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Proteasomal ubiquitin receptor ADRM1 (110 kDa cell membrane glycoprotein) (Gp110) (Adhesion-regulating molecule 1) (ARM-1) (Proteasome regulatory particle non-ATPase 13) (hRpn13) (Rpn13 homolog)

 ADRM1_HUMAN             Reviewed;         407 AA.
Q16186; A0PKB1; Q96FJ7; Q9H1P2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
25-OCT-2017, entry version 158.
RecName: Full=Proteasomal ubiquitin receptor ADRM1;
AltName: Full=110 kDa cell membrane glycoprotein;
Short=Gp110;
AltName: Full=Adhesion-regulating molecule 1;
Short=ARM-1;
AltName: Full=Proteasome regulatory particle non-ATPase 13;
Short=hRpn13;
AltName: Full=Rpn13 homolog;
Name=ADRM1; Synonyms=GP110;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8033103;
Shimada S., Ogawa M., Takahashi M., Schlom J., Greiner J.W.;
"Molecular cloning and characterization of the complementary DNA of an
M(r) 110,000 antigen expressed by human gastric carcinoma cells and
upregulated by gamma-interferon.";
Cancer Res. 54:3831-3836(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PSMD1 AND
UCHL5, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16990800; DOI=10.1038/sj.emboj.7601338;
Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K.,
Murata S.;
"A novel proteasome-interacting protein recruits the deubiquitinating
enzyme UCH37 to 26S proteasomes.";
EMBO J. 25:4524-4536(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH UCHL5, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17139257; DOI=10.1038/sj.emboj.7601450;
Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.;
"hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the
deubiquitinating enzyme, UCH37.";
EMBO J. 25:5742-5753(2006).
[6]
FUNCTION, INTERACTION WITH 26S PROTEASOME, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16815440; DOI=10.1016/j.jmb.2006.06.011;
Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K.,
Johnsen A.H., Hendil K.B., Hartmann-Petersen R.;
"Adrm1, a putative cell adhesion regulating protein, is a novel
proteasome-associated factor.";
J. Mol. Biol. 360:1043-1052(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16906146; DOI=10.1038/ncb1460;
Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
"Proteasome recruitment and activation of the Uch37 deubiquitinating
enzyme by Adrm1.";
Nat. Cell Biol. 8:994-1002(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[10]
FUNCTION, INTERACTION WITH UBIQUITIN, AND REGION.
PubMed=18497817; DOI=10.1038/nature06926;
Husnjak K., Elsasser S., Zhang N., Chen X., Randles L., Shi Y.,
Hofmann K., Walters K.J., Finley D., Dikic I.;
"Proteasome subunit Rpn13 is a novel ubiquitin receptor.";
Nature 453:481-488(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND THR-217, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND THR-217, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127 AND SER-140, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
STRUCTURE BY NMR OF 1-407, INTERACTION WITH PSMD1, AND REGION.
PubMed=20471946; DOI=10.1016/j.molcel.2010.04.019;
Chen X., Lee B.H., Finley D., Walters K.J.;
"Structure of proteasome ubiquitin receptor hRpn13 and its activation
by the scaffolding protein hRpn2.";
Mol. Cell 38:404-415(2010).
[19]
STRUCTURE BY NMR OF 270-407, INTERACTION WITH UCHL5, AND FUNCTION.
PubMed=24752541; DOI=10.1007/s13238-014-0046-z;
Jiao L., Ouyang S., Shaw N., Song G., Feng Y., Niu F., Qiu W., Zhu H.,
Hung L.W., Zuo X., Eleonora Shtykova V., Zhu P., Dong Y.H., Xu R.,
Liu Z.J.;
"Mechanism of the Rpn13-induced activation of Uch37.";
Protein Cell 5:616-630(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 266-388, INTERACTION WITH
UCHL5, AND FUNCTION.
