(data stored in ACNUC21429 zone)

SWISSPROT: UBQL1_HUMAN

ID   UBQL1_HUMAN             Reviewed;         589 AA.
AC   Q9UMX0; A0A024R284; Q5T6J5; Q5T6J9; Q8IXS9; Q8N2Q3; Q9H0T8; Q9H3R4; Q9HAZ5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   11-DEC-2019, entry version 189.
DE   RecName: Full=Ubiquilin-1;
DE   AltName: Full=Protein linking IAP with cytoskeleton 1;
DE            Short=PLIC-1;
DE            Short=hPLIC-1;
GN   Name=UBQLN1; Synonyms=DA41, PLIC1;
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] (ISOFORM 1), INTERACTION WITH PSEN1 AND PSEN2,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11076969; DOI=10.1083/jcb.151.4.847;
RA   Mah A.L., Perry G., Smith M.A., Monteiro M.J.;
RT   "Identification of ubiquilin, a novel presenilin interactor that increases
RT   presenilin protein accumulation.";
RL   J. Cell Biol. 151:847-862(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Mah A.L., Monteiro M.J.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH UBE3A; BTRC
RP   AND THE PROTEASOME.
RC   TISSUE=B-cell;
RX   PubMed=10983987; DOI=10.1016/s1097-2765(00)00040-x;
RA   Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L.,
RA   Gill G., Howley P.M.;
RT   "The hPLIC proteins may provide a link between the ubiquitination machinery
RT   and the proteasome.";
RL   Mol. Cell 6:409-419(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=10807547; DOI=10.1007/s100380050209;
RA   Hanaoka E., Ozaki T., Ohira M., Nakamura Y., Suzuki M., Takahashi E.,
RA   Moriya H., Nakagawara A., Sakiyama S.;
RT   "Molecular cloning and expression analysis of the human DA41 gene and its
RT   mapping to chromosome 9q21.2-q21.3.";
RL   J. Hum. Genet. 45:188-191(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li J.Y.;
RT   "Human testis protein.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Muscle;
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316.
RC   TISSUE=Embryo;
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   [11]
RP   PROTEIN SEQUENCE OF 71-83; 207-236; 244-253 AND 547-582, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [12]
RP   PHOSPHORYLATION, INTERACTION WITH MTOR, AND TISSUE SPECIFICITY.
RX   PubMed=11853878; DOI=10.1016/s0167-4889(01)00164-1;
RA   Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.;
RT   "Characterization of ubiquilin 1, an mTOR-interacting protein.";
RL   Biochim. Biophys. Acta 1542:41-56(2002).
RN   [13]
RP   INTERACTION WITH P4HB.
RX   PubMed=12095988; DOI=10.1074/jbc.m203412200;
RA   Ko H.S., Uehara T., Nomura Y.;
RT   "Role of ubiquilin associated with protein-disulfide isomerase in the
RT   endoplasmic reticulum in stress-induced apoptotic cell death.";
RL   J. Biol. Chem. 277:35386-35392(2002).
RN   [14]
RP   FUNCTION, DOMAIN UBIQUITIN-LIKE, DOMAIN UBA, AND INTERACTION WITH UBA52;
RP   PSMD3 AND PSMD4.
RX   PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
RA   Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
RT   "Ubiquilin interacts with ubiquitylated proteins and proteasome through its
RT   ubiquitin-associated and ubiquitin-like domains.";
RL   FEBS Lett. 566:110-114(2004).
RN   [15]
RP   INTERACTION WITH EPS15; EPS15L1; HGS AND STAM2, SUBCELLULAR LOCATION, AND
RP   UBIQUITINATION.
RX   PubMed=16159959; DOI=10.1242/jcs.02571;
RA   Regan-Klapisz E., Sorokina I., Voortman J., de Keizer P., Roovers R.C.,
RA   Verheesen P., Urbe S., Fallon L., Fon E.A., Verkleij A., Benmerah A.,
RA   van Bergen en Henegouwen P.M.;
RT   "Ubiquilin recruits Eps15 into ubiquitin-rich cytoplasmic aggregates via a
RT   UIM-UBL interaction.";
RL   J. Cell Sci. 118:4437-4450(2005).
RN   [16]
RP   SUBUNIT, HETERODIMERIZATION WITH UBQLN2, AND INTERACTION WITH PSEN1 AND
RP   PSEN2.
RX   PubMed=16813565; DOI=10.1042/bj20060441;
RA   Ford D.L., Monteiro M.J.;
RT   "Dimerization of ubiquilin is dependent upon the central region of the
RT   protein: evidence that the monomer, but not the dimer, is involved in
RT   binding presenilins.";
RL   Biochem. J. 399:397-404(2006).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17323924; DOI=10.1021/bi061994u;
RA   Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT   "Mass spectrometric characterization of the affinity-purified human 26S
RT   proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH HERPUD1.
