GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)

 PSMD1_HUMAN             Reviewed;         953 AA.
Q99460; B8ZZH9; Q24JU0; Q53TI2; Q6GMU5; Q6P2P4; Q6PJM7; Q6PKG9; Q86VU1;
Q8IV79;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
31-AUG-2004, sequence version 2.
07-APR-2021, entry version 197.
RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
AltName: Full=26S proteasome regulatory subunit RPN2;
AltName: Full=26S proteasome regulatory subunit S1;
AltName: Full=26S proteasome subunit p112;
Name=PSMD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8816993; DOI=10.1091/mbc.7.6.853;
Yokota K., Kagawa S., Shimizu Y., Akioka H., Tsurumi C., Noda C.,
Fujimuro M., Yokosawa H., Fujiwara T., Takahashi E., Ohba M., Yamasaki M.,
DeMartino G.N., Slaughter C.A., Toh-e A., Tanaka K.;
"cDNA cloning of p112, the largest regulatory subunit of the human 26s
proteasome, and functional analysis of its yeast homologue, sen3p.";
Mol. Biol. Cell 7:853-870(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and
4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cervix, Liver, Lymph, Placenta, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes ATP
and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[5]
INTERACTION WITH ADRM1.
PubMed=16990800; DOI=10.1038/sj.emboj.7601338;
Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.;
"A novel proteasome-interacting protein recruits the deubiquitinating
enzyme UCH37 to 26S proteasomes.";
EMBO J. 25:4524-4536(2006).
[6]
INTERACTION WITH ADRM1.
PubMed=16906146; DOI=10.1038/ncb1460;
Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K.,
Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.;
"Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme
by Adrm1.";
Nat. Cell Biol. 8:994-1002(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-290; THR-311 AND
SER-315, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S
proteasome complex.";
Biochemistry 46:3553-3565(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; THR-311; SER-315;
THR-830 AND SER-834, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
INTERACTION WITH ZFAND1.
PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
Schlosser A., Hofmann K., Buchberger A.;
"ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
arsenite-induced stress granules.";
Mol. Cell 70:906-919(2018).
[19]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[20]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated proteins.
This complex plays a key role in the maintenance of protein homeostasis
by removing misfolded or damaged proteins, which could impair cellular
functions, and by removing proteins whose functions are no longer
required. Therefore, the proteasome participates in numerous cellular
processes, including cell cycle progression, apoptosis, or DNA damage
repair. {ECO:0000269|PubMed:1317798}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
The 26S proteasome consists of a 20S core particle (CP) and two 19S
regulatory subunits (RP). The regulatory particle is made of a lid
composed of 9 subunits, a base containing 6 ATPases and few additional
components including PSMD1 (PubMed:27428775, PubMed:27342858).
Interacts with ADRM1 (PubMed:16990800, PubMed:16906146). Interacts with
ZFAND1 (PubMed:29804830). {ECO:0000269|PubMed:16906146,
ECO:0000269|PubMed:16990800, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:29804830}.
-!- INTERACTION:
Q99460; Q16186: ADRM1; NbExp=5; IntAct=EBI-357874, EBI-954387;
Q99460-1; Q9JKV1: Adrm1; Xeno; NbExp=2; IntAct=EBI-15703973, EBI-8762776;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99460-1; Sequence=Displayed;
Name=2;
IsoId=Q99460-2; Sequence=VSP_011475;
-!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01053.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH14013.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH39845.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH47897.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH64398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH73833.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; D44466; BAA07918.1; -; mRNA.
EMBL; AC009407; AAX93127.1; -; Genomic_DNA.
EMBL; BC001053; AAH01053.1; ALT_SEQ; mRNA.
EMBL; BC014013; AAH14013.1; ALT_SEQ; mRNA.
EMBL; BC039845; AAH39845.1; ALT_SEQ; mRNA.
EMBL; BC047897; AAH47897.1; ALT_SEQ; mRNA.
EMBL; BC064398; AAH64398.1; ALT_SEQ; mRNA.
EMBL; BC073833; AAH73833.1; ALT_SEQ; mRNA.
EMBL; BC094720; AAH94720.1; -; mRNA.
EMBL; BC112344; AAI12345.1; -; mRNA.
EMBL; BC114434; AAI14435.1; -; mRNA.
CCDS; CCDS2482.1; -. [Q99460-1]
CCDS; CCDS54436.1; -. [Q99460-2]
RefSeq; NP_001177966.1; NM_001191037.1. [Q99460-2]
RefSeq; NP_002798.2; NM_002807.3. [Q99460-1]
PDB; 5GJQ; EM; 4.50 A; N=1-953.
