PRS6A_HUMAN
ID PRS6A_HUMAN Reviewed; 439 AA.
AC P17980; B2R8V1; Q3B757; Q3B865; Q53HU5; Q6GPG8; Q6IBS1; Q96HD3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=26S proteasome regulatory subunit 6A;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
DE AltName: Full=Proteasome 26S subunit ATPase 3;
DE AltName: Full=Proteasome subunit P50;
DE AltName: Full=Tat-binding protein 1;
DE Short=TBP-1;
GN Name=PSMC3; Synonyms=TBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8419915; DOI=10.1073/pnas.90.1.138;
RA Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.;
RT "The type 1 human immunodeficiency virus Tat binding protein is a
RT transcriptional activator belonging to an additional family of
RT evolutionarily conserved genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Lung, and Peripheral nerve;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-439.
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, AND INTERACTION WITH HIV-1 TAT.
RX PubMed=2194290; DOI=10.1126/science.2194290;
RA Nelbock P., Dillion P.J., Perkins A., Rosen C.A.;
RT "A cDNA for a protein that interacts with the human immunodeficiency virus
RT Tat transactivator.";
RL Science 248:1650-1653(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294; 309-327;
RP 335-344; 351-362; 372-386 AND 398-409, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
RA Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
RA Hisamatsu H., Tanaka K., Slaughter C.A.;
RT "Identification, purification, and characterization of a PA700-dependent
RT activator of the proteasome.";
RL J. Biol. Chem. 271:3112-3118(1996).
RN [10]
RP FUNCTION.
RX PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA Tanaka K., Ichihara A.;
RT "Demonstration that a human 26S proteolytic complex consists of a
RT proteasome and multiple associated protein components and hydrolyzes ATP
RT and ubiquitin-ligated proteins by closely linked mechanisms.";
RL Eur. J. Biochem. 206:567-578(1992).
RN [11]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates proteasome
RT activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [13]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and inducible
RT SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-376, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
RN [23]
RP INVOLVEMENT IN DCIDP.
RX PubMed=32500975; DOI=10.15252/emmm.201911861;
RA Kroell-Hermi A., Ebstein F., Stoetzel C., Geoffroy V., Schaefer E.,
RA Scheidecker S., Baer S., Takamiya M., Kawakami K., Zieba B.A., Studer F.,
RA Pelletier V., Eyermann C., Speeg-Schatz C., Laugel V., Lipsker D.,
RA Sandron F., McGinn S., Boland A., Deleuze J.F., Kuhn L., Chicher J.,
RA Hammann P., Friant S., Etard C., Krueger E., Muller J., Straehle U.,
RA Dollfus H.;
RT "Proteasome subunit PSMC3 variants cause neurosensory syndrome combining
RT deafness and cataract due to proteotoxic stress.";
RL EMBO Mol. Med. 12:e11861-e11861(2020).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. PSMC3 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000269|PubMed:1317798}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases including PSMC3 and
CC few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC with PAAF1 (PubMed:15831487). {ECO:0000269|PubMed:15831487,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:2194290}.
CC -!- INTERACTION:
CC P17980; Q9Y2J4: AMOTL2; NbExp=5; IntAct=EBI-359720, EBI-746752;
CC P17980; Q9Y2J4-4: AMOTL2; NbExp=5; IntAct=EBI-359720, EBI-10187270;
CC P17980; P05067: APP; NbExp=6; IntAct=EBI-359720, EBI-77613;
CC P17980; P54253: ATXN1; NbExp=7; IntAct=EBI-359720, EBI-930964;
CC P17980; P12532: CKMT1B; NbExp=3; IntAct=EBI-359720, EBI-1050662;
CC P17980; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-359720, EBI-25840379;
CC P17980; Q9C005: DPY30; NbExp=3; IntAct=EBI-359720, EBI-744973;
CC P17980; Q9NVF7: FBXO28; NbExp=4; IntAct=EBI-359720, EBI-740282;
CC P17980; O43464: HTRA2; NbExp=3; IntAct=EBI-359720, EBI-517086;
CC P17980; P42858: HTT; NbExp=6; IntAct=EBI-359720, EBI-466029;
CC P17980; O14561: NDUFAB1; NbExp=6; IntAct=EBI-359720, EBI-1246261;
CC P17980; P17980: PSMC3; NbExp=4; IntAct=EBI-359720, EBI-359720;
CC P17980; P62333: PSMC6; NbExp=16; IntAct=EBI-359720, EBI-357669;
CC P17980; O00233: PSMD9; NbExp=16; IntAct=EBI-359720, EBI-750973;
CC P17980; P37840: SNCA; NbExp=6; IntAct=EBI-359720, EBI-985879;
CC P17980; P00441: SOD1; NbExp=3; IntAct=EBI-359720, EBI-990792;
CC P17980; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-359720, EBI-3650647;
CC P17980; A8K2R3; NbExp=3; IntAct=EBI-359720, EBI-9977437;
CC P17980; P03255-1; Xeno; NbExp=2; IntAct=EBI-359720, EBI-6692439;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC Note=Colocalizes with TRIM5 in the cytoplasmic bodies.
