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Database: UniProt
Entry: P17980
LinkDB: P17980
Original site: P17980 
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   02-JUN-2021, entry version 227.
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).
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   -!- 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   SMR; P17980; -.
DR   BioGRID; 111675; 281.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P17980; -.
DR   DIP; DIP-27555N; -.
DR   IntAct; P17980; 143.
DR   MINT; P17980; -.
DR   STRING; 9606.ENSP00000481029; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   DrugBank; DB12695; Phenethyl Isothiocyanate.
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; 512 antibodies.
DR   DNASU; 5702; -.
DR   Ensembl; ENST00000298852; ENSP00000298852; ENSG00000165916.
DR   Ensembl; ENST00000619920; ENSP00000481029; ENSG00000165916.
DR   GeneID; 5702; -.
DR   KEGG; hsa:5702; -.
DR   UCSC; uc001nfh.2; human.
DR   CTD; 5702; -.
DR   DisGeNET; 5702; -.
DR   GeneCards; PSMC3; -.
DR   HGNC; HGNC:9549; PSMC3.
DR   HPA; ENSG00000165916; Tissue enhanced (skeletal).
DR   MIM; 186852; gene.
DR   neXtProt; NX_P17980; -.
DR   NIAGADS; ENSG00000165916; -.
DR   OpenTargets; ENSG00000165916; -.
DR   PharmGKB; PA33894; -.
DR   VEuPathDB; HostDB:ENSG00000165916.8; -.
DR   eggNOG; KOG0652; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   InParanoid; P17980; -.
DR   OMA; KPTEQYT; -.
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-68827; CDT1 association with the CDC6:ORC:origin 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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P17980; -.
DR   BioGRID-ORCS; 5702; 801 hits in 964 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 heart left ventricle and 237 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:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IEA:InterPro.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0043921; P:modulation by host of viral transcription; IDA:GO_Central.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
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; Cytoplasm;
KW   Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT   CHAIN           1..439
FT                   /note="26S proteasome regulatory subunit 6A"
FT                   /id="PRO_0000084698"
FT   NP_BIND         227..234
FT                   /note="ATP"
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
//
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