ID TIFAB_MOUSE Reviewed; 147 AA.
AC Q8JZM6; Q05DP7; Q571I3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=TRAF-interacting protein with FHA domain-containing protein B;
DE AltName: Full=TIFA-like protein;
GN Name=Tifab {ECO:0000250|UniProtKB:Q6ZNK6};
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] {ECO:0000312|EMBL:BAC29516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29516.1}, and
RC NOD {ECO:0000312|EMBL:BAE41737.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAC29516.1},
RC Dendritic cell {ECO:0000312|EMBL:BAE41737.1}, and
RC Thymus {ECO:0000312|EMBL:BAE32135.1};
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] {ECO:0000312|EMBL:BAD90131.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:BAD90131.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAH27057.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH05528.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH27057.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH27057.1};
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 [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15047173; DOI=10.1016/j.bbrc.2004.03.030;
RA Matsumura T., Semba K., Azuma S., Ikawa S., Gohda J., Akiyama T., Inoue J.;
RT "TIFAB inhibits TIFA, TRAF-interacting protein with a forkhead-associated
RT domain.";
RL Biochem. Biophys. Res. Commun. 317:230-234(2004).
CC -!- FUNCTION: Inhibits TIFA-mediated TRAF6 activation possibly by inducing
CC a conformational change in TIFA. {ECO:0000269|PubMed:15047173}.
CC -!- SUBUNIT: Interacts with TIFA. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in spleen and at moderate
CC levels in lung, thymus, and small intestine.
CC {ECO:0000269|PubMed:15047173}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90131.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK036643; BAC29516.1; -; mRNA.
DR EMBL; AK153654; BAE32135.1; -; mRNA.
DR EMBL; AK170349; BAE41737.1; -; mRNA.
DR EMBL; AK220206; BAD90131.1; ALT_INIT; mRNA.
DR EMBL; BC005528; AAH05528.1; -; mRNA.
DR EMBL; BC027057; AAH27057.1; -; mRNA.
DR EMBL; BC031130; AAH31130.1; -; mRNA.
DR CCDS; CCDS26558.1; -.
DR RefSeq; NP_001162086.1; NM_001168615.1.
DR RefSeq; NP_666088.1; NM_145976.4.
DR RefSeq; XP_006517267.1; XM_006517204.3.
DR RefSeq; XP_006517268.1; XM_006517205.3.
DR AlphaFoldDB; Q8JZM6; -.
DR SMR; Q8JZM6; -.
DR STRING; 10090.ENSMUSP00000131162; -.
DR MaxQB; Q8JZM6; -.
DR PaxDb; 10090-ENSMUSP00000131162; -.
DR ProteomicsDB; 259445; -.
DR Antibodypedia; 53591; 60 antibodies from 13 providers.
DR DNASU; 212937; -.
DR Ensembl; ENSMUST00000169652.3; ENSMUSP00000131162.2; ENSMUSG00000049625.7.
DR Ensembl; ENSMUST00000225063.2; ENSMUSP00000152976.2; ENSMUSG00000049625.7.
DR GeneID; 212937; -.
DR KEGG; mmu:212937; -.
DR UCSC; uc007qsj.2; mouse.
DR AGR; MGI:2385852; -.
DR CTD; 497189; -.
DR MGI; MGI:2385852; Tifab.
DR VEuPathDB; HostDB:ENSMUSG00000049625; -.
DR eggNOG; ENOG502SPI3; Eukaryota.
DR GeneTree; ENSGT00940000154589; -.
DR HOGENOM; CLU_116346_0_0_1; -.
DR InParanoid; Q8JZM6; -.
DR OMA; PLIYRPQ; -.
DR OrthoDB; 5342708at2759; -.
DR PhylomeDB; Q8JZM6; -.
DR TreeFam; TF333218; -.
DR BioGRID-ORCS; 212937; 1 hit in 76 CRISPR screens.
DR PRO; PR:Q8JZM6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8JZM6; Protein.
DR Bgee; ENSMUSG00000049625; Expressed in mesodermal cell in embryo and 80 other cell types or tissues.
DR Genevisible; Q8JZM6; MM.
DR GO; GO:0035800; F:deubiquitinase activator activity; IMP:MGI.
DR GO; GO:0031223; P:auditory behavior; ISO:MGI.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:InterPro.
DR GO; GO:0090102; P:cochlea development; ISO:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; ISO:MGI.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; ISO:MGI.
DR GO; GO:0048806; P:genitalia development; ISO:MGI.
DR GO; GO:0035112; P:genitalia morphogenesis; ISO:MGI.
DR GO; GO:1905748; P:hard palate morphogenesis; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; ISO:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:MGI.
DR GO; GO:0098583; P:learned vocalization behavior; ISO:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
DR GO; GO:0071626; P:mastication; ISO:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:1901078; P:negative regulation of relaxation of muscle; ISO:MGI.
DR GO; GO:1905747; P:negative regulation of saliva secretion; ISO:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:MGI.
DR GO; GO:0030432; P:peristalsis; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:1902238; P:regulation of intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator; IMP:MGI.
DR GO; GO:0048634; P:regulation of muscle organ development; ISO:MGI.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISO:MGI.
DR GO; GO:0038008; P:TRAF-mediated signal transduction; IMP:MGI.
DR GO; GO:0021559; P:trigeminal nerve development; ISO:MGI.
DR GO; GO:0021650; P:vestibulocochlear nerve formation; ISO:MGI.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR033621; TIFA.
DR PANTHER; PTHR31266; TRAF-INTERACTING PROTEIN WITH FHA DOMAIN-CONTAINING PROTEIN A FAMILY MEMBER; 1.
DR PANTHER; PTHR31266:SF3; TRAF-INTERACTING PROTEIN WITH FHA DOMAIN-CONTAINING PROTEIN B; 1.
DR Pfam; PF00498; FHA; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..147
FT /note="TRAF-interacting protein with FHA domain-containing
FT protein B"
FT /id="PRO_0000320693"
FT DOMAIN 36..108
FT /note="FHA"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="P -> S (in Ref. 3; AAH05528)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="H -> Q (in Ref. 3; AAH05528)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="Q -> P (in Ref. 3; AAH05528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16636 MW; 8A0A097F81697E79 CRC64;
MERPLTVLQV SLYHPTQGPV AFAHVPQQLQ HDASRLLVGR GQNTHLQLQL PQLSRYHLSL
EPYLEKGSSL LAFCLKVLTR KSCVWVNGLP LRYLEQVPLG TINRISFSGI QMLVRKEGGA
SLETFVCYFH LSPSPLIYRP KAQETDE
//
