ID ADRM1_BOVIN Reviewed; 407 AA.
AC A1L5A6;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 28-JAN-2026, entry version 101.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1;
DE AltName: Full=Rpn13 homolog;
GN Name=ADRM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
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. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. Within the complex, functions as a proteasomal ubiquitin
CC receptor. Engages and activates 19S-associated deubiquitinases UCHL5
CC and PSMD14 during protein degradation. UCHL5 reversibly associate with
CC the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of
CC the proteasome lid subcomplex. {ECO:0000250|UniProtKB:Q16186}.
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). Interacts with the proteasomal scaffolding
CC protein PSMD1. Interacts with deubiquitinase UCHL5; this interaction
CC activates the auto-inhibited UCHL5 by deoligomerizing it. Interacts
CC with UBQLN2 and ubiquitin. {ECO:0000250|UniProtKB:Q16186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16186}. Nucleus
CC {ECO:0000250|UniProtKB:Q16186}.
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:0000250|UniProtKB:Q16186}.
CC -!- PTM: Ubiquitinated by UBE3C in response to proteotoxic stress.
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR EMBL; BT029893; ABM21559.1; -; mRNA.
DR RefSeq; NP_001073751.1; NM_001080282.1.
DR RefSeq; XP_059748591.1; XM_059892608.1.
DR AlphaFoldDB; A1L5A6; -.
DR SMR; A1L5A6; -.
DR FunCoup; A1L5A6; 3359.
DR STRING; 9913.ENSBTAP00000003974; -.
DR GlyGen; A1L5A6; 2 sites.
DR PaxDb; 9913-ENSBTAP00000003974; -.
DR PeptideAtlas; A1L5A6; -.
DR Ensembl; ENSBTAT00000003974.6; ENSBTAP00000003974.4; ENSBTAG00000003058.7.
DR Ensembl; ENSBTAT00085018864; ENSBTAP00085022438; ENSBTAG00085010564.
DR Ensembl; ENSBTAT00090068220; ENSBTAP00090037394; ENSBTAG00090032232.
DR GeneID; 519729; -.
DR KEGG; bta:519729; -.
DR CTD; 11047; -.
DR VEuPathDB; HostDB:ENSBTAG00000003058; -.
DR VGNC; VGNC:25699; ADRM1.
DR eggNOG; KOG3037; Eukaryota.
DR GeneTree; ENSGT00390000013839; -.
DR HOGENOM; CLU_041798_2_0_1; -.
DR InParanoid; A1L5A6; -.
DR OMA; SNQRHFF; -.
DR OrthoDB; 340431at2759; -.
DR Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-BTA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-BTA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-BTA-202424; Downstream TCR signaling.
DR Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR Reactome; R-BTA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-BTA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-BTA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-BTA-382556; ABC-family proteins mediated transport.
DR Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-BTA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-BTA-4641257; Degradation of AXIN.
DR Reactome; R-BTA-4641258; Degradation of DVL.
DR Reactome; R-BTA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-BTA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-BTA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-BTA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-BTA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-BTA-5632684; Hedgehog 'on' state.
DR Reactome; R-BTA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-BTA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-BTA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-BTA-5689603; UCH proteinases.
DR Reactome; R-BTA-5689880; Ub-specific processing proteases.
DR Reactome; R-BTA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-BTA-68949; Orc1 removal from chromatin.
DR Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-BTA-69481; G2/M Checkpoints.
DR Reactome; R-BTA-69601; Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-BTA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-BTA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-BTA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-BTA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-BTA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-BTA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-BTA-8951664; Neddylation.
DR Reactome; R-BTA-9020702; Interleukin-1 signaling.
DR Reactome; R-BTA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-BTA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-BTA-9766229; Degradation of CDH1.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Reactome; R-BTA-9907900; Proteasome assembly.
DR Reactome; R-BTA-9932298; Degradation of CRY and PER proteins.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000003058; Expressed in spermatid and 105 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; ISS:UniProtKB.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR GO; GO:0061133; F:endopeptidase activator activity; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR CDD; cd13314; PH_Rpn13; 1.
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 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT CHAIN 2..407
FT /note="Proteasomal ubiquitin receptor ADRM1"
FT /id="PRO_0000286070"
FT DOMAIN 18..131
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 277..391
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 2..132
FT /note="Interaction with PSMD1"
FT /evidence="ECO:0000250"
FT REGION 196..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..407
FT /note="Interaction with UCHL5"
FT /evidence="ECO:0000250"
FT REGION 378..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16186"
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 /evidence="ECO:0000250|UniProtKB:Q16186"
SQ SEQUENCE 407 AA; 41955 MW; 622F17326AD66E64 CRC64;
MTTSGALFPS LVPGSRGSSN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ QTDDSLIHFC
WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA GSKRLFFWMQ EPKTDQDEEH
CRKVNEYLNN PPMPGALGAS GSGGHELSAL GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL
GGLGALTGPG LASLLGSGGP PASSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT
SPSPAPSSGD GASTAASPAQ PIQLSDLQSI LATMSVPAGP GGGQQVDLAS VLTPEIMAPI
LANADVQERL LPYLPSGESL PQTAEEIQNT LTSPQFQQAL GMFSAALASG QLGPLMCQFG
LPAEAVEAAN KGDVEAFAKA MQNSASPEQQ EGDGKDKKDE EEDMSLD
//
