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26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)

 PSMD4_HUMAN             Reviewed;         377 AA.
P55036; D3DV16; Q5VWC5; Q9NS92;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
07-APR-2021, entry version 213.
RecName: Full=26S proteasome non-ATPase regulatory subunit 4;
AltName: Full=26S proteasome regulatory subunit RPN10;
AltName: Full=26S proteasome regulatory subunit S5A;
AltName: Full=Antisecretory factor 1;
Short=AF;
Short=ASF;
AltName: Full=Multiubiquitin chain-binding protein;
Name=PSMD4; Synonyms=MCB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-75 AND 130-140.
TISSUE=Pituitary;
PubMed=7657640; DOI=10.1074/jbc.270.35.20615;
Johansson E., Loennroth I., Lange S., Jonson I., Jennische E.,
Loennroth C.;
"Molecular cloning and expression of a pituitary gland protein modulating
intestinal fluid secretion.";
J. Biol. Chem. 270:20615-20620(1995).
[2]
SEQUENCE REVISION.
Loennroth I.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8641424; DOI=10.1016/0014-5793(96)00101-9;
Ferrell K., Deveraux Q., van Nocker S., Rechsteiner M.;
"Molecular cloning and expression of a multiubiquitin chain binding subunit
of the human 26S protease.";
FEBS Lett. 381:143-148(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Fetal brain;
PubMed=10921894; DOI=10.1093/emboj/19.15.4144;
Kawahara H., Kasahara M., Nishiyama A., Ohsumi K., Goto T., Kishimoto T.,
Saeki Y., Yokosawa H., Shimbara N., Murata S., Chiba T., Suzuki K.,
Tanaka K.;
"Developmentally regulated, alternative splicing of the Rpn10 gene
generates multiple forms of 26S proteasomes.";
EMBO J. 19:4144-4153(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Lung;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 70-377.
TISSUE=Brain;
Fraser P.E., Levesque G., Rogaeva E.A., Yu G., St George-Hyslop P.H.;
"Proteolysis of presenilin 1 is associated with the 26S proteasome and is
altered in Alzheimer's disease.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[9]
CHARACTERIZATION.
PubMed=3524692; DOI=10.1016/0304-4165(86)90144-3;
Loennroth I., Lange S.;
"Purification and characterization of the antisecretory factor: a protein
in the central nervous system and in the gut which inhibits intestinal
hypersecretion induced by cholera toxin.";
Biochim. Biophys. Acta 883:138-144(1986).
[10]
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).
[11]
POLYUBIQUITIN BINDING SITES.
PubMed=9488668; DOI=10.1074/jbc.273.10.5461;
Young P., Deveraux Q., Beal R.E., Pickart C.M., Rechsteiner M.;
"Characterization of two polyubiquitin binding sites in the 26 S protease
subunit 5a.";
J. Biol. Chem. 273:5461-5467(1998).
[12]
INTERACTION WITH NUB1.
PubMed=11585840; DOI=10.1074/jbc.m108636200;
Kamitani T., Kito K., Fukuda-Kamitani T., Yeh E.T.H.;
"Targeting of NEDD8 and its conjugates for proteasomal degradation by
NUB1.";
J. Biol. Chem. 276:46655-46660(2001).
[13]
INTERACTION WITH UBQLN1.
PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
"Ubiquilin interacts with ubiquitylated proteins and proteasome through its
ubiquitin-associated and ubiquitin-like domains.";
FEBS Lett. 566:110-114(2004).
[14]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[15]
INTERACTION WITH UBQLN4.
PubMed=15280365; DOI=10.1074/jbc.m406284200;
Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.;
"The effects of the polyglutamine repeat protein ataxin-1 on the UbL-UBA
protein A1Up.";
J. Biol. Chem. 279:42290-42301(2004).
[16]
INTERACTION WITH SQSTM1.
PubMed=15340068; DOI=10.1128/mcb.24.18.8055-8068.2004;
Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
Wooten M.W.;
"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in
ubiquitin proteasome degradation.";
Mol. Cell. Biol. 24:8055-8068(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-361, AND
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
INTERACTION WITH UBE3A.
PubMed=22645313; DOI=10.1128/mcb.00201-12;
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M.,
Harper J.W., Howley P.M.;
"Identification and proteomic analysis of distinct UBE3A/E6AP protein
complexes.";
Mol. Cell. Biol. 32:3095-3106(2012).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-358 AND SER-361, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[26]
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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
INTERACTION WITH DDI2.
PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035;
Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.;
"Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome
Integrity.";
Mol. Cell 69:24-35.E5(2018).
[29]
STRUCTURE BY NMR OF 263-306 IN COMPLEX WITH HR23A UBIQUITIN-LIKE DOMAIN.
PubMed=12970176; DOI=10.1093/emboj/cdg467;
Mueller T.D., Feigon J.;
"Structural determinants for the binding of ubiquitin-like domains to the
proteasome.";
EMBO J. 22:4634-4645(2003).
[30]
STRUCTURE BY NMR OF 260-307 IN COMPLEX WITH HR23B UBIQUITIN-LIKE DOMAIN.
PubMed=14585839; DOI=10.1074/jbc.m309448200;
Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C.,
Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.;
"Structure of the ubiquitin-interacting motif of S5a bound to the
ubiquitin-like domain of HR23B.";
J. Biol. Chem. 279:4760-4767(2004).
[31]
STRUCTURE BY NMR OF 192-306, FUNCTION, AND DOMAIN.
PubMed=15826667; DOI=10.1016/j.jmb.2005.03.007;
Wang Q., Young P., Walters K.J.;
"Structure of S5a bound to monoubiquitin provides a model for polyubiquitin
recognition.";
J. Mol. Biol. 348:727-739(2005).
[32]
STRUCTURE BY NMR OF 196-306, AND DOMAIN.
PubMed=19683493; DOI=10.1016/j.molcel.2009.06.010;
Zhang N., Wang Q., Ehlinger A., Randles L., Lary J.W., Kang Y.,
Haririnia A., Storaska A.J., Cole J.L., Fushman D., Walters K.J.;
"Structure of the s5a:k48-linked diubiquitin complex and its interactions
with rpn13.";
Mol. Cell 35:280-290(2009).
[33]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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).
[34]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), 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. PSMD4 acts as an ubiquitin receptor subunit through ubiquitin-
interacting motifs and selects ubiquitin-conjugates for destruction.
Displays a preferred selectivity for longer polyubiquitin chains.
{ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:15826667}.
-!- 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 and few additional
components including PSMD4 (PubMed:27428775, PubMed:27342858).
Interacts with NUB1 (PubMed:11585840). Interacts with SQSTM1
(PubMed:15340068). Interacts with UBQLN4 (PubMed:15280365). Interacts
with UBE3A (PubMed:22645313). Interacts with UBQLN1 (via ubiquitin-like
domain) (PubMed:15147878). Interacts with DDI2 (PubMed:29290612).
{ECO:0000269|PubMed:11585840, ECO:0000269|PubMed:12970176,
ECO:0000269|PubMed:14585839, ECO:0000269|PubMed:15147878,
ECO:0000269|PubMed:15280365, ECO:0000269|PubMed:15340068,
ECO:0000269|PubMed:22645313, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:29290612}.
-!- INTERACTION:
P55036; Q16186: ADRM1; NbExp=5; IntAct=EBI-359318, EBI-954387;
P55036; P42858: HTT; NbExp=5; IntAct=EBI-359318, EBI-466029;
P55036; P28066: PSMA5; NbExp=2; IntAct=EBI-359318, EBI-355475;
P55036; P62191: PSMC1; NbExp=2; IntAct=EBI-359318, EBI-357598;
P55036; P62195: PSMC5; NbExp=2; IntAct=EBI-359318, EBI-357745;
P55036; O00232: PSMD12; NbExp=2; IntAct=EBI-359318, EBI-359733;
P55036; Q13200: PSMD2; NbExp=3; IntAct=EBI-359318, EBI-357648;
P55036; P55036: PSMD4; NbExp=3; IntAct=EBI-359318, EBI-359318;
P55036; P54725: RAD23A; NbExp=15; IntAct=EBI-359318, EBI-746453;
P55036; P54727: RAD23B; NbExp=11; IntAct=EBI-359318, EBI-954531;
P55036; P0DPB3: SCHIP1; NbExp=2; IntAct=EBI-359318, EBI-1397509;
P55036; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-359318, EBI-1752330;
P55036; Q9NUJ3: TCP11L1; NbExp=5; IntAct=EBI-359318, EBI-2555179;
P55036; P0CG48: UBC; NbExp=4; IntAct=EBI-359318, EBI-3390054;
P55036; Q05086: UBE3A; NbExp=3; IntAct=EBI-359318, EBI-954357;
P55036; Q05086-2: UBE3A; NbExp=3; IntAct=EBI-359318, EBI-10175863;
P55036; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-359318, EBI-741480;
P55036; Q9Y5K5: UCHL5; NbExp=5; IntAct=EBI-359318, EBI-1051183;
P55036; P24610: Pax3; Xeno; NbExp=3; IntAct=EBI-359318, EBI-1208116;
P55036; Q62921: Rbck1; Xeno; NbExp=3; IntAct=EBI-359318, EBI-7266339;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=Rpn10A;
IsoId=P55036-1; Sequence=Displayed;
Name=Rpn10E;
IsoId=P55036-2; Sequence=VSP_005291, VSP_005292;
-!- DOMAIN: The 2 UIM motifs are involved in the binding to a multi-
ubiquitin chain in a cooperative way. {ECO:0000269|PubMed:15826667,
ECO:0000269|PubMed:19683493}.
-!- MISCELLANEOUS: [Isoform Rpn10E]: May be produced at very low levels due
to a premature stop codon in the mRNA, leading to nonsense-mediated
mRNA decay. {ECO:0000305}.
-!- SIMILARITY: Belongs to the proteasome subunit S5A family.
{ECO:0000305}.
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EMBL; U51007; AAC50433.1; -; mRNA.
EMBL; U24704; AAB54057.1; -; mRNA.
EMBL; AB033605; BAA97581.1; -; mRNA.
EMBL; AL391069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL592424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53457.1; -; Genomic_DNA.
EMBL; CH471121; EAW53458.1; -; Genomic_DNA.
EMBL; BC002365; AAH02365.1; -; mRNA.
EMBL; BC072008; AAH72008.1; -; mRNA.
EMBL; U72664; AAB68598.1; -; mRNA.
CCDS; CCDS991.1; -. [P55036-1]
PIR; S63671; S63671.
RefSeq; NP_002801.1; NM_002810.2. [P55036-1]
PDB; 1P9C; NMR; -; A=263-307.
PDB; 1P9D; NMR; -; S=263-307.
PDB; 1UEL; NMR; -; B=263-307.
PDB; 1YX4; NMR; -; A=196-306.
PDB; 1YX5; NMR; -; A=192-306.
PDB; 1YX6; NMR; -; A=196-306.
PDB; 2KDE; NMR; -; A=196-306.
PDB; 2KDF; NMR; -; A=196-306.
PDB; 5GJQ; EM; 4.50 A; W=1-377.
PDB; 5GJR; EM; 3.50 A; AA/W=1-377.
PDB; 5L4K; EM; 4.50 A; W=1-377.
PDB; 5LN3; EM; 6.80 A; W=1-377.
PDB; 5M32; EM; 3.80 A; p=1-377.
PDB; 5T0C; EM; 3.80 A; Ab/Bb=1-377.
PDB; 5T0G; EM; 4.40 A; b=1-377.
PDB; 5T0H; EM; 6.80 A; b=1-377.
PDB; 5T0I; EM; 8.00 A; b=1-377.
PDB; 5T0J; EM; 8.00 A; b=1-377.
PDB; 5VFP; EM; 4.20 A; b=1-191.
PDB; 5VFQ; EM; 4.20 A; b=1-191.
PDB; 5VFR; EM; 4.90 A; b=1-191.
PDB; 5VFS; EM; 3.60 A; b=1-191.
PDB; 5VFT; EM; 7.00 A; b=1-191.
PDB; 5VFU; EM; 5.80 A; b=1-191.
PDB; 5VGZ; EM; 3.70 A; b=1-191.
PDB; 5VHF; EM; 5.70 A; b=1-191.
PDB; 5VHH; EM; 6.10 A; b=1-191.
PDB; 5VHI; EM; 6.80 A; b=1-191.
PDB; 5VHS; EM; 8.80 A; b=1-191.
PDB; 6MSB; EM; 3.00 A; b=1-377.
PDB; 6MSD; EM; 3.20 A; b=1-377.
PDB; 6MSE; EM; 3.30 A; H/h=286-362.
PDB; 6MSG; EM; 3.50 A; b=1-377.
PDB; 6MSH; EM; 3.60 A; b=1-377.
PDB; 6MSJ; EM; 3.30 A; b=1-377.
PDB; 6MSK; EM; 3.20 A; b=1-377.
PDB; 6MUN; NMR; -; A=196-306.
PDB; 6U19; NMR; -; A=305-377.
PDB; 6WJD; EM; 4.80 A; b=1-377.
PDB; 6WJN; EM; 5.70 A; b=1-191.
PDBsum; 1P9C; -.
PDBsum; 1P9D; -.
PDBsum; 1UEL; -.
PDBsum; 1YX4; -.
PDBsum; 1YX5; -.
PDBsum; 1YX6; -.
PDBsum; 2KDE; -.
PDBsum; 2KDF; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
PDBsum; 6MSB; -.
PDBsum; 6MSD; -.
PDBsum; 6MSE; -.
PDBsum; 6MSG; -.
PDBsum; 6MSH; -.
PDBsum; 6MSJ; -.
PDBsum; 6MSK; -.
PDBsum; 6MUN; -.
PDBsum; 6U19; -.
PDBsum; 6WJD; -.
PDBsum; 6WJN; -.
BMRB; P55036; -.
SMR; P55036; -.
BioGRID; 111683; 284.
ComplexPortal; CPX-5993; 26S Proteasome complex.
CORUM; P55036; -.
DIP; DIP-38189N; -.
IntAct; P55036; 110.
MINT; P55036; -.
STRING; 9606.ENSP00000357879; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; P55036; -.
MetOSite; P55036; -.
PhosphoSitePlus; P55036; -.
BioMuta; PSMD4; -.
DMDM; 1709796; -.
EPD; P55036; -.
jPOST; P55036; -.
MassIVE; P55036; -.
MaxQB; P55036; -.
PaxDb; P55036; -.
PeptideAtlas; P55036; -.
PRIDE; P55036; -.
ProteomicsDB; 56762; -. [P55036-1]
ProteomicsDB; 56763; -. [P55036-2]
Antibodypedia; 20322; 426 antibodies.
CPTC; P55036; 3 antibodies.
DNASU; 5710; -.
Ensembl; ENST00000368884; ENSP00000357879; ENSG00000159352. [P55036-1]
GeneID; 5710; -.
KEGG; hsa:5710; -.
UCSC; uc001exl.4; human. [P55036-1]
CTD; 5710; -.
DisGeNET; 5710; -.
GeneCards; PSMD4; -.
HGNC; HGNC:9561; PSMD4.
HPA; ENSG00000159352; Low tissue specificity.
MIM; 601648; gene.
neXtProt; NX_P55036; -.
OpenTargets; ENSG00000159352; -.
PharmGKB; PA33907; -.
VEuPathDB; HostDB:ENSG00000159352.15; -.
eggNOG; KOG2884; Eukaryota.
GeneTree; ENSGT00530000064050; -.
HOGENOM; CLU_033293_0_1_1; -.
InParanoid; P55036; -.
PhylomeDB; P55036; -.
TreeFam; TF106232; -.
PathwayCommons; P55036; -.
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-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 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-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
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-8939902; Regulation of RUNX2 expression and activity.
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-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
BioGRID-ORCS; 5710; 706 hits in 1005 CRISPR screens.
ChiTaRS; PSMD4; human.
EvolutionaryTrace; P55036; -.
GeneWiki; PSMD4; -.
GenomeRNAi; 5710; -.
Pharos; P55036; Tbio.
PRO; PR:P55036; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P55036; protein.
Bgee; ENSG00000159352; Expressed in testis and 245 other tissues.
ExpressionAtlas; P55036; baseline and differential.
Genevisible; P55036; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
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:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
GO; GO:0043248; P:proteasome assembly; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
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:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DisProt; DP01192; -.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR003903; UIM_dom.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF02809; UIM; 2.
Pfam; PF13519; VWA_2; 1.
SMART; SM00726; UIM; 2.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50330; UIM; 2.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Direct protein sequencing;
Isopeptide bond; Phosphoprotein; Proteasome; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1..377
/note="26S proteasome non-ATPase regulatory subunit 4"
/id="PRO_0000173828"
DOMAIN 5..188
/note="VWFA"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
DOMAIN 211..230
/note="UIM 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
DOMAIN 282..301
/note="UIM 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
REGION 197..262
/note="Interaction with UBQLN1"
/evidence="ECO:0000269|PubMed:15147878"
REGION 216..220
/note="Essential for ubiquitin-binding"
REGION 287..291
/note="Essential for ubiquitin-binding"
COMPBIAS 238..246
/note="Poly-Ala"
MOD_RES 250
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O35226"
MOD_RES 253
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:O35226"
MOD_RES 256
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O35226"
MOD_RES 266
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17525332,
ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 358
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:23186163"
MOD_RES 361
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17323924,
ECO:0007744|PubMed:23186163"
CROSSLNK 122
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
VAR_SEQ 255..268
/note="DSDDALLKMTISQQ -> GERGGIRSPGTAGC (in isoform
Rpn10E)"
/evidence="ECO:0000305"
/id="VSP_005291"
VAR_SEQ 269..377
/note="Missing (in isoform Rpn10E)"
/evidence="ECO:0000305"
/id="VSP_005292"
TURN 197..199
/evidence="ECO:0007744|PDB:6MUN"
STRAND 201..203
/evidence="ECO:0007744|PDB:1YX4"
STRAND 205..208
/evidence="ECO:0007744|PDB:2KDE"
HELIX 210..212
/evidence="ECO:0007744|PDB:1YX4"
HELIX 214..244
/evidence="ECO:0007744|PDB:1YX4"
STRAND 245..249
/evidence="ECO:0007744|PDB:1YX4"
STRAND 268..270
/evidence="ECO:0007744|PDB:1P9C"
STRAND 273..275
/evidence="ECO:0007744|PDB:1P9C"
HELIX 278..294
/evidence="ECO:0007744|PDB:1P9C"
STRAND 296..300
/evidence="ECO:0007744|PDB:1P9C"
STRAND 302..304
/evidence="ECO:0007744|PDB:2KDE"
TURN 309..313
/evidence="ECO:0007744|PDB:6U19"
HELIX 322..325
/evidence="ECO:0007744|PDB:6U19"
HELIX 328..330
/evidence="ECO:0007744|PDB:6U19"
HELIX 332..341
/evidence="ECO:0007744|PDB:6U19"
HELIX 350..363
/evidence="ECO:0007744|PDB:6U19"
SEQUENCE 377 AA; 40737 MW; EC712EC4DB1CE9AB CRC64;
MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV
LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN
EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA
DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA
ASAAEAGIAT TGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF
GQAESADIDA SSAMDTSEPA KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE AIRNAMGSLA
SQATKDGKKD KKEEDKK


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EIAAB32851 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,AF,Antisecretory factor 1,ASF,Homo sapiens,Human,MCB1,Multiubiquitin chain-
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EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32798 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Homo sapiens,Human,PSMD13
EIAAB32789 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Homo sapiens,Human,PSMD11
EIAAB32858 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Breast cancer-associated protein SGA-113M,Homo sapiens,Human,KIAA0107,p42A,P
EIAAB32842 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Homo sapiens,Human,PSMD1
EIAAB32841 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Psmd1,Rat,Rattus norvegicus
EIAAB32848 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Homo sapiens,Human,Proteasome subunit p58,PSMD3
EIAAB32796 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Psmd13,Rat,Rattus norvegicus
EIAAB32799 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Bos taurus,Bovine,PSMD13
EIAAB32791 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Mouse,Mus musculus,Psmd11
EIAAB32797 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Mouse,Mus musculus,Psmd13
EIAAB32807 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Mouse,Mov34,Mov-34,Mov34 protein,Mus musculus,Proteasome subunit p40,Psmd7
EIAAB32844 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Mouse,Mus musculus,Psmd2
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
EIAAB32862 26S proteasome non-ATPase regulatory subunit 8,26S proteasome regulatory subunit RPN12,26S proteasome regulatory subunit S14,Homo sapiens,Human,p31,PSMD8
EIAAB32859 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Mouse,Mus musculus,p42A,Psmd6
EIAAB32853 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,Bos taurus,Bovine,PSMD4
15-288-22830 26S proteasome non-ATPase regulatory subunit 1 - 26S proteasome regulatory subunit RPN2; 26S proteasome regulatory subunit S1; 26S proteasome subunit p112 Polyclonal 0.1 mg
Pathways :
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1691: Proteasome
WP158: Proteasome Degradation
WP1694: Pyrimidine metabolism
WP1626: Benzoate degradation via CoA ligation
WP1644: DNA replication
WP470: Proteasome Degradation
WP1493: Carbon assimilation C4 pathway
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP1693: Purine metabolism
WP1909: Signal regulatory protein (SIRP) family interactions
WP1614: 1- and 2-Methylnaphthalene degradation
WP1663: Homologous recombination
WP1672: Mismatch repair
WP1655: Geraniol degradation
WP519: Proteasome Degradation
WP1079: Proteasome Degradation
WP1671: Methane metabolism
WP1711: Trinitrotoluene degradation
WP267: Proteasome Degradation
WP1718: Vitamin B6 metabolism
WP1680: Oxidative phosphorylation
WP183: Proteasome Degradation

Related Genes :
[PSMD4 MCB1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)
[RPN10 MBP1 MCB1 At4g38630 F20M13.190 T9A14.7] 26S proteasome non-ATPase regulatory subunit 4 homolog (26S proteasome regulatory subunit RPN10) (AtRPN10) (26S proteasome regulatory subunit S5A homolog) (Multiubiquitin chain-binding protein 1) (AtMCB1)
[Psmd4 Mcb1] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Multiubiquitin chain-binding protein)
[Rpn10 PROS-54 Pros54 CG7619] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (54 kDa subunit of mu particle) (Multiubiquitin chain-binding protein) (p54)
[RPN10 MCB1 SUN1 YHR200W] 26S proteasome regulatory subunit RPN10
[PSMD2 TRAP2] 26S proteasome non-ATPase regulatory subunit 2 (26S proteasome regulatory subunit RPN1) (26S proteasome regulatory subunit S2) (26S proteasome subunit p97) (Protein 55.11) (Tumor necrosis factor type 1 receptor-associated protein 2)
[PSMD6 KIAA0107 PFAAP4] 26S proteasome non-ATPase regulatory subunit 6 (26S proteasome regulatory subunit RPN7) (26S proteasome regulatory subunit S10) (Breast cancer-associated protein SGA-113M) (Phosphonoformate immuno-associated protein 4) (Proteasome regulatory particle subunit p44S10) (p42A)
[PSMC4 MIP224 TBP7] 26S proteasome regulatory subunit 6B (26S proteasome AAA-ATPase subunit RPT3) (MB67-interacting protein) (MIP224) (Proteasome 26S subunit ATPase 4) (Tat-binding protein 7) (TBP-7)
[RPT5A ATS6A.2 TBP1 At3g05530 F22F7.1] 26S proteasome regulatory subunit 6A homolog A (26S proteasome AAA-ATPase subunit RPT5a) (Proteasome 26S subunit 6A homolog A) (Regulatory particle triple-A ATPase subunit 5a) (Tat-binding protein 1 homolog A) (TBP-1 homolog A)
[PSMD3] 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit RPN3) (26S proteasome regulatory subunit S3) (Proteasome subunit p58)
[RPT5B TBP1 At1g09100 F7G19.2] 26S proteasome regulatory subunit 6A homolog B (26S proteasome AAA-ATPase subunit RPT5b) (Proteasome 26S subunit 6A homolog B) (Regulatory particle triple-A ATPase subunit 5b) (Tat-binding protein 1 homolog B) (TBP-1 homolog B)
[RPT2A HLR At4g29040 F19B15.70 F25O24.6] 26S proteasome regulatory subunit 4 homolog A (26S proteasome AAA-ATPase subunit RPT2a) (26S proteasome subunit 4 homolog A) (Protein HALTED ROOT) (Regulatory particle triple-A ATPase subunit 2a)
[PSMD13] 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5)
[PSMD11] 26S proteasome non-ATPase regulatory subunit 11 (26S proteasome regulatory subunit RPN6) (26S proteasome regulatory subunit S9) (26S proteasome regulatory subunit p44.5)
[PSMC3 TBP1] 26S proteasome regulatory subunit 6A (26S proteasome AAA-ATPase subunit RPT5) (Proteasome 26S subunit ATPase 3) (Proteasome subunit P50) (Tat-binding protein 1) (TBP-1)
[PSMD1] 26S proteasome non-ATPase regulatory subunit 1 (26S proteasome regulatory subunit RPN2) (26S proteasome regulatory subunit S1) (26S proteasome subunit p112)
[PSMC5 SUG1] 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)
[rpn-10 B0205.3] 26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit rpn-10)
[RPT2B At2g20140 T2G17.6] 26S proteasome regulatory subunit 4 homolog B (26S proteasome AAA-ATPase subunit RPT2b) (26S proteasome subunit 4 homolog B) (Regulatory particle triple-A ATPase subunit 2b)
[PSMC6 SUG2] 26S proteasome regulatory subunit 10B (26S proteasome AAA-ATPase subunit RPT4) (Proteasome 26S subunit ATPase 6) (Proteasome subunit p42)
[PSMC1] 26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)
[PSMD14 POH1] 26S proteasome non-ATPase regulatory subunit 14 (EC 3.4.19.-) (26S proteasome regulatory subunit RPN11) (26S proteasome-associated PAD1 homolog 1)
[Psmc5 Sug1] 26S proteasome regulatory subunit 8 (26S proteasome AAA-ATPase subunit RPT6) (Proteasome 26S subunit ATPase 5) (Proteasome subunit p45) (p45/SUG) (mSUG1)
[RPN1A At2g20580 F23N11.10] 26S proteasome non-ATPase regulatory subunit 2 homolog A (26S proteasome regulatory subunit RPN1a) (AtRPN1a) (26S proteasome regulatory subunit S2 homolog A)
[RPN12A At1g64520 F1N19.9] 26S proteasome non-ATPase regulatory subunit 8 homolog A (26S proteasome regulatory subunit RPN12a) (AtRPN12a) (26S proteasome regulatory subunit S14 homolog A)
[PSMD7 MOV34L] 26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)
[Psmc5 Sug1] 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)
[PSMC2 MSS1] 26S proteasome regulatory subunit 7 (26S proteasome AAA-ATPase subunit RPT1) (Proteasome 26S subunit ATPase 2) (Protein MSS1)
[PSMD12] 26S proteasome non-ATPase regulatory subunit 12 (26S proteasome regulatory subunit RPN5) (26S proteasome regulatory subunit p55)
[PSMD8] 26S proteasome non-ATPase regulatory subunit 8 (26S proteasome regulatory subunit RPN12) (26S proteasome regulatory subunit S14) (p31)

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