PRS7_HUMAN
ID PRS7_HUMAN Reviewed; 433 AA.
AC P35998; A4D0Q1; B7Z5E2; Q3LIA5; Q9UDI3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=26S proteasome regulatory subunit 7;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT1;
DE AltName: Full=Proteasome 26S subunit ATPase 2;
GN Name=PSMC2; Synonyms=MSS1 {ECO:0000303|PubMed:8500623};
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] (ISOFORM 1), AND INTERACTION WITH HIV-1 TAT
RP (MICROBIAL INFECTION).
RX PubMed=1377363; DOI=10.1038/357700a0;
RA Shibuya H., Irie K., Ninomiya-Tsuji J., Goebl M., Taniguchi T.,
RA Matsumoto K.;
RT "New human gene encoding a positive modulator of HIV Tat-mediated
RT transactivation.";
RL Nature 357:700-702(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [8]
RP PROTEIN SEQUENCE OF 2-23; 139-158 AND 320-331.
RC TISSUE=Blood;
RX PubMed=8500623; DOI=10.1016/0014-5793(93)81356-5;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated
RT transactivation, as subunit 7 of the 26 S protease.";
RL FEBS Lett. 323:276-278(1993).
RN [9]
RP PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 85-97; 101-110; 201-210; 269-284 AND 298-312, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
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 [12]
RP FUNCTION, INTERACTION WITH NDC80, AND INDUCTION.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome and
RT modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [13]
RP INTERACTION WITH NDC80.
RX PubMed=10409732; DOI=10.1128/mcb.19.8.5417;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [15]
RP INTERACTION WITH SQSTM1.
RX PubMed=15340068; DOI=10.1128/mcb.24.18.8055-8068.2004;
RA Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
RA Wooten M.W.;
RT "Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in
RT ubiquitin proteasome degradation.";
RL Mol. Cell. Biol. 24:8055-8068(2004).
RN [16]
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 [17]
RP IDENTIFICATION BY 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 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
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 [20]
RP INTERACTION WITH TRIM5, AND SUBCELLULAR LOCATION.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [21]
RP IDENTIFICATION BY 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., 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 [22]
RP UBIQUITINATION.
RX PubMed=24811749; DOI=10.1002/embj.201386906;
RA Besche H.C., Sha Z., Kukushkin N.V., Peth A., Hock E.M., Kim W., Gygi S.,
RA Gutierrez J.A., Liao H., Dick L., Goldberg A.L.;
RT "Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of
RT ubiquitin conjugates.";
RL EMBO J. 33:1159-1176(2014).
RN [23]
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 [24]
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 [25]
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. PSMC2 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, ECO:0000269|PubMed:9295362}.
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) (PubMed:27428775, PubMed:27342858). The
CC regulatory particle is made of a lid composed of 9 subunits, a base
CC containing 6 ATPases including PSMC2 and few additional components
CC (PubMed:27428775, PubMed:27342858). Interacts with NDC80/HEC; this
CC interaction is detected only during M phase (PubMed:9295362,
CC PubMed:10409732). Interacts and SQSTM1 (PubMed:15340068). Interacts
CC with PAAF1 (PubMed:15831487). Directly interacts with TRIM5
CC (PubMed:22078707). {ECO:0000269|PubMed:10409732,
CC ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:15831487,
CC ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:9295362}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
CC {ECO:0000269|PubMed:1377363}.
CC -!- INTERACTION:
CC P35998; O14901: KLF11; NbExp=3; IntAct=EBI-359710, EBI-948266;
CC P35998; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-359710, EBI-2811583;
CC P35998; Q96CV9: OPTN; NbExp=3; IntAct=EBI-359710, EBI-748974;
CC P35998; P62191: PSMC1; NbExp=6; IntAct=EBI-359710, EBI-357598;
CC P35998; P62195: PSMC5; NbExp=11; IntAct=EBI-359710, EBI-357745;
CC P35998; Q13200: PSMD2; NbExp=4; IntAct=EBI-359710, EBI-357648;
CC P35998; Q16401: PSMD5; NbExp=23; IntAct=EBI-359710, EBI-752143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}.
CC Note=Colocalizes with TRIM5 in cytoplasmic bodies.
CC {ECO:0000269|PubMed:22078707}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35998-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35998-2; Sequence=VSP_056178;
CC -!- INDUCTION: Expression is not cell cycle-dependent and occurs throughout
CC the cell cycle. {ECO:0000269|PubMed:9295362}.
CC -!- PTM: Monoubiquitinated by RNF181. {ECO:0000269|PubMed:24811749}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D11094; BAA01868.1; -; mRNA.
DR EMBL; AB075520; BAE45763.1; -; mRNA.
DR EMBL; AK298821; BAH12878.1; -; mRNA.
DR EMBL; AC004668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24412.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83332.1; -; Genomic_DNA.
DR EMBL; BC002589; AAH02589.1; -; mRNA.
DR CCDS; CCDS5731.1; -. [P35998-1]
DR PIR; S24353; S24353.
DR RefSeq; NP_001191382.1; NM_001204453.1.
DR RefSeq; NP_002794.1; NM_002803.3. [P35998-1]
DR PDB; 5GJQ; EM; 4.50 A; H=1-433.
DR PDB; 5GJR; EM; 3.50 A; H/v=1-433.
DR PDB; 5L4G; EM; 4.02 A; H=1-433.
DR PDB; 5LN3; EM; 6.80 A; H=1-433.
DR PDB; 5M32; EM; 3.80 A; c=1-433.
DR PDB; 5T0C; EM; 3.80 A; AA/BA=1-433.
DR PDB; 5T0G; EM; 4.40 A; A=1-433.
DR PDB; 5T0H; EM; 6.80 A; A=1-433.
DR PDB; 5T0I; EM; 8.00 A; A=1-433.
DR PDB; 5T0J; EM; 8.00 A; A=1-433.
DR PDB; 5VFP; EM; 4.20 A; A=35-433.
DR PDB; 5VFQ; EM; 4.20 A; A=35-433.
DR PDB; 5VFR; EM; 4.90 A; A=35-433.
DR PDB; 5VFS; EM; 3.60 A; A=1-433.
DR PDB; 5VFT; EM; 7.00 A; A=73-433.
DR PDB; 5VFU; EM; 5.80 A; A=73-433.
DR PDB; 5VGZ; EM; 3.70 A; A=73-155.
DR PDB; 5VHF; EM; 5.70 A; A=73-424.
DR PDB; 5VHH; EM; 6.10 A; A=73-424.
DR PDB; 5VHI; EM; 6.80 A; A=73-424.
DR PDB; 5VHJ; EM; 8.50 A; A=180-424.
DR PDB; 5VHM; EM; 8.30 A; A=159-424.
DR PDB; 5VHN; EM; 7.30 A; A=159-424.
DR PDB; 5VHO; EM; 8.30 A; A=158-424.
DR PDB; 5VHP; EM; 7.90 A; A=159-424.
DR PDB; 5VHQ; EM; 8.90 A; A=159-424.
DR PDB; 5VHR; EM; 7.70 A; A=159-424.
DR PDB; 5VHS; EM; 8.80 A; A=73-424.
DR PDB; 6MSB; EM; 3.00 A; A=1-433.
DR PDB; 6MSD; EM; 3.20 A; A=1-433.
DR PDB; 6MSE; EM; 3.30 A; M/m=94-136.
DR PDB; 6MSG; EM; 3.50 A; A=1-433.
DR PDB; 6MSH; EM; 3.60 A; A=1-433.
DR PDB; 6MSJ; EM; 3.30 A; A=1-433.
DR PDB; 6MSK; EM; 3.20 A; A=1-433.
DR PDB; 6WJD; EM; 4.80 A; A=1-433.
DR PDB; 6WJN; EM; 5.70 A; A=35-433.
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; P35998; -.
DR SMR; P35998; -.
DR BioGRID; 111674; 285.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P35998; -.
DR DIP; DIP-27554N; -.
DR IntAct; P35998; 105.
DR MINT; P35998; -.
DR STRING; 9606.ENSP00000391211; -.
DR ChEMBL; CHEMBL2364701; -.
DR GlyGen; P35998; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35998; -.
DR MetOSite; P35998; -.
DR PhosphoSitePlus; P35998; -.
DR SwissPalm; P35998; -.
DR BioMuta; PSMC2; -.
DR DMDM; 547930; -.
DR OGP; P35998; -.
DR REPRODUCTION-2DPAGE; IPI00021435; -.
DR REPRODUCTION-2DPAGE; P35998; -.
DR EPD; P35998; -.
DR jPOST; P35998; -.
DR MassIVE; P35998; -.
DR MaxQB; P35998; -.
DR PaxDb; P35998; -.
DR PeptideAtlas; P35998; -.
DR PRIDE; P35998; -.
DR ProteomicsDB; 55172; -. [P35998-1]
DR ProteomicsDB; 6682; -.
DR Antibodypedia; 16901; 365 antibodies from 34 providers.
DR DNASU; 5701; -.
DR Ensembl; ENST00000292644.5; ENSP00000292644.3; ENSG00000161057.13. [P35998-1]
DR Ensembl; ENST00000435765.5; ENSP00000391211.1; ENSG00000161057.13. [P35998-1]
DR Ensembl; ENST00000678493.1; ENSP00000502939.1; ENSG00000161057.13. [P35998-1]
DR Ensembl; ENST00000679205.1; ENSP00000503179.1; ENSG00000161057.13. [P35998-1]
DR Ensembl; ENST00000679250.1; ENSP00000503663.1; ENSG00000161057.13. [P35998-2]
DR Ensembl; ENST00000679341.1; ENSP00000504608.1; ENSG00000161057.13. [P35998-1]
DR GeneID; 5701; -.
DR KEGG; hsa:5701; -.
DR MANE-Select; ENST00000292644.5; ENSP00000292644.3; NM_002803.4; NP_002794.1.
DR UCSC; uc003vbs.4; human. [P35998-1]
DR CTD; 5701; -.
DR DisGeNET; 5701; -.
DR GeneCards; PSMC2; -.
DR HGNC; HGNC:9548; PSMC2.
DR HPA; ENSG00000161057; Low tissue specificity.
DR MIM; 154365; gene.
DR neXtProt; NX_P35998; -.
DR OpenTargets; ENSG00000161057; -.
DR PharmGKB; PA33893; -.
DR VEuPathDB; HostDB:ENSG00000161057; -.
DR eggNOG; KOG0729; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_6_1_1; -.
DR InParanoid; P35998; -.
DR OMA; INGYKKF; -.
DR PhylomeDB; P35998; -.
DR TreeFam; TF105661; -.
DR PathwayCommons; P35998; -.
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; P35998; -.
DR SIGNOR; P35998; -.
DR BioGRID-ORCS; 5701; 716 hits in 1098 CRISPR screens.
DR ChiTaRS; PSMC2; human.
DR GeneWiki; PSMC2; -.
DR GenomeRNAi; 5701; -.
DR Pharos; P35998; Tbio.
DR PRO; PR:P35998; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P35998; protein.
DR Bgee; ENSG00000161057; Expressed in skeletal muscle tissue of biceps brachii and 212 other tissues.
DR ExpressionAtlas; P35998; baseline and differential.
DR Genevisible; P35998; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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; HDA:UniProtKB.
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:0036402; F:proteasome-activating activity; IDA:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IC:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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; IPR035245; PSMC2.
DR PANTHER; PTHR23073:SF13; PTHR23073:SF13; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Proteasome;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:8500623"
FT CHAIN 2..433
FT /note="26S proteasome regulatory subunit 7"
FT /id="PRO_0000084709"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 422
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056178"
FT CONFLICT 15
FT /note="D -> V (in Ref. 2; BAE45763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 48634 MW; 85FD95F6DF7A3E84 CRC64;
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED DIQQLLKKIN
ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK IINADSEDPK YIINVKQFAK
FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC
KEQIEKLREV VETPLLHPER FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIRV
IGSELVQKYV GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG RTHIFKIHAR
SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR RKIATEKDFL EAVNKVIKSY
AKFSATPRYM TYN
