TAB3_MOUSE
ID TAB3_MOUSE Reviewed; 716 AA.
AC Q571K4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 3;
DE AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 3;
DE AltName: Full=TAK1-binding protein 3;
DE Short=TAB-3;
DE AltName: Full=TGF-beta-activated kinase 1-binding protein 3;
GN Name=Tab3; Synonyms=Kiaa4135, Map3k7ip3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 688-716 IN COMPLEX WITH
RP 'LYS-63'-LINKED DI-UBIQUITIN, NZF DOMAIN, INTERACTION WITH UBIQUITIN, AND
RP SUBUNIT.
RX PubMed=19927120; DOI=10.1038/emboj.2009.345;
RA Sato Y., Yoshikawa A., Yamashita M., Yamagata A., Fukai S.;
RT "Structural basis for specific recognition of Lys 63-linked polyubiquitin
RT chains by NZF domains of TAB2 and TAB3.";
RL EMBO J. 28:3903-3909(2009).
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). Acts as an
CC adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin
CC chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-
CC 63'-linked polyubiquitin chains unanchored or anchored to the substrate
CC proteins such as RIPK1/RIP1: this acts as a scaffold to organize a
CC large signaling complex to promote autophosphorylation of MAP3K7/TAK1,
CC and subsequent activation of I-kappa-B-kinase (IKK) core complex by
CC MAP3K7/TAK1. {ECO:0000250|UniProtKB:Q8N5C8}.
CC -!- SUBUNIT: Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6. The
CC minimal TAB3-containing complex (TAB1-MAP3K7-TAB3) appears not to
CC contain TAB2. However, it seems sensible to consider that TAB2 may also
CC join this complex and may act in a cooperative manner with TAB3.
CC Interacts with DYNC2I2 (via the WD domains). Interacts with RBCK1.
CC Binds 'Lys-63'-linked polyubiquitin chains. Interacts with TRIM5.
CC Interacts with TRIM38 (via B30.2/SPRY domain), leading to its
CC translocation to lysosomes and degradation.
CC {ECO:0000250|UniProtKB:Q8N5C8}.
CC -!- INTERACTION:
CC Q571K4; P62991: Ubc; NbExp=2; IntAct=EBI-7606337, EBI-413074;
CC -!- DOMAIN: The RanBP2-type zinc finger (NZF) mediates binding to two
CC consecutive 'Lys-63'-linked ubiquitins. {ECO:0000269|PubMed:19927120}.
CC -!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression.
CC {ECO:0000250|UniProtKB:Q8N5C8}.
CC -!- PTM: Degraded in a lysosome-dependent manner following interactiuon
CC with TRIM38. {ECO:0000250|UniProtKB:Q8N5C8}.
CC -!- PTM: Phosphorylated at Ser-510 by MAPKAPK2 and MAPKAPK3 following IL1
CC treatment. {ECO:0000250|UniProtKB:Q8N5C8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90370.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK220185; BAD90370.1; ALT_INIT; mRNA.
DR CCDS; CCDS41049.1; -.
DR RefSeq; NP_080005.2; NM_025729.4.
DR RefSeq; XP_006528301.1; XM_006528238.3.
DR RefSeq; XP_006528302.1; XM_006528239.2.
DR RefSeq; XP_017174093.1; XM_017318604.1.
DR PDB; 3A9K; X-ray; 1.40 A; C=688-716.
DR PDBsum; 3A9K; -.
DR AlphaFoldDB; Q571K4; -.
DR SMR; Q571K4; -.
DR BioGRID; 211673; 7.
DR IntAct; Q571K4; 1.
DR MINT; Q571K4; -.
DR STRING; 10090.ENSMUSP00000039668; -.
DR iPTMnet; Q571K4; -.
DR PhosphoSitePlus; Q571K4; -.
DR EPD; Q571K4; -.
DR jPOST; Q571K4; -.
DR MaxQB; Q571K4; -.
DR PaxDb; Q571K4; -.
DR PRIDE; Q571K4; -.
DR ProteomicsDB; 263240; -.
DR Antibodypedia; 24709; 297 antibodies from 39 providers.
DR Ensembl; ENSMUST00000048250; ENSMUSP00000039668; ENSMUSG00000035476.
DR GeneID; 66724; -.
DR KEGG; mmu:66724; -.
DR UCSC; uc009trt.2; mouse.
DR CTD; 257397; -.
DR MGI; MGI:1913974; Tab3.
DR VEuPathDB; HostDB:ENSMUSG00000035476; -.
DR eggNOG; ENOG502QVTR; Eukaryota.
DR GeneTree; ENSGT00940000159499; -.
DR HOGENOM; CLU_025065_1_0_1; -.
DR InParanoid; Q571K4; -.
DR OMA; WACNLCT; -.
DR OrthoDB; 324984at2759; -.
DR PhylomeDB; Q571K4; -.
DR TreeFam; TF332021; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-MMU-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR BioGRID-ORCS; 66724; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tab3; mouse.
DR EvolutionaryTrace; Q571K4; -.
DR PRO; PR:Q571K4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q571K4; protein.
DR Bgee; ENSMUSG00000035476; Expressed in metanephric ureteric bud and 255 other tissues.
DR ExpressionAtlas; Q571K4; baseline and differential.
DR Genevisible; Q571K4; MM.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
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; Acetylation; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT CHAIN 2..716
FT /note="TGF-beta-activated kinase 1 and MAP3K7-binding
FT protein 3"
FT /id="PRO_0000226973"
FT DOMAIN 8..51
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 686..716
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 141..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 521..564
FT /evidence="ECO:0000255"
FT COMPBIAS 172..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT MOD_RES 510
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q8N5C8"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:3A9K"
FT TURN 708..710
FT /evidence="ECO:0007829|PDB:3A9K"
SQ SEQUENCE 716 AA; 79029 MW; 65B3FCC60C4A1CB1 CRC64;
MAQNSPQLDI QVLHDLRQRF PEIPEGVVSQ CMLQNNNNLE ACCRALSQES SKYLYMEYHS
PEDNRMNRNR LLHINLGIHS PSSYHPGDGA HLNGGRTLVH SSSDGHIDPQ HTAGKQLICL
VQEPHSAPAV VAATPNYNPF FMNEQNRSAA TPPSQPPQQP SSMQTGMNPS AMQGPSPPPP
PPSYMHIPRY STNPITVTVS QNLPSGQTVP RALQILPQIP SNLYGSPGSI FIRQTSQSSS
GRQTPQNAPW QSSPQGPVPH YSQRPLPVYP HQQNYQPSQY SPKQQQIPQS VYHSPPPSQC
PSPFSSPQHQ VQPPQLGHPS SHVFMPPSPS TTPPHLYQQG PPSYQKPGSH SVAYLPYTAS
SLPKGSMKKI EITVEPSQRP GTAITRSPSP ISNQPSPRNQ HSLYTATTPP SSSPSRGISS
QPKPPFSVNP VYITYTQPTG PSCAPSPSPR VIPNPTTVFK ITVGRATTEN LLNLVDQEER
SAAPEPIQPI SVIPGSGGEK GNHKYQRSSS SGSDDYAYTQ ALLLHQRARM ERLAKQLKLE
KEELERLKAE VNSMEHDLMQ RRLRRVSCTT AIPTPEEMTR LRSTNRQLQI NVDCTLKEVD
LLQSRGNFDP KAINNFYDHI EPGPVVPPKP SKKDSSDSCA IERKARRISV TSKAPVDIHD
AQAAAADEHL SICKQSARTQ PRDEDYEGAP WNCDSCTFLN HPALNRCEQC EMPRYT
