TMUB1_MOUSE
ID TMUB1_MOUSE Reviewed; 245 AA.
AC Q9JMG3; Q53AQ3;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
DE AltName: Full=Hepatocyte odd protein shuttling protein;
DE Contains:
DE RecName: Full=iHOPS {ECO:0000303|PubMed:24240191};
GN Name=Tmub1; Synonyms=Hops;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA Inoue S., Sano H., Ohta M.;
RT "Growth suppression of Escherichia coli by induction of expression of
RT mammalian genes with transmembrane or ATPase domains.";
RL Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH EEF1A1, AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=16014383; DOI=10.1242/jcs.02452;
RA Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V.,
RA Piobbico D., Viola-Magni M., Servillo G.;
RT "HOPS: a novel cAMP-dependent shuttling protein involved in protein
RT synthesis regulation.";
RL J. Cell Sci. 118:3185-3194(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 [5]
RP FUNCTION.
RX PubMed=18418082; DOI=10.4161/cc.7.10.5882;
RA Pieroni S., Della Fazia M.A., Castelli M., Piobbico D., Bartoli D.,
RA Brunacci C., Bellet M.M., Viola-Magni M., Servillo G.;
RT "HOPS is an essential constituent of centrosome assembly.";
RL Cell Cycle 7:1462-1466(2008).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH GRIA2 AND
RP GRIP1.
RX PubMed=18665261; DOI=10.1371/journal.pone.0002809;
RA Yang H., Takagi H., Konishi Y., Ageta H., Ikegami K., Yao I., Sato S.,
RA Hatanaka K., Inokuchi K., Seog D.H., Setou M.;
RT "Transmembrane and ubiquitin-like domain-containing protein 1 (Tmub1/HOPS)
RT facilitates surface expression of GluR2-containing AMPA receptors.";
RL PLoS ONE 3:E2809-E2809(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [8]
RP SUBCELLULAR LOCATION, INTERACTION WITH CAMLG, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RX PubMed=20582322; DOI=10.1371/journal.pone.0011261;
RA Zhang W., Savelieva K.V., Suwanichkul A., Small D.L., Kirkpatrick L.L.,
RA Xu N., Lanthorn T.H., Ye G.L.;
RT "Transmembrane and ubiquitin-like domain containing 1 (Tmub1) regulates
RT locomotor activity and wakefulness in mice and interacts with CAMLG.";
RL PLoS ONE 5:E11261-E11261(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPM1 AND CDKN2A.
RX PubMed=22890319; DOI=10.1038/onc.2012.353;
RA Castelli M., Pieroni S., Brunacci C., Piobbico D., Bartoli D., Bellet M.M.,
RA Colombo E., Pelicci P.G., Della Fazia M.A., Servillo G.;
RT "Hepatocyte odd protein shuttling (HOPS) is a bridging protein in the
RT nucleophosmin-p19 Arf network.";
RL Oncogene 32:3350-3358(2013).
RN [10]
RP ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (IHOPS), INTERACTION WITH NPM,
RP PROTEOLYTIC CLEAVAGE (IHOPS), AND TISSUE SPECIFICITY.
RX PubMed=24240191; DOI=10.4161/cc.27054;
RA Castelli M., Piobbico D., Bartoli D., Pieroni S., Brunacci C., Bellet M.M.,
RA Chiacchiaretta M., Della Fazia M.A., Servillo G.;
RT "Different functions of HOPS isoforms in the cell: HOPS shuttling isoform
RT is determined by RIP cleavage system.";
RL Cell Cycle 13:293-302(2014).
CC -!- FUNCTION: Involved in sterol-regulated ubiquitination and degradation
CC of HMG-CoA reductase HMGCR (By similarity). Involved in positive
CC regulation of AMPA-selective glutamate receptor GRIA2 recycling to the
CC cell surface (By similarity). Acts as negative regulator of hepatocyte
CC growth during regeneration (By similarity).
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8,
CC ECO:0000269|PubMed:16014383, ECO:0000269|PubMed:18418082,
CC ECO:0000269|PubMed:22890319}.
