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26S proteasome regulatory subunit rpn1 (19S regulatory cap region of 26S protease subunit 2) (Proteasome non-ATPase subunit mts4)

 RPN1_SCHPO              Reviewed;         891 AA.
P87048; Q9HDV7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-AUG-2001, sequence version 2.
10-OCT-2018, entry version 146.
RecName: Full=26S proteasome regulatory subunit rpn1;
AltName: Full=19S regulatory cap region of 26S protease subunit 2;
AltName: Full=Proteasome non-ATPase subunit mts4;
Name=rpn1; Synonyms=mts4; ORFNames=SPBP19A11.03c;
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=9325304; DOI=10.1074/jbc.272.41.25768;
Wilkinson C.R., Wallace M., Seeger M., Dubiel W., Gordon C.B.;
"Mts4, a non-ATPase subunit of the 26 S protease in fission yeast is
essential for mitosis and interacts directly with the ATPase subunit
Mts2.";
J. Biol. Chem. 272:25768-25777(1997).
[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).
[3]
INTERACTION WITH UBP6.
PubMed=15533439; DOI=10.1016/j.jmb.2004.09.057;
Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D.,
Wallace M., Gordon C.;
"Uch2/Uch37 is the major deubiquitinating enzyme associated with the
26S proteasome in fission yeast.";
J. Mol. Biol. 344:697-706(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
is involved in the ATP-dependent degradation of ubiquitinated
proteins.
-!- SUBUNIT: Component of the 26S proteasome. Interacts with ubp6.
{ECO:0000269|PubMed:15533439}.
-!- INTERACTION:
P38937:cut8; NbExp=4; IntAct=EBI-1152810, EBI-1152591;
-!- SIMILARITY: Belongs to the proteasome subunit S2 family.
{ECO:0000305}.
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EMBL; Y09819; CAA70948.1; -; mRNA.
EMBL; CU329671; CAC19753.1; -; Genomic_DNA.
PIR; T52488; T52488.
RefSeq; NP_596171.1; NM_001022091.2.
ProteinModelPortal; P87048; -.
BioGrid; 277782; 25.
IntAct; P87048; 3.
STRING; 4896.SPBP19A11.03c.1; -.
iPTMnet; P87048; -.
MaxQB; P87048; -.
PaxDb; P87048; -.
PRIDE; P87048; -.
EnsemblFungi; SPBP19A11.03c.1; SPBP19A11.03c.1:pep; SPBP19A11.03c.
GeneID; 2541268; -.
KEGG; spo:SPBP19A11.03c; -.
EuPathDB; FungiDB:SPBP19A11.03c; -.
PomBase; SPBP19A11.03c; -.
HOGENOM; HOG000176022; -.
InParanoid; P87048; -.
KO; K03028; -.
OMA; MVDICAY; -.
OrthoDB; EOG092C0RGR; -.
PhylomeDB; P87048; -.
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-382556; ABC-family proteins mediated transport.
Reactome; R-SPO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-SPO-5689603; UCH proteinases.
Reactome; R-SPO-5689880; Ub-specific processing proteases.
Reactome; R-SPO-6798695; Neutrophil degranulation.
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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:P87048; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0005838; C:proteasome regulatory particle; IDA:PomBase.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:PomBase.
GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IC:PomBase.
GO; GO:0010498; P:proteasomal protein catabolic process; EXP:PomBase.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IPI:PomBase.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR016643; 26S_Psome_Rpn1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002015; Proteasome/cyclosome_rpt.
PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
Pfam; PF01851; PC_rep; 2.
PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
Complete proteome; Phosphoprotein; Proteasome; Reference proteome;
Repeat.
CHAIN 1 891 26S proteasome regulatory subunit rpn1.
/FTId=PRO_0000173814.
REPEAT 408 441 PC 1.
REPEAT 442 478 PC 2.
REPEAT 479 513 PC 3.
REPEAT 517 550 PC 4.
REPEAT 673 704 PC 5.
REPEAT 705 739 PC 6.
MOD_RES 10 10 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
CONFLICT 72 72 V -> E (in Ref. 1; CAA70948).
{ECO:0000305}.
CONFLICT 870 891 PLTSLEGIVILKKNTEDIEMTA -> TFDFVGRYCYFKKKY
GGH (in Ref. 1; CAA70948). {ECO:0000305}.
SEQUENCE 891 AA; 97999 MW; 03FC9AB767745C5A CRC64;
MSSKDISSKS PSGNDALNDK KGTKTSETND RNSTNNTKER DELEDLSEED LQLKNDLELL
VQAVQDATPE LVGSSLTQLK EIIRTSTSSM TAVPKPLKFL RPHYFTLVKI YDSWPQSPQK
TQLADILSVL GMSYSNTSKH ESLKYRLQGV TTDPSLWGHE YVRHLASEIE EEFASRQEEE
APTDDLMELA LTIVPFFLTH NAEADAIDLL QELGAIEKVV PFVELDNASR VCLYITSCVN
LLPFPEDVAM LRTAHAIYRK FDQLTQALNV AIRLDDMSLI KEDCEAATDP LLKKQMSYML
ARQQIPMDMG DEELNDALNN THLSDHFHYL GKELNLMDPK VPEDIFKTHL EVARTGLGAS
GVYSAKQNLA NTFVNALVNA GYSNDRLILV DDEKTSWIYK NKESGLISAT ASIGLLQLWN
VDMGLSLLDK YLYSSEENTK AGALLGIGVT NVAVRNEADP AMAILSEYLE TGSVKLRASA
ILGLGLAYSG ANREDLLDML SPIVTDTDCP MQLSCLAALS LGLIFVGTCN GDVASTILQT
LMEREESAQN DQWGRFMALG LALLFNGKQD LADATVETLK AIEGKIARQA EILVDICSYA
GTGNVLHIQK LLHICSEPPS DDAKESETTI QTFAALGVAT IAMGEDIGAE MVLRHFDHMM
HYGEPSIRKA IPLALGLLSA SNPQMRIFDT LSRYSHDNDL DVAYNAIFAM GLVGAGTSNA
RLAQLLRQLA SYYHKESNAL FMVRIAQGLL YLGKGTMTLN PYHTERQILG QTAFAGLMTV
VLAMLDANTF VLDTSHWLLY AITLAIRPRM LITLGEDGQY LPVSVRVGQA VDVVGQAGRP
KVITGWVTHT TPVLLHHNER AELATEAYTP LTSLEGIVIL KKNTEDIEMT A


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