P25788 (PSA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-3
EC=3.4.25.1

Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8

Gene names

Name:	PSMA3
Synonyms:	HC8, PSC8

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	255 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	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2. Ref.8 Ref.21
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with AURKB. Interacts with CDKN1A. Interacts with HIV-1 TAT protein. Interacts with hepatitis C virus (HCV) F protein. Interacts with Epstein-Barr virus EBNA3 proteins. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.21 Ref.25
Subcellular location	Cytoplasm. Nucleus.
Induction	Down-regulated by antioxidants BO-653 and probucol. Up-regulated by bacterial lipopolysaccharides (LPS) and TNF. Ref.7 Ref.10 Ref.17
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease Threonine protease
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 Traceable author statement. Source: Reactome regulation of cellular amino acid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome core complex Inferred from direct assay PubMed 19208651. Source: BHF-UCL proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PML	P29590	2	EBI-348380,EBI-295890
PSMA1	P25786	3	EBI-348380,EBI-359352
PSMA4	P25789	4	EBI-348380,EBI-359310
PSMA6	P60900	2	EBI-348380,EBI-357793
PSMA7	O14818	4	EBI-348380,EBI-603272

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P25788-1)

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: P25788-2)

The sequence of this isoform differs from the canonical sequence as follows:
     136-142: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 255	254	Proteasome subunit alpha type-3		PRO_0000124091
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.9
	Modified residue	57	1	N6-acetyllysine Ref.27
	Modified residue	206	1	N6-acetyllysine Ref.27
	Modified residue	230	1	N6-acetyllysine Ref.27
	Modified residue	243	1	Phosphoserine Ref.19
	Modified residue	250	1	Phosphoserine Ref.9 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.30
Natural variations
	Alternative sequence	136 – 142	7	Missing in isoform 2.		VSP_005280
Experimental info
	Sequence conflict	91	1	I → M in AAH29402. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A1854ED3C0650FB1	FASTA	255	28,433
	10 20 30 40 50 60 MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE 70 80 90 100 110 120 EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV 130 140 150 160 170 180 HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL 190 200 210 220 230 240 QMKEMTCRDI VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TNGRHEIVPK DIREEAEKYA 250 KESLKEEDES DDDNM
	Isoform 2 [UniParc]. Checksum: E1C4F1C97EC83DAD	FASTA	248	27,647
	10 20 30 40 50 60 MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE 70 80 90 100 110 120 EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV 130 140 150 160 170 180 HAYTLYSAVR PFGCSVNDGA QLYMIDPSGV SYGYWGCAIG KARQAAKTEI EKLQMKEMTC 190 200 210 220 230 240 RDIVKEVAKI IYIVHDEVKD KAFELELSWV GELTNGRHEI VPKDIREEAE KYAKESLKEE DESDDDNM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes)." Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K., Ichihara A. Biochim. Biophys. Acta 1089:95-102(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[3]	"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: Testis.
[4]	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].
[5]	"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] (ISOFORMS 1 AND 2). Tissue: Bone marrow, Pancreas and Urinary bladder.
[6]	"Human proteasome subunits from 2-dimensional gels identified by partial sequencing." Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B. Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 116-130.
[7]	"Gene expression induced by BO-653, probucol and BHQ in human endothelial cells." Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H., Hamakubo T., Niki E., Kodama T., Noguchi N. J. Atheroscler. Thromb. 7:223-230(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY BO-653 AND PROBUCOL.
[8]	"A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome." Touitou R., Richardson J., Bose S., Nakanishi M., Rivett J., Allday M.J. EMBO J. 20:2367-2375(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDKN1A.
[9]	"Mapping and structural dissection of human 20 s proteasome using proteomic approaches." Claverol S., Burlet-Schiltz O., Girbal-Neuhauser E., Gairin J.E., Monsarrat B. Mol. Cell. Proteomics 1:567-578(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-250.
