RPN51_SCHPO
ID RPN51_SCHPO Reviewed; 443 AA.
AC P0CU17; O14381; Q9UTM3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=26S proteasome regulatory subunit rpn501;
GN Name=rpn501; Synonyms=rpn5, rpn5a; ORFNames=SPAC1420.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-58.
RC STRAIN=972 / ATCC 24843;
RA Jang Y.-J., Yoo H.-S.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SP870;
RX PubMed=12783882; DOI=10.1074/jbc.m302093200;
RA Yen H.-C.S., Espiritu C., Chang E.C.;
RT "Rpn5 is a conserved proteasome subunit and required for proper proteasome
RT localization and assembly.";
RL J. Biol. Chem. 278:30669-30676(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC Required for proper proteasome assembly. {ECO:0000269|PubMed:12783882}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12783882}.
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63869.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB57322.1; -; Genomic_DNA.
DR EMBL; U97377; AAB63869.1; ALT_INIT; mRNA.
DR PIR; T37666; T37666.
DR RefSeq; NP_593278.1; NM_001018674.2.
DR RefSeq; NP_594776.1; NM_001020204.2.
DR AlphaFoldDB; P0CU17; -.
DR SMR; P0CU17; -.
DR STRING; 4896.SPAC1420.03.1; -.
DR iPTMnet; P0CU17; -.
DR EnsemblFungi; SPAC1420.03.1; SPAC1420.03.1:pep; SPAC1420.03.
DR EnsemblFungi; SPAPB8E5.02c.1; SPAPB8E5.02c.1:pep; SPAPB8E5.02c.
DR GeneID; 2542907; -.
DR GeneID; 2543347; -.
DR KEGG; spo:SPAC1420.03; -.
DR KEGG; spo:SPAPB8E5.02c; -.
DR PomBase; SPAC1420.03; rpn501.
DR VEuPathDB; FungiDB:SPAC1420.03; -.
DR VEuPathDB; FungiDB:SPAPB8E5.02c; -.
DR eggNOG; KOG1498; Eukaryota.
DR OMA; AENEMFK; -.
DR PhylomeDB; P0CU17; -.
DR Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P0CU17; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0031595; C:nuclear proteasome complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR GO; GO:0006508; P:proteolysis; NAS:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR035297; PSMD12.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR040896; RPN5_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855; PTHR10855; 1.
DR PANTHER; PTHR10855:SF1; PTHR10855:SF1; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18098; RPN5_C; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..443
FT /note="26S proteasome regulatory subunit rpn501"
FT /id="PRO_0000173864"
FT DOMAIN 230..402
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 57..58
FT /note="YI -> SC (in Ref. 2; AAB63869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51618 MW; 84FF37D3162AF0F4 CRC64;
MEQKPEVDYS EKFAELQKSL NNLNTIDIDA NLEKLLIFEK QVRQASDTST NTKVLIYIAD
LLFRAGDFQG LNEQLVSLFK KHGQLKQSMT SLVQHVMTYL PGIDDLKTKI NLIETLRTIT
DGKIYVEVER ARLTQLLSQI KEEQGDIKSA QEILCNEPVE TYGSFDLKEK VAFILDQVRL
FLLRSDYYMA STYTKKINVK FFEKEDVQSL KLKYYEQKIR IGLHDDAYLD VCKYYRAVYD
TAVVQEDPEK WKEILENVVC FALLTPYDNE QADLLHRINA DHKLNSLPLL QQLVKCFIVN
ELMRWPKIAE IYGSALRSNP VFAENDEKGE KRWSELRKRV IEHNIRVVAN YYSRIHCSRL
GVLLDMSPSE TEQFLCDLIA KHHFYAKIDR PAQVISFKKS QNVQEQLNEW GSNITELLGK
LEKVRQLIIK EEMMNSIQQA VAK
