GID8_MOUSE
ID GID8_MOUSE Reviewed; 228 AA.
AC Q9D7M1;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glucose-induced degradation protein 8 homolog;
DE AltName: Full=Two hybrid-associated protein 1 with RanBPM;
DE Short=Twa1 {ECO:0000303|PubMed:27920276};
GN Name=Gid8;
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 STRAIN=C57BL/6J; TISSUE=Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12559565; DOI=10.1016/s0378-1119(02)01153-8;
RA Umeda M., Nishitani H., Nishimoto T.;
RT "A novel nuclear protein, Twa1, and Muskelin comprise a complex with
RT RanBPM.";
RL Gene 303:47-54(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [5]
RP SUBUNIT.
RX PubMed=27920276; DOI=10.1042/bsr20160401;
RA Francis O., Baker G.E., Race P.R., Adams J.C.;
RT "Studies of recombinant TWA1 reveal constitutive dimerization.";
RL Biosci. Rep. 37:0-0(2017).
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. Acts as a positive regulator of Wnt
CC signaling pathway by promoting beta-catenin (CTNNB1) nuclear
CC accumulation. {ECO:0000250|UniProtKB:Q9NWU2}.
CC -!- SUBUNIT: Homodimer; may also form higher oligomers (PubMed:27920276).
CC Identified in the CTLH complex that contains GID4, RANBP9 and/or
CC RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B),
CC GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA, RMND5A (or
CC alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or
CC RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5
CC have ancillary roles. Interacts with RANBP9. Part of a complex
CC consisting of RANBP9, MKLN1 and GID8. Interacts with CTNNB1, AXIN1 and
CC GSK3B (By similarity). {ECO:0000250|UniProtKB:Q9NWU2,
CC ECO:0000269|PubMed:27920276}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NWU2}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NWU2}. Note=Localizes in the cytoplasm in the
CC absence of Wnt stimulation and in the nucleus in the presence of Wnt
CC stimulation. {ECO:0000250|UniProtKB:Q9NWU2}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12559565}.
CC -!- PTM: Polyubiquitinated through 'Lys-48'-polyubiquitin chains, leading
CC to proteasomal degradation in the absence of Wnt stimulation.
CC {ECO:0000250|UniProtKB:Q9NWU2}.
CC -!- SIMILARITY: Belongs to the GID8 family. {ECO:0000305}.
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DR EMBL; AK009106; BAB26074.1; -; mRNA.
DR EMBL; BC059022; AAH59022.1; -; mRNA.
DR CCDS; CCDS17185.1; -.
DR RefSeq; NP_001276580.1; NM_001289651.1.
DR RefSeq; NP_001276581.1; NM_001289652.1.
DR RefSeq; NP_083883.1; NM_029607.2.
DR AlphaFoldDB; Q9D7M1; -.
DR SMR; Q9D7M1; -.
DR BioGRID; 218123; 1.
DR IntAct; Q9D7M1; 1.
DR STRING; 10090.ENSMUSP00000077753; -.
DR iPTMnet; Q9D7M1; -.
DR PhosphoSitePlus; Q9D7M1; -.
DR EPD; Q9D7M1; -.
DR MaxQB; Q9D7M1; -.
DR PaxDb; Q9D7M1; -.
DR PeptideAtlas; Q9D7M1; -.
DR PRIDE; Q9D7M1; -.
DR ProteomicsDB; 267447; -.
DR Antibodypedia; 29626; 157 antibodies from 28 providers.
DR DNASU; 76425; -.
DR Ensembl; ENSMUST00000029090; ENSMUSP00000029090; ENSMUSG00000027573.
DR Ensembl; ENSMUST00000078687; ENSMUSP00000077753; ENSMUSG00000027573.
DR GeneID; 76425; -.
DR KEGG; mmu:76425; -.
DR UCSC; uc008ojy.2; mouse.
DR CTD; 54994; -.
DR MGI; MGI:1923675; Gid8.
DR VEuPathDB; HostDB:ENSMUSG00000027573; -.
DR eggNOG; KOG2659; Eukaryota.
DR GeneTree; ENSGT00390000015162; -.
DR HOGENOM; CLU_073203_1_0_1; -.
DR InParanoid; Q9D7M1; -.
DR OMA; QNGRIQE; -.
DR OrthoDB; 1365635at2759; -.
DR PhylomeDB; Q9D7M1; -.
DR TreeFam; TF300176; -.
DR BioGRID-ORCS; 76425; 6 hits in 71 CRISPR screens.
DR ChiTaRS; Gid8; mouse.
DR PRO; PR:Q9D7M1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7M1; protein.
DR Bgee; ENSMUSG00000027573; Expressed in interventricular septum and 227 other tissues.
DR Genevisible; Q9D7M1; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF08513; LisH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..228
FT /note="Glucose-induced degradation protein 8 homolog"
FT /id="PRO_0000079412"
FT DOMAIN 25..57
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 63..120
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 116..212
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000250|UniProtKB:Q9NWU2"
SQ SEQUENCE 228 AA; 26779 MW; 21514CECB335C781 CRC64;
MSYAEKPDEI TKDEWMEKLN NLHVQRADMN RLIMNYLVTE GFKEAAEKFR MESGIEPSVD
LETLDERIKI REMILKGQIQ EAIALINSLH PELLDTNRYL YFHLQQQHLI ELIRQRETEA
ALEFAQTQLA EQGEESRECL TEMERTLALL AFDSPEESPF GDLLHMMQRQ KVWSEVNQAV
LDYENRESTP KLAKLLKLLL WAQNELDQKK VKYPKMTDLS KGVIEEPK