CC {ECO:0000250|UniProtKB:O88685}.
CC -!- PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli.
CC {ECO:0000269|PubMed:17709345}.
CC -!- DISEASE: Deafness, cataract, impaired intellectual development, and
CC polyneuropathy (DCIDP) [MIM:619354]: An autosomal recessive disease
CC characterized by early onset of deafness, cataract, severe
CC developmental delay, and severely impaired intellectual development.
CC Patients later develop polyneuropathy of the lower extremities,
CC associated with depigmentation of the hair in that area.
CC {ECO:0000269|PubMed:32500975}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07805.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK313518; BAG36298.1; -; mRNA.
DR EMBL; CH471064; EAW67916.1; -; Genomic_DNA.
DR EMBL; BC008713; AAH08713.4; -; mRNA.
DR EMBL; BC073165; AAH73165.3; -; mRNA.
DR EMBL; BC106920; AAI06921.1; -; mRNA.
DR EMBL; BC107804; AAI07805.1; ALT_INIT; mRNA.
DR EMBL; AK222485; BAD96205.1; -; mRNA.
DR EMBL; M34079; AAA36666.1; -; mRNA.
DR EMBL; CR456731; CAG33012.1; -; mRNA.
DR CCDS; CCDS7935.1; -.
DR PIR; A34832; A34832.
DR RefSeq; NP_002795.2; NM_002804.4.
DR PDB; 5GJQ; EM; 4.50 A; M=1-439.
DR PDB; 5GJR; EM; 3.50 A; 0/M=1-439.
DR PDB; 5L4G; EM; 4.02 A; M=1-439.
DR PDB; 5LN3; EM; 6.80 A; M=1-439.
DR PDB; 5M32; EM; 3.80 A; g=1-439.
DR PDB; 5T0C; EM; 3.80 A; AF/BF=1-439.
DR PDB; 5T0G; EM; 4.40 A; F=1-439.
DR PDB; 5T0H; EM; 6.80 A; F=1-439.
DR PDB; 5T0I; EM; 8.00 A; F=1-439.
DR PDB; 5T0J; EM; 8.00 A; F=1-439.
DR PDB; 5VFP; EM; 4.20 A; F=44-439.
DR PDB; 5VFQ; EM; 4.20 A; F=44-439.
DR PDB; 5VFR; EM; 4.90 A; F=44-439.
DR PDB; 5VFS; EM; 3.60 A; F=1-439.
DR PDB; 5VFT; EM; 7.00 A; F=63-439.
DR PDB; 5VFU; EM; 5.80 A; F=63-439.
DR PDB; 5VGZ; EM; 3.70 A; F=53-167.
DR PDB; 5VHF; EM; 5.70 A; F=53-432.
DR PDB; 5VHH; EM; 6.10 A; F=53-432.
DR PDB; 5VHI; EM; 6.80 A; F=53-432.
DR PDB; 5VHJ; EM; 8.50 A; F=166-432.
DR PDB; 5VHM; EM; 8.30 A; F=166-432.
DR PDB; 5VHN; EM; 7.30 A; F=166-432.
DR PDB; 5VHO; EM; 8.30 A; F=166-432.
DR PDB; 5VHP; EM; 7.90 A; F=166-432.
DR PDB; 5VHQ; EM; 8.90 A; F=166-432.
DR PDB; 5VHR; EM; 7.70 A; F=166-432.
DR PDB; 5VHS; EM; 8.80 A; F=53-432.
DR PDB; 6MSB; EM; 3.00 A; F=1-439.
DR PDB; 6MSD; EM; 3.20 A; F=1-439.
DR PDB; 6MSE; EM; 3.30 A; F=1-439.
DR PDB; 6MSG; EM; 3.50 A; F=1-439.
DR PDB; 6MSH; EM; 3.60 A; F=1-439.
DR PDB; 6MSJ; EM; 3.30 A; F=1-439.
DR PDB; 6MSK; EM; 3.20 A; F=1-439.
DR PDB; 6WJD; EM; 4.80 A; F=1-439.
DR PDB; 6WJN; EM; 5.70 A; F=44-439.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 5VGZ; -.
DR PDBsum; 5VHF; -.
DR PDBsum; 5VHH; -.
DR PDBsum; 5VHI; -.
DR PDBsum; 5VHJ; -.
DR PDBsum; 5VHM; -.
DR PDBsum; 5VHN; -.
DR PDBsum; 5VHO; -.
DR PDBsum; 5VHP; -.
DR PDBsum; 5VHQ; -.
DR PDBsum; 5VHR; -.
DR PDBsum; 5VHS; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P17980; -.
DR SMR; P17980; -.
DR BioGRID; 111675; 310.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P17980; -.
DR DIP; DIP-27555N; -.
DR IntAct; P17980; 152.
DR MINT; P17980; -.
DR STRING; 9606.ENSP00000481029; -.
DR ChEMBL; CHEMBL2364701; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P17980; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P17980; -.
DR MetOSite; P17980; -.
DR PhosphoSitePlus; P17980; -.
DR SwissPalm; P17980; -.
DR BioMuta; PSMC3; -.
DR DMDM; 20532406; -.
DR REPRODUCTION-2DPAGE; IPI00018398; -.
DR EPD; P17980; -.
DR jPOST; P17980; -.
DR MassIVE; P17980; -.
DR MaxQB; P17980; -.
DR PaxDb; P17980; -.
DR PeptideAtlas; P17980; -.
DR PRIDE; P17980; -.
DR ProteomicsDB; 53537; -.
DR Antibodypedia; 1816; 549 antibodies from 36 providers.
DR DNASU; 5702; -.
DR Ensembl; ENST00000298852.8; ENSP00000298852.3; ENSG00000165916.9.
DR Ensembl; ENST00000619920.4; ENSP00000481029.1; ENSG00000165916.9.
DR GeneID; 5702; -.
DR KEGG; hsa:5702; -.
DR MANE-Select; ENST00000298852.8; ENSP00000298852.3; NM_002804.5; NP_002795.2.
DR UCSC; uc001nfh.2; human.
DR CTD; 5702; -.
DR DisGeNET; 5702; -.
DR GeneCards; PSMC3; -.
DR HGNC; HGNC:9549; PSMC3.
DR HPA; ENSG00000165916; Low tissue specificity.
DR MIM; 186852; gene.
DR MIM; 619354; phenotype.
DR neXtProt; NX_P17980; -.
DR NIAGADS; ENSG00000165916; -.
DR OpenTargets; ENSG00000165916; -.
DR PharmGKB; PA33894; -.
DR VEuPathDB; HostDB:ENSG00000165916; -.
DR eggNOG; KOG0652; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR InParanoid; P17980; -.
DR OMA; HEKAAMG; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; P17980; -.
DR TreeFam; TF105648; -.
DR PathwayCommons; P17980; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P17980; -.
DR SIGNOR; P17980; -.
DR BioGRID-ORCS; 5702; 811 hits in 1049 CRISPR screens.
DR ChiTaRS; PSMC3; human.
DR GeneWiki; PSMC3; -.
DR GenomeRNAi; 5702; -.
DR Pharos; P17980; Tbio.
DR PRO; PR:P17980; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P17980; protein.
DR Bgee; ENSG00000165916; Expressed in apex of heart and 201 other tissues.
DR ExpressionAtlas; P17980; baseline and differential.
DR Genevisible; P17980; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036402; F:proteasome-activating activity; ISS:UniProtKB.
DR GO; GO:0043921; P:modulation by host of viral transcription; IDA:GO_Central.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IC:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035254; PSMC3.
DR PANTHER; PTHR23073:SF90; PTHR23073:SF90; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cataract; Cytoplasm; Deafness;
KW Direct protein sequencing; Host-virus interaction; Intellectual disability;
KW Neuropathy; Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..439
FT /note="26S proteasome regulatory subunit 6A"
FT /id="PRO_0000084698"
FT BINDING 227..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17323924,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 356
FT /note="M -> T (in Ref. 5; BAD96205)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="R -> A (in Ref. 6; AAA36666)"
FT /evidence="ECO:0000305"
SQ 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
