GenomeNet

Database: UniProt
Entry: Q15008
LinkDB: Q15008
Original site: Q15008 
ID   PSMD6_HUMAN             Reviewed;         389 AA.
AC   Q15008; A8K2E0; E9PHI9; Q6UV22;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 198.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 6;
DE   AltName: Full=26S proteasome regulatory subunit RPN7;
DE   AltName: Full=26S proteasome regulatory subunit S10;
DE   AltName: Full=Breast cancer-associated protein SGA-113M;
DE   AltName: Full=Phosphonoformate immuno-associated protein 4;
DE   AltName: Full=Proteasome regulatory particle subunit p44S10;
DE   AltName: Full=p42A;
GN   Name=PSMD6; Synonyms=KIAA0107, PFAAP4;
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).
RC   TISSUE=Mammary cancer;
RX   PubMed=10723133; DOI=10.1038/sj.onc.1203462;
RA   Ren S., Smith M.J., Louro I.D., McKie-Bell P., Bani M.R., Wagner M.,
RA   Zochodne B., Redden D.T., Grizzle W.E., Wang N.D., Smith D.I., Herbst R.A.,
RA   Bardenheuer W., Opalka B., Schutte J., Trent J.M., Ben-David Y.,
RA   Ruppert J.M.;
RT   "The p44S10 locus, encoding a subunit of the proteasome regulatory
RT   particle, is amplified during progression of cutaneous malignant
RT   melanoma.";
RL   Oncogene 19:1419-1427(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Liu Y., Cheng J., Lu Y.;
RT   "Screening and cloning of a new immuno-associated gene regulated by
RT   phosphonoformate.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RC   TISSUE=Testis;
RA   Gu A.H., Wang H., Fang X., Lu L., Xu Z.Y., Xu M., Yin L.L., Li J.M.,
RA   Zhou Z.M., Sha J.H.;
RT   "Cloning of an isoform of KIAA0107 gene related to spermatogenesis.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Petroziello J.M.;
RT   "Breast cancer associated protein.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Bone marrow;
RX   PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA   Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S.,
RA   Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. III. The
RT   coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 2:37-43(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thalamus;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [9]
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph, Ovary, and Placenta;
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   [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   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   [13]
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   [14]
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [15]
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   [16]
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   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-389, 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   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-389, 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 PSMD6, a base containing 6 ATPases and
CC       few additional components. {ECO:0000269|PubMed:27342858,
CC       ECO:0000269|PubMed:27428775}.
CC   -!- INTERACTION:
CC       Q15008; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-359701, EBI-2807956;
CC       Q15008; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-359701, EBI-739467;
CC       Q15008; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-359701, EBI-741480;
CC       Q15008; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-359701, EBI-10173939;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q15008-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q15008-2; Sequence=VSP_047711;
CC       Name=3;
CC         IsoId=Q15008-3; Sequence=VSP_055177;
CC       Name=4;
CC         IsoId=Q15008-4; Sequence=VSP_055178;
CC   -!- SIMILARITY: Belongs to the proteasome subunit S10 family.
CC       {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; AF215935; AAF65540.1; -; mRNA.
DR   EMBL; AF530062; AAQ09946.1; -; mRNA.
DR   EMBL; AY359879; AAQ63402.1; -; mRNA.
DR   EMBL; AY568086; AAS68366.1; -; mRNA.
DR   EMBL; D14663; BAA03497.1; -; mRNA.
DR   EMBL; BX647742; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK290205; BAF82894.1; -; mRNA.
DR   EMBL; AC012557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW65424.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW65427.1; -; Genomic_DNA.
DR   EMBL; BC000630; AAH00630.1; -; mRNA.
DR   EMBL; BC000904; AAH00904.1; -; mRNA.
DR   EMBL; BC012369; AAH12369.1; -; mRNA.
DR   CCDS; CCDS2901.1; -. [Q15008-1]
DR   CCDS; CCDS63677.1; -. [Q15008-4]
DR   CCDS; CCDS63678.1; -. [Q15008-3]
DR   CCDS; CCDS63679.1; -. [Q15008-2]
DR   RefSeq; NP_001258708.1; NM_001271779.1. [Q15008-4]
DR   RefSeq; NP_001258709.1; NM_001271780.1. [Q15008-2]
DR   RefSeq; NP_001258710.1; NM_001271781.1. [Q15008-3]
DR   RefSeq; NP_055629.1; NM_014814.2. [Q15008-1]
DR   PDB; 5GJQ; EM; 4.50 A; R=1-389.
DR   PDB; 5GJR; EM; 3.50 A; 5/R=1-389.
DR   PDB; 5L4K; EM; 4.50 A; R=1-389.
DR   PDB; 5LN3; EM; 6.80 A; R=1-389.
DR   PDB; 5M32; EM; 3.80 A; m=1-389.
DR   PDB; 5T0C; EM; 3.80 A; AY/BY=1-389.
DR   PDB; 5T0G; EM; 4.40 A; Y=1-389.
DR   PDB; 5T0H; EM; 6.80 A; Y=1-389.
DR   PDB; 5T0I; EM; 8.00 A; Y=1-389.
DR   PDB; 5T0J; EM; 8.00 A; Y=1-389.
DR   PDB; 5VFP; EM; 4.20 A; Y=12-389.
DR   PDB; 5VFQ; EM; 4.20 A; Y=12-389.
DR   PDB; 5VFR; EM; 4.90 A; Y=12-389.
DR   PDB; 5VFS; EM; 3.60 A; Y=12-389.
DR   PDB; 5VFT; EM; 7.00 A; Y=12-389.
DR   PDB; 5VFU; EM; 5.80 A; Y=12-389.
DR   PDB; 5VGZ; EM; 3.70 A; Y=12-389.
DR   PDB; 5VHF; EM; 5.70 A; Y=12-389.
DR   PDB; 5VHH; EM; 6.10 A; Y=12-389.
DR   PDB; 5VHI; EM; 6.80 A; Y=12-389.
DR   PDB; 5VHS; EM; 8.80 A; Y=12-389.
DR   PDB; 6MSB; EM; 3.00 A; Y=1-389.
DR   PDB; 6MSD; EM; 3.20 A; Y=1-389.
DR   PDB; 6MSG; EM; 3.50 A; Y=1-389.
DR   PDB; 6MSH; EM; 3.60 A; Y=1-389.
DR   PDB; 6MSJ; EM; 3.30 A; Y=1-389.
DR   PDB; 6MSK; EM; 3.20 A; Y=1-389.
DR   PDB; 6WJD; EM; 4.80 A; Y=1-389.
DR   PDB; 6WJN; EM; 5.70 A; Y=12-389.
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; Q15008; -.
DR   BioGRID; 115195; 169.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; Q15008; -.
DR   DIP; DIP-27590N; -.
DR   IntAct; Q15008; 66.
DR   MINT; Q15008; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   iPTMnet; Q15008; -.
DR   MetOSite; Q15008; -.
DR   PhosphoSitePlus; Q15008; -.
DR   SwissPalm; Q15008; -.
DR   BioMuta; PSMD6; -.
DR   DMDM; 2494625; -.
DR   EPD; Q15008; -.
DR   jPOST; Q15008; -.
DR   MassIVE; Q15008; -.
DR   MaxQB; Q15008; -.
DR   PaxDb; Q15008; -.
DR   PeptideAtlas; Q15008; -.
DR   PRIDE; Q15008; -.
DR   ProteomicsDB; 20548; -.
DR   ProteomicsDB; 60360; -. [Q15008-1]
DR   ProteomicsDB; 67429; -.
DR   TopDownProteomics; Q15008-1; -. [Q15008-1]
DR   Antibodypedia; 31765; 288 antibodies.
DR   DNASU; 9861; -.
DR   Ensembl; ENST00000295901; ENSP00000295901; ENSG00000163636. [Q15008-1]
DR   Ensembl; ENST00000394431; ENSP00000377952; ENSG00000163636. [Q15008-2]
DR   Ensembl; ENST00000482510; ENSP00000419227; ENSG00000163636. [Q15008-3]
DR   Ensembl; ENST00000492933; ENSP00000418695; ENSG00000163636. [Q15008-4]
DR   GeneID; 9861; -.
DR   KEGG; hsa:9861; -.
DR   UCSC; uc003dma.3; human. [Q15008-1]
DR   CTD; 9861; -.
DR   DisGeNET; 9861; -.
DR   GeneCards; PSMD6; -.
DR   HGNC; HGNC:9564; PSMD6.
DR   HPA; ENSG00000163636; Low tissue specificity.
DR   MIM; 617857; gene.
DR   neXtProt; NX_Q15008; -.
DR   OpenTargets; ENSG00000163636; -.
DR   PharmGKB; PA33910; -.
DR   VEuPathDB; HostDB:ENSG00000163636.10; -.
DR   GeneTree; ENSGT00510000046608; -.
DR   HOGENOM; CLU_031814_0_0_1; -.
DR   InParanoid; Q15008; -.
DR   OMA; VDYIDQE; -.
DR   OrthoDB; 1194691at2759; -.
DR   PhylomeDB; Q15008; -.
DR   TreeFam; TF313819; -.
DR   PathwayCommons; Q15008; -.
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; Q15008; -.
DR   BioGRID-ORCS; 9861; 775 hits in 1000 CRISPR screens.
DR   ChiTaRS; PSMD6; human.
DR   GeneWiki; PSMD6; -.
DR   GenomeRNAi; 9861; -.
DR   Pharos; Q15008; Tbio.
DR   PRO; PR:Q15008; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q15008; protein.
DR   Bgee; ENSG00000163636; Expressed in body of pancreas and 243 other tissues.
DR   ExpressionAtlas; Q15008; baseline and differential.
DR   Genevisible; Q15008; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; IBA:GO_Central.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0016887; F:ATPase activity; NAS:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
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: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:0006508; P:proteolysis; NAS:UniProtKB.
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; IPR000717; PCI_dom.
DR   InterPro; IPR035268; PSMD6.
DR   InterPro; IPR019585; Rpn7/CSN1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR14145:SF1; PTHR14145:SF1; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF10602; RPN7; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Proteasome; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..389
FT                   /note="26S proteasome non-ATPase regulatory subunit 6"
FT                   /id="PRO_0000173838"
FT   DOMAIN          193..361
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   VAR_SEQ         1..49
FT                   /note="MPLENLEEEGLPKNPDLRIAQLRFLLSLPEHRGDAAVRDELMAAVRDNN ->
FT                   MNESNDSTNYD (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_047711"
FT   VAR_SEQ         10..49
FT                   /note="GLPKNPDLRIAQLRFLLSLPEHRGDAAVRDELMAAVRDNN -> D (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_055177"
FT   VAR_SEQ         49
FT                   /note="N -> NFWNRIRQEQTEDCPPSSPSRGWHCQDWPSRKPPTSIRLCFAKPIIK
FT                   RHRMPSY (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_055178"
SQ   SEQUENCE   389 AA;  45531 MW;  8843E6684AE91ACD CRC64;
     MPLENLEEEG LPKNPDLRIA QLRFLLSLPE HRGDAAVRDE LMAAVRDNNM APYYEALCKS
     LDWQIDVDLL NKMKKANEDE LKRLDEELED AEKNLGESEI RDAMMAKAEY LCRIGDKEGA
     LTAFRKTYDK TVALGHRLDI VFYLLRIGLF YMDNDLITRN TEKAKSLIEE GGDWDRRNRL
     KVYQGLYCVA IRDFKQAAEL FLDTVSTFTS YELMDYKTFV TYTVYVSMIA LERPDLREKV
     IKGAEILEVL HSLPAVRQYL FSLYECRYSV FFQSLAVVEQ EMKKDWLFAP HYRYYVREMR
     IHAYSQLLES YRSLTLGYMA EAFGVGVEFI DQELSRFIAA GRLHCKIDKV NEIVETNRPD
     SKNWQYQETI KKGDLLLNRV QKLSRVINM
//
DBGET integrated database retrieval system