Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P61289 (PSME3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome activator complex subunit 3
Alternative name(s):
11S regulator complex subunit gamma
Short name=REG-gamma
Activator of multicatalytic protease subunit 3
Ki nuclear autoantigen
Proteasome activator 28 subunit gamma
Short name=PA28g
Short name=PA28gamma
Gene names
Name:PSME3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Ref.11 Ref.12 Ref.14 Ref.22 Ref.24 Ref.25

Subunit structure

Homoheptamer; the stability of the heptamer is essential for the specific activation of the trypsine-like subunit and inhibition of the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of the proteasome. Interacts with p53/TP53 and MDM2. Interacts with MAP3K3 By similarity. Associates with the proteasome. Ref.11 Ref.12 Ref.14 Ref.21 Ref.22 Ref.25

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase By similarity. Ref.13 Ref.23

Induction

Up-regulated in thyroid carcinoma cells. Ref.23

Domain

The C-terminal sequences affect heptamer stability and proteasome affinity. Ref.14

Post-translational modification

Phosphorylated by MAP3K3 By similarity.

Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates. Deacetylated by SIRT1. Ref.9 Ref.21

Sequence similarities

Belongs to the PA28 family.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay Ref.25. Source: UniProtKB

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of endopeptidase activity

Inferred from direct assay Ref.25. Source: GOC

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of proteasomal protein catabolic process

Inferred from direct assay Ref.25. Source: UniProtKB

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

proteasome activator complex

Inferred from electronic annotation. Source: InterPro

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

   Molecular_functionMDM2/MDM4 family protein binding

Inferred from direct assay Ref.25. Source: UniProtKB

endopeptidase activator activity

Inferred from direct assay Ref.25. Source: UniProtKB

p53 binding

Inferred from direct assay Ref.25. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P61289-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P61289-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: T → TPSGKGPHICFDLQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 254253Proteasome activator complex subunit 3
PRO_0000161789

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.20
Modified residue61N6-acetyllysine
Modified residue141N6-acetyllysine
Modified residue241Phosphoserine Ref.16
Modified residue1951N6-acetyllysine; by P300/CBP Ref.21

Natural variations

Alternative sequence1351T → TPSGKGPHICFDLQ in isoform 2.
VSP_004516

Experimental info

Mutagenesis1881K → E, D, A, C, N, Q, H, F, S, I or P: Assembles into less stable hexamers/heptamers and therefore impairs specificity of activation of trypsin-like subunits of the proteasome. Ref.22
Sequence conflict251E → K in AAB60335. Ref.2
Sequence conflict941E → K in AAA93227. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 1.
Checksum: 116FAB47D60A26C0

FASTA25429,506
        10         20         30         40         50         60 
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS 

        70         80         90        100        110        120 
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK VFVMPNGMLK SNQQLVDIIE 

       130        140        150        160        170        180 
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS 

       190        200        210        220        230        240 
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE 

