ID   Q59EG8_HUMAN            Unreviewed;       913 AA.
AC   Q59EG8;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   22-FEB-2023, entry version 88.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 2 {ECO:0000256|ARBA:ARBA00014928};
DE   Flags: Fragment;
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 {ECO:0000313|EMBL:BAD93080.1};
RN   [1] {ECO:0000313|EMBL:BAD93080.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Aorta endothelial cell {ECO:0000313|EMBL:BAD93080.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to the intracellular domain of tumor necrosis factor
CC       type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside
CC       the death domain of TNFR1. {ECO:0000256|ARBA:ARBA00004031}.
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. {ECO:0000256|ARBA:ARBA00002362}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S2 family.
CC       {ECO:0000256|ARBA:ARBA00005460}.
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DR   EMBL; AB209843; BAD93080.1; -; mRNA.
DR   AlphaFoldDB; Q59EG8; -.
DR   IntAct; Q59EG8; 1.
DR   MINT; Q59EG8; -.
DR   PeptideAtlas; Q59EG8; -.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR016643; 26S_Psome_Rpn1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR041433; RPN1_C.
DR   InterPro; IPR040892; RPN1_N.
DR   PANTHER; PTHR10943; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10943:SF1; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 2; 1.
DR   Pfam; PF01851; PC_rep; 2.
DR   Pfam; PF18051; RPN1_C; 1.
DR   Pfam; PF17781; RPN1_RPN2_N; 1.
DR   PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   2: Evidence at transcript level;
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:BAD93080.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          61..359
FT                   /note="RPN1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17781"
FT   DOMAIN          858..911
FT                   /note="26S proteasome non-ATPase regulatory subunit RPN1 C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18051"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD93080.1"
SQ   SEQUENCE   913 AA;  100588 MW;  C450F8B4395A5938 CRC64;
     AVAAEMEEGG RDKAPVQPQQ SPAAAPGGTD EKPSGKERRD AGDKDKEQEL SEEDKQLQDE
     LEMLVERLGE KDTSLYRPAL EELRRQIRSS TTSMTSVPKP LKFLRPHYGK LKEIYENMAP
     GENKRFAADI ISVLAMTMSG ERECLKYRLV GSQEELASWG HEYVRHLAGE VAKEWQELDD
     AEKVQREPLL TLVKEIVPYN MAHNAEHEAC DLLMEIEQVD MLEKDIDENA YAKVCLYLTS
     CVNYVPEPEN SALLCCALGV FRKFSRFPEA LRLALMLNDM ELVEDIFTSC KDVVVQKQMA
     FMLGRHGVFL ELSEDVEEYE DLTEIMSNVQ LNSNFLALAR ELDIMEPKVP DDIYKTHLEN
     NRFGGSGSQV DSARMNLASS FVNGFVNAAF GQDKLLTDDG NKWLYKNKDH GMLSAAASLG
     MILLWDVDGG LTQIDKYLYS SEDYIKSGAL LACGIVNSGV RNECDPALAL LSDYVLHNSN
     TMRLGSIFGL GLAYAGSNRE DVLTLLLPVM GDSKSSMEVA GVTALACGMI AVGSCNGDVT
     STILQTIMEK SETELKDTYA RWLPLGLGLN HLGKGEAIEA ILAALEVVSE PFRSFANTLV
     DVCAYAGSGN VLKVQQLLHI CSEHFDSKEK EEDKDKKEKK DKDKKEAPAD MGAHQGVAVL
     GIALIAMGEE IGAEMALRTF GHLLRYGEPT LRRAVPLALA LISVSNPRLN ILDTLSKFSH
     DADPEVSYNS IFAMGMVGSG TNNARLAAML RQLAQYHAKD PNNLFMVRLA QGLTHLGKGT
     LTLCPYHSDR QLMSQVAVAG LLTVLVSFLD VRNIILGKSH YVLYGLVAAM QPRMLVTFDE
     ELRPLPVSVR VGQAVDVVGQ AGKPKTITGF QTHTTPVLLA HGERAELATE EFLPVTPILE
     GFVILRKNPN YDL
//