CC -!- FUNCTION: [iHOPS]: May contribute to the regulation of translation
CC during cell-cycle progression. May contribute to the regulation of cell
CC proliferation (PubMed:16014383). May be involved in centrosome assembly
CC (PubMed:18418082). Modulates stabilization and nucleolar localization
CC of tumor suppressor CDKN2A and enhances association between CDKN2A and
CC NPM1 (PubMed:22890319). {ECO:0000269|PubMed:18418082,
CC ECO:0000269|PubMed:22890319}.
CC -!- SUBUNIT: Interacts with EEF1A1, CAMLG, GRIA2 and GRIP1. Interacts with
CC NPM1 and CDKN2A; TMUB1 can enhance interaction between NPM1 and CDKN2A
CC and is proposed to bridge the proteins; proposed to be mediated by
CC iHOPS (PubMed:16014383, PubMed:18665261, PubMed:20582322,
CC PubMed:22890319, PubMed:24240191). Interacts with TUBG1 (By
CC similarity). Interacts with ERLIN2 and AMFR; TMUB1 promotes the
CC interaction of ERLIN2 with AMFR (By similarity).
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000250|UniProtKB:Q9BVT8,
CC ECO:0000269|PubMed:16014383, ECO:0000269|PubMed:18665261,
CC ECO:0000269|PubMed:20582322, ECO:0000269|PubMed:22890319,
CC ECO:0000269|PubMed:24240191}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18665261}; Multi-
CC pass membrane protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:18665261}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q53AQ4}. Cytoplasm {ECO:0000269|PubMed:16014383,
CC ECO:0000269|PubMed:20582322}. Nucleus {ECO:0000269|PubMed:16014383}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:22890319}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000305|PubMed:24240191}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane
CC {ECO:0000250|UniProtKB:Q53AQ4, ECO:0000305|PubMed:24240191}.
CC -!- SUBCELLULAR LOCATION: [iHOPS]: Cytoplasm {ECO:0000250|UniProtKB:Q53AQ4,
CC ECO:0000305|PubMed:24240191}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000305|PubMed:24240191}. Nucleus,
CC nucleolus {ECO:0000305|PubMed:24240191}. Nucleus
CC {ECO:0000305|PubMed:24240191}. Note=iHOPS is proposed to be the
CC shuttling form across different cellular compartments
CC (PubMed:24240191). XPO1-dependent exported from the nucleus in dividing
CC cells. Predominantly nuclear during growth arrest (PubMed:16014383).
CC {ECO:0000269|PubMed:16014383, ECO:0000305|PubMed:24240191}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=lHOPS;
CC IsoId=Q9JMG3-1; Sequence=Displayed;
CC Name=2; Synonyms=sHOPS;
CC IsoId=Q9JMG3-2; Sequence=VSP_058102;
CC -!- TISSUE SPECIFICITY: Expressed in adult brain; at protein level
CC (PubMed:18665261, PubMed:20582322). Isoform 1 (lHOPS) is highly
CC expressed in small intestine, stomach and epididymis. Isoform 2 (sHOPS)
CC and iHOPS are abundantly expressed in brain, liver and adrenal gland
CC (PubMed:24240191). {ECO:0000269|PubMed:20582322,
CC ECO:0000269|PubMed:24240191}.
CC -!- INDUCTION: Up-regulated in regenerating liver.
CC {ECO:0000269|PubMed:16014383}.
CC -!- PTM: [iHOPS]: Isoform 1 (lHOPS) is processed by regulated intramembrane
CC proteolysis (RIP) in the N-terminus to release iHOPS from membranes.
CC {ECO:0000269|PubMed:24240191}.
CC -!- PTM: Isoform 2 seems to undergo a selective cleavage in the C-terminal
CC region to release an additional cytoplasmic form.
CC {ECO:0000269|PubMed:24240191}.
CC -!- DISRUPTION PHENOTYPE: Strong increase in home cage locomotor activity
CC during the dark phase (subjective day) of the light:dark (L:D) cycle.
CC There were no changes in activity during the light period and in
CC locomotor activity observed in other assays, e.g. novel open-field.