PubMed=25702870; DOI=10.1016/j.molcel.2014.12.039;
Sahtoe D.D., van Dijk W.J., El Oualid F., Ekkebus R., Ovaa H.,
Sixma T.K.;
"Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in
RPN13 and INO80G.";
Mol. Cell 57:887-900(2015).
[21]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 285-386, INTERACTION WITH
UCHL5, AND FUNCTION.
PubMed=25702872; DOI=10.1016/j.molcel.2015.01.016;
VanderLinden R.T., Hemmis C.W., Schmitt B., Ndoja A., Whitby F.G.,
Robinson H., Cohen R.E., Yao T., Hill C.P.;
"Structural basis for the activation and inhibition of the UCH37
deubiquitylase.";
Mol. Cell 57:901-911(2015).
[22]
STRUCTURE BY NMR OF 1-150, AND INTERACTION WITH UBIQUITIN AND UBQLN2.
PubMed=27396824; DOI=10.1016/j.str.2016.05.018;
Chen X., Randles L., Shi K., Tarasov S.G., Aihara H., Walters K.J.;
"Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding
mechanisms between substrate receptors and shuttle factors of the
proteasome.";
Structure 24:1257-1270(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair. Within the complex,
functions as a proteasomal ubiquitin receptor. Engages and
activates 19S-associated deubiquitinases UCHL5 and PSMD14 during
protein degradation. UCHL5 reversibly associate with the 19S
regulatory particle whereas PSMD14 is an intrinsic subunit of the
proteasome lid subcomplex. {ECO:0000269|PubMed:16815440,
ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800,
ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817,
ECO:0000269|PubMed:24752541, ECO:0000269|PubMed:25702870,
ECO:0000269|PubMed:25702872}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP) (PubMed:16990800). Interacts
with the proteasomal scaffolding protein PSMD1
(PubMed:16990800,PubMed:16815440, PubMed:16906146,
PubMed:20471946). Interacts with deubiquitinase UCHL5; this
interaction activates the auto-inhibited UCHL5 by deoligomerizing
it (PubMed:17139257, PubMed:24752541, PubMed:25702870,
PubMed:25702872). Interacts with UBQLN2 and ubiquitin
(PubMed:27396824). {ECO:0000269|PubMed:16815440,
ECO:0000269|PubMed:16906146, ECO:0000269|PubMed:16990800,
ECO:0000269|PubMed:17139257, ECO:0000269|PubMed:18497817,
ECO:0000269|PubMed:20471946, ECO:0000269|PubMed:24752541,
ECO:0000269|PubMed:25702872, ECO:0000269|PubMed:27396824}.
-!- INTERACTION:
P48510:DSK2 (xeno); NbExp=4; IntAct=EBI-954387, EBI-6174;
O35593:Psmd14 (xeno); NbExp=2; IntAct=EBI-954387, EBI-772796;
P55036:PSMD4; NbExp=4; IntAct=EBI-954387, EBI-359318;
P54727:RAD23B; NbExp=2; IntAct=EBI-954387, EBI-954531;
P0CG48:UBC; NbExp=10; IntAct=EBI-954387, EBI-3390054;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-954387, EBI-741480;
Q9UHD9:UBQLN2; NbExp=5; IntAct=EBI-954387, EBI-947187;
Q9Y5K5:UCHL5; NbExp=20; IntAct=EBI-954387, EBI-1051183;
Q9Y5K5-3:UCHL5; NbExp=5; IntAct=EBI-954387, EBI-11749875;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16990800}.
Nucleus {ECO:0000269|PubMed:16990800}.
-!- DOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain
mediates interactions with PSMD1 and ubiquitin. Preferential
binding to the proximal subunit of K48-linked diubiquitin allows
UCHL5 access to the distal subunit. {ECO:0000269|PubMed:18497817}.
-!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
-!- CAUTION: Although initially described as a cell membrane
glycoprotein, ADRM1 is intracellular and non-glycosylated, and has
probably no direct role in cell adhesion. {ECO:0000305}.
