TMUB1_HUMAN
ID TMUB1_HUMAN Reviewed; 246 AA.
AC Q9BVT8; D3DX06; Q53AQ2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
DE AltName: Full=Dendritic cell-derived ubiquitin-like protein;
DE Short=DULP;
DE AltName: Full=Hepatocyte odd protein shuttling protein;
DE AltName: Full=Ubiquitin-like protein SB144;
DE Contains:
DE RecName: Full=iHOPS;
GN Name=TMUB1; Synonyms=C7orf21, DULP, HOPS; ORFNames=SB144, UNQ763/PRO1555;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Dendritic cell;
RX PubMed=19254477; DOI=10.1038/cmi.2009.4;
RA Liu G.Y., Liu S.X., Li P., Tang L., Han Y.M., An H.Z., Li J.Y., Dai X.K.,
RA Li N., Cao X.T., Yu Y.Z.;
RT "Cloning and characterization of DULP, a novel ubiquitin-like molecule from
RT human dendritic cells.";
RL Cell. Mol. Immunol. 6:27-33(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Placenta;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; THR-92 AND SER-98, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-98, 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 [11]
RP FUNCTION, AND INTERACTION WITH ERLIN2 AND AMFR.
RX PubMed=21343306; DOI=10.1074/jbc.m110.211326;
RA Jo Y., Sguigna P.V., DeBose-Boyd R.A.;
RT "Membrane-associated ubiquitin ligase complex containing gp78 mediates
RT sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A
RT reductase.";
RL J. Biol. Chem. 286:15022-15031(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-73 AND SER-127, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP 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 (PubMed:21343306). 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:Q9JMG3,
CC ECO:0000269|PubMed:21343306}.
CC -!- FUNCTION: [iHOPS]: May contribute to the regulation of translation
CC during cell-cycle progression. May contribute to the regulation of cell
CC proliferation (By similarity). May be involved in centrosome assembly.
CC Modulates stabilization and nucleolar localization of tumor suppressor
CC CDKN2A and enhances association between CDKN2A and NPM1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBUNIT: Interacts with EEF1A1, GRIA2, GRIP1, CAMLG, TUBG1 (By
CC similarity). Interacts with NPM1 and CDKN2A; TMUB1 can enhance
CC interaction between NPM1 and CDKN2A and is proposed to bridge the
CC proteins; proposed to be mediated by iHOPS (By similarity). Interacts
CC with ERLIN2 and AMFR; TMUB1 promotes the interaction of ERLIN2 with
CC AMFR (PubMed:21343306). {ECO:0000250|UniProtKB:Q53AQ4,
CC ECO:0000250|UniProtKB:Q9JMG3, ECO:0000269|PubMed:21343306}.
CC -!- INTERACTION:
CC Q9BVT8; Q9UKV5: AMFR; NbExp=2; IntAct=EBI-11425701, EBI-1046367;
CC Q9BVT8; O94905: ERLIN2; NbExp=5; IntAct=EBI-11425701, EBI-4400770;
CC Q9BVT8; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-11425701, EBI-712073;
CC Q9BVT8; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11425701, EBI-1055254;
CC Q9BVT8; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-11425701, EBI-744081;
CC Q9BVT8; P55061: TMBIM6; NbExp=3; IntAct=EBI-11425701, EBI-1045825;
CC Q9BVT8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-11425701, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9JMG3}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9JMG3}. Postsynaptic cell
CC membrane {ECO:0000250|UniProtKB:Q9JMG3}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q53AQ4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus {ECO:0000250|UniProtKB:Q9JMG3}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- SUBCELLULAR LOCATION: [iHOPS]: Cytoplasm {ECO:0000250|UniProtKB:Q53AQ4,
CC ECO:0000250|UniProtKB:Q9JMG3}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9JMG3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9JMG3}. Note=iHOPS is proposed to be the
CC shuttling form across different cellular compartments. XPO1-dependent
CC exported from the nucleus in dividing cells. Predominantly nuclear
CC during growth arrest. {ECO:0000250|UniProtKB:Q9JMG3}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC mammary and thyroid glands, bone marrow and spleen; limited expression
CC in cardiac, pancreatic and ovarian tissues.
CC {ECO:0000269|PubMed:24240191}.
CC -!- PTM: [iHOPS]: Processed by regulated intramembrane proteolysis (RIP)in
CC the N-terminus to release iHOPS from membranes (By similarity).
CC {ECO:0000250|UniProtKB:Q9JMG3}.
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DR EMBL; AY603380; AAU00156.1; -; mRNA.
DR EMBL; AY037155; AAK67645.1; -; mRNA.
DR EMBL; AY358481; AAQ88845.1; -; mRNA.
DR EMBL; AK314035; BAG36745.1; -; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471173; EAW54030.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54032.1; -; Genomic_DNA.
