ID ADRM1_HUMAN Reviewed; 407 AA.
AC Q16186; A0PKB1; Q96FJ7; Q9H1P2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 28-JAN-2026, entry version 209.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE AltName: Full=110 kDa cell membrane glycoprotein;
DE Short=Gp110;
DE AltName: Full=Adhesion-regulating molecule 1;
DE Short=ARM-1;
DE AltName: Full=Proteasome regulatory particle non-ATPase 13;
DE Short=hRpn13;
DE AltName: Full=Rpn13 homolog;
GN Name=ADRM1; Synonyms=GP110;
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=8033103;
RA Shimada S., Ogawa M., Takahashi M., Schlom J., Greiner J.W.;
RT "Molecular cloning and characterization of the complementary DNA of an M(r)
RT 110,000 antigen expressed by human gastric carcinoma cells and upregulated
RT by gamma-interferon.";
RL Cancer Res. 54:3831-3836(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PSMD1 AND UCHL5,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16990800; DOI=10.1038/sj.emboj.7601338;
RA Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.;
RT "A novel proteasome-interacting protein recruits the deubiquitinating
RT enzyme UCH37 to 26S proteasomes.";
RL EMBO J. 25:4524-4536(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pancreas;
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, INTERACTION WITH UCHL5, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
RA Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
RT "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
RT deubiquitinating enzyme, UCH37.";
RL EMBO J. 25:5742-5753(2006).
RN [6]
RP FUNCTION, INTERACTION WITH 26S PROTEASOME, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16815440; DOI=10.1016/j.jmb.2006.06.011;
RA Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K., Johnsen A.H.,
RA Hendil K.B., Hartmann-Petersen R.;
RT "Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-
RT associated factor.";
RL J. Mol. Biol. 360:1043-1052(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16906146; DOI=10.1038/ncb1460;
RA Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
RA Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
RT "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme
RT by Adrm1.";
RL Nat. Cell Biol. 8:994-1002(2006).
RN [9]
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 [10]
RP FUNCTION, INTERACTION WITH UBIQUITIN, AND REGION.
RX PubMed=18497817; DOI=10.1038/nature06926;
RA Husnjak K., Elsasser S., Zhang N., Chen X., Randles L., Shi Y., Hofmann K.,
RA Walters K.J., Finley D., Dikic I.;
RT "Proteasome subunit Rpn13 is a novel ubiquitin receptor.";
RL Nature 453:481-488(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND THR-217, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND THR-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
RP UBIQUITINATION.
RX PubMed=24811749; DOI=10.1002/embj.201386906;
RA Besche H.C., Sha Z., Kukushkin N.V., Peth A., Hock E.M., Kim W., Gygi S.,
RA Gutierrez J.A., Liao H., Dick L., Goldberg A.L.;
RT "Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of
RT ubiquitin conjugates.";
RL EMBO J. 33:1159-1176(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127 AND SER-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP UBIQUITINATION.
RX PubMed=31375563; DOI=10.1074/jbc.ra119.009654;
RA Gottlieb C.D., Thompson A.C.S., Ordureau A., Harper J.W., Kopito R.R.;
RT "Acute unfolding of a single protein immediately stimulates recruitment of
RT ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes.";
RL J. Biol. Chem. 294:16511-16524(2019).
RN [20]
RP STRUCTURE BY NMR OF 1-407, INTERACTION WITH PSMD1, AND REGION.
RX PubMed=20471946; DOI=10.1016/j.molcel.2010.04.019;
RA Chen X., Lee B.H., Finley D., Walters K.J.;
RT "Structure of proteasome ubiquitin receptor hRpn13 and its activation by
RT the scaffolding protein hRpn2.";
RL Mol. Cell 38:404-415(2010).
RN [21]
RP STRUCTURE BY NMR OF 270-407, INTERACTION WITH UCHL5, AND FUNCTION.
RX PubMed=24752541; DOI=10.1007/s13238-014-0046-z;
RA Jiao L., Ouyang S., Shaw N., Song G., Feng Y., Niu F., Qiu W., Zhu H.,
RA Hung L.W., Zuo X., Eleonora Shtykova V., Zhu P., Dong Y.H., Xu R.,
RA Liu Z.J.;
RT "Mechanism of the Rpn13-induced activation of Uch37.";
RL Protein Cell 5:616-630(2014).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 266-388, INTERACTION WITH UCHL5,
RP AND FUNCTION.
RX PubMed=25702870; DOI=10.1016/j.molcel.2014.12.039;
RA Sahtoe D.D., van Dijk W.J., El Oualid F., Ekkebus R., Ovaa H., Sixma T.K.;
RT "Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13
RT and INO80G.";
RL Mol. Cell 57:887-900(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 285-386, INTERACTION WITH UCHL5,
RP AND FUNCTION.
