Proteasome activator complex subunit 1

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Q06323 (PSME1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proteasome activator complex subunit 1

Alternative name(s):
11S regulator complex subunit alpha
Short name=REG-alpha
Activator of multicatalytic protease subunit 1
Interferon gamma up-regulated I-5111 protein
Short name=IGUP I-5111
Proteasome activator 28 subunit alpha
Short name=PA28a
Short name=PA28alpha

Gene names

Name:	PSME1
Synonyms:	IFI5111

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
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 hexadimeric ring. PSME1 can form homoheptamers. Ref.8
Induction	By IFNG/IFN-gamma.
Sequence similarities	Belongs to the PA28 family.

Ontologies

Keywords
Cellular component	Proteasome
Coding sequence diversity	Polymorphism
Technical term	3D-structure 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 peptide antigen via MHC class I Traceable author statement. Source: Reactome apoptotic process 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 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Proteasome activator complex subunit 1

PRO_0000161779

Natural variations

Natural variant

S → N.
Corresponds to variant rs1803830 [ dbSNP | Ensembl ].

VAR_011993

Natural variant

244

T → K.
Corresponds to variant rs14930 [ dbSNP | Ensembl ].

VAR_011994

Secondary structure

249

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q06323 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5E27727E5A0B0AAB
Show »

FASTA

249

28,723

        10         20         30         40         50         60 
MAMLRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP 

        70         80         90        100        110        120 
LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE 

       130        140        150        160        170        180 
IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TSLHTKLEGF HTQISKYFSE 

       190        200        210        220        230        240 
RGDAVTKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP 


RGETKGMIY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interferon-gamma up-regulates a unique set of proteins in human keratinocytes. Molecular cloning and expression of the cDNA encoding the RGD-sequence-containing protein IGUP I-5111." Honore B., Leffers H., Madsen P., Celis J.E. Eur. J. Biochem. 218:421-430(1993) [PubMed: 8269930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung fibroblast.
[2]	"Molecular cloning and expression of a gamma-interferon-inducible activator of the multicatalytic