PDB; 5GJR; EM; 3.50 A; 1/N=1-953.
PDB; 5L4K; EM; 4.50 A; N=1-953.
PDB; 5LN3; EM; 6.80 A; N=1-953.
PDB; 5M32; EM; 3.80 A; i=1-953.
PDB; 5T0C; EM; 3.80 A; AU/BU=1-953.
PDB; 5T0G; EM; 4.40 A; U=1-953.
PDB; 5T0H; EM; 6.80 A; U=1-953.
PDB; 5T0I; EM; 8.00 A; U=1-953.
PDB; 5T0J; EM; 8.00 A; U=1-953.
PDB; 5V1Y; X-ray; 1.42 A; E/F=940-953.
PDB; 5V1Z; X-ray; 2.00 A; E/F=932-953.
PDB; 5VFP; EM; 4.20 A; U=7-917.
PDB; 5VFQ; EM; 4.20 A; U=7-917.
PDB; 5VFR; EM; 4.90 A; U=7-917.
PDB; 5VFS; EM; 3.60 A; U=7-917.
PDB; 5VFT; EM; 7.00 A; U=7-917.
PDB; 5VFU; EM; 5.80 A; U=7-917.
PDB; 5VGZ; EM; 3.70 A; U=1-935.
PDB; 5VHF; EM; 5.70 A; U=95-935.
PDB; 5VHH; EM; 6.10 A; U=1-935.
PDB; 5VHI; EM; 6.80 A; U=1-935.
PDB; 5VHS; EM; 8.80 A; U=1-935.
PDB; 6CO4; NMR; -; B=940-953.
PDB; 6MSB; EM; 3.00 A; U=1-953.
PDB; 6MSD; EM; 3.20 A; U=1-953.
PDB; 6MSE; EM; 3.30 A; C=142-210.
PDB; 6MSG; EM; 3.50 A; U=1-953.
PDB; 6MSH; EM; 3.60 A; U=1-953.
PDB; 6MSJ; EM; 3.30 A; U=1-953.
PDB; 6MSK; EM; 3.20 A; U=1-953.
PDB; 6OI4; X-ray; 1.76 A; E/F=940-952.
PDB; 6UYI; NMR; -; B=940-953.
PDB; 6UYJ; NMR; -; B=940-953.
PDB; 6WJD; EM; 4.80 A; U=1-953.
PDB; 6WJN; EM; 5.70 A; U=7-917.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5V1Y; -.
PDBsum; 5V1Z; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
PDBsum; 6CO4; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
PDBsum; 6OI4; -.
PDBsum; 6UYI; -.
PDBsum; 6UYJ; -.
PDBsum; 6WJD; -.
PDBsum; 6WJN; -.
SMR; Q99460; -.
BioGRID; 111680; 268.
ComplexPortal; CPX-5993; 26S Proteasome complex.
CORUM; Q99460; -.
DIP; DIP-27548N; -.
IntAct; Q99460; 79.
MINT; Q99460; -.
STRING; 9606.ENSP00000309474; -.
ChEMBL; CHEMBL2364701; -.
DrugCentral; Q99460; -.
iPTMnet; Q99460; -.
MetOSite; Q99460; -.
PhosphoSitePlus; Q99460; -.
SwissPalm; Q99460; -.
BioMuta; PSMD1; -.
DMDM; 51704332; -.
CPTAC; CPTAC-119; -.
CPTAC; CPTAC-120; -.
EPD; Q99460; -.
jPOST; Q99460; -.
MassIVE; Q99460; -.
MaxQB; Q99460; -.
PaxDb; Q99460; -.
PeptideAtlas; Q99460; -.
PRIDE; Q99460; -.
ProteomicsDB; 78278; -. [Q99460-1]
ProteomicsDB; 78279; -. [Q99460-2]
Antibodypedia; 34412; 131 antibodies.
Ensembl; ENST00000308696; ENSP00000309474; ENSG00000173692. [Q99460-1]
Ensembl; ENST00000373635; ENSP00000362738; ENSG00000173692. [Q99460-2]
Ensembl; ENST00000677230; ENSP00000503068; ENSG00000173692. [Q99460-1]
GeneID; 5707; -.
KEGG; hsa:5707; -.
UCSC; uc002vrm.3; human. [Q99460-1]
CTD; 5707; -.
DisGeNET; 5707; -.