DR EMBL; BC000936; AAH00936.1; -; mRNA.
DR EMBL; BC033182; AAH33182.1; -; mRNA.
DR CCDS; CCDS5920.1; -.
DR RefSeq; NP_001129516.1; NM_001136044.1.
DR RefSeq; NP_113622.1; NM_031434.3.
DR AlphaFoldDB; Q9BVT8; -.
DR SMR; Q9BVT8; -.
DR BioGRID; 123686; 86.
DR CORUM; Q9BVT8; -.
DR IntAct; Q9BVT8; 20.
DR STRING; 9606.ENSP00000376565; -.
DR TCDB; 8.A.62.1.1; the transmembrane and ubiquitin-like domain-containing protein 1 (tmub1) family.
DR GlyGen; Q9BVT8; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVT8; -.
DR PhosphoSitePlus; Q9BVT8; -.
DR BioMuta; TMUB1; -.
DR DMDM; 34922062; -.
DR EPD; Q9BVT8; -.
DR jPOST; Q9BVT8; -.
DR MassIVE; Q9BVT8; -.
DR MaxQB; Q9BVT8; -.
DR PaxDb; Q9BVT8; -.
DR PeptideAtlas; Q9BVT8; -.
DR PRIDE; Q9BVT8; -.
DR ProteomicsDB; 79233; -.
DR TopDownProteomics; Q9BVT8; -.
DR Antibodypedia; 32973; 107 antibodies from 17 providers.
DR DNASU; 83590; -.
DR Ensembl; ENST00000297533.9; ENSP00000297533.4; ENSG00000164897.14.
DR Ensembl; ENST00000392818.7; ENSP00000376565.3; ENSG00000164897.14.
DR Ensembl; ENST00000462940.1; ENSP00000417519.1; ENSG00000164897.14.
DR Ensembl; ENST00000476627.5; ENSP00000419214.1; ENSG00000164897.14.
DR Ensembl; ENST00000482202.5; ENSP00000418709.1; ENSG00000164897.14.
DR GeneID; 83590; -.
DR KEGG; hsa:83590; -.
DR MANE-Select; ENST00000297533.9; ENSP00000297533.4; NM_001136044.2; NP_001129516.1.
DR UCSC; uc003wjb.4; human.
DR CTD; 83590; -.
DR DisGeNET; 83590; -.
DR GeneCards; TMUB1; -.
DR HGNC; HGNC:21709; TMUB1.
DR HPA; ENSG00000164897; Low tissue specificity.
DR MIM; 614792; gene.
DR neXtProt; NX_Q9BVT8; -.
DR OpenTargets; ENSG00000164897; -.
DR PharmGKB; PA134863959; -.
DR VEuPathDB; HostDB:ENSG00000164897; -.
DR eggNOG; ENOG502QU8U; Eukaryota.
DR GeneTree; ENSGT00390000014069; -.
DR HOGENOM; CLU_053940_1_0_1; -.
DR InParanoid; Q9BVT8; -.
DR OrthoDB; 1164744at2759; -.
DR PhylomeDB; Q9BVT8; -.
DR TreeFam; TF329265; -.
DR PathwayCommons; Q9BVT8; -.
DR SignaLink; Q9BVT8; -.
DR BioGRID-ORCS; 83590; 8 hits in 1084 CRISPR screens.
DR ChiTaRS; TMUB1; human.
DR GenomeRNAi; 83590; -.
DR Pharos; Q9BVT8; Tbio.
DR PRO; PR:Q9BVT8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9BVT8; protein.
DR Bgee; ENSG00000164897; Expressed in mucosa of transverse colon and 97 other tissues.
DR ExpressionAtlas; Q9BVT8; baseline and differential.
DR Genevisible; Q9BVT8; HS.
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; IMP:UniProtKB.
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 SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..246
FT /note="Transmembrane and ubiquitin-like domain-containing
FT protein 1"
FT /id="PRO_0000114922"
FT CHAIN ?..246
FT /note="iHOPS"
FT /id="PRO_0000435488"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..176
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:0000250|UniProtKB:Q9JMG3"
FT REGION 34..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 246 AA; 26261 MW; E08E25A6B37665B3 CRC64;
MTLIEGVGDE VTVLFSVLAC LLVLALAWVS THTAEGGDPL PQPSGTPTPS QPSAAMAATD
SMRGEAPGAE TPSLRHRGQA AQPEPSTGFT ATPPAPDSPQ EPLVLRLKFL NDSEQVARAW
PHDTIGSLKR TQFPGREQQV RLIYQGQLLG DDTQTLGSLH LPPNCVLHCH VSTRVGPPNP
PCPPGSEPGP SGLEIGSLLL PLLLLLLLLL WYCQIQYRPF FPLTATLGLA GFTLLLSLLA
FAMYRP
