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Database: UniProt
Entry: P48556
LinkDB: P48556
Original site: P48556 
ID   PSMD8_HUMAN             Reviewed;         350 AA.
AC   P48556; B4DX18; Q6P1L7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   02-JUN-2021, entry version 197.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 8;
DE   AltName: Full=26S proteasome regulatory subunit RPN12;
DE   AltName: Full=26S proteasome regulatory subunit S14;
DE   AltName: Full=p31;
GN   Name=PSMD8;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-350.
RC   TISSUE=Muscle, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 71-350.
RX   PubMed=7621825; DOI=10.1002/j.1460-2075.1995.tb07313.x;
RA   Kominami K., DeMartino G.N., Moomaw C., Slaughter C.A., Shimbara N.,
RA   Fujimuro M., Yokosawa H., Hisamatsu H., Tanahashi N., Shimizu Y.,
RA   Tanaka K., Toh-e A.;
RT   "Nin1p, a regulatory subunit of the 26S proteasome, is necessary for
RT   activation of Cdc28p kinase of Saccharomyces cerevisiae.";
RL   EMBO J. 14:3105-3115(1995).
RN   [6]
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   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [11]
RP   INTERACTION WITH DDI2.
RX   PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035;
RA   Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.;
RT   "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome
RT   Integrity.";
RL   Mol. Cell 69:24-35.E5(2018).
RN   [12]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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   [13]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), 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. {ECO:0000269|PubMed:1317798}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits including PSMD8, a base containing 6 ATPases and
CC       few additional components. Interacts with DDI2 (PubMed:29290612).
CC       Interacts with TASOR (By similarity). {ECO:0000250|UniProtKB:Q9CX56,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:29290612}.
CC   -!- INTERACTION:
CC       P48556; P30041: PRDX6; NbExp=3; IntAct=EBI-359304, EBI-2255129;
CC       P48556; Q92529: SHC3; NbExp=3; IntAct=EBI-359304, EBI-79084;
CC   -!- SIMILARITY: Belongs to the proteasome subunit S14 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-64 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62833.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAH01164.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH65006.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA07237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK301771; BAG63230.1; -; mRNA.
DR   EMBL; AC005789; AAC62833.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CH471126; EAW56785.1; -; Genomic_DNA.
DR   EMBL; BC001164; AAH01164.3; ALT_INIT; mRNA.
DR   EMBL; BC065006; AAH65006.2; ALT_INIT; mRNA.
DR   EMBL; D38047; BAA07237.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12515.2; -.
DR   PIR; S56108; S56108.
DR   RefSeq; NP_002803.2; NM_002812.4.
DR   PDB; 5GJQ; EM; 4.50 A; T=1-350.
DR   PDB; 5GJR; EM; 3.50 A; 7/T=1-350.
DR   PDB; 5L4K; EM; 4.50 A; T=1-350.
DR   PDB; 5LN3; EM; 6.80 A; T=1-350.
DR   PDB; 5M32; EM; 3.80 A; r=1-350.
DR   PDB; 5T0C; EM; 3.80 A; Ad/Bd=94-350.
DR   PDB; 5T0G; EM; 4.40 A; d=2-350.
DR   PDB; 5T0H; EM; 6.80 A; d=2-350.
DR   PDB; 5T0I; EM; 8.00 A; d=2-350.
DR   PDB; 5T0J; EM; 8.00 A; d=2-350.
DR   PDB; 5VFP; EM; 4.20 A; d=94-350.
DR   PDB; 5VFQ; EM; 4.20 A; d=94-350.
DR   PDB; 5VFR; EM; 4.90 A; d=94-350.
DR   PDB; 5VFS; EM; 3.60 A; d=94-350.
DR   PDB; 5VFT; EM; 7.00 A; d=94-350.
DR   PDB; 5VFU; EM; 5.80 A; d=94-350.
DR   PDB; 5VGZ; EM; 3.70 A; d=94-350.
DR   PDB; 5VHF; EM; 5.70 A; d=215-350.
DR   PDB; 5VHH; EM; 6.10 A; d=94-350.
DR   PDB; 5VHI; EM; 6.80 A; d=94-350.
DR   PDB; 5VHS; EM; 8.80 A; d=94-350.
DR   PDB; 6MSB; EM; 3.00 A; d=2-350.
DR   PDB; 6MSD; EM; 3.20 A; d=2-350.
DR   PDB; 6MSG; EM; 3.50 A; d=2-350.
DR   PDB; 6MSH; EM; 3.60 A; d=2-350.
DR   PDB; 6MSJ; EM; 3.30 A; d=2-350.
DR   PDB; 6MSK; EM; 3.20 A; d=2-350.
DR   PDB; 6WJD; EM; 4.80 A; d=2-350.
DR   PDB; 6WJN; EM; 5.70 A; d=94-350.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4K; -.
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; 5VHS; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   SMR; P48556; -.
DR   BioGRID; 111686; 121.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P48556; -.
DR   IntAct; P48556; 42.
DR   MINT; P48556; -.
DR   STRING; 9606.ENSP00000215071; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   iPTMnet; P48556; -.
DR   MetOSite; P48556; -.
DR   PhosphoSitePlus; P48556; -.
DR   SwissPalm; P48556; -.
DR   BioMuta; PSMD8; -.
DR   DMDM; 308153477; -.
DR   EPD; P48556; -.
DR   jPOST; P48556; -.
DR   MassIVE; P48556; -.
DR   PaxDb; P48556; -.
DR   PeptideAtlas; P48556; -.
DR   PRIDE; P48556; -.
DR   ProteomicsDB; 55910; -.
DR   Antibodypedia; 1714; 160 antibodies.
DR   DNASU; 5714; -.
DR   Ensembl; ENST00000215071; ENSP00000215071; ENSG00000099341.
DR   Ensembl; ENST00000620216; ENSP00000481136; ENSG00000099341.
DR   GeneID; 5714; -.
DR   KEGG; hsa:5714; -.
DR   CTD; 5714; -.
DR   DisGeNET; 5714; -.
DR   GeneCards; PSMD8; -.
DR   HGNC; HGNC:9566; PSMD8.
DR   HPA; ENSG00000099341; Low tissue specificity.
DR   MIM; 617844; gene.
DR   neXtProt; NX_P48556; -.
DR   OpenTargets; ENSG00000099341; -.
DR   PharmGKB; PA33912; -.
DR   VEuPathDB; HostDB:ENSG00000099341.11; -.
DR   eggNOG; KOG3151; Eukaryota.
DR   GeneTree; ENSGT00390000014682; -.
DR   InParanoid; P48556; -.
DR   OMA; LEIGAFW; -.
DR   OrthoDB; 1183195at2759; -.
DR   PhylomeDB; P48556; -.
DR   TreeFam; TF106233; -.
DR   PathwayCommons; P48556; -.
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-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; P48556; -.
DR   BioGRID-ORCS; 5714; 509 hits in 1007 CRISPR screens.
DR   ChiTaRS; PSMD8; human.
DR   GeneWiki; PSMD8; -.
DR   GenomeRNAi; 5714; -.
DR   Pharos; P48556; Tbio.
DR   PRO; PR:P48556; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P48556; protein.
DR   Bgee; ENSG00000099341; Expressed in gastrocnemius and 246 other tissues.
DR   ExpressionAtlas; P48556; baseline and differential.
DR   Genevisible; P48556; HS.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; ISS:FlyBase.
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:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO: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; IBA:GO_Central.
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:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   InterPro; IPR006746; 26S_Psome_Rpn12.
DR   InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR12387; PTHR12387; 1.
DR   Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isopeptide bond; Phosphoprotein; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..350
FT                   /note="26S proteasome non-ATPase regulatory subunit 8"
FT                   /id="PRO_0000173846"
FT   DOMAIN          162..331
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        297
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
SQ   SEQUENCE   350 AA;  39612 MW;  FF20203213333CB3 CRC64;
     MFIKGRAPRA PPRERRRATR GGLRQVVAPP RALGSTSRPH FRRASVCRRR CRKSGGLLAA
     SRKMAAAAVN GAAGFSSSGP AATSGAVLQA ATGMYEQLKG EWNRKSPNLS KCGEELGRLK
     LVLLELNFLP TTGTKLTKQQ LILARDILEI GAQWSILRKD IPSFERYMAQ LKCYYFDYKE
     QLPESAYMHQ LLGLNLLFLL SQNRVAEFHT ELERLPAKDI QTNVYIKHPV SLEQYLMEGS
     YNKVFLAKGN IPAESYTFFI DILLDTIRDE IAGCIEKAYE KILFTEATRI LFFNTPKKMT
     DYAKKRGWVL GPNNYYSFAS QQQKPEDTTI PSTELAKQVI EYARQLEMIV
//
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