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EMBL; D64154; BAA11023.1; -; mRNA.
EMBL; AL354836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BR000321; FAA00246.1; -; mRNA.
EMBL; BC010733; AAH10733.1; -; mRNA.
EMBL; BC017245; AAH17245.1; -; mRNA.
CCDS; CCDS13496.1; -.
PIR; I52703; I52703.
RefSeq; NP_001268366.1; NM_001281437.1.
RefSeq; NP_001268367.1; NM_001281438.1.
RefSeq; NP_008933.2; NM_007002.3.
RefSeq; NP_783163.1; NM_175573.2.
RefSeq; XP_005260314.1; XM_005260257.1.
UniGene; Hs.90107; -.
PDB; 2KQZ; NMR; -; A=253-407.
PDB; 2KR0; NMR; -; A=1-407.
PDB; 2L5V; NMR; -; A=260-407.
PDB; 2MKZ; NMR; -; A=270-407.
PDB; 2NBK; NMR; -; A=20-130.
PDB; 2NBV; NMR; -; A=1-150.
PDB; 4UEL; X-ray; 2.30 A; C=266-388.
PDB; 4UEM; X-ray; 2.82 A; B=266-388.
PDB; 4WLQ; X-ray; 2.85 A; B=286-384.
PDB; 4WLR; X-ray; 2.00 A; B=285-386.
PDB; 5IRS; X-ray; 1.80 A; A=2-150.
PDB; 5V1Y; X-ray; 1.42 A; A/B=19-132.
PDB; 5V1Z; X-ray; 2.00 A; A/B=19-132.
PDBsum; 2KQZ; -.
PDBsum; 2KR0; -.
PDBsum; 2L5V; -.
PDBsum; 2MKZ; -.
PDBsum; 2NBK; -.
PDBsum; 2NBV; -.
PDBsum; 4UEL; -.
PDBsum; 4UEM; -.
PDBsum; 4WLQ; -.
PDBsum; 4WLR; -.
PDBsum; 5IRS; -.
PDBsum; 5V1Y; -.
PDBsum; 5V1Z; -.
DisProt; DP00839; -.
ProteinModelPortal; Q16186; -.
SMR; Q16186; -.
BioGrid; 116235; 77.
DIP; DIP-42668N; -.
IntAct; Q16186; 58.
MINT; MINT-2869171; -.
STRING; 9606.ENSP00000253003; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; Q16186; -.
PhosphoSitePlus; Q16186; -.
DMDM; 20141265; -.
EPD; Q16186; -.
MaxQB; Q16186; -.
PaxDb; Q16186; -.
PeptideAtlas; Q16186; -.
PRIDE; Q16186; -.
DNASU; 11047; -.
Ensembl; ENST00000253003; ENSP00000253003; ENSG00000130706.
Ensembl; ENST00000491935; ENSP00000478877; ENSG00000130706.
GeneID; 11047; -.
KEGG; hsa:11047; -.
UCSC; uc002ycn.5; human.
CTD; 11047; -.
DisGeNET; 11047; -.
EuPathDB; HostDB:ENSG00000130706.12; -.
GeneCards; ADRM1; -.
HGNC; HGNC:15759; ADRM1.
HPA; HPA042266; -.
MIM; 610650; gene.
neXtProt; NX_Q16186; -.
OpenTargets; ENSG00000130706; -.
PharmGKB; PA24599; -.
eggNOG; KOG3037; Eukaryota.
eggNOG; ENOG410XSJJ; LUCA.
GeneTree; ENSGT00390000013839; -.
HOGENOM; HOG000005947; -.
HOVERGEN; HBG073518; -.
InParanoid; Q16186; -.
KO; K06691; -.
OMA; GKMVHPD; -.
OrthoDB; EOG091G0FEO; -.
PhylomeDB; Q16186; -.
TreeFam; TF313410; -.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; ADRM1; human.