[10]	"Analysis of gene expression during maturation of immature dendritic cells derived from peripheral blood monocytes." Matsunaga T., Ishida T., Takekawa M., Nishimura S., Adachi M., Imai K. Scand. J. Immunol. 56:593-601(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[11]	"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits." Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E. FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[12]	"Human Aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner." Shu F., Guo S., Dang Y., Qi M., Zhou G., Guo Z., Zhang Y., Wu C., Zhao S., Yu L. Mol. Cell. Biochem. 254:157-162(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AURKB.
[13]	"Epstein-Barr virus EBNA3 proteins bind to the C8/alpha7 subunit of the 20S proteasome and are degraded by 20S proteasomes in vitro, but are very stable in latently infected B cells." Touitou R., O'Nions J., Heaney J., Allday M.J. J. Gen. Virol. 86:1269-1277(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EBNA3.
[14]	"MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein." Sdek P., Ying H., Chang D.L., Qiu W., Zheng H., Touitou R., Allday M.J., Xiao Z.X. Mol. Cell 20:699-708(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MDM2 AND RB1.
[15]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element." Takabe W., Matsukawa N., Kodama T., Tanaka K., Noguchi N. Free Radic. Res. 40:21-30(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY BO-653.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Prostate cancer.
[21]	"Low expression of cell-surface thromboxane A2 receptor beta-isoform through the negative regulation of its membrane traffic by proteasomes." Sasaki M., Sukegawa J., Miyosawa K., Yanagisawa T., Ohkubo S., Nakahata N. Prostaglandins Other Lipid Mediat. 83:237-249(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TBXA2R.
[22]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: T-cell.
[23]	"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-250, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Liver.
[25]	"Ubiquitin-independent degradation of hepatitis C virus F protein." Yuksek K., Chen W.-L., Chien D., Ou J.-H. J. Virol. 83:612-621(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCV F PROTEIN.
[26]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-206 AND LYS-230, MASS SPECTROMETRY.
[28]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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].
[30]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D00762 mRNA. Translation: BAA00659.1. BT006711 mRNA. Translation: AAP35357.1. BT019715 mRNA. Translation: AAV38520.1. AK315158 mRNA. Translation: BAG37603.1. CH471061 Genomic DNA. Translation: EAW80719.1. BC005265 mRNA. Translation: AAH05265.1. BC029402 mRNA. Translation: AAH29402.1. BC038990 mRNA. Translation: AAH38990.1.
IPI	IPI00171199. IPI00419249.
PIR	SNHUC8. S15971.
RefSeq	NP_002779.1. NM_002788.3. NP_687033.1. NM_152132.2.
UniGene	Hs.558799.
3D structure databases
ProteinModelPortal	P25788.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25788. 38 interactions.
MINT	MINT-1035201.
STRING	9606.ENSP00000216455.
Protein family/group databases
MEROPS	T01.977.
PTM databases
PhosphoSite	P25788.
Polymorphism databases
DMDM	130859.
2D gel databases
OGP	P25788.
REPRODUCTION-2DPAGE	IPI00171199.
Proteomic databases
PaxDb	P25788.
PRIDE	P25788.
Protocols and materials databases
DNASU	5684.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216455; ENSP00000216455; ENSG00000100567. ENST00000412908; ENSP00000390491; ENSG00000100567.
GeneID	5684.
KEGG	hsa:5684.
UCSC	uc001xdj.2. human. uc001xdk.2. human.
Organism-specific databases
CTD	5684.
GeneCards	GC14P058711.
H-InvDB	HIX0155215.
HGNC	HGNC:9532. PSMA3.
HPA	HPA000905.
MIM	176843. gene. 176845. gene.
neXtProt	NX_P25788.
PharmGKB	PA33877.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091086.
HOVERGEN	HBG105566.
InParanoid	P25788.
KO	K02727.
OMA	NKRIFNI.
OrthoDB	EOG4P5K9W.
PhylomeDB	P25788.
Enzyme and pathway databases
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
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	P25788.
Bgee	P25788.
CleanEx	HS_PSMA3.
Genevestigator	P25788.
GermOnline	ENSG00000100567. Homo sapiens.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_N. IPR023332. Proteasome_suA-type. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
SMART	SM00948. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5684.
NextBio	22072.
SOURCE	Search...

Entry information

Entry name

PSA3_HUMAN

Accession

Primary (citable) accession number: P25788
Secondary accession number(s): B2RCK6 , Q86U83, Q8N1D8, Q9BS70

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 153 of the entry and version 2 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.