RX   PubMed=18307982; DOI=10.1016/j.bbrc.2008.02.086;
RA   Kim T.Y., Kim E., Yoon S.K., Yoon J.B.;
RT   "Herp enhances ER-associated protein degradation by recruiting
RT   ubiquilins.";
RL   Biochem. Biophys. Res. Commun. 369:741-746(2008).
RN   [19]
RP   INTERACTION WITH EPS15.
RX   PubMed=18199683; DOI=10.1091/mbc.e07-08-0775;
RA   N'Diaye E.N., Hanyaloglu A.C., Kajihara K.K., Puthenveedu M.A., Wu P.,
RA   von Zastrow M., Brown E.J.;
RT   "The ubiquitin-like protein PLIC-2 is a negative regulator of G protein-
RT   coupled receptor endocytosis.";
RL   Mol. Biol. Cell 19:1252-1260(2008).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [21]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN UBA.
RX   PubMed=19148225; DOI=10.1038/embor.2008.238;
RA   N'Diaye E.N., Kajihara K.K., Hsieh I., Morisaki H., Debnath J., Brown E.J.;
RT   "PLIC proteins or ubiquilins regulate autophagy-dependent cell survival
RT   during nutrient starvation.";
RL   EMBO Rep. 10:173-179(2009).
RN   [22]
RP   FUNCTION, INTERACTION WITH UBXN4, IDENTIFICATION IN A COMPLEX WITH UBXN4
RP   AND VCP, AND SUBCELLULAR LOCATION.
RX   PubMed=19822669; DOI=10.1083/jcb.200903024;
RA   Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
RA   Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
RT   "Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD.";
RL   J. Cell Biol. 187:201-217(2009).
RN   [23]
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18953672; DOI=10.1007/s12031-008-9155-6;
RA   Lu A., Hiltunen M., Romano D.M., Soininen H., Hyman B.T., Bertram L.,
RA   Tanzi R.E.;
RT   "Effects of ubiquilin 1 on the unfolded protein response.";
RL   J. Mol. Neurosci. 38:19-30(2009).
RN   [24]
RP   REVIEW.
RX   PubMed=20729634; DOI=10.4161/auto.6.7.13118;
RA   Rothenberg C., Monteiro M.J.;
RT   "Ubiquilin at a crossroads in protein degradation pathways.";
RL   Autophagy 6:979-980(2010).
RN   [25]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH UBQLN2 AND
RP   MAP1LC3A/B/C, AND PROTEOLYTIC DEGRADATION.
RX   PubMed=20529957; DOI=10.1093/hmg/ddq231;
RA   Rothenberg C., Srinivasan D., Mah L., Kaushik S., Peterhoff C.M.,
RA   Ugolino J., Fang S., Cuervo A.M., Nixon R.A., Monteiro M.J.;
RT   "Ubiquilin functions in autophagy and is degraded by chaperone-mediated
RT   autophagy.";
RL   Hum. Mol. Genet. 19:3219-3232(2010).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [28]
RP   REVIEW.
RX   PubMed=21966562; DOI=10.4161/cib.4.4.15283;
RA   Haapasalo A., Viswanathan J., Kurkinen K.M., Bertram L., Soininen H.,
RA   Dantuma N.P., Tanzi R.E., Hiltunen M.;
RT   "Involvement of ubiquilin-1 transcript variants in protein degradation and
RT   accumulation.";
RL   Commun. Integr. Biol. 4:428-432(2011).
RN   [29]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TICAM1.
RX   PubMed=21695056; DOI=10.1371/journal.pone.0021153;
RA   Biswas N., Liu S., Ronni T., Aussenberg S.E., Liu W., Fujita T., Wang T.;
RT   "The ubiquitin-like protein PLIC-1 or ubiquilin 1 inhibits TLR3-Trif
RT   signaling.";
RL   PLoS ONE 6:E21153-E21153(2011).
RN   [30]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [31]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1.
RX   PubMed=21143716; DOI=10.1111/j.1600-0854.2010.01149.x;
RA   Viswanathan J., Haapasalo A., Bottcher C., Miettinen R., Kurkinen K.M.,
RA   Lu A., Thomas A., Maynard C.J., Romano D., Hyman B.T., Berezovska O.,
RA   Bertram L., Soininen H., Dantuma N.P., Tanzi R.E., Hiltunen M.;
RT   "Alzheimer's disease-associated ubiquilin-1 regulates presenilin-1
RT   accumulation and aggresome formation.";
RL   Traffic 12:330-348(2011).
RN   [32]
RP   REVIEW.
RX   PubMed=22628307; DOI=10.1515/hsz-2012-0120;
RA   Lee D.Y., Brown E.J.;
RT   "Ubiquilins in the crosstalk among proteolytic pathways.";
RL   Biol. Chem. 393:441-447(2012).
RN   [33]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [34]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN4 AND
RP   MAP1LC3A/B/C.
RX   PubMed=23459205; DOI=10.1038/embor.2013.22;
RA   Lee D.Y., Arnott D., Brown E.J.;
RT   "Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy
RT   machinery.";
RL   EMBO Rep. 14:373-381(2013).
RN   [35]
RP   REVIEW.
RX   PubMed=23600477; DOI=10.1517/14728222.2013.791284;
RA   Takalo M., Haapasalo A., Natunen T., Viswanathan J., Kurkinen K.M.,
RA   Tanzi R.E., Soininen H., Hiltunen M.;
RT   "Targeting ubiquilin-1 in Alzheimer's disease.";
RL   Expert Opin. Ther. Targets 17:795-810(2013).
RN   [36]
RP   INTERACTION WITH TREX1, AND SUBCELLULAR LOCATION.
RX   PubMed=23979357; DOI=10.1074/jbc.m113.503391;
RA   Orebaugh C.D., Fye J.M., Harvey S., Hollis T., Wilkinson J.C.,
RA   Perrino F.W.;
RT   "The TREX1 C-terminal region controls cellular localization through
RT   ubiquitination.";
RL   J. Biol. Chem. 288:28881-28892(2013).
RN   [37]
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   [38]
RP   FUNCTION, INTERACTION WITH ORAI1, AND SUBCELLULAR LOCATION.
RX   PubMed=23307288; DOI=10.1007/s10059-013-2268-7;
RA   Lee J.E., Jeon I.S., Han N.E., Song H.J., Kim E.G., Choi J.W., Song K.D.,
RA   Lee H.K., Choi J.K.;
RT   "Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization.";
RL   Mol. Cells 35:41-46(2013).
RN   [39]
RP   REVIEW.
RX   PubMed=24674348; DOI=10.1186/1471-2148-14-63;
RA   Marin I.;
RT   "The ubiquilin gene family: evolutionary patterns and functional
RT   insights.";
RL   BMC Evol. Biol. 14:63-63(2014).
RN   [40]
RP   STRUCTURE BY NMR OF 541-586 ALONE AND IN COMPLEX WITH UBIQUITIN.
RX   PubMed=18241885; DOI=10.1016/j.jmb.2007.12.029;
RA   Zhang D., Raasi S., Fushman D.;
RT   "Affinity makes the difference: nonselective interaction of the UBA domain
RT   of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains.";
RL   J. Mol. Biol. 377:162-180(2008).
CC   -!- FUNCTION: Plays an important role in the regulation of different
CC       protein degradation mechanisms and pathways including ubiquitin-
CC       proteasome system (UPS), autophagy and endoplasmic reticulum-associated
CC       protein degradation (ERAD) pathway. Mediates the proteasomal targeting
CC       of misfolded or accumulated proteins for degradation by binding (via
CC       UBA domain) to their polyubiquitin chains and by interacting (via
CC       ubiquitin-like domain) with the subunits of the proteasome
CC       (PubMed:15147878). Plays a role in the ERAD pathway via its interaction
CC       with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link
CC       between the polyubiquitinated ERAD substrates and the proteasome
CC       (PubMed:19822669, PubMed:18307982). Isoform 1, isoform 2 and isoform 3
CC       play a role in unfolded protein response (UPR) by attenuating the
CC       induction of UPR-inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER
CC       stress (PubMed:18953672). Involved in the regulation of macroautophagy
CC       and autophagosome formation; required for maturation of autophagy-
CC       related protein LC3 from the cytosolic form LC3-I to the membrane-bound
CC       form LC3-II and may assist in the maturation of autophagosomes to
CC       autolysosomes by mediating autophagosome-lysosome fusion
CC       (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively
CC       regulates the TICAM1/TRIF-dependent toll-like receptor signaling
CC       pathway by decreasing the abundance of TICAM1 via the autophagic
CC       pathway (PubMed:21695056). Isoform 1 and isoform 3 play a key role in
CC       the regulation of the levels of PSEN1 by targeting its accumulation to
CC       aggresomes which may then be removed from cells by autophagocytosis
CC       (PubMed:21143716). Promotes the ubiquitination and lysosomal
CC       degradation of ORAI1, consequently downregulating the ORAI1-mediated
CC       Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and
CC       proteasomal degradation of amyloid beta A4 protein (A4) by stimulating
CC       the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of
CC       A4 by sequestering it in the Golgi apparatus and preventing its
CC       transport to the cell surface for subsequent processing (By
CC       similarity). {ECO:0000250|UniProtKB:Q9JJP9,
CC       ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:18953672,
CC       ECO:0000269|PubMed:19148225, ECO:0000269|PubMed:19822669,
CC       ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716,
CC       ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288,
CC       ECO:0000269|PubMed:23459205, ECO:0000303|PubMed:15147878}.
CC   -!- SUBUNIT: Monomer and homodimer. Heterodimer with UBQLN2
CC       (PubMed:16813565). Binds CD47, NBL1, GABRA1, GABRA2, GABRA3, GABRA6,
CC       GABRB1, GABRB2 and GABRB3 (By similarity). Binds UBE3A, BTRC, P4HB and
CC       MTOR. Interacts with the proteasome 19S subunit. Interacts (via
CC       ubiquitin-like domain) with TREX1; the interaction is direct and may
CC       control TREX1 subcellular location. Forms a complex with UBXN4 and VCP.
CC       Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like domain).
CC       Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric form
CC       interacts with PSEN2 and the monomeric forms of isoform 1 and isoform 3
CC       interact with PSEN1. Interacts with ORAI1. Interacts (via UBA domain)
CC       with TICAM1. Interacts with EPS15. Interacts (via UBA domain) with
CC       UBA52 and (via ubiquitin-like domain) with PSMD3 and PSMD4. Interacts
CC       with HERPUD1. Interacts with MAP1LC3A/B/C in the presence of UBQLN4.
CC       Interacts (via ubiquitin-like domain) with EPS15 (via UIM domains) and
CC       both the ubiquitinated and non-ubiquitinated forms can interact with
CC       EPS15. Interacts (via ubiquitin-like domain) with EPS15L1, HGS (via UIM
CC       domain) and STAM2 (via UIM domain). {ECO:0000250|UniProtKB:Q8R317,
CC       ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:10983987,
CC       ECO:0000269|PubMed:11076969, ECO:0000269|PubMed:11853878,
CC       ECO:0000269|PubMed:12095988, ECO:0000269|PubMed:15147878,
CC       ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:16813565,
CC       ECO:0000269|PubMed:18199683, ECO:0000269|PubMed:18241885,
CC       ECO:0000269|PubMed:18307982, ECO:0000269|PubMed:19822669,
CC       ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716,
CC       ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288,
CC       ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:23979357}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-741480, EBI-741480;
CC       Q8WU02:-; NbExp=3; IntAct=EBI-741480, EBI-747182;
CC       Q96FB2:-; NbExp=3; IntAct=EBI-10173939, EBI-2857623;
CC       O00154:ACOT7; NbExp=3; IntAct=EBI-10173939, EBI-948905;
CC       Q16186:ADRM1; NbExp=4; IntAct=EBI-741480, EBI-954387;
CC       Q9NUQ2:AGPAT5; NbExp=5; IntAct=EBI-741480, EBI-6916385;
CC       O95994:AGR2; NbExp=7; IntAct=EBI-741480, EBI-712648;
CC       Q8TD06:AGR3; NbExp=3; IntAct=EBI-10173939, EBI-3925742;
CC       Q9NP55:BPIFA1; NbExp=3; IntAct=EBI-10173939, EBI-953896;
CC       Q9BXJ5:C1QTNF2; NbExp=3; IntAct=EBI-10173939, EBI-2817707;
CC       O43852:CALU; NbExp=3; IntAct=EBI-10173939, EBI-1171069;
CC       P80098:CCL7; NbExp=3; IntAct=EBI-10173939, EBI-718759;
CC       Q8TCZ2:CD99L2; NbExp=6; IntAct=EBI-741480, EBI-2824782;
CC       P51788-4:CLCN2; NbExp=3; IntAct=EBI-10173939, EBI-16431116;
CC       Q03692:COL10A1; NbExp=5; IntAct=EBI-741480, EBI-2528309;
CC       A0A0S2Z3K0:COL1A2; NbExp=3; IntAct=EBI-10173939, EBI-16431143;
CC       P08123:COL1A2; NbExp=6; IntAct=EBI-10173939, EBI-983038;
CC       Q8IYK4:COLGALT2; NbExp=3; IntAct=EBI-10173939, EBI-10263496;
CC       Q86VU5:COMTD1; NbExp=3; IntAct=EBI-10173939, EBI-2836030;
CC       P33240:CSTF2; NbExp=6; IntAct=EBI-741480, EBI-711360;
CC       Q9H0L4:CSTF2T; NbExp=6; IntAct=EBI-741480, EBI-747012;
CC       P78358:CTAG1B; NbExp=7; IntAct=EBI-741480, EBI-1188472;
CC       O75638:CTAG2; NbExp=3; IntAct=EBI-10173939, EBI-10188927;
CC       Q9UHQ9:CYB5R1; NbExp=3; IntAct=EBI-10173939, EBI-953870;
CC       Q01524:DEFA6; NbExp=3; IntAct=EBI-10173939, EBI-10222451;
CC       A0A0S2Z5Y1:DOLK; NbExp=3; IntAct=EBI-741480, EBI-16431159;
CC       O95967:EFEMP2; NbExp=4; IntAct=EBI-741480, EBI-743414;
CC       P42566:EPS15; NbExp=5; IntAct=EBI-741480, EBI-396684;
CC       Q96DN0:ERP27; NbExp=3; IntAct=EBI-741480, EBI-953772;
CC       Q9HBU6:ETNK1; NbExp=3; IntAct=EBI-10173939, EBI-2834493;
CC       P12318:FCGR2A; NbExp=3; IntAct=EBI-741480, EBI-1395970;
CC       P26885:FKBP2; NbExp=3; IntAct=EBI-10173939, EBI-719873;
CC       P02751:FN1; NbExp=3; IntAct=EBI-741480, EBI-1220319;
CC       O75084:FZD7; NbExp=3; IntAct=EBI-741480, EBI-746917;
CC       O14764:GABRD; NbExp=4; IntAct=EBI-741480, EBI-744352;
CC       Q9UBU3:GHRL; NbExp=3; IntAct=EBI-741480, EBI-10319458;
CC       P22352:GPX3; NbExp=3; IntAct=EBI-10173939, EBI-2832946;
CC       Q14416:GRM2; NbExp=3; IntAct=EBI-10173939, EBI-10232876;
CC       P06028:GYPB; NbExp=6; IntAct=EBI-741480, EBI-10194756;
CC       P52789:HK2; NbExp=4; IntAct=EBI-741480, EBI-741469;
CC       Q53GQ0:HSD17B12; NbExp=3; IntAct=EBI-741480, EBI-2963255;
CC       P48723:HSPA13; NbExp=7; IntAct=EBI-741480, EBI-750892;
CC       Q6PIK1:IGL@; NbExp=3; IntAct=EBI-10173939, EBI-10253735;
CC       Q6PIQ7:IGL@; NbExp=3; IntAct=EBI-741480, EBI-6677651;
CC       Q8N355:IGL@; NbExp=4; IntAct=EBI-741480, EBI-748681;
CC       Q17RA0:IL6ST; NbExp=3; IntAct=EBI-10173939, EBI-10238517;
CC       P53990:IST1; NbExp=3; IntAct=EBI-741480, EBI-945994;
CC       Q6GPH6:ITPRIPL1; NbExp=3; IntAct=EBI-741480, EBI-953819;
CC       Q9P2K6:KLHL42; NbExp=3; IntAct=EBI-10173939, EBI-739890;
CC       A0A0S2Z5S9:LHX4; NbExp=3; IntAct=EBI-741480, EBI-16429099;
CC       Q99732:LITAF; NbExp=7; IntAct=EBI-10173939, EBI-725647;
CC       Q9NQG1:MANBAL; NbExp=3; IntAct=EBI-10173939, EBI-3867271;
CC       P33993:MCM7; NbExp=3; IntAct=EBI-10173939, EBI-355924;
CC       Q9NQG6:MIEF1; NbExp=3; IntAct=EBI-10173939, EBI-740987;
CC       Q96C03:MIEF2; NbExp=4; IntAct=EBI-741480, EBI-750153;
CC       P55198:MLLT6; NbExp=3; IntAct=EBI-10173939, EBI-740216;
CC       Q8IW45:NAXD; NbExp=3; IntAct=EBI-10173939, EBI-8650724;
CC       P41271:NBL1; NbExp=3; IntAct=EBI-10173939, EBI-10208650;
CC       Q96IV0:NGLY1; NbExp=5; IntAct=EBI-741480, EBI-6165879;
CC       A0A0S2Z5K2:NLGN3; NbExp=3; IntAct=EBI-10173939, EBI-16431177;
CC       Q13232:NME3; NbExp=5; IntAct=EBI-741480, EBI-713684;
CC       P01160:NPPA; NbExp=3; IntAct=EBI-741480, EBI-953859;
CC       Q9BVL2:NUP58; NbExp=3; IntAct=EBI-10173939, EBI-2811583;
CC       C3PTT6:PAUF; NbExp=3; IntAct=EBI-10173939, EBI-3505892;
CC       Q96AQ6:PBXIP1; NbExp=3; IntAct=EBI-10173939, EBI-740845;
CC       Q96FE7:PIK3IP1; NbExp=3; IntAct=EBI-10173939, EBI-10285708;
CC       P53816:PLAAT3; NbExp=6; IntAct=EBI-741480, EBI-746318;
CC       Q8ND90:PNMA1; NbExp=4; IntAct=EBI-741480, EBI-302345;
CC       P23284:PPIB; NbExp=3; IntAct=EBI-741480, EBI-359252;
CC       P45877:PPIC; NbExp=3; IntAct=EBI-741480, EBI-953909;
CC       Q96NZ9:PRAP1; NbExp=5; IntAct=EBI-741480, EBI-2116102;
CC       A5D903:PRB1; NbExp=3; IntAct=EBI-10173939, EBI-10173935;
CC       P55036:PSMD4; NbExp=4; IntAct=EBI-741480, EBI-359318;
CC       Q15008:PSMD6; NbExp=3; IntAct=EBI-10173939, EBI-359701;
CC       Q9NPQ8:RIC8A; NbExp=3; IntAct=EBI-741480, EBI-717509;
CC       Q9NPQ8-4:RIC8A; NbExp=3; IntAct=EBI-741480, EBI-9091816;
CC       Q9H0X6:RNF208; NbExp=3; IntAct=EBI-741480, EBI-751555;
CC       P04843:RPN1; NbExp=3; IntAct=EBI-741480, EBI-355963;
CC       Q7L4I2-2:RSRC2; NbExp=3; IntAct=EBI-741480, EBI-10256202;
CC       Q9BWD3:RTL8A; NbExp=4; IntAct=EBI-741480, EBI-741643;
CC       Q17RB0:RTL8B; NbExp=5; IntAct=EBI-741480, EBI-10238588;
CC       A6ZKI3:RTL8C; NbExp=5; IntAct=EBI-741480, EBI-10174072;
CC       P13521:SCG2; NbExp=3; IntAct=EBI-741480, EBI-947132;
CC       P05408:SCG5; NbExp=3; IntAct=EBI-741480, EBI-722635;
CC       Q96GD3:SCMH1; NbExp=3; IntAct=EBI-10173939, EBI-713793;
CC       P05121:SERPINE1; NbExp=3; IntAct=EBI-10173939, EBI-953978;
CC       O75830:SERPINI2; NbExp=8; IntAct=EBI-741480, EBI-750144;
CC       Q9H173:SIL1; NbExp=3; IntAct=EBI-741480, EBI-2840325;
CC       Q9BVW6:SMIM2; NbExp=3; IntAct=EBI-741480, EBI-10300146;
CC       P02814:SMR3B; NbExp=3; IntAct=EBI-741480, EBI-738612;
CC       P10124:SRGN; NbExp=5; IntAct=EBI-741480, EBI-744915;
CC       P04155:TFF1; NbExp=3; IntAct=EBI-741480, EBI-743871;
CC       Q96DC7:TMCO6; NbExp=5; IntAct=EBI-741480, EBI-746174;
CC       Q96DC7-2:TMCO6; NbExp=3; IntAct=EBI-741480, EBI-10284552;
CC       Q5JXX7:TMEM31; NbExp=3; IntAct=EBI-10173939, EBI-10244617;
CC       A0A0S2Z5T9:TMEM67; NbExp=3; IntAct=EBI-10173939, EBI-16431189;
CC       Q71RG4:TMUB2; NbExp=3; IntAct=EBI-10173939, EBI-2820477;
CC       Q13049:TRIM32; NbExp=8; IntAct=EBI-741480, EBI-742790;
CC       O95881:TXNDC12; NbExp=3; IntAct=EBI-741480, EBI-2564581;
CC       Q5U5U6:UBB; NbExp=3; IntAct=EBI-741480, EBI-1642104;
CC       Q96C32:UBC; NbExp=3; IntAct=EBI-741480, EBI-745483;
CC       Q13404:UBE2V1; NbExp=5; IntAct=EBI-741480, EBI-1050671;
CC       Q9NRR5:UBQLN4; NbExp=8; IntAct=EBI-741480, EBI-711226;
CC       Q04323:UBXN1; NbExp=3; IntAct=EBI-741480, EBI-1058647;
CC       Q92575:UBXN4; NbExp=5; IntAct=EBI-741480, EBI-723441;
CC       Q0VG75:XPO4; NbExp=3; IntAct=EBI-741480, EBI-10226948;
CC       Q8WV99:ZFAND2B; NbExp=3; IntAct=EBI-10173939, EBI-747823;
CC       O60844:ZG16; NbExp=8; IntAct=EBI-741480, EBI-746479;
CC       Q5VZL5:ZMYM4; NbExp=3; IntAct=EBI-741480, EBI-2514659;
CC       Q6P1L6:ZNF343; NbExp=3; IntAct=EBI-741480, EBI-10252492;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16159959,
CC       ECO:0000269|PubMed:23979357}. Nucleus {ECO:0000269|PubMed:23979357}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:19822669}. Cytoplasmic
CC       vesicle, autophagosome {ECO:0000269|PubMed:19148225,
CC       ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:21143716,
CC       ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288,
CC       ECO:0000269|PubMed:23459205}. Cell membrane
CC       {ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:23307288}.
CC       Note=Detected in neuronal processes and at synapses (By similarity).
CC       Recruited to the ER during ER-associated protein degradation (ERAD)
CC       (PubMed:19822669). Isoform 1 and isoform 3 colocalize with PSEN1 in the
CC       cell membrane and in cytoplasmic juxtanuclear structures called
CC       aggresomes (PubMed:21143716). Colocalizes with ORAI1 and TICAM1 in the
CC       autophagosome (PubMed:23307288, PubMed:21695056). Colocalizes with
CC       EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not
CC       endocytic compartments and with EPS15 also in aggresomes
CC       (PubMed:16159959). {ECO:0000250|UniProtKB:Q9JJP9,
CC       ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19822669,
CC       ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056,
CC       ECO:0000269|PubMed:23307288}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9UMX0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UMX0-2; Sequence=VSP_009787;
CC       Name=3;
CC         IsoId=Q9UMX0-3; Sequence=VSP_057689;
CC       Name=4;
CC         IsoId=Q9UMX0-4; Sequence=VSP_057690, VSP_057691;
CC   -!- TISSUE SPECIFICITY: Brain (at protein level) (PubMed:18953672).
CC       Ubiquitous. Highly expressed throughout the brain; detected in neurons
CC       and in neuropathological lesions, such as neurofibrillary tangles and
CC       Lewy bodies. Highly expressed in heart, placenta, pancreas, lung,
CC       liver, skeletal muscle and kidney. {ECO:0000269|PubMed:11076969,
CC       ECO:0000269|PubMed:11853878, ECO:0000269|PubMed:18953672}.
CC   -!- DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It also
CC       binds ubiquitin with micromolar affinity, independently of
CC       polyubiquitin linkage type. Essential for its association with
CC       microtubule-associated protein 1 light chain 3 (MAP1LC3).
CC       {ECO:0000269|PubMed:11076969, ECO:0000269|PubMed:15147878,
CC       ECO:0000269|PubMed:19148225}.
CC   -!- DOMAIN: The ubiquitin-like domain mediates its association with the
CC       subunits of the proteasome. {ECO:0000269|PubMed:15147878}.
CC   -!- DOMAIN: Dimerization is dependent upon the central region of the
CC       protein containing the STI1 domains and is independent of its
CC       ubiquitin-like and UBA domains. {ECO:0000269|PubMed:16813565}.
CC   -!- PTM: Degraded during both macroautophagy and during chaperone-mediated
CC       autophagy (CMA). {ECO:0000269|PubMed:20529957}.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11853878}.
CC   -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16159959}.
DR   EMBL; AF176069; AAD49751.3; -; mRNA.
DR   EMBL; AF293384; AAG02473.1; -; mRNA.
DR   EMBL; AB035275; BAB20436.1; -; mRNA.
DR   EMBL; HM005532; AEE61129.1; -; mRNA.
DR   EMBL; AL136643; CAB66578.1; -; mRNA.
DR   EMBL; AL354920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62659.1; -; Genomic_DNA.
DR   EMBL; CH471089; EAW62661.1; -; Genomic_DNA.
DR   EMBL; CH471089; EAW62664.1; -; Genomic_DNA.
DR   EMBL; BC010066; AAH10066.1; -; mRNA.
DR   EMBL; BC039294; AAH39294.1; -; mRNA.
DR   EMBL; AK074535; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS6663.1; -. [Q9UMX0-1]
DR   CCDS; CCDS6664.1; -. [Q9UMX0-2]
DR   RefSeq; NP_038466.2; NM_013438.4. [Q9UMX0-1]
DR   RefSeq; NP_444295.1; NM_053067.2. [Q9UMX0-2]
DR   PDB; 2JY5; NMR; -; A=541-586.
DR   PDB; 2JY6; NMR; -; B=541-586.
DR   PDB; 2KLC; NMR; -; A=34-112.
DR   PDBsum; 2JY5; -.
DR   PDBsum; 2JY6; -.
DR   PDBsum; 2KLC; -.
DR   SMR; Q9UMX0; -.
DR   BioGrid; 119007; 266.
DR   CORUM; Q9UMX0; -.
DR   DIP; DIP-41629N; -.
DR   IntAct; Q9UMX0; 206.
DR   MINT; Q9UMX0; -.
DR   STRING; 9606.ENSP00000365576; -.
DR   iPTMnet; Q9UMX0; -.
DR   PhosphoSitePlus; Q9UMX0; -.
DR   BioMuta; UBQLN1; -.
DR   DMDM; 48475013; -.
DR   REPRODUCTION-2DPAGE; IPI00071180; -.
DR   EPD; Q9UMX0; -.
DR   jPOST; Q9UMX0; -.
DR   MassIVE; Q9UMX0; -.
DR   PaxDb; Q9UMX0; -.
DR   PeptideAtlas; Q9UMX0; -.
DR   PRIDE; Q9UMX0; -.
DR   ProteomicsDB; 85215; -. [Q9UMX0-1]
DR   ProteomicsDB; 85216; -. [Q9UMX0-2]
DR   Ensembl; ENST00000257468; ENSP00000257468; ENSG00000135018. [Q9UMX0-2]
DR   Ensembl; ENST00000376395; ENSP00000365576; ENSG00000135018. [Q9UMX0-1]
DR   GeneID; 29979; -.
DR   KEGG; hsa:29979; -.
DR   UCSC; uc004amv.4; human. [Q9UMX0-1]
DR   CTD; 29979; -.
DR   DisGeNET; 29979; -.
DR   EuPathDB; HostDB:ENSG00000135018.13; -.
DR   GeneCards; UBQLN1; -.
DR   HGNC; HGNC:12508; UBQLN1.
DR   HPA; CAB037256; -.
DR   HPA; HPA054143; -.
DR   MIM; 605046; gene.
DR   neXtProt; NX_Q9UMX0; -.
DR   OpenTargets; ENSG00000135018; -.
DR   PharmGKB; PA37155; -.
DR   eggNOG; KOG0010; Eukaryota.
DR   eggNOG; COG5272; LUCA.
DR   GeneTree; ENSGT00940000156437; -.
DR   InParanoid; Q9UMX0; -.
DR   KO; K04523; -.
DR   OMA; AGMFNTP; -.
DR   OrthoDB; 1553668at2759; -.
DR   PhylomeDB; Q9UMX0; -.
DR   TreeFam; TF314412; -.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   ChiTaRS; UBQLN1; human.
DR   EvolutionaryTrace; Q9UMX0; -.
DR   GeneWiki; UBQLN1; -.
DR   GenomeRNAi; 29979; -.
DR   Pharos; Q9UMX0; Tbio.
DR   PRO; PR:Q9UMX0; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9UMX0; protein.
DR   Bgee; ENSG00000135018; Expressed in 209 organ(s), highest expression level in placenta.
DR   ExpressionAtlas; Q9UMX0; baseline and differential.
DR   Genevisible; Q9UMX0; HS.
DR   GO; GO:0016235; C:aggresome; IDA:UniProtKB.
DR   GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; IDA:LIFEdb.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR   GO; GO:0035973; P:aggrephagy; IDA:UniProtKB.
DR   GO; GO:0000045; P:autophagosome assembly; IMP:GO_Central.
DR   GO; GO:0097352; P:autophagosome maturation; IMP:GO_Central.
DR   GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR   GO; GO:0016236; P:macroautophagy; IMP:GO_Central.
DR   GO; GO:1901340; P:negative regulation of store-operated calcium channel activity; IMP:UniProtKB.
DR   GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR   GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0016241; P:regulation of macroautophagy; IBA:GO_Central.
DR   GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IDA:HGNC-UCL.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR015496; Ubiquilin.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR028799; UBQLN1.
DR   PANTHER; PTHR10677; PTHR10677; 1.
DR   PANTHER; PTHR10677:SF16; PTHR10677:SF16; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00727; STI1; 4.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9UMX0.
DR   SWISS-2DPAGE; Q9UMX0.
KW   3D-structure; Acetylation; Alternative splicing; Autophagy; Cell membrane;
KW   Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW   Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:22223895"
FT   CHAIN           2..589
FT                   /note="Ubiquilin-1"
FT                   /id="PRO_0000211008"
FT   DOMAIN          37..111
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          182..210
FT                   /note="STI1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          212..251
FT                   /note="STI1 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          387..434
FT                   /note="STI1 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          438..470
FT                   /note="STI1 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          546..586
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          178..428
FT                   /note="Interaction with UBXN4"
FT                   /evidence="ECO:0000269|PubMed:19822669"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:22223895"
FT   VAR_SEQ         61..237
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:18953672"
FT                   /id="VSP_057689"
FT   VAR_SEQ         150..181
FT                   /note="GGLGGLAGLSSLGLNTTNFSELQSQMQRQLLS -> DVGTCQESSNDAGDDE
FT                   EPGPSFEQPRKHPRGI (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:18953672"
FT                   /id="VSP_057690"
FT   VAR_SEQ         182..589
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:18953672"
FT                   /id="VSP_057691"
FT   VAR_SEQ         417..444
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:18953672"
FT                   /id="VSP_009787"
FT   CONFLICT        25
FT                   /note="A -> T (in Ref. 9; AAH39294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="V -> A (in Ref. 4; BAB20436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="F -> S (in Ref. 4; BAB20436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="L -> S (in Ref. 4; BAB20436)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="S -> G (in Ref. 6; CAB66578)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="P -> H (in Ref. 9; AAH39294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        537..538
FT                   /note="NP -> YS (in Ref. 4; BAB20436)"
FT                   /evidence="ECO:0000305"
FT   STRAND          37..42
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   STRAND          47..52
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   HELIX           58..69
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   HELIX           73..75
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   STRAND          76..80
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   STRAND          83..85
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   HELIX           92..94
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   STRAND          101..106
FT                   /evidence="ECO:0000244|PDB:2KLC"
FT   TURN            543..547
FT                   /evidence="ECO:0000244|PDB:2JY5"
FT   HELIX           548..556
FT                   /evidence="ECO:0000244|PDB:2JY5"
FT   HELIX           562..572
FT                   /evidence="ECO:0000244|PDB:2JY5"
FT   HELIX           576..583
FT                   /evidence="ECO:0000244|PDB:2JY5"
SQ   SEQUENCE   589 AA;  62519 MW;  8B4756B6113B7025 CRC64;
     MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF AVPENSSVQQ
     FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL TVHLVIKTQN RPQDHSAQQT
     NTAGSNVTTS STPNSNSTSG SATSNPFGLG GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL
     SNPEMMVQIM ENPFVQSMLS NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE
     LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV
     SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA SGTSGQSTTA
     PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM RSMMQSLSQN PDLAAQMMLN
     NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT LSAMSNPRAM QALLQIQQGL QTLATEAPGL
     IPGFTPGLGA LGSTGGSSGT NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL
     QNPEVRFQQQ LEQLSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS
//

If you have problems or comments...

PBIL Back to PBIL home page