CC {ECO:0000269|PubMed:20582322}.
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DR EMBL; AB030183; BAA92747.1; -; mRNA.
DR EMBL; AY603379; AAU00155.1; -; mRNA.
DR EMBL; AK008109; BAB25465.1; -; mRNA.
DR EMBL; BC019547; AAH19547.1; -; mRNA.
DR CCDS; CCDS19121.1; -. [Q9JMG3-1]
DR RefSeq; NP_071863.1; NM_022418.3. [Q9JMG3-1]
DR RefSeq; XP_006535849.1; XM_006535786.2. [Q9JMG3-1]
DR AlphaFoldDB; Q9JMG3; -.
DR SMR; Q9JMG3; -.
DR BioGRID; 211057; 3.
DR IntAct; Q9JMG3; 2.
DR STRING; 10090.ENSMUSP00000030799; -.
DR iPTMnet; Q9JMG3; -.
DR PhosphoSitePlus; Q9JMG3; -.
DR MaxQB; Q9JMG3; -.
DR PaxDb; Q9JMG3; -.
DR PRIDE; Q9JMG3; -.
DR ProteomicsDB; 259057; -. [Q9JMG3-1]
DR ProteomicsDB; 259058; -. [Q9JMG3-2]
DR Antibodypedia; 32973; 107 antibodies from 17 providers.
DR DNASU; 64295; -.
DR Ensembl; ENSMUST00000030799; ENSMUSP00000030799; ENSMUSG00000028958. [Q9JMG3-1]
DR Ensembl; ENSMUST00000115033; ENSMUSP00000110685; ENSMUSG00000028958. [Q9JMG3-1]
DR GeneID; 64295; -.
DR KEGG; mmu:64295; -.
DR UCSC; uc008wrt.2; mouse. [Q9JMG3-1]
DR CTD; 83590; -.
DR MGI; MGI:1923764; Tmub1.
DR VEuPathDB; HostDB:ENSMUSG00000028958; -.
DR eggNOG; ENOG502QU8U; Eukaryota.
DR GeneTree; ENSGT00390000014069; -.
DR HOGENOM; CLU_053940_1_0_1; -.
DR InParanoid; Q9JMG3; -.
DR OMA; AWISTHT; -.
DR OrthoDB; 1164744at2759; -.
DR PhylomeDB; Q9JMG3; -.
DR TreeFam; TF329265; -.
DR BioGRID-ORCS; 64295; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tmub1; mouse.
DR PRO; PR:Q9JMG3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JMG3; protein.
DR Bgee; ENSMUSG00000028958; Expressed in hindlimb stylopod muscle and 92 other tissues.
DR ExpressionAtlas; Q9JMG3; baseline and differential.
DR Genevisible; Q9JMG3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR InterPro; IPR040352; TMUB1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR14557; PTHR14557; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Cytoplasm; Cytoskeleton; Endosome;
KW Membrane; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..245
FT /note="Transmembrane and ubiquitin-like domain-containing
FT protein 1"
FT /id="PRO_0000114923"
FT CHAIN ?..245
FT /note="iHOPS"
FT /id="PRO_0000435489"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 102..175
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 2..30
FT /note="Required to release iHOPS from membranes"
FT /evidence="ECO:0000269|PubMed:24240191"
FT REGION 33..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVT8"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:24240191"
FT /id="VSP_058102"
FT CONFLICT 233
FT /note="L -> Q (in Ref. 2; AAU00155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 26316 MW; 02C1D1B24C13139D CRC64;
MALIEGVGDE VTVLFAVLAC LLVLALAWVS THTTESTDPQ PQPPGTTTPA QPSEAMSASD
SIREEAPGAE SPSLRHRGPS AQPEPDTGVT ASTPPDSPQE PLLLRLKFLN DSEQVARAWP
QDTIGSLKRT QFPGQEQQVR LIYQGQLLGD DTQTLGSLHL PPNCVLHCHV STRVGPPHPP
CPPGSEPGPS GLEIGSLLLP LLLLLLLLLW YCQIQYRPFF PLTATLGLAG FTLLLSLLAF
AMYRP