GeneCards; PSMD1; -.
HGNC; HGNC:9554; PSMD1.
HPA; ENSG00000173692; Low tissue specificity.
MIM; 617842; gene.
neXtProt; NX_Q99460; -.
OpenTargets; ENSG00000173692; -.
PharmGKB; PA33899; -.
VEuPathDB; HostDB:ENSG00000173692.12; -.
eggNOG; KOG2062; Eukaryota.
GeneTree; ENSGT00940000153386; -.
HOGENOM; CLU_002323_0_0_1; -.
InParanoid; Q99460; -.
OMA; TGNLNMA; -.
OrthoDB; 235012at2759; -.
PhylomeDB; Q99460; -.
TreeFam; TF105742; -.
PathwayCommons; Q99460; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; Q99460; -.
BioGRID-ORCS; 5707; 771 hits in 1000 CRISPR screens.
ChiTaRS; PSMD1; human.
GeneWiki; PSMD1; -.
GenomeRNAi; 5707; -.
Pharos; Q99460; Tbio.
PRO; PR:Q99460; -.
Proteomes; UP000005640; Chromosome 2.
RNAct; Q99460; protein.
Bgee; ENSG00000173692; Expressed in tendon and 251 other tissues.
ExpressionAtlas; Q99460; baseline and differential.
Genevisible; Q99460; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR016642; 26S_Psome_Rpn2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002015; Proteasome/cyclosome_rpt.
InterPro; IPR035266; PSMD1.
InterPro; IPR040623; RPN2_C.
PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
Pfam; PF01851; PC_rep; 3.
Pfam; PF18004; RPN2_C; 1.
PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
Proteasome; Reference proteome; Repeat.
CHAIN 1..953
/note="26S proteasome non-ATPase regulatory subunit 1"
/id="PRO_0000173801"
REPEAT 403..436
/note="PC 1"
REPEAT 441..474
/note="PC 2"
REPEAT 476..510
/note="PC 3"
REPEAT 511..545
/note="PC 4"
REPEAT 547..580
/note="PC 5"
REPEAT 581..616
/note="PC 6"
REPEAT 617..649
/note="PC 7"
REPEAT 651..685
/note="PC 8"
REPEAT 686..726
/note="PC 9"
REPEAT 729..761
/note="PC 10"
COMPBIAS 936..943
/note="Poly-Glu"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:22223895"
MOD_RES 273
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:23186163"
MOD_RES 290
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924"
MOD_RES 310
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:19608861"
MOD_RES 311
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 315
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 720
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:Q3TXS7"
MOD_RES 830
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 834
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
VAR_SEQ 797..827
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_011475"
CONFLICT 85
/note="G -> R (in Ref. 1; BAA07918)"
/evidence="ECO:0000305"
CONFLICT 616
/note="R -> S (in Ref. 1; BAA07918)"
/evidence="ECO:0000305"
SEQUENCE 953 AA; 105836 MW; B8682146082D21FA CRC64;
MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE
GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS
LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE
EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL
QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG
LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ
HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR
RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC
AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK
HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK
KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY
QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD


Related products :

Catalog number Product name Quantity
EIAAB32842 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Homo sapiens,Human,PSMD1
EIAAB32841 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Psmd1,Rat,Rattus norvegicus
15-288-22830 26S proteasome non-ATPase regulatory subunit 1 - 26S proteasome regulatory subunit RPN2; 26S proteasome regulatory subunit S1; 26S proteasome subunit p112 Polyclonal 0.1 mg
15-288-22830 26S proteasome non-ATPase regulatory subunit 1 - 26S proteasome regulatory subunit RPN2; 26S proteasome regulatory subunit S1; 26S proteasome subunit p112 Polyclonal 0.05 mg
EIAAB32808 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Homo sapiens,Human,Mov34 protein homolog,MOV34L,Proteasome subunit p40,PSMD7
EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32798 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Homo sapiens,Human,PSMD13
EIAAB32789 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Homo sapiens,Human,PSMD11
EIAAB32840 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,Mouse,Mus musculus,Psmd1
EIAAB32848 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Homo sapiens,Human,Proteasome subunit p58,PSMD3
EIAAB32791 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Mouse,Mus musculus,Psmd11
EIAAB32797 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Mouse,Mus musculus,Psmd13
EIAAB32796 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Psmd13,Rat,Rattus norvegicus
