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26S proteasome regulatory subunit rpn12

 RPN12_SCHPO             Reviewed;         270 AA.
P50524; Q9UUC3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
28-MAR-2018, entry version 122.
RecName: Full=26S proteasome regulatory subunit rpn12;
Name=rpn12; Synonyms=mts3; ORFNames=SPBC16G5.01, SPBC342.07;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8621436; DOI=10.1074/jbc.271.10.5704;
Gordon C.B., McGurk G., Wallace M., Hastie N.D.;
"A conditional lethal mutant in the fission yeast 26 S protease
subunit mts3+ is defective in metaphase to anaphase transition.";
J. Biol. Chem. 271:5704-5711(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which
is involved in the ATP-dependent degradation of ubiquitinated
proteins.
-!- INTERACTION:
P38937:cut8; NbExp=2; IntAct=EBI-1152607, EBI-1152591;
-!- SIMILARITY: Belongs to the proteasome subunit S14 family.
{ECO:0000305}.
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EMBL; X92682; CAA63366.1; -; mRNA.
EMBL; CU329671; CAB46777.1; -; Genomic_DNA.
PIR; T40280; T40280.
RefSeq; NP_596750.2; NM_001023770.2.
PDB; 4B0Z; X-ray; 1.58 A; A/B=1-224.
PDBsum; 4B0Z; -.
ProteinModelPortal; P50524; -.
SMR; P50524; -.
BioGrid; 276569; 19.
IntAct; P50524; 2.
STRING; 4896.SPBC16G5.01.1; -.
iPTMnet; P50524; -.
MaxQB; P50524; -.
PaxDb; P50524; -.
PRIDE; P50524; -.
EnsemblFungi; SPBC16G5.01.1; SPBC16G5.01.1:pep; SPBC16G5.01.
GeneID; 2540025; -.
KEGG; spo:SPBC16G5.01; -.
EuPathDB; FungiDB:SPBC16G5.01; -.
PomBase; SPBC16G5.01; rpn12.
HOGENOM; HOG000196008; -.
InParanoid; P50524; -.
KO; K03031; -.
OMA; LEIGAFW; -.
OrthoDB; EOG092C40NW; -.
PhylomeDB; P50524; -.
Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-SPO-5689603; UCH proteinases.
Reactome; R-SPO-5689880; Ub-specific processing proteases.
Reactome; R-SPO-68949; Orc1 removal from chromatin.
Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:P50524; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IC:PomBase.
GO; GO:0043248; P:proteasome assembly; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
GO; GO:0035103; P:sterol regulatory element binding protein cleavage; EXP:PomBase.
InterPro; IPR006746; 26S_Psome_Rpn12.
InterPro; IPR033464; CSN8_PSD8_EIF3K.
PANTHER; PTHR12387; PTHR12387; 1.
Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
PROSITE; PS50250; PCI; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Proteasome; Reference proteome.
CHAIN 1 270 26S proteasome regulatory subunit rpn12.
/FTId=PRO_0000173850.
DOMAIN 65 237 PCI. {ECO:0000255|PROSITE-
ProRule:PRU01185}.
HELIX 7 14 {ECO:0000244|PDB:4B0Z}.
HELIX 18 34 {ECO:0000244|PDB:4B0Z}.
HELIX 44 63 {ECO:0000244|PDB:4B0Z}.
HELIX 67 81 {ECO:0000244|PDB:4B0Z}.
HELIX 91 104 {ECO:0000244|PDB:4B0Z}.
HELIX 108 117 {ECO:0000244|PDB:4B0Z}.
HELIX 123 126 {ECO:0000244|PDB:4B0Z}.
HELIX 128 141 {ECO:0000244|PDB:4B0Z}.
HELIX 145 153 {ECO:0000244|PDB:4B0Z}.
HELIX 158 160 {ECO:0000244|PDB:4B0Z}.
HELIX 161 182 {ECO:0000244|PDB:4B0Z}.
STRAND 184 187 {ECO:0000244|PDB:4B0Z}.
HELIX 188 194 {ECO:0000244|PDB:4B0Z}.
HELIX 200 210 {ECO:0000244|PDB:4B0Z}.
STRAND 213 215 {ECO:0000244|PDB:4B0Z}.
STRAND 218 220 {ECO:0000244|PDB:4B0Z}.
SEQUENCE 270 AA; 30899 MW; C1BC6571722A034D CRC64;
MSTLDLNHLA DLYDRKDWNA CKKELLKLKV ELAKQNLFVP TSDKEKASFA RNVFEYGVLV
SIQTCDIESF ARYASQVIPF YHDSLVPSSR MGLVTGLNLL YLLSENRIAE FHTALESVPD
KSLFERDPYV EWVISLEQNV MEGAFDKVAS MIRSCNFPEF SYFMKIVMSM VRNEIATCAE
KVYSEIPLSN ATSLLYLENT KETEKLAEER GWDIRDGVIY FPKEANALET EDGMLIDEED
ELELPPTASK HTISSIRQLL SYTSELEQIV


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