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Database: UniProt
Entry: P35998
LinkDB: P35998
Original site: P35998 
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   02-JUN-2021, entry version 215.
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;
DE   AltName: Full=Protein MSS1;
GN   Name=PSMC2; Synonyms=MSS1;
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).
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   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   [23]
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   [24]
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). The regulatory particle is made of a lid
CC       composed of 9 subunits, a base containing 6 ATPases including PSMC2 and
CC       few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC       with NDC80/HEC; this interaction is detected only during M phase.
CC       Interacts and SQSTM1 (PubMed:15340068). Interacts with PAAF1
CC       (PubMed:15831487). Directly interacts with TRIM5 (PubMed:22078707).
CC       {ECO:0000269|PubMed:10409732, ECO:0000269|PubMed:15340068,
CC       ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:22078707,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:9295362}.
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   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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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   SMR; P35998; -.
DR   BioGRID; 111674; 250.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P35998; -.
DR   DIP; DIP-27554N; -.
DR   IntAct; P35998; 94.
DR   MINT; P35998; -.
DR   STRING; 9606.ENSP00000391211; -.
DR   ChEMBL; CHEMBL2364701; -.
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; 356 antibodies.
DR   DNASU; 5701; -.
DR   Ensembl; ENST00000292644; ENSP00000292644; ENSG00000161057. [P35998-1]
DR   Ensembl; ENST00000435765; ENSP00000391211; ENSG00000161057. [P35998-1]
DR   Ensembl; ENST00000678493; ENSP00000502939; ENSG00000161057. [P35998-1]
DR   Ensembl; ENST00000679205; ENSP00000503179; ENSG00000161057. [P35998-1]
DR   Ensembl; ENST00000679250; ENSP00000503663; ENSG00000161057. [P35998-2]
DR   Ensembl; ENST00000679341; ENSP00000504608; ENSG00000161057. [P35998-1]
DR   GeneID; 5701; -.
DR   KEGG; hsa:5701; -.
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:ENSG00000161057.10; -.
DR   eggNOG; KOG0729; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_6_1_1; -.
DR   InParanoid; P35998; -.
DR   OMA; IHANTMN; -.
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-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; P35998; -.
DR   BioGRID-ORCS; 5701; 711 hits in 1014 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 biceps brachii and 250 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:0043197; C:dendritic spine; IBA:GO_Central.
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:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IEA:InterPro.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
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: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:0001649; P:osteoblast differentiation; HDA:UniProtKB.
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: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:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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; 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.
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   NP_BIND         216..223
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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
//
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