RPN2_SCHPO
ID RPN2_SCHPO Reviewed; 965 AA.
AC O74762;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=26S proteasome regulatory subunit rpn2;
GN Name=rpn2; ORFNames=SPBC17D11.07c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952, 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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21078.1; -; Genomic_DNA.
DR PIR; T39718; T39718.
DR RefSeq; NP_596381.1; NM_001022302.2.
DR AlphaFoldDB; O74762; -.
DR SMR; O74762; -.
DR BioGRID; 276724; 13.
DR IntAct; O74762; 2.
DR STRING; 4896.SPBC17D11.07c.1; -.
DR iPTMnet; O74762; -.
DR SwissPalm; O74762; -.
DR MaxQB; O74762; -.
DR PaxDb; O74762; -.
DR PRIDE; O74762; -.
DR EnsemblFungi; SPBC17D11.07c.1; SPBC17D11.07c.1:pep; SPBC17D11.07c.
DR GeneID; 2540191; -.
DR KEGG; spo:SPBC17D11.07c; -.
DR PomBase; SPBC17D11.07c; rpn2.
DR VEuPathDB; FungiDB:SPBC17D11.07c; -.
DR eggNOG; KOG2062; Eukaryota.
DR HOGENOM; CLU_002323_0_0_1; -.
DR InParanoid; O74762; -.
DR OMA; MIMVQQN; -.
DR PhylomeDB; O74762; -.
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:O74762; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:PomBase.
DR GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016642; 26S_Psome_Rpn2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR035266; PSMD1.
DR InterPro; IPR040623; RPN2_C.
DR PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR Pfam; PF01851; PC_rep; 3.
DR Pfam; PF18004; RPN2_C; 1.
DR PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..965
FT /note="26S proteasome regulatory subunit rpn2"
FT /id="PRO_0000173807"
FT REPEAT 385..418
FT /note="PC 1"
FT REPEAT 424..457
FT /note="PC 2"
FT REPEAT 459..493
FT /note="PC 3"
FT REPEAT 494..528
FT /note="PC 4"
FT REPEAT 530..563
FT /note="PC 5"
FT REPEAT 564..599
FT /note="PC 6"
FT REPEAT 600..632
FT /note="PC 7"
FT REPEAT 634..668
FT /note="PC 8"
FT REPEAT 669..699
FT /note="PC 9"
FT REPEAT 712..744
FT /note="PC 10"
FT REGION 826..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..965
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 965 AA; 107276 MW; E8D1758722127F31 CRC64;
MTMVYSDNTS IITSAGGLMA LLDEQERELQ VHALLKIYEF IDQLWPEISD DVTKIEVMYE
DHSFPERELA ALVVSKVYYY LGEYDEALLF ALSSGPKFLH DKNSDYKETL IFKCIDMFIH
KSAELYKNPK ADPLDERLSG VVEGIFQKCY AKNEWRHVLG IAIEAHRLDI IEYILNADKE
TDLKPYVLEL AMTVVLDIEF RNRLLRLLLS SFLTETEPDY FSVGKCVVHL NDASVAAKLL
MKLSSQNDDK SLLTAYQLAF DLEDSAPQEF LNSVMDLLPS PSVANSEEDA NADSKKEDSS
PCGYIIRILS GEQTVKYDRE FLYAHNNTDM LILNRTKDSL EARNSVFHNA VTFANAFMNF
GTSSDSFFRD NLSWLSKANN WSKFTATAAL GVIHRGYYNQ AMNILRPYLP EEDAPSSSTY
SEGGAFYAMG LIHANHGRGV TEYLREQLKH TEDEIVQYGL LLGIGLTGMA SRDETLYESV
KTILFNDNAV AGSAAGISMG LIMLGTASSA AIDEMLQYAH ETQHEKIIRG LGIGIALIVY
GRQQEADGII KELNNDLDPT LRYAGMFATA LAYCGTSNSK IVRDVLHISV SDVNDDVRRA
AVCALGFICF KDPNALISTV ELLVDSYNPH VRYGSAIALG IACANSGSNA ALDLLSRLVE
DATDFVRQGA MIAQAMILTQ HNDQLNSKVS GIRKHFEQVI NEKHEDALAK LGATLAQGII
DAGGRNVTIA LQTATGSLKL SAIVGLTVFL QYWYWFPLTH FMSLSFSPTA LIGLDKNLNA
PKFSFISNVR PKLFAYPPKS VQPTAKTVQK VETAVLSTTV KAQARAKRAE REKASKGSND
DEMKIDKKTT EEKEATPMEM DEEKSQDISI NGNSKKEEPK SETLENFTRV VPAQLPYISF
NLNGRYYPVR KFTGGVLMLI DRESDKAPDL IELNRDAVPA SADTEPGEQE ASPPEDFEYP
FDDDD