       250 
KIKRPRSSNA ETLY 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 76E7E6ECCC65589F
Show »

FASTA26730,887

References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus."
Nikaido T., Shimada K., Shibata M., Hata M., Sakamoto M., Takasaki Y., Sato C., Takahashi T., Nishida Y.
Clin. Exp. Immunol. 79:209-214(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21."
Albertsen H.M., Smith S.A., Mazoyer S., Fujimoto E., Stevens J., Williams B., Rodriguez P., Cropp C.S., Slijepcevic P., Carlson M., Robertson M., Bradley P., Lawrence E., Harrington T., Sheng Z.M., Hoopes R., Sternberg N., Brothman A. expand/collapse author list , Callahan R., Ponder B.A.J., White R.
Nat. Genet. 7:472-479(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: B-cell and Fetal brain.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Thymus.
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung, Ovary and Placenta.
[9]Bienvenut W.V., Ramsay A., Leung H.Y.
Submitted (FEB-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12 AND 111-121, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1."
Miki Y., Swensen J., Shattuck-Eidens D., Futreal P.A., Harshman K., Tavtigian S., Liu Q., Cochran C., Bennett L.M., Ding W., Bell R., Rosenthal J., Hussey C., Tran T., McClure M., Frye C., Hattier T., Phelps R. expand/collapse author list , Haugen-Strano A., Katcher H., Yakumo K., Gholami Z., Shaffer D., Stone S., Bayer S., Wray C., Bogden R., Dayananth P., Ward J., Tonin P., Narod S., Bristow P.K., Norris F.H., Helvering L., Morrison P., Rosteck P., Lai M., Barrett J.C., Lewis C., Neuhausen S., Cannon-Albright L., Godlgar D., Wiseman R., Kamb A., Skolnick M.H.
Science 266:66-71(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-135.
Tissue: Ovary.
[11]"Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators."
Realini C., Jensen C.C., Zhang Z., Johnston S.C., Knowlton J.R., Hill C.P., Rechsteiner M.
J. Biol. Chem. 272:25483-25492(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH THE PROTEASOME, CALCIUM-BINDING.
[12]"Properties of the nuclear proteasome activator PA28gamma (REGgamma)."
Wilk S., Chen W.-E., Magnusson R.P.
Arch. Biochem. Biophys. 383:265-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[13]"Subcellular localization of proteasomes and their regulatory complexes in mammalian cells."
Brooks P., Fuertes G., Murray R.Z., Bose S., Knecht E., Rechsteiner M.C., Hendil K.B., Tanaka K., Dyson J., Rivett J.
Biochem. J. 346:155-161(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"The proteasome activator 11 S REG or PA28: chimeras implicate carboxyl-terminal sequences in oligomerization and proteasome binding but not in the activation of specific proteasome catalytic subunits."
Li J., Gao X., Joss L., Rechsteiner M.
J. Mol. Biol. 299:641-654(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH THE PROTEASOME, SUBUNIT.
[15]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Site-specific acetylation of the proteasome activator REGgamma directs its heptameric structure and functions."
Liu J., Wang Y., Li L., Zhou L., Wei H., Zhou Q., Liu J., Wang W., Ji L., Shan P., Wang Y., Yang Y., Jung S.Y., Zhang P., Wang C., Long W., Zhang B., Li X.
J. Biol. Chem. 288:16567-16578(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-195, SUBUNIT.
[22]"Lysine 188 substitutions convert the pattern of proteasome activation by REGgamma to that of REGs alpha and beta."
Li J., Gao X., Ortega J., Nazif T., Joss L., Bogyo M., Steven A.C., Rechsteiner M.
EMBO J. 20:3359-3369(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ELECTRON MICROSCOPY, SUBUNIT, FUNCTION, MUTAGENESIS OF LYS-188.
[23]"Abnormally high expression of proteasome activator-gamma in thyroid neoplasm."
Okamura T., Taniguchi S., Ohkura T., Yoshida A., Shimizu H., Sakai M., Maeta H., Fukui H., Ueta Y., Hisatome I., Shigemasa C.
J. Clin. Endocrinol. Metab. 88:1374-1383(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, SUBCELLULAR LOCATION.
[24]"Purification procedures determine the proteasome activation properties of REG gamma (PA28 gamma)."
Gao X., Li J., Pratt G., Wilk S., Rechsteiner M.
Arch. Biochem. Biophys. 425:158-164(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation."
Zhang Z., Zhang R.
EMBO J. 27:852-864(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53 AND MDM2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U11292 mRNA. Translation: AAB60335.1.
BT019386 mRNA. Translation: AAV38193.1.
AK292618 mRNA. Translation: BAF85307.1.
AK074999 mRNA. Translation: BAG52046.1.
AC016889 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60893.1.
BC001423 mRNA. Translation: AAH01423.1.
BC002684 mRNA. Translation: AAH02684.1.
BC008020 mRNA. Translation: AAH08020.1.
U25756 Genomic DNA. Translation: AAA93227.1.
PIRA60537. I38702.
RefSeqNP_005780.2. NM_005789.3.
NP_789839.1. NM_176863.2.
UniGeneHs.152978.

3D structure databases

ProteinModelPortalP61289.
SMRP61289. Positions 5-64, 112-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115492. 69 interactions.
IntActP61289. 39 interactions.
MINTMINT-5002653.
STRING9606.ENSP00000293362.

PTM databases

PhosphoSiteP61289.

Polymorphism databases

DMDM47117724.

Proteomic databases

PaxDbP61289.
PRIDEP61289.

Protocols and materials databases

DNASU10197.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293362; ENSP00000293362; ENSG00000131467. [P61289-2]
ENST00000590720; ENSP00000466794; ENSG00000131467. [P61289-1]
GeneID10197.
KEGGhsa:10197.
UCSCuc002ibp.3. human.
uc002ibq.4. human. [P61289-2]

Organism-specific databases

CTD10197.
GeneCardsGC17P040985.
HGNCHGNC:9570. PSME3.
HPACAB008388.
HPA012510.
MIM605129. gene.
neXtProtNX_P61289.
PharmGKBPA33916.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236353.
HOVERGENHBG053745.
InParanoidP61289.
KOK06698.
OMALKMWISF.
PhylomeDBP61289.
TreeFamTF106236.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP61289.
BgeeP61289.
CleanExHS_PSME3.
GenevestigatorP61289.

Family and domain databases

Gene3D1.20.120.180. 1 hit.
1.20.5.120. 1 hit.
InterProIPR009077. Proteasome_activ_pa28.
IPR003186. Proteasome_activ_pa28_C.
IPR003185. Proteasome_activ_pa28_N.
[Graphical view]
PANTHERPTHR10660. PTHR10660. 1 hit.
PfamPF02251. PA28_alpha. 1 hit.
PF02252. PA28_beta. 1 hit.
[Graphical view]
SUPFAMSSF47216. SSF47216. 2 hits.
ProtoNetSearch...

Other

ChiTaRSPSME3. human.
GeneWikiPSME3.
GenomeRNAi10197.
NextBio38592.
PMAP-CutDBP61289.
PROP61289.
SOURCESearch...

Entry information

Entry namePSME3_HUMAN
AccessionPrimary (citable) accession number: P61289
Secondary accession number(s): A8K9A3 expand/collapse secondary AC list , O35563, P97373, Q12920, Q13172, Q9BQD9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM