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26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (Thyroid hormone receptor-interacting protein 1) (TRIP1) (p45/SUG)

 PRS8_HUMAN              Reviewed;         406 AA.
P62195; A8K3Z3; A8K763; O35051; O43208; P47210; P52915; P52916;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
25-OCT-2017, entry version 148.
RecName: Full=26S proteasome regulatory subunit 8;
AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
AltName: Full=Proteasome 26S subunit ATPase 5;
AltName: Full=Proteasome subunit p45;
AltName: Full=Thyroid hormone receptor-interacting protein 1;
Short=TRIP1;
AltName: Full=p45/SUG;
Name=PSMC5; Synonyms=SUG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hepatoma;
PubMed=7729537; DOI=10.1016/0014-5793(95)00304-R;
Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N.,
Slaughter C.A., Noda C., Tanaka K.;
"cDNA cloning of a new putative ATPase subunit p45 of the human 26S
proteasome, a homolog of yeast transcriptional factor Sug1p.";
FEBS Lett. 363:151-156(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
"Two classes of proteins dependent on either the presence or absence
of thyroid hormone for interaction with the thyroid hormone
receptor.";
Mol. Endocrinol. 9:243-254(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung carcinoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[7]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N.,
Yoshimura T., Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes
ATP and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[8]
INTERACTION WITH NDC80.
PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
Chen Y., Sharp Z.D., Lee W.-H.;
"HEC binds to the seventh regulatory subunit of the 26 S proteasome
and modulates the proteolysis of mitotic cyclins.";
J. Biol. Chem. 272:24081-24087(1997).
[9]
INTERACTION WITH NDC80.
PubMed=10409732; DOI=10.1128/MCB.19.8.5417;
Zheng L., Chen Y., Lee W.-H.;
"Hec1p, an evolutionarily conserved coiled-coil protein, modulates
chromosome segregation through interaction with SMC proteins.";
Mol. Cell. Biol. 19:5417-5428(1999).
[10]
INTERACTION WITH PAAF1.
PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
"Proteasomal ATPase-associated factor 1 negatively regulates
proteasome activity by interacting with proteasomal ATPases.";
Mol. Cell. Biol. 25:3842-3853(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH TRIM5.
PubMed=22078707; DOI=10.1186/1742-4690-8-93;
Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
Luban J., Campbell E.M.;
"TRIM5alpha associates with proteasomal subunits in cells while in
complex with HIV-1 virions.";
Retrovirology 8:93-93(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ACETYLATION [LARGE SCALE
ANALYSIS] AT MET-1 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
PubMed=23824326; DOI=10.1101/gad.211037.112;
Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
Giles K.E., Ma L., Wang H.;
"USP49 deubiquitinates histone H2B and regulates cotranscriptional
pre-mRNA splicing.";
Genes Dev. 27:1581-1595(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, AND STRUCTURE BY NMR
OF 320-395.
Northeast structural genomics consortium (NESG);
"Crystal structure of a domain of 26s proteasome regulatory subunit 8
from Homo sapiens. Northeast structural genomics consortium target ID
HR3102A.";
Submitted (JAN-2010) to the PDB data bank.
[23]
VARIANT [LARGE SCALE ANALYSIS] GLN-60.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, AND
SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[25]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, AND
SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair. PSMC5 belongs to the
heterohexameric ring of AAA (ATPases associated with diverse
cellular activities) proteins that unfolds ubiquitinated target
proteins that are concurrently translocated into a proteolytic
chamber and degraded into peptides. {ECO:0000269|PubMed:1317798}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits, a base containing 6 ATPases
including PSMC5 and few additional components (PubMed:27428775,
PubMed:27342858). Component of a complex with USP49 and RUVBL1
(PubMed:23824326). Interacts with PRPF19. Interacts with TRIM5
(PubMed:22078707). Interacts with NDC80 (PubMed:9295362,
PubMed:10409732). Interacts with PAAF1 (PubMed:15831487).
Interacts, in vitro, with the thyroid hormone receptor (in a
thyroid hormone T3-dependent manner) and with retinoid X receptor
(RXR). {ECO:0000250|UniProtKB:P62196,
ECO:0000250|UniProtKB:P62198, ECO:0000269|PubMed:10409732,
ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:22078707,
ECO:0000269|PubMed:23824326, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:9295362}.
-!- INTERACTION:
P03255-1:- (xeno); NbExp=2; IntAct=EBI-357745, EBI-6692439;
P11275:Camk2a (xeno); NbExp=4; IntAct=EBI-357745, EBI-2640645;
P08413:Camk2b (xeno); NbExp=3; IntAct=EBI-357745, EBI-916155;
P19447:ERCC3; NbExp=4; IntAct=EBI-357745, EBI-1183307;
Q6FG41:FOS; NbExp=3; IntAct=EBI-357745, EBI-10198738;
O76015:KRT38; NbExp=3; IntAct=EBI-357745, EBI-1047263;
Q6A162:KRT40; NbExp=3; IntAct=EBI-357745, EBI-10171697;
Q9BRP4:PAAF1; NbExp=2; IntAct=EBI-357745, EBI-1056358;
Q13371:PDCL; NbExp=6; IntAct=EBI-357745, EBI-5772890;
Q53GL0:PLEKHO1; NbExp=10; IntAct=EBI-357745, EBI-949945;
P35998:PSMC2; NbExp=10; IntAct=EBI-357745, EBI-359710;
P43686:PSMC4; NbExp=13; IntAct=EBI-357745, EBI-743997;
P62333:PSMC6; NbExp=10; IntAct=EBI-357745, EBI-357669;
Q13200:PSMD2; NbExp=9; IntAct=EBI-357745, EBI-357648;
Q96BD8:SKA1; NbExp=3; IntAct=EBI-357745, EBI-741854;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62195-1; Sequence=Displayed;
Name=2;
IsoId=P62195-2; Sequence=VSP_045441;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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EMBL; D44467; BAA07919.1; -; mRNA.
EMBL; L38810; AAC41735.1; -; mRNA.
EMBL; AK290758; BAF83447.1; -; mRNA.
EMBL; AK291878; BAF84567.1; -; mRNA.
EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94270.1; -; Genomic_DNA.
EMBL; CH471109; EAW94271.1; -; Genomic_DNA.
EMBL; CH471109; EAW94272.1; -; Genomic_DNA.
EMBL; BC001932; AAH01932.1; -; mRNA.
EMBL; BC002367; AAH02367.3; -; mRNA.
EMBL; AF035309; AAB88187.1; -; mRNA.
CCDS; CCDS11645.1; -. [P62195-1]
CCDS; CCDS56043.1; -. [P62195-2]
PIR; S60343; S60343.
PIR; S65536; S65536.
RefSeq; NP_001186092.1; NM_001199163.1. [P62195-2]
RefSeq; NP_002796.4; NM_002805.5. [P62195-1]
UniGene; Hs.79387; -.
PDB; 2KRK; NMR; -; A=320-395.
PDB; 3KW6; X-ray; 2.10 A; A=318-395.
PDB; 5GJQ; EM; 4.50 A; J=1-406.
PDB; 5GJR; EM; 3.50 A; J/x=1-406.
PDB; 5L4G; EM; 4.02 A; J=1-406.
PDB; 5LN3; EM; 6.80 A; J=1-406.
PDB; 5M32; EM; 3.80 A; h=38-392.
PDB; 5T0C; EM; 3.80 A; AC/BC=1-406.
PDB; 5T0G; EM; 4.40 A; C=9-406.
PDB; 5T0H; EM; 6.80 A; C=9-406.
PDB; 5T0I; EM; 8.00 A; C=9-406.
PDB; 5T0J; EM; 8.00 A; C=9-406.
PDB; 5VGZ; EM; 3.70 A; C=11-128.
PDB; 5VHF; EM; 5.70 A; C=11-395.
PDB; 5VHH; EM; 6.10 A; C=11-395.
PDB; 5VHI; EM; 6.80 A; C=11-395.
PDB; 5VHJ; EM; 8.50 A; C=130-395.
PDB; 5VHM; EM; 8.30 A; C=130-395.
PDB; 5VHN; EM; 7.30 A; C=130-395.
PDB; 5VHO; EM; 8.30 A; C=130-395.
PDB; 5VHP; EM; 7.90 A; C=130-395.
PDB; 5VHQ; EM; 8.90 A; C=130-395.
PDB; 5VHR; EM; 7.70 A; C=130-395.
PDB; 5VHS; EM; 8.80 A; C=11-395.
PDBsum; 2KRK; -.
PDBsum; 3KW6; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHJ; -.
PDBsum; 5VHM; -.
PDBsum; 5VHN; -.
PDBsum; 5VHO; -.
PDBsum; 5VHP; -.
PDBsum; 5VHQ; -.
PDBsum; 5VHR; -.
PDBsum; 5VHS; -.
ProteinModelPortal; P62195; -.
SMR; P62195; -.
BioGrid; 111678; 222.
CORUM; P62195; -.
DIP; DIP-36645N; -.
IntAct; P62195; 86.
MINT; MINT-5004394; -.
STRING; 9606.ENSP00000310572; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; P62195; -.
PhosphoSitePlus; P62195; -.
SwissPalm; P62195; -.
BioMuta; PSMC5; -.
DMDM; 49065819; -.
EPD; P62195; -.
MaxQB; P62195; -.
PaxDb; P62195; -.
PeptideAtlas; P62195; -.
PRIDE; P62195; -.
DNASU; 5705; -.
Ensembl; ENST00000310144; ENSP00000310572; ENSG00000087191. [P62195-1]
Ensembl; ENST00000375812; ENSP00000364970; ENSG00000087191. [P62195-2]
Ensembl; ENST00000580864; ENSP00000462495; ENSG00000087191. [P62195-2]
Ensembl; ENST00000581882; ENSP00000463938; ENSG00000087191. [P62195-2]
GeneID; 5705; -.
KEGG; hsa:5705; -.
UCSC; uc002jcb.4; human. [P62195-1]
CTD; 5705; -.
DisGeNET; 5705; -.
EuPathDB; HostDB:ENSG00000087191.12; -.
GeneCards; PSMC5; -.
HGNC; HGNC:9552; PSMC5.
HPA; HPA017871; -.
HPA; HPA064293; -.
MIM; 601681; gene.
neXtProt; NX_P62195; -.
OpenTargets; ENSG00000087191; -.
PharmGKB; PA33897; -.
eggNOG; KOG0728; Eukaryota.
eggNOG; COG1222; LUCA.
GeneTree; ENSGT00550000074947; -.
HOGENOM; HOG000225143; -.
HOVERGEN; HBG000109; -.
InParanoid; P62195; -.
KO; K03066; -.
OMA; HGNNQEA; -.
OrthoDB; EOG091G096W; -.
PhylomeDB; P62195; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMC5; human.
EvolutionaryTrace; P62195; -.
GeneWiki; PSMC5; -.
GenomeRNAi; 5705; -.
PRO; PR:P62195; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000087191; -.
CleanEx; HS_PSMC5; -.
ExpressionAtlas; P62195; baseline and differential.
Genevisible; P62195; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central.
GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:GO_Central.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0090261; P:positive regulation of inclusion body assembly; IEA:Ensembl.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:GO_Central.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.10.330.10; -; 1.
InterPro; IPR005937; 26S_Psome_P45-like.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR029067; CDC48_domain_2-like.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR035261; PSMC5.
PANTHER; PTHR23073:SF12; PTHR23073:SF12; 1.
Pfam; PF00004; AAA; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01242; 26Sp45; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Proteasome; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052}.
CHAIN 2 406 26S proteasome regulatory subunit 8.
/FTId=PRO_0000084721.
NP_BIND 190 197 ATP. {ECO:0000255}.
REGION 186 406 May mediate interaction with PRPF9.
{ECO:0000250|UniProtKB:P62196}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 222 222 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 8 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045441.
VARIANT 60 60 R -> Q (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035901.
VARIANT 258 258 R -> W (in dbSNP:rs11543211).
/FTId=VAR_048119.
CONFLICT 61 61 E -> R (in Ref. 1; BAA07919).
{ECO:0000305}.
CONFLICT 127 128 LP -> ML (in Ref. 6; AAB88187).
{ECO:0000305}.
CONFLICT 266 266 D -> S (in Ref. 2; AAC41735).
{ECO:0000305}.
CONFLICT 272 272 T -> Q (in Ref. 2; AAC41735).
{ECO:0000305}.
CONFLICT 300 300 I -> M (in Ref. 2; AAC41735).
{ECO:0000305}.
HELIX 322 333 {ECO:0000244|PDB:3KW6}.
STRAND 336 338 {ECO:0000244|PDB:3KW6}.
HELIX 344 349 {ECO:0000244|PDB:3KW6}.
HELIX 356 372 {ECO:0000244|PDB:3KW6}.
STRAND 376 378 {ECO:0000244|PDB:3KW6}.
HELIX 380 391 {ECO:0000244|PDB:3KW6}.
SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK


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