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   09-DEC-2015, entry version 174.
DE   RecName: Full=26S protease 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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   virus 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;
RP   309-327; 335-344; 351-362; 372-386 AND 398-409, AND IDENTIFICATION BY
RP   MASS 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-
RT   dependent activator of the proteasome.";
RL   J. Biol. Chem. 271:3112-3118(1996).
RN   [10]
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
RT   proteasome activity by interacting with proteasomal ATPases.";
RL   Mol. Cell. Biol. 25:3842-3853(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
RP   MASS 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
RT   26S proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [12]
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
RT   inducible SUMOylation.";
RL   Nucleic Acids Res. 35:E109-E109(2007).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
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.,
RA   Buerckstuemmer T., 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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [18]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the
CC       26S complex (By similarity). In case of HIV-1 infection,
CC       suppresses Tat-mediated transactivation. {ECO:0000250}.
CC   -!- SUBUNIT: May form a heterodimer with a related family member.
CC       Interacts with PAAF1. Interacts with HIV-1 Tat.
CC       {ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:2194290}.
CC   -!- INTERACTION:
CC       A8K2R3:-; NbExp=3; IntAct=EBI-359720, EBI-9977437;
CC       P03255-1:- (xeno); NbExp=2; IntAct=EBI-359720, EBI-6692439;
CC       Q9Y2J4-4:AMOTL2; NbExp=5; IntAct=EBI-359720, EBI-10187270;
CC       P62333:PSMC6; NbExp=10; IntAct=EBI-359720, EBI-357669;
CC       O00233:PSMD9; NbExp=9; IntAct=EBI-359720, EBI-750973;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
CC       {ECO:0000305}. Cytoplasm, P-body {ECO:0000250}. Note=Colocalizes
CC       with TRIM5 in the cytoplasmic bodies. {ECO:0000250}.
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=Translation N-terminally shortened.; 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   RefSeq; XP_011518534.1; XM_011520232.1.
DR   UniGene; Hs.250758; -.
DR   ProteinModelPortal; P17980; -.
DR   SMR; P17980; 52-439.
DR   BioGrid; 111675; 175.
DR   DIP; DIP-27555N; -.
DR   IntAct; P17980; 34.
DR   MINT; MINT-1149785; -.
DR   STRING; 9606.ENSP00000298852; -.
DR   PhosphoSite; P17980; -.
DR   BioMuta; PSMC3; -.
DR   DMDM; 20532406; -.
DR   REPRODUCTION-2DPAGE; IPI00018398; -.
DR   MaxQB; P17980; -.
DR   PaxDb; P17980; -.
DR   PeptideAtlas; P17980; -.
DR   PRIDE; P17980; -.
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   GeneCards; PSMC3; -.
DR   HGNC; HGNC:9549; PSMC3.
DR   HPA; HPA006065; -.
DR   MIM; 186852; gene.
DR   neXtProt; NX_P17980; -.
DR   PharmGKB; PA33894; -.
DR   eggNOG; KOG0652; Eukaryota.
DR   eggNOG; COG1222; LUCA.
DR   GeneTree; ENSGT00730000111070; -.
DR   HOVERGEN; HBG000109; -.
DR   InParanoid; P17980; -.
DR   KO; K03065; -.
DR   OMA; RKMAVDD; -.
DR   OrthoDB; EOG7TMZRN; -.
DR   PhylomeDB; P17980; -.
DR   TreeFam; TF105648; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
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-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 that don't undergo autocatalytic processing 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-5687128; MAPK6/MAPK4 signaling.
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-69229; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   ChiTaRS; PSMC3; human.
DR   GeneWiki; PSMC3; -.
DR   GenomeRNAi; 5702; -.
DR   NextBio; 22154; -.
DR   PMAP-CutDB; P17980; -.
DR   PRO; PR:P17980; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; P17980; -.
DR   CleanEx; HS_PSMC3; -.
DR   ExpressionAtlas; P17980; baseline and differential.
DR   Genevisible; P17980; HS.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA: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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; 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:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR   GO; GO:0006915; P:apoptotic process; TAS:Reactome.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR   GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
DR   GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:1903507; P:negative regulation of nucleic acid-templated transcription; TAS:GOC.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IBA:GOC.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
DR   GO; GO:0012501; P:programmed cell death; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR   GO; GO:0044281; P:small molecule metabolic 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:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; TAS:Reactome.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 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   Acetylation; ATP-binding; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Host-virus interaction; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Proteasome; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN         1    439       26S protease regulatory subunit 6A.
FT                                /FTId=PRO_0000084698.
FT   NP_BIND     227    234       ATP. {ECO:0000255}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:22814378}.
FT   MOD_RES       9      9       Phosphoserine.
FT                                {ECO:0000244|PubMed:17323924,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MUTAGEN     233    233       K->H: Loss of function.
FT   MUTAGEN     289    289       D->A: Loss of function.
FT   CONFLICT    356    356       M -> T (in Ref. 5; BAD96205).
FT                                {ECO:0000305}.
FT   CONFLICT    409    409       R -> A (in Ref. 6; AAA36666).
FT                                {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
//