P61289 (PSME3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.22 Ref.23
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.20 Ref.23
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.21
Induction	Up-regulated in thyroid carcinoma cells. Ref.21
Domain	The C-terminal sequences affect heptamer stability and proteasome affinity. Ref.14
Post-translational modification	Phosphorylated by MAP3K3 By similarity.
Sequence similarities	Belongs to the PA28 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle 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, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Traceable author statement. Source: Reactome 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 Inferred from direct assay Ref.23. Source: UniProtKB regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome regulation of proteasomal protein catabolic process Inferred from direct assay Ref.23. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome activator complex Inferred from electronic annotation. Source: InterPro proteasome complex Traceable author statement PubMed 8811196. Source: ProtInc
Molecular_function	MDM2/MDM4 family protein binding Inferred from direct assay Ref.23. Source: UniProtKB endopeptidase activator activity Inferred from direct assay Ref.23. Source: UniProtKB p53 binding Inferred from direct assay Ref.23. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATN1	P54259	3	EBI-355546,EBI-945980
COIL	P38432	3	EBI-355546,EBI-945751
NCOA3	Q9Y6Q9	5	EBI-355546,EBI-81196
vif	P12504	2	EBI-355546,EBI-779991	From a different organism.

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.9
	Chain	2 – 254	253	Proteasome activator complex subunit 3		PRO_0000161789
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9
	Modified residue	24	1	Phosphoserine Ref.16
	Modified residue	205	1	Phosphothreonine By similarity
	Modified residue	207	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	135	1	T → TPSGKGPHICFDLQ in isoform 2.		VSP_004516
Experimental info
	Mutagenesis	188	1	K → 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.20
	Sequence conflict	25	1	E → K in AAB60335. Ref.2
	Sequence conflict	94	1	E → K in AAA93227. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 1. Checksum: 116FAB47D60A26C0	FASTA	254	29,506
	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
	Isoform 2 [UniParc] [UniParc]. Checksum: 76E7E6ECCC65589F	FASTA	267	30,887
	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 EKCNTPSGKG PHICFDLQVK MWVQLLIPRI EDGNNFGVSI QEETVAELRT 190 200 210 220 230 240 VESEAASYLD QISRYYITRA KLVSKIAKYP HVEDYRRTVT EIDEKEYISL RLIISELRNQ 250 260 YVTLHDMILK NIEKIKRPRS SNAETLY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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. , 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, 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. , 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, MASS SPECTROMETRY. 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]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
IPI	IPI00030243. IPI00219445.
PIR	A60537. I38702.
RefSeq	NP_005780.2. NM_005789.3. NP_789839.1. NM_176863.2.
UniGene	Hs.152978.
3D structure databases
ProteinModelPortal	P61289.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61289. 29 interactions.
MINT	MINT-5002653.
STRING	9606.ENSP00000293362.
PTM databases
PhosphoSite	P61289.
Polymorphism databases
DMDM	47117724.
Proteomic databases
PaxDb	P61289.
PRIDE	P61289.
Protocols and materials databases
DNASU	10197.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293362; ENSP00000293362; ENSG00000131467. ENST00000590720; ENSP00000466794; ENSG00000131467.
GeneID	10197.
KEGG	hsa:10197.
UCSC	uc002ibp.3. human. uc002ibq.3. human.
Organism-specific databases
CTD	10197.
GeneCards	GC17P040985.
HGNC	HGNC:9570. PSME3.
HPA	CAB008388. HPA012510.
MIM	605129. gene.
neXtProt	NX_P61289.
PharmGKB	PA33916.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236353.
HOVERGEN	HBG053745.
InParanoid	P61289.
KO	K06698.
OMA	LKMWISF.
OrthoDB	EOG4NS3C9.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	P61289.
Bgee	P61289.
CleanEx	HS_PSME3.
Genevestigator	P61289.
GermOnline	ENSG00000131467. Homo sapiens.
Family and domain databases
Gene3D	1.20.120.180. 1 hit. 1.20.5.120. 1 hit.
InterPro	IPR003185. Proteasome_activ_REG_asu. IPR009077. Proteasome_activ_REG_asu/bsu. IPR003186. Proteasome_activ_REG_bsu. [Graphical view]
PANTHER	PTHR10660. PTHR10660. 1 hit.
Pfam	PF02251. PA28_alpha. 1 hit. PF02252. PA28_beta. 1 hit. [Graphical view]
SUPFAM	SSF47216. Prot_act_regA. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PSME3. human.
GenomeRNAi	10197.
NextBio	38592.
PMAP-CutDB	P61289.
SOURCE	Search...

Entry information

Entry name

PSME3_HUMAN

Accession

Primary (citable) accession number: P61289
Secondary accession number(s): A8K9A3 , O35563, P97373, Q12920, Q13172, Q9BQD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.