RX PubMed=25702872; DOI=10.1016/j.molcel.2015.01.016;
RA VanderLinden R.T., Hemmis C.W., Schmitt B., Ndoja A., Whitby F.G.,
RA Robinson H., Cohen R.E., Yao T., Hill C.P.;
RT "Structural basis for the activation and inhibition of the UCH37
RT deubiquitylase.";
RL Mol. Cell 57:901-911(2015).
RN [24]
RP STRUCTURE BY NMR OF 1-150, AND INTERACTION WITH UBIQUITIN AND UBQLN2.
RX PubMed=27396824; DOI=10.1016/j.str.2016.05.018;
RA Chen X., Randles L., Shi K., Tarasov S.G., Aihara H., Walters K.J.;
RT "Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding
RT mechanisms between substrate receptors and shuttle factors of the
RT proteasome.";
RL Structure 24:1257-1270(2016).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins
CC (PubMed:16815440, PubMed:16906146, PubMed:16990800, PubMed:17139257,
CC PubMed:18497817, PubMed:24752541, PubMed:25702870, PubMed:25702872).
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required (PubMed:16815440, PubMed:16906146, PubMed:16990800,
CC PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870,
CC PubMed:25702872). Therefore, the proteasome participates in numerous
CC cellular processes, including cell cycle progression, apoptosis, or DNA
CC damage repair (PubMed:16815440, PubMed:16906146, PubMed:16990800,
CC PubMed:17139257, PubMed:18497817, PubMed:24752541, PubMed:25702870,
CC PubMed:25702872). Within the complex, functions as a proteasomal
CC ubiquitin receptor (PubMed:18497817). Engages and activates 19S-
CC associated deubiquitinases UCHL5 and PSMD14 during protein degradation
CC (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541).
CC UCHL5 reversibly associate with the 19S regulatory particle whereas
CC PSMD14 is an intrinsic subunit of the proteasome lid subcomplex
CC (PubMed:16906146, PubMed:16990800, PubMed:17139257, PubMed:24752541).
CC {ECO:0000269|PubMed:16815440, ECO:0000269|PubMed:16906146,
CC ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:17139257,
CC ECO:0000269|PubMed:18497817, ECO:0000269|PubMed:24752541,
CC ECO:0000269|PubMed:25702870, ECO:0000269|PubMed:25702872}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP) (PubMed:16990800). Interacts with the
CC proteasomal scaffolding protein PSMD1 (PubMed:16815440,
CC PubMed:16906146, PubMed:16990800, PubMed:20471946). Interacts with
CC deubiquitinase UCHL5; this interaction activates the auto-inhibited
CC UCHL5 by deoligomerizing it (PubMed:17139257, PubMed:24752541,
CC PubMed:25702870, PubMed:25702872). Interacts with UBQLN2 and ubiquitin
CC (PubMed:27396824). {ECO:0000269|PubMed:16815440,
CC ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800,
CC ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817,
CC ECO:0000269|PubMed:20471946, ECO:0000269|PubMed:24752541,
CC ECO:0000269|PubMed:25702872, ECO:0000269|PubMed:27396824}.
CC -!- INTERACTION:
CC Q16186; Q99460: PSMD1; NbExp=7; IntAct=EBI-954387, EBI-357874;
CC Q16186; Q13200: PSMD2; NbExp=6; IntAct=EBI-954387, EBI-357648;
CC Q16186; P55036: PSMD4; NbExp=6; IntAct=EBI-954387, EBI-359318;
CC Q16186; P54727: RAD23B; NbExp=2; IntAct=EBI-954387, EBI-954531;
CC Q16186; P0CG48: UBC; NbExp=11; IntAct=EBI-954387, EBI-3390054;
CC Q16186; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-954387, EBI-741480;
CC Q16186; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-954387, EBI-947187;
CC Q16186; Q9Y5K5: UCHL5; NbExp=24; IntAct=EBI-954387, EBI-1051183;
CC Q16186; Q9Y5K5-3: UCHL5; NbExp=5; IntAct=EBI-954387, EBI-11749875;
CC Q16186; P48510: DSK2; Xeno; NbExp=4; IntAct=EBI-954387, EBI-6174;
CC Q16186; O35593: Psmd14; Xeno; NbExp=2; IntAct=EBI-954387, EBI-772796;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16990800}. Nucleus
CC {ECO:0000269|PubMed:16990800}.
CC -!- DOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain
CC mediates interactions with PSMD1 and ubiquitin. Preferential binding to
CC the proximal subunit of 'Lys-48'-linked diubiquitin allows UCHL5 access
CC to the distal subunit. {ECO:0000269|PubMed:18497817}.
CC -!- PTM: Ubiquitinated by UBE3C in response to proteotoxic stress.
CC {ECO:0000269|PubMed:24811749, ECO:0000269|PubMed:31375563}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
CC -!- CAUTION: Although initially described as a cell membrane glycoprotein,
CC ADRM1 is intracellular and non-glycosylated, and has probably no direct
CC role in cell adhesion. {ECO:0000305}.
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DR EMBL; D64154; BAA11023.1; -; mRNA.
DR EMBL; AL354836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BR000321; FAA00246.1; -; mRNA.
DR EMBL; BC010733; AAH10733.1; -; mRNA.
DR EMBL; BC017245; AAH17245.1; -; mRNA.
DR CCDS; CCDS13496.1; -.
DR PIR; I52703; I52703.
DR RefSeq; NP_001268366.1; NM_001281437.1.
DR RefSeq; NP_001268367.1; NM_001281438.1.
DR RefSeq; NP_008933.2; NM_007002.3.
DR RefSeq; NP_783163.1; NM_175573.2.
DR PDB; 2KQZ; NMR; -; A=253-407.
DR PDB; 2KR0; NMR; -; A=1-407.
DR PDB; 2L5V; NMR; -; A=260-407.
DR PDB; 2MKZ; NMR; -; A=270-407.
DR PDB; 2NBV; NMR; -; A=1-150.
DR PDB; 4UEL; X-ray; 2.30 A; C=266-388.
DR PDB; 4UEM; X-ray; 2.82 A; B=266-388.
DR PDB; 4WLQ; X-ray; 2.85 A; B=286-384.
DR PDB; 4WLR; X-ray; 2.00 A; B=285-386.
DR PDB; 5IRS; X-ray; 1.80 A; A=2-150.
DR PDB; 5V1Y; X-ray; 1.42 A; A/B=19-132.
DR PDB; 5V1Z; X-ray; 2.00 A; A/B=19-132.
DR PDB; 5YMY; NMR; -; C=1-150.
DR PDB; 6CO4; NMR; -; A=1-150.
DR PDB; 6OI4; X-ray; 1.76 A; A/B=20-132.
DR PDB; 6UYI; NMR; -; A=1-150.
DR PDB; 6UYJ; NMR; -; A=1-150.
DR PDB; 7KXI; NMR; -; A=1-150.
DR PDB; 8FTQ; X-ray; 2.10 A; A/B=2-150.
DR PDB; 8VWO; X-ray; 1.85 A; A=1-150.
DR PDB; 9E7K; X-ray; 2.41 A; B=269-388.
DR PDBsum; 2KQZ; -.
DR PDBsum; 2KR0; -.
DR PDBsum; 2L5V; -.
DR PDBsum; 2MKZ; -.
DR PDBsum; 2NBV; -.
DR PDBsum; 4UEL; -.
DR PDBsum; 4UEM; -.
DR PDBsum; 4WLQ; -.
DR PDBsum; 4WLR; -.
DR PDBsum; 5IRS; -.
DR PDBsum; 5V1Y; -.
DR PDBsum; 5V1Z; -.
DR PDBsum; 5YMY; -.
DR PDBsum; 6CO4; -.
DR PDBsum; 6OI4; -.
DR PDBsum; 6UYI; -.
DR PDBsum; 6UYJ; -.
DR PDBsum; 7KXI; -.
DR PDBsum; 8FTQ; -.
DR PDBsum; 8VWO; -.
DR PDBsum; 9E7K; -.
DR AlphaFoldDB; Q16186; -.
DR BMRB; Q16186; -.
DR EMDB; EMD-60138; -.
DR EMDB; EMD-60139; -.
DR SMR; Q16186; -.
DR BioGRID; 116235; 278.
DR ComplexPortal; CPX-5993; 26S proteasome complex.
DR ComplexPortal; CPX-8964; 19S proteasome regulatory complex.
DR ComplexPortal; CPX-9082; 19S-20S-PA28-alphabeta hybrid proteasome complex.
DR ComplexPortal; CPX-9085; 19S-20S-PA28-gamma hybrid proteasome complex.
DR ComplexPortal; CPX-9086; 30S proteasome complex.
DR DIP; DIP-42668N; -.
DR FunCoup; Q16186; 2057.
DR IntAct; Q16186; 104.
DR MINT; Q16186; -.
DR STRING; 9606.ENSP00000478877; -.
DR BindingDB; Q16186; -.
DR ChEMBL; CHEMBL3710002; -.
DR GlyCosmos; Q16186; 10 sites, 2 glycans.
DR GlyGen; Q16186; 11 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q16186; -.
DR PhosphoSitePlus; Q16186; -.
DR SwissPalm; Q16186; -.
DR BioMuta; ADRM1; -.
DR DMDM; 20141265; -.
DR jPOST; Q16186; -.
DR MassIVE; Q16186; -.
DR PaxDb; 9606-ENSP00000478877; -.
DR PeptideAtlas; Q16186; -.
DR ProteomicsDB; 60836; -.
DR Pumba; Q16186; -.
DR Antibodypedia; 29483; 309 antibodies from 36 providers.
DR DNASU; 11047; -.
DR Ensembl; ENST00000253003.7; ENSP00000253003.2; ENSG00000130706.14.
DR Ensembl; ENST00000491935.5; ENSP00000478877.1; ENSG00000130706.14.
DR GeneID; 11047; -.
DR KEGG; hsa:11047; -.
DR MANE-Select; ENST00000253003.7; ENSP00000253003.2; NM_007002.4; NP_008933.2.
DR UCSC; uc002ycn.5; human.
DR AGR; HGNC:15759; -.
DR ClinPGx; PA24599; -.
DR CTD; 11047; -.
DR DisGeNET; 11047; -.
DR GeneCards; ADRM1; -.
DR HGNC; HGNC:15759; ADRM1.
DR HPA; ENSG00000130706; Tissue enhanced (skeletal).
DR MalaCards; ADRM1; -.
DR MIM; 610650; gene.
DR OpenTargets; ENSG00000130706; -.
DR VEuPathDB; HostDB:ENSG00000130706; -.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; Q16186; -.
DR OMA; SNQRHFF; -.
DR OrthoDB; 340431at2759; -.
DR PAN-GO; Q16186; 5 GO annotations based on evolutionary models.
DR PhylomeDB; Q16186; -.
DR PathwayCommons; Q16186; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-9766229; Degradation of CDH1.
DR Reactome; R-HSA-9824272; Somitogenesis.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-HSA-9907900; Proteasome assembly.
DR Reactome; R-HSA-9932298; Degradation of CRY and PER proteins.
DR SignaLink; Q16186; -.
DR SIGNOR; Q16186; -.
DR Agora; ENSG00000130706; -.
DR BioGRID-ORCS; 11047; 253 hits in 1159 CRISPR screens.
DR ChiTaRS; ADRM1; human.
DR EvolutionaryTrace; Q16186; -.
DR GeneWiki; ADRM1; -.
DR GenomeRNAi; 11047; -.
DR Pharos; Q16186; Tbio.
DR PRO; PR:Q16186; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q16186; protein.
DR Bgee; ENSG00000130706; Expressed in gastrocnemius and 188 other cell types or tissues.
DR ExpressionAtlas; Q16186; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB.
DR GO; GO:0140678; F:molecular function inhibitor activity; EXP:DisProt.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0043248; P:proteasome assembly; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd13314; PH_Rpn13; 1.
DR DisProt; DP00839; -.
DR FunFam; 1.10.2020.20:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR IDEAL; IID00671; -.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Proteasome; Proteomics identification; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..407
FT /note="Proteasomal ubiquitin receptor ADRM1"
FT /id="PRO_0000020631"
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265,
FT ECO:0000269|PubMed:18497817"
FT DOMAIN 277..391
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 194..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..407
FT /note="Interaction with UCHL5"
FT /evidence="ECO:0000269|PubMed:20471946"
FT REGION 379..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMB5"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CONFLICT 142
FT /note="S -> T (in Ref. 1; BAA11023)"
FT /evidence="ECO:0000305"
FT STRAND 23..34
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5V1Y"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5V1Y"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6OI4"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5V1Y"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5V1Y"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5V1Y"
FT TURN 191..195
FT /evidence="ECO:0007829|PDB:2KR0"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2KR0"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2KR0"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2KR0"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:2KQZ"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2KR0"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2KQZ"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 334..348
FT /evidence="ECO:0007829|PDB:4WLR"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:4UEM"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:4WLR"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:4WLR"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2KR0"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:2MKZ"
SQ SEQUENCE 407 AA; 42153 MW; 2D38811DCA231864 CRC64;
MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNEYLNN PPMPGALGAS GSSGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSSGP PGSSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT
SPSPAPSSGN GASTAASPTQ PIQLSDLQSI LATMNVPAGP AGGQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNNAKPEQK EGDTKDKKDE EEDMSLD
//