EIAAB32799 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Bos taurus,Bovine,PSMD13
EIAAB32858 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Breast cancer-associated protein SGA-113M,Homo sapiens,Human,KIAA0107,p42A,P
EIAAB32851 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,AF,Antisecretory factor 1,ASF,Homo sapiens,Human,MCB1,Multiubiquitin chain-
EIAAB32852 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,Mcb1,Mouse,Multiubiquitin chain-binding protein,Mus musculus,Psmd4
EIAAB32844 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Mouse,Mus musculus,Psmd2
EIAAB32807 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Mouse,Mov34,Mov-34,Mov34 protein,Mus musculus,Proteasome subunit p40,Psmd7
EIAAB32843 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,Chicken,Gallus gallus,PSMD1,RCJMB04_3m24
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
EIAAB32859 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Mouse,Mus musculus,p42A,Psmd6
EIAAB32862 26S proteasome non-ATPase regulatory subunit 8,26S proteasome regulatory subunit RPN12,26S proteasome regulatory subunit S14,Homo sapiens,Human,p31,PSMD8
Pathways :
WP1079: Proteasome Degradation
WP281: Proteasome Degradation
WP519: Proteasome Degradation
WP1691: Proteasome
WP960: Proteasome Degradation
WP158: Proteasome Degradation
WP267: Proteasome Degradation
WP470: Proteasome Degradation
WP1196: Proteasome Degradation
WP841: Proteasome Degradation
WP183: Proteasome Degradation
WP302: Proteasome Degradation
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism
WP1614: 1- and 2-Methylnaphthalene degradation
WP2272: Pathogenic Escherichia coli infection
WP1644: DNA replication
WP1671: Methane metabolism
WP1711: Trinitrotoluene degradation
WP1240: Proteasome Degradation
WP1634: Butanoate metabolism
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1694: Pyrimidine metabolism
WP1566: Citrate cycle (TCA cycle)

Related Genes :
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[PSMD2 TRAP2] 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2)
[RPN2B At1g04810 F13M7.20] 26S proteasome non-ATPase regulatory subunit 1 homolog B (26S proteasome regulatory subunit RPN2b) (AtRPN2b) (26S proteasome regulatory subunit S1 homolog B)
[RPN1A At2g20580 F23N11.10] 26S proteasome non-ATPase regulatory subunit 2 homolog A (26S proteasome regulatory subunit RPN1a) (AtRPN1a) (26S proteasome regulatory subunit S2 homolog A)
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[PSMC5 SUG1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
[PSMD13] 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5)
[RPT5A ATS6A.2 TBP1 At3g05530 F22F7.1] 26S proteasome regulatory subunit 6A homolog A (26S proteasome AAA-ATPase subunit RPT5a) (Proteasome 26S subunit 6A homolog A) (Regulatory particle triple-A ATPase subunit 5a) (Tat-binding protein 1 homolog A) (TBP-1 homolog A)
[RPT5B TBP1 At1g09100 F7G19.2] 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
[RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7] 26S proteasome non-ATPase regulatory subunit 4 homolog (26S proteasome regulatory subunit RPN10) (AtRPN10) (26S proteasome regulatory subunit S5A homolog) (Multiubiquitin chain-binding protein 1) (AtMCB1)
[PSMD6 KIAA0107 PFAAP4] 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A)
[RPN12A At1g64520 F1N19.9] 26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A)
[PSMD7 MOV34L] 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)
[RPT2A HLR At4g29040 F19B15.70 F25O24.6] 26S proteasome regulatory subunit 4 homolog A (26S proteasome AAA-ATPase subunit RPT2a) (26S proteasome subunit 4 homolog A) (Protein HALTED ROOT) (Regulatory particle triple-A ATPase subunit 2a)
[PSMC3 TBP1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1)
[RPT2B At2g20140 T2G17.6] 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1)
[PSMC1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[PSMD12] 26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5) (26S proteasome regulatory subunit p55)
[PSMD8] 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) (p31)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)
[PSMC2 MSS1] 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (Protein MSS1)
[Rpn10 PROS-54 Pros54 CG7619] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (54 kDa subunit of mu particle) (Multiubiquitin chain-binding protein) (p54)
[PSMC6 SUG2] 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42)
[Psmd4 Mcb1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
[RPN2A At2g32730 F24L7.13] 26S proteasome non-ATPase regulatory subunit 1 homolog A (26S proteasome regulatory subunit RPN2a) (AtRPN2a) (26S proteasome regulatory subunit S1 homolog A)
[PSMC4 MIP224 TBP7] 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7)

Bibliography :
No related Items