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RPN9_SCHPO
ID   RPN9_SCHPO              Reviewed;         381 AA.
AC   Q9US13;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable 26S proteasome regulatory subunit rpn9;
GN   Name=rpn9; ORFNames=SPAC607.05;
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).
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 S11 family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB63792.1; -; Genomic_DNA.
DR   PIR; T50225; T50225.
DR   RefSeq; NP_593594.1; NM_001019025.2.
DR   AlphaFoldDB; Q9US13; -.
DR   SMR; Q9US13; -.
DR   BioGRID; 279546; 12.
DR   STRING; 4896.SPAC607.05.1; -.
DR   MaxQB; Q9US13; -.
DR   PaxDb; Q9US13; -.
DR   EnsemblFungi; SPAC607.05.1; SPAC607.05.1:pep; SPAC607.05.
DR   GeneID; 2543114; -.
DR   KEGG; spo:SPAC607.05; -.
DR   PomBase; SPAC607.05; rpn9.
DR   VEuPathDB; FungiDB:SPAC607.05; -.
DR   eggNOG; KOG2908; Eukaryota.
DR   HOGENOM; CLU_042989_0_0_1; -.
DR   InParanoid; Q9US13; -.
DR   OMA; TWVQPRI; -.
DR   PhylomeDB; Q9US13; -.
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:Q9US13; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035298; PSMD13.
DR   InterPro; IPR040798; Rpn9_C.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10539; PTHR10539; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18261; Rpn9_C; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Probable 26S proteasome regulatory subunit rpn9"
FT                   /id="PRO_0000173869"
FT   DOMAIN          177..343
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
SQ   SEQUENCE   381 AA;  43457 MW;  994D3916EDB6B1B0 CRC64;
     MDTEMSVNMS DFLHDQATRA PESLQQSYIL MEDLYERKLW KQLTDALIVF FDTPETVPLR
     LPLYTNFVNS FRPNINQLKA VYMGLKAFES CSNDEALRNL NQIVNELDEE KYKDAYVYSI
     VAIARIKLIS GKLDEARELL VKASKIIDHI DYVESLIHSS YYSVSADYYK AKADYAQYYR
     HCLLYLSCID LDKCSHTELV ERAVDLSVAA ILGDIYNFGE LLLHPVFELL VGTQHEWLHD
     LVIAMNVGDL PLFERLMGQI NKMPLLQSSV ALLGQKIRLM ALIELVFQLP PNQRTLTFDT
     IARATRIPSN EVELLIMRAL SVGLITGVID EVTQIVTISS VQSRILNHSQ IASMESRLRE
     WNQNIKNLSN VVEISGKGVF V
 
 
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