Q9UL46 (PSME2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome activator complex subunit 2

Alternative name(s):
11S regulator complex subunit beta
Short name=REG-beta
Activator of multicatalytic protease subunit 2
Proteasome activator 28 subunit beta
Short name=PA28b
Short name=PA28beta

Gene names

Name:

PSME2

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	239 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	Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.
Subunit structure	Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
Induction	By IFNG/IFN-gamma.
Sequence similarities	Belongs to the PA28 family.

Ontologies

Keywords
Cellular component	Proteasome
Coding sequence diversity	Polymorphism
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
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 239	238	Proteasome activator complex subunit 2		PRO_0000161785
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5
	Modified residue	10	1	Phosphoserine Ref.7
Natural variations
	Natural variant	89	1	H → P. Ref.1 Ref.2 Ref.4 Corresponds to variant rs7146672 [ dbSNP | Ensembl ].		VAR_063111
Experimental info
	Sequence conflict	229	1	N → T in BAA08205. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UL46 [UniParc]. Last modified May 18, 2010. Version 4. Checksum: 98A30D83B3F93A91	FASTA	239	27,402
	10 20 30 40 50 60 MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL 70 80 90 100 110 120 RAPLDIPIPD PPPKDDEMET DKQEKKEVHK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL 130 140 150 160 170 180 VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK 190 200 210 220 230 ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of the genes encoding the human proteasome activators PA28alpha and beta." McCusker D., Wilson M., Trowsdale J. Immunogenetics 49:438-445(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-89.
[2]	"Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome." Ahn J.Y., Tanahashi N., Akiyama K., Hisamatsu H., Noda C., Tanaka K., Chung C.H., Shibmara N., Willy P.J., Mott J.D., Slaughter C.A., DeMartino G.N. FEBS Lett. 366:37-42(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-89.
[3]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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], VARIANT PRO-89. Tissue: Liver, Pancreas and Placenta.
[5]	Bienvenut W.V. Submitted (OCT-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-61; 91-115; 132-145; 155-171; 181-226 AND 232-239, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[6]	"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.
[7]	"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-10, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF079558 Genomic DNA. Translation: AAF02218.1. D45248 mRNA. Translation: BAA08205.1. AL136295 Genomic DNA. No translation available. BC004368 mRNA. Translation: AAH04368.1. BC019885 mRNA. Translation: AAH19885.1. BC072025 mRNA. Translation: AAH72025.1.
IPI	IPI00943181.
PIR	I53518.
RefSeq	NP_002809.2. NM_002818.2.
UniGene	Hs.434081. Hs.512410.
3D structure databases
ProteinModelPortal	Q9UL46.
SMR	Q9UL46. Positions 7-66, 97-232.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UL46. 12 interactions.
MINT	MINT-1478095.
STRING	9606.ENSP00000216802.
PTM databases
PhosphoSite	Q9UL46.
Polymorphism databases
DMDM	296453017.
2D gel databases
OGP	Q9UL46.
REPRODUCTION-2DPAGE	IPI00384051.
Proteomic databases
PaxDb	Q9UL46.
PRIDE	Q9UL46.
Protocols and materials databases
DNASU	5721.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216802; ENSP00000216802; ENSG00000100911.
GeneID	5721.
KEGG	hsa:5721.
UCSC	uc001wmj.3. human.
Organism-specific databases
CTD	5721.
GeneCards	GC14M024612.
HGNC	HGNC:9569. PSME2.
MIM	602161. gene.
neXtProt	NX_Q9UL46.
PharmGKB	PA33915.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280316.
HOGENOM	HOG000282822.
HOVERGEN	HBG053745.
KO	K06697.
OMA	DIRGFYA.
OrthoDB	EOG402WT1.
PhylomeDB	Q9UL46.
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	Q9UL46.
Bgee	Q9UL46.
CleanEx	HS_PSME2.
Genevestigator	Q9UL46.
GermOnline	ENSG00000100911. 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	PSME2. human.
GenomeRNAi	5721.
NextBio	22238.
SOURCE	Search...

Entry information

Entry name

PSME2_HUMAN

Accession

Primary (citable) accession number: Q9UL46
Secondary accession number(s): Q15129

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 119 of the entry and version 4 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.