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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)

 PRS6A_HUMAN             Reviewed;         439 AA.
P17980; B2R8V1; Q3B757; Q3B865; Q53HU5; Q6GPG8; Q6IBS1; Q96HD3;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 3.
23-FEB-2022, entry version 229.
RecName: Full=26S proteasome regulatory subunit 6A;
AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
AltName: Full=Proteasome 26S subunit ATPase 3;
AltName: Full=Proteasome subunit P50;
AltName: Full=Tat-binding protein 1;
Short=TBP-1;
Name=PSMC3; Synonyms=TBP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8419915; DOI=10.1073/pnas.90.1.138;
Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.;
"The type 1 human immunodeficiency virus Tat binding protein is a
transcriptional activator belonging to an additional family of
evolutionarily conserved genes.";
Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, Lung, and Peripheral nerve;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-439.
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, AND INTERACTION WITH HIV-1 TAT.
PubMed=2194290; DOI=10.1126/science.2194290;
Nelbock P., Dillion P.J., Perkins A., Rosen C.A.;
"A cDNA for a protein that interacts with the human immunodeficiency virus
Tat transactivator.";
Science 248:1650-1653(1990).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294; 309-327;
335-344; 351-362; 372-386 AND 398-409, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PARTIAL PROTEIN SEQUENCE.
PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
Hisamatsu H., Tanaka K., Slaughter C.A.;
"Identification, purification, and characterization of a PA700-dependent
activator of the proteasome.";
J. Biol. Chem. 271:3112-3118(1996).
[10]
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).
[11]
INTERACTION WITH PAAF1.
PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005;
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
"Proteasomal ATPase-associated factor 1 negatively regulates proteasome
activity by interacting with proteasomal ATPases.";
Mol. Cell. Biol. 25:3842-3853(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, 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).
[13]
SUMOYLATION.
PubMed=17709345; DOI=10.1093/nar/gkm617;
Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
"Ubc9 fusion-directed SUMOylation identifies constitutive and inducible
SUMOylation.";
Nucleic Acids Res. 35:E109-E109(2007).
[14]
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).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-9, AND 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).
[16]
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
ANALYSIS] AT SER-9, 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).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-376, 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).
[20]
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).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, 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).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, 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. PSMC3 belongs to the heterohexameric ring of AAA (ATPases
associated with diverse cellular activities) proteins that unfolds
ubiquitinated target proteins that are concurrently translocated into a
proteolytic chamber and degraded into peptides.
{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 including PSMC3 and
few additional components (PubMed:27428775, PubMed:27342858). Interacts
with PAAF1 (PubMed:15831487). {ECO:0000269|PubMed:15831487,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
{ECO:0000269|PubMed:2194290}.
-!- INTERACTION:
P17980; Q9Y2J4: AMOTL2; NbExp=5; IntAct=EBI-359720, EBI-746752;
P17980; Q9Y2J4-4: AMOTL2; NbExp=5; IntAct=EBI-359720, EBI-10187270;
P17980; P05067: APP; NbExp=6; IntAct=EBI-359720, EBI-77613;
P17980; P54253: ATXN1; NbExp=7; IntAct=EBI-359720, EBI-930964;
P17980; P12532: CKMT1B; NbExp=3; IntAct=EBI-359720, EBI-1050662;
P17980; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-359720, EBI-25840379;
P17980; Q9C005: DPY30; NbExp=3; IntAct=EBI-359720, EBI-744973;
P17980; Q9NVF7: FBXO28; NbExp=4; IntAct=EBI-359720, EBI-740282;
P17980; O43464: HTRA2; NbExp=3; IntAct=EBI-359720, EBI-517086;
P17980; P42858: HTT; NbExp=6; IntAct=EBI-359720, EBI-466029;
P17980; O14561: NDUFAB1; NbExp=6; IntAct=EBI-359720, EBI-1246261;
P17980; P17980: PSMC3; NbExp=4; IntAct=EBI-359720, EBI-359720;
P17980; P62333: PSMC6; NbExp=16; IntAct=EBI-359720, EBI-357669;
P17980; O00233: PSMD9; NbExp=16; IntAct=EBI-359720, EBI-750973;
P17980; P37840: SNCA; NbExp=6; IntAct=EBI-359720, EBI-985879;
P17980; P00441: SOD1; NbExp=3; IntAct=EBI-359720, EBI-990792;
P17980; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-359720, EBI-3650647;
P17980; A8K2R3; NbExp=3; IntAct=EBI-359720, EBI-9977437;
P17980; P03255-1; Xeno; NbExp=2; IntAct=EBI-359720, EBI-6692439;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Note=Colocalizes with TRIM5 in the cytoplasmic bodies.
{ECO:0000250|UniProtKB:O88685}.
-!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
{ECO:0000269|PubMed:17709345}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI07805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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EMBL; AK313518; BAG36298.1; -; mRNA.
EMBL; CH471064; EAW67916.1; -; Genomic_DNA.
EMBL; BC008713; AAH08713.4; -; mRNA.
EMBL; BC073165; AAH73165.3; -; mRNA.
EMBL; BC106920; AAI06921.1; -; mRNA.
EMBL; BC107804; AAI07805.1; ALT_INIT; mRNA.
EMBL; AK222485; BAD96205.1; -; mRNA.
EMBL; M34079; AAA36666.1; -; mRNA.
EMBL; CR456731; CAG33012.1; -; mRNA.
CCDS; CCDS7935.1; -.
PIR; A34832; A34832.
RefSeq; NP_002795.2; NM_002804.4.
PDB; 5GJQ; EM; 4.50 A; M=1-439.
PDB; 5GJR; EM; 3.50 A; 0/M=1-439.
PDB; 5L4G; EM; 4.02 A; M=1-439.
PDB; 5LN3; EM; 6.80 A; M=1-439.
PDB; 5M32; EM; 3.80 A; g=1-439.
PDB; 5T0C; EM; 3.80 A; AF/BF=1-439.
PDB; 5T0G; EM; 4.40 A; F=1-439.
PDB; 5T0H; EM; 6.80 A; F=1-439.
PDB; 5T0I; EM; 8.00 A; F=1-439.
PDB; 5T0J; EM; 8.00 A; F=1-439.
PDB; 5VFP; EM; 4.20 A; F=44-439.
PDB; 5VFQ; EM; 4.20 A; F=44-439.
PDB; 5VFR; EM; 4.90 A; F=44-439.
PDB; 5VFS; EM; 3.60 A; F=1-439.
PDB; 5VFT; EM; 7.00 A; F=63-439.
PDB; 5VFU; EM; 5.80 A; F=63-439.
PDB; 5VGZ; EM; 3.70 A; F=53-167.
PDB; 5VHF; EM; 5.70 A; F=53-432.
PDB; 5VHH; EM; 6.10 A; F=53-432.
PDB; 5VHI; EM; 6.80 A; F=53-432.
PDB; 5VHJ; EM; 8.50 A; F=166-432.
PDB; 5VHM; EM; 8.30 A; F=166-432.
PDB; 5VHN; EM; 7.30 A; F=166-432.
PDB; 5VHO; EM; 8.30 A; F=166-432.
PDB; 5VHP; EM; 7.90 A; F=166-432.
PDB; 5VHQ; EM; 8.90 A; F=166-432.
PDB; 5VHR; EM; 7.70 A; F=166-432.
PDB; 5VHS; EM; 8.80 A; F=53-432.
PDB; 6MSB; EM; 3.00 A; F=1-439.
PDB; 6MSD; EM; 3.20 A; F=1-439.
PDB; 6MSE; EM; 3.30 A; F=1-439.
PDB; 6MSG; EM; 3.50 A; F=1-439.
PDB; 6MSH; EM; 3.60 A; F=1-439.
PDB; 6MSJ; EM; 3.30 A; F=1-439.
PDB; 6MSK; EM; 3.20 A; F=1-439.
PDB; 6WJD; EM; 4.80 A; F=1-439.
PDB; 6WJN; EM; 5.70 A; F=44-439.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHJ; -.
PDBsum; 5VHM; -.
PDBsum; 5VHN; -.
PDBsum; 5VHO; -.
PDBsum; 5VHP; -.
PDBsum; 5VHQ; -.
PDBsum; 5VHR; -.
PDBsum; 5VHS; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
PDBsum; 6WJD; -.
PDBsum; 6WJN; -.
SMR; P17980; -.
BioGRID; 111675; 301.
ComplexPortal; CPX-5993; 26S Proteasome complex.
CORUM; P17980; -.
DIP; DIP-27555N; -.
IntAct; P17980; 144.
MINT; P17980; -.
STRING; 9606.ENSP00000481029; -.
ChEMBL; CHEMBL2364701; -.
DrugBank; DB12695; Phenethyl Isothiocyanate.
GlyGen; P17980; 1 site, 1 O-linked glycan (1 site).
iPTMnet; P17980; -.
MetOSite; P17980; -.
PhosphoSitePlus; P17980; -.
SwissPalm; P17980; -.
BioMuta; PSMC3; -.
DMDM; 20532406; -.
REPRODUCTION-2DPAGE; IPI00018398; -.
EPD; P17980; -.
jPOST; P17980; -.
MassIVE; P17980; -.
MaxQB; P17980; -.
PaxDb; P17980; -.
PeptideAtlas; P17980; -.
PRIDE; P17980; -.
ProteomicsDB; 53537; -.
Antibodypedia; 1816; 519 antibodies from 36 providers.
DNASU; 5702; -.
Ensembl; ENST00000298852; ENSP00000298852; ENSG00000165916.
Ensembl; ENST00000619920; ENSP00000481029; ENSG00000165916.
GeneID; 5702; -.
KEGG; hsa:5702; -.
MANE-Select; ENST00000298852.8; ENSP00000298852.3; NM_002804.5; NP_002795.2.
UCSC; uc001nfh.2; human.
CTD; 5702; -.
DisGeNET; 5702; -.
GeneCards; PSMC3; -.
HGNC; HGNC:9549; PSMC3.
HPA; ENSG00000165916; Low tissue specificity.
MIM; 186852; gene.
neXtProt; NX_P17980; -.
NIAGADS; ENSG00000165916; -.
OpenTargets; ENSG00000165916; -.
PharmGKB; PA33894; -.
VEuPathDB; HostDB:ENSG00000165916; -.
eggNOG; KOG0652; Eukaryota.
GeneTree; ENSGT01020000230346; -.
InParanoid; P17980; -.
OMA; KPTEQYT; -.
OrthoDB; 571919at2759; -.
PhylomeDB; P17980; -.
TreeFam; TF105648; -.
PathwayCommons; P17980; -.
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-8932339; ROS sensing by NFE2L2.
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.
SignaLink; P17980; -.
SIGNOR; P17980; -.
BioGRID-ORCS; 5702; 806 hits in 1016 CRISPR screens.
ChiTaRS; PSMC3; human.
GeneWiki; PSMC3; -.
GenomeRNAi; 5702; -.
Pharos; P17980; Tbio.
PRO; PR:P17980; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; P17980; protein.
Bgee; ENSG00000165916; Expressed in heart left ventricle and 237 other tissues.
ExpressionAtlas; P17980; baseline and differential.
Genevisible; P17980; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:GO_Central.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0036402; F:proteasome-activating activity; ISS:UniProtKB.
GO; GO:0043921; P:modulation by host of viral transcription; IDA:GO_Central.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IC:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
Gene3D; 3.40.50.300; -; 1.
InterPro; IPR005937; 26S_Psome_P45-like.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR041569; AAA_lid_3.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR032501; Prot_ATP_ID_OB.
InterPro; IPR035254; PSMC3.
PANTHER; PTHR23073:SF90; PTHR23073:SF90; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF17862; AAA_lid_3; 1.
Pfam; PF16450; Prot_ATP_ID_OB; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01242; 26Sp45; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
Nucleus; Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
CHAIN 1..439
/note="26S proteasome regulatory subunit 6A"
/id="PRO_0000084698"
NP_BIND 227..234
/note="ATP"
/evidence="ECO:0000255"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0007744|PubMed:19413330,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:22814378"
MOD_RES 9
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
ECO:0007744|PubMed:23186163"
MOD_RES 376
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
CONFLICT 356
/note="M -> T (in Ref. 5; BAD96205)"
/evidence="ECO:0000305"
CONFLICT 409
/note="R -> A (in Ref. 6; AAA36666)"
/evidence="ECO:0000305"
SEQUENCE 439 AA; 49204 MW; 0E443465DDDEBB0B CRC64;
MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS EIKIMKSEVL
RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD PNDQEEDGAN IDLDSQRKGK
CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL VGVNKDSYLI LETLPTEYDS RVKAMEVDER
PTEQYSDIGG LDKQIQELVE AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC
AAQTKATFLK LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR KIEFPMPNEE
ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC VEAGMIALRR GATELTHEDY
MEGILEVQAK KKANLQYYA


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EIAAB32656 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Proteasome 26S subunit ATPase 3,Psmc3,Rat,Rattus norvegicus,Spermatogenic cell_sperm-associated Tat-binding protein homolog SA
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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
EIAAB32666 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,Homo sapiens,Human,p45_SUG,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,SUG1,Thyroid hormone receptor-interacti
EIAAB32665 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,Psmc5,Rat,Rattus norvegicus,Sug1,Thyroid hormone receptor-intera
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EIAAB32593 26S protease regulatory subunit 10B,26S proteasome AAA-ATPase subunit RPT4,Homo sapiens,Human,Proteasome 26S subunit ATPase 6,Proteasome subunit p42,PSMC6,SUG2
EIAAB32668 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,Bos taurus,Bovine,p45_SUG,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,SUG1
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EIAAB32594 26S protease regulatory subunit 10B,26S proteasome AAA-ATPase subunit RPT4,Mouse,Mus musculus,Proteasome 26S subunit ATPase 6,Proteasome subunit p42,Psmc6,Sug2
EIAAB32660 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,Proteasome 26S subunit ATPase 4,Psmc4,Rat,Rattus norvegicus,S6 ATPase,Tat-binding protein 7,Tbp7,TBP-7
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
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
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
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
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
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
EIAAB32657 26S protease regulatory subunit 6B,26S proteasome AAA-ATPase subunit RPT3,CIP21,MB67-interacting protein,MIP224,Mouse,Mus musculus,Proteasome 26S subunit ATPase 4,Psmc4,Tat-binding protein 7,Tbp7,TBP-
Pathways :
WP1691: Proteasome
WP2292: Chemokine signaling pathway
WP470: Proteasome Degradation
WP2272: Pathogenic Escherichia coli infection
WP1644: DNA replication
WP1694: Pyrimidine metabolism
WP1693: Purine metabolism
WP158: Proteasome Degradation
WP1663: Homologous recombination
WP1566: Citrate cycle (TCA cycle)
WP1672: Mismatch repair
WP960: Proteasome Degradation
WP1196: Proteasome Degradation
WP281: Proteasome Degradation
WP1655: Geraniol degradation
WP1671: Methane metabolism
WP1634: Butanoate metabolism
WP1680: Oxidative phosphorylation
WP267: Proteasome Degradation
WP1711: Trinitrotoluene degradation
WP519: Proteasome Degradation
WP1718: Vitamin B6 metabolism
WP1626: Benzoate degradation via CoA ligation
WP183: Proteasome Degradation
WP841: Proteasome Degradation

Related Genes :
[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)
[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)
[RPT5 YTA1 YOR117W O3258 YOR3258W] 26S proteasome regulatory subunit 6A (Tat-binding protein homolog 1) (TBP-1)
[Psmc3 Tbp1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Tat-binding protein 1) (TBP-1)
[Psmc3 Tbp1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Spermatogenic cell/sperm-associated Tat-binding protein homolog SATA) (Tat-binding protein 1) (TBP-1)
[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)
[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)
[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)
[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)
[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)
[Psmc1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMC2 MSS1] 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2)
[PSMC6 SUG2] 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42)
[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)
[RPT1 CIM5 YTA3 YKL145W] 26S proteasome regulatory subunit 7 homolog (Protein CIM5) (Tat-binding homolog 3)
[RPT3 YNT1 YTA2 YDR394W D9509.14] 26S proteasome regulatory subunit 6B homolog (Protein YNT1) (Tat-binding homolog 2)
[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)
[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)
[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)
[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)
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[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)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)
[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)
[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)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
[RPT6 CIM3 CRL3 SUG1 TBPY TBY1 YGL048C] 26S proteasome regulatory subunit 8 homolog (Protein CIM3) (Protein SUG1) (Tat-binding protein TBY1)

Bibliography :