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26S proteasome regulatory subunit 4 (P26s4) (26S proteasome AAA-ATPase subunit RPT2) (Proteasome 26S subunit ATPase 1)

 PRS4_HUMAN              Reviewed;         440 AA.
P62191; B4DR63; P49014; Q03527; Q6IAW0; Q6NW36; Q96AZ3;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=26S proteasome regulatory subunit 4;
Short=P26s4;
AltName: Full=26S proteasome AAA-ATPase subunit RPT2;
AltName: Full=Proteasome 26S subunit ATPase 1;
Name=PSMC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=1429620;
Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.;
"Subunit 4 of the 26 S protease is a member of a novel eukaryotic
ATPase family.";
J. Biol. Chem. 267:22699-22702(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Brain, Lung, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
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).
[7]
INTERACTION WITH SCA7.
PubMed=11734547; DOI=10.1093/hmg/10.24.2821;
Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A.,
van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.;
"Association of ataxin-7 with the proteasome subunit S4 of the 19S
regulatory complex.";
Hum. Mol. Genet. 10:2821-2831(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
INTERACTION WITH NGLY1.
PubMed=15358861; DOI=10.1073/pnas.0405663101;
Katiyar S., Li G., Lennarz W.J.;
"A complex between peptide:N-glycanase and two proteasome-linked
proteins suggests a mechanism for the degradation of misfolded
glycoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
[10]
INTERACTION WITH PAAF1.
PubMed=15831487; DOI=10.1128/MCB.25.9.3842-3853.2005;
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
"Proteasomal ATPase-associated factor 1 negatively regulates
proteasome activity by interacting with proteasomal ATPases.";
Mol. Cell. Biol. 25:3842-3853(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=17370265; DOI=10.1002/pmic.200600410;
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
"Tryptic digestion of ubiquitin standards reveals an improved strategy
for identifying ubiquitinated proteins by mass spectrometry.";
Proteomics 7:868-874(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-258, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
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).
[16]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53 AND THR-434, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53, AND 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).
[19]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[20]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25807930; DOI=10.1002/anie.201500342;
Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J.,
Magee A.I., Tate E.W.;
"Multifunctional reagents for quantitative proteome-wide analysis of
protein modification in human cells and dynamic profiling of protein
lipidation during vertebrate development.";
Angew. Chem. Int. Ed. 54:5948-5951(2015).
[21]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, AND
SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, AND
SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair. PSMC1 belongs to the
heterohexameric ring of AAA (ATPases associated with diverse
cellular activities) proteins that unfolds ubiquitinated target
proteins that are concurrently translocated into a proteolytic
chamber and degraded into peptides. {ECO:0000269|PubMed:1317798}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits, a base containing 6 ATPases
including PSMC1 and few additional components (PubMed:27428775,
PubMed:27342858). Interacts with SCA7 (PubMed:11734547). Interacts
with NGLY1 (PubMed:15358861). Interacts with PAAF1
(PubMed:15831487). {ECO:0000269|PubMed:11734547,
ECO:0000269|PubMed:15358861, ECO:0000269|PubMed:15831487,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
O60341:KDM1A; NbExp=2; IntAct=EBI-357598, EBI-710124;
P50222:MEOX2; NbExp=3; IntAct=EBI-357598, EBI-748397;
P35998:PSMC2; NbExp=5; IntAct=EBI-357598, EBI-359710;
P43686:PSMC4; NbExp=2; IntAct=EBI-357598, EBI-743997;
P62333:PSMC6; NbExp=4; IntAct=EBI-357598, EBI-357669;
Q13200:PSMD2; NbExp=16; IntAct=EBI-357598, EBI-357648;
P55036:PSMD4; NbExp=2; IntAct=EBI-357598, EBI-359318;
Q16401:PSMD5; NbExp=9; IntAct=EBI-357598, EBI-752143;
O43463:SUV39H1; NbExp=2; IntAct=EBI-357598, EBI-349968;
Q96BR9:ZBTB8A; NbExp=3; IntAct=EBI-357598, EBI-742740;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000305};
Lipid-anchor {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62191-1; Sequence=Displayed;
Name=2;
IsoId=P62191-2; Sequence=VSP_055768;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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EMBL; L02426; AAA35484.1; -; mRNA.
EMBL; AK299121; BAG61175.1; -; mRNA.
EMBL; CR457044; CAG33325.1; -; mRNA.
EMBL; AL161662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000512; AAH00512.1; -; mRNA.
EMBL; BC016368; AAH16368.1; -; mRNA.
EMBL; BC067741; AAH67741.1; -; mRNA.
EMBL; BC073818; AAH73818.1; -; mRNA.
CCDS; CCDS32139.1; -. [P62191-1]
CCDS; CCDS81837.1; -. [P62191-2]
PIR; A44468; A44468.
RefSeq; NP_001317141.1; NM_001330212.1. [P62191-2]
RefSeq; NP_002793.2; NM_002802.2. [P62191-1]
RefSeq; XP_016876959.1; XM_017021470.1. [P62191-2]
UniGene; Hs.356654; -.
UniGene; Hs.476697; -.
PDB; 5GJQ; EM; 4.50 A; I=1-440.
PDB; 5GJR; EM; 3.50 A; I/w=1-440.
PDB; 5L4G; EM; 4.02 A; I=1-440.
PDB; 5LN3; EM; 6.80 A; I=1-440.
PDB; 5M32; EM; 3.80 A; d=1-428.
PDB; 5T0C; EM; 3.80 A; AB/BB=1-440.
PDB; 5T0G; EM; 4.40 A; B=1-440.
PDB; 5T0H; EM; 6.80 A; B=1-440.
PDB; 5T0I; EM; 8.00 A; B=1-440.
PDB; 5T0J; EM; 8.00 A; B=1-440.
PDB; 5VGZ; EM; 3.70 A; B=93-165.
PDB; 5VHF; EM; 5.70 A; B=93-432.
PDB; 5VHH; EM; 6.10 A; B=93-432.
PDB; 5VHI; EM; 6.80 A; B=93-433.
PDB; 5VHJ; EM; 8.50 A; B=167-432.
PDB; 5VHM; EM; 8.30 A; B=167-432.
PDB; 5VHN; EM; 7.30 A; B=167-432.
PDB; 5VHO; EM; 8.30 A; B=167-433.
PDB; 5VHP; EM; 7.90 A; B=167-432.
PDB; 5VHQ; EM; 8.90 A; B=167-433.
PDB; 5VHR; EM; 7.70 A; B=167-433.
PDB; 5VHS; EM; 8.80 A; B=93-433.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHJ; -.
PDBsum; 5VHM; -.
PDBsum; 5VHN; -.
PDBsum; 5VHO; -.
PDBsum; 5VHP; -.
PDBsum; 5VHQ; -.
PDBsum; 5VHR; -.
PDBsum; 5VHS; -.
ProteinModelPortal; P62191; -.
SMR; P62191; -.
BioGrid; 111673; 134.
CORUM; P62191; -.
IntAct; P62191; 81.
MINT; MINT-1141832; -.
STRING; 9606.ENSP00000261303; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; P62191; -.
PhosphoSitePlus; P62191; -.
SwissPalm; P62191; -.
BioMuta; PSMC1; -.
DMDM; 49065817; -.
EPD; P62191; -.
PaxDb; P62191; -.
PeptideAtlas; P62191; -.
PRIDE; P62191; -.
DNASU; 5700; -.
Ensembl; ENST00000261303; ENSP00000261303; ENSG00000100764. [P62191-1]
Ensembl; ENST00000543772; ENSP00000445147; ENSG00000100764. [P62191-2]
GeneID; 5700; -.
KEGG; hsa:5700; -.
UCSC; uc001xyg.4; human. [P62191-1]
CTD; 5700; -.
DisGeNET; 5700; -.
EuPathDB; HostDB:ENSG00000100764.13; -.
GeneCards; PSMC1; -.
H-InvDB; HIX0030744; -.
HGNC; HGNC:9547; PSMC1.
HPA; HPA000872; -.
MIM; 602706; gene.
neXtProt; NX_P62191; -.
OpenTargets; ENSG00000100764; -.
PharmGKB; PA33892; -.
eggNOG; KOG0726; Eukaryota.
eggNOG; COG1222; LUCA.
GeneTree; ENSGT00550000074818; -.
HOGENOM; HOG000225143; -.
HOVERGEN; HBG000109; -.
InParanoid; P62191; -.
KO; K03062; -.
OMA; NATFIRV; -.
OrthoDB; EOG091G07NC; -.
PhylomeDB; P62191; -.
TreeFam; TF106226; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMC1; human.
GeneWiki; PSMC1; -.
GenomeRNAi; 5700; -.
PRO; PR:P62191; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100764; -.
CleanEx; HS_PSMC1; -.
ExpressionAtlas; P62191; baseline and differential.
Genevisible; P62191; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO: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:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR005937; 26S_Psome_P45-like.
InterPro; IPR035244; 26S_subunit_4.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR23073:SF24; PTHR23073:SF24; 1.
Pfam; PF00004; AAA; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01242; 26Sp45; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
Nucleus; Phosphoprotein; Proteasome; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:22223895,
ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CHAIN 2 440 26S proteasome regulatory subunit 4.
/FTId=PRO_0000084677.
NP_BIND 226 233 ATP. {ECO:0000255}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 53 53 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 258 258 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 434 434 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 439 439 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:22223895,
ECO:0000269|PubMed:25255805,
ECO:0000269|PubMed:25807930}.
CROSSLNK 237 237 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:17370265}.
VAR_SEQ 1 73 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055768.
CONFLICT 19 19 K -> E (in Ref. 1; AAA35484).
{ECO:0000305}.
CONFLICT 70 70 D -> G (in Ref. 5; AAH67741).
{ECO:0000305}.
CONFLICT 120 120 H -> R (in Ref. 5; AAH16368).
{ECO:0000305}.
SEQUENCE 440 AA; 49185 MW; ACA80782F4F96F49 CRC64;
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL
KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
KSKENVLYKK QEGTPEGLYL


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