
DR GeneTree; ENSGT00940000158473; -.
DR HOGENOM; CLU_025065_0_0_1; -.
DR InParanoid; Q9NYJ8; -.
DR OMA; GPTFIHH; -.
DR OrthoDB; 324984at2759; -.
DR PhylomeDB; Q9NYJ8; -.
DR TreeFam; TF332021; -.
DR PathwayCommons; Q9NYJ8; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR SignaLink; Q9NYJ8; -.
DR SIGNOR; Q9NYJ8; -.
DR BioGRID-ORCS; 23118; 15 hits in 1030 CRISPR screens.
DR ChiTaRS; TAB2; human.
DR EvolutionaryTrace; Q9NYJ8; -.
DR GeneWiki; MAP3K7IP2; -.
DR GenomeRNAi; 23118; -.
DR Pharos; Q9NYJ8; Tbio.
DR PRO; PR:Q9NYJ8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NYJ8; protein.
DR Bgee; ENSG00000055208; Expressed in parotid gland and 212 other tissues.
DR ExpressionAtlas; Q9NYJ8; baseline and differential.
DR Genevisible; Q9NYJ8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:ARUK-UCL.
DR CDD; cd14362; CUE_TAB2_TAB3; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041911; TAB2/3_CUE.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Coiled coil;
KW Cytoplasm; Disease variant; Endosome; Lysosome; Membrane; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..693
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 2"
FT /id="PRO_0000225695"
FT DOMAIN 8..51
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 663..693
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 91..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..685
FT /note="Interaction with polyubiquitin"
FT /evidence="ECO:0000269|PubMed:19935683"
FT COILED 532..619
FT /evidence="ECO:0000255"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 673
FT /note="(Microbial infection) S-methylcysteine"
FT /evidence="ECO:0000269|PubMed:22158122,
FT ECO:0000269|PubMed:25412445"
FT VAR_SEQ 535..536
FT /note="AL -> DI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT /id="VSP_017419"
FT VAR_SEQ 537..693
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT /id="VSP_017420"
FT VARIANT 208
FT /note="P -> S (in CHTD2; dbSNP:rs267607101)"
FT /evidence="ECO:0000269|PubMed:20493459"
FT /id="VAR_063774"
FT VARIANT 230
FT /note="Q -> K (in CHTD2; dbSNP:rs267607100)"
FT /evidence="ECO:0000269|PubMed:20493459"
FT /id="VAR_063775"
FT VARIANT 569
FT /note="E -> K (found in an patient with a form of
FT frontometaphyseal dysplasia; unknown pathological
FT significance; dbSNP:rs886039238)"
FT /evidence="ECO:0000269|PubMed:27426733"
FT /id="VAR_077348"
FT MUTAGEN 670
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-673."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 673
FT /note="C->L,M: Abolished Cys methylation and ability to
FT bind 'Lys-63'-linked ubiquitin."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 675
FT /note="F->A: Abolishes ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:19935683"
FT MUTAGEN 678
FT /note="H->A: Abolishes ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:19935683"
FT MUTAGEN 681
FT /note="L->A: Abolishes ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:19935683"
FT MUTAGEN 684
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-673."
FT /evidence="ECO:0000269|PubMed:22158122"
FT MUTAGEN 685
FT /note="E->A: Abolishes ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:19935683"
FT MUTAGEN 687
FT /note="C->S: Disrupted zinc-finger; abolished methylation
FT at C-673."
FT /evidence="ECO:0000269|PubMed:22158122"
FT CONFLICT 196
FT /note="H -> R (in Ref. 5; CAG33668)"
FT /evidence="ECO:0000305"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:2DAE"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2DAE"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2DAE"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2DAE"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:2DAE"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2DAE"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:2WWZ"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:2WWZ"
SQ SEQUENCE 693 AA; 76494 MW; 47BB8709320084D7 CRC64;
MAQGSHQIDF QVLHDLRQKF PEVPEVVVSR CMLQNNNNLD ACCAVLSQES TRYLYGEGDL
NFSDDSGISG LRNHMTSLNL DLQSQNIYHH GREGSRMNGS RTLTHSISDG QLQGGQSNSE
LFQQEPQTAP AQVPQGFNVF GMSSSSGASN SAPHLGFHLG SKGTSSLSQQ TPRFNPIMVT
LAPNIQTGRN TPTSLHIHGV PPPVLNSPQG NSIYIRPYIT TPGGTTRQTQ QHSGWVSQFN
PMNPQQVYQP SQPGPWTTCP ASNPLSHTSS QQPNQQGHQT SHVYMPISSP TTSQPPTIHS
SGSSQSSAHS QYNIQNISTG PRKNQIEIKL EPPQRNNSSK LRSSGPRTSS TSSSVNSQTL
NRNQPTVYIA ASPPNTDELM SRSQPKVYIS ANAATGDEQV MRNQPTLFIS TNSGASAASR
NMSGQVSMGP AFIHHHPPKS RAIGNNSATS PRVVVTQPNT KYTFKITVSP NKPPAVSPGV
VSPTFELTNL LNHPDHYVET ENIQHLTDPT LAHVDRISET RKLSMGSDDA AYTQALLVHQ
KARMERLQRE LEIQKKKLDK LKSEVNEMEN NLTRRRLKRS NSISQIPSLE EMQQLRSCNR
QLQIDIDCLT KEIDLFQARG PHFNPSAIHN FYDNIGFVGP VPPKPKDQRS IIKTPKTQDT
EDDEGAQWNC TACTFLNHPA LIRCEQCEMP RHF