EvolutionaryTrace; Q16186; -.
GeneWiki; ADRM1; -.
GenomeRNAi; 11047; -.
PRO; PR:Q16186; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000130706; -.
CleanEx; HS_ADRM1; -.
ExpressionAtlas; Q16186; baseline and differential.
Genevisible; Q16186; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
GO; GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
GO; GO:0043248; P:proteasome assembly; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
InterPro; IPR006773; 26S_Psome_Ubiquitin-recp_Rpn13.
InterPro; IPR032368; RPN13_C.
PANTHER; PTHR12225; PTHR12225; 1.
Pfam; PF04683; Proteasom_Rpn13; 1.
Pfam; PF16550; RPN13_C; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Isopeptide bond; Nucleus; Phosphoprotein; Proteasome;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 407 Proteasomal ubiquitin receptor ADRM1.
/FTId=PRO_0000020631.
REGION 22 130 Pru (pleckstrin-like receptor for
ubiquitin) domain.
{ECO:0000269|PubMed:18497817}.
REGION 253 407 Interaction with UCHL5.
{ECO:0000269|PubMed:20471946}.
COMPBIAS 135 202 Gly-rich.
COMPBIAS 193 257 Ser-rich.
COMPBIAS 203 213 Poly-Ser.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 127 127 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 217 217 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JMB5}.
CROSSLNK 34 34 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CONFLICT 142 142 S -> T (in Ref. 1; BAA11023).
{ECO:0000305}.
STRAND 23 34 {ECO:0000244|PDB:5IRS}.
STRAND 37 40 {ECO:0000244|PDB:5IRS}.
STRAND 45 51 {ECO:0000244|PDB:5IRS}.
STRAND 57 63 {ECO:0000244|PDB:5IRS}.
TURN 64 66 {ECO:0000244|PDB:5IRS}.
STRAND 69 74 {ECO:0000244|PDB:5IRS}.
STRAND 79 84 {ECO:0000244|PDB:5IRS}.
STRAND 89 91 {ECO:0000244|PDB:2KR0}.
STRAND 93 102 {ECO:0000244|PDB:5IRS}.
STRAND 104 109 {ECO:0000244|PDB:5IRS}.
STRAND 112 114 {ECO:0000244|PDB:5IRS}.
HELIX 117 129 {ECO:0000244|PDB:5IRS}.
TURN 191 195 {ECO:0000244|PDB:2KR0}.
STRAND 202 204 {ECO:0000244|PDB:2KR0}.
STRAND 249 253 {ECO:0000244|PDB:2KR0}.
TURN 254 256 {ECO:0000244|PDB:2KR0}.
HELIX 266 273 {ECO:0000244|PDB:2KQZ}.
STRAND 276 278 {ECO:0000244|PDB:2KR0}.
STRAND 282 284 {ECO:0000244|PDB:2KQZ}.
HELIX 288 291 {ECO:0000244|PDB:4WLR}.
HELIX 294 297 {ECO:0000244|PDB:4WLR}.
HELIX 300 302 {ECO:0000244|PDB:4WLR}.
HELIX 304 310 {ECO:0000244|PDB:4WLR}.
HELIX 311 313 {ECO:0000244|PDB:4WLR}.
HELIX 324 326 {ECO:0000244|PDB:4WLR}.
HELIX 327 332 {ECO:0000244|PDB:4WLR}.
HELIX 334 348 {ECO:0000244|PDB:4WLR}.
TURN 349 351 {ECO:0000244|PDB:4UEM}.
HELIX 353 358 {ECO:0000244|PDB:4WLR}.
HELIX 363 371 {ECO:0000244|PDB:4WLR}.
HELIX 374 383 {ECO:0000244|PDB:4WLR}.
STRAND 386 388 {ECO:0000244|PDB:2KR0}.
STRAND 395 397 {ECO:0000244|PDB:2MKZ}.
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


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