FUB1_SCHPO
ID FUB1_SCHPO Reviewed; 265 AA.
AC Q9UTI1; Q9P773;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Silencing boundary-establishment protein FUB1-like protein {ECO:0000250|UniProtKB:P25659, ECO:0000305};
DE AltName: Full=Proteasome inhibitor PI31-like protein SPAC15E1.10 {ECO:0000250|UniProtKB:Q92530, ECO:0000305};
GN ORFNames=SPAC15E1.10 {ECO:0000312|PomBase:SPAC15E1.10}, SPAP7G5.01;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: May play a role in the establishment of transcriptional
CC silencing boundaries, preventing the propagation of heterochromatic
CC silencing. {ECO:0000250|UniProtKB:P25659}.
CC -!- SUBUNIT: Interacts with the 20S proteasome.
CC {ECO:0000250|UniProtKB:P25659}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB52429.1; -; Genomic_DNA.
DR PIR; T37725; T37725.
DR RefSeq; NP_594311.2; NM_001019734.2.
DR AlphaFoldDB; Q9UTI1; -.
DR BioGRID; 279214; 20.
DR STRING; 4896.SPAC15E1.10.1; -.
DR iPTMnet; Q9UTI1; -.
DR MaxQB; Q9UTI1; -.
DR PaxDb; Q9UTI1; -.
DR PRIDE; Q9UTI1; -.
DR EnsemblFungi; SPAC15E1.10.1; SPAC15E1.10.1:pep; SPAC15E1.10.
DR GeneID; 2542764; -.
DR KEGG; spo:SPAC15E1.10; -.
DR PomBase; SPAC15E1.10; -.
DR VEuPathDB; FungiDB:SPAC15E1.10; -.
DR eggNOG; ENOG502RZMJ; Eukaryota.
DR HOGENOM; CLU_1027307_0_0_1; -.
DR InParanoid; Q9UTI1; -.
DR OMA; HPIFHPE; -.
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-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:Q9UTI1; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; ISS:PomBase.
DR GO; GO:0070628; F:proteasome binding; ISS:PomBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR045128; PI31-like.
DR InterPro; IPR013886; PI31_Prot_C.
DR PANTHER; PTHR13266; PTHR13266; 1.
DR Pfam; PF08577; PI31_Prot_C; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..265
FT /note="Silencing boundary-establishment protein FUB1-like
FT protein"
FT /id="PRO_0000116837"
FT REGION 194..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 265 AA; 29593 MW; FF832B4964339BD0 CRC64;
MNNPTSDDRL RFQQKCHKSM LNTGAIFKNC KLRNGDVLQE VTESLTEDSE FNYIVNESQN
VSTRLIFWNK WIYILCANTS SNITATRIFR LDDDQPWNLE SLVAEVCPVD TDNRLAEHAA
RTAKDTSANE LNYESYQEKS RAPFGFAGPF GAMPGSQPMF PSIGASDLYP AGIGGSDMGN
DGGMIPTFNH PIFHPENRSR NEQASANRTN IPPGARYDPT GPGDFRGFGR DERKPQFPFK
GPRSQFPGEP DNDDFMPPGS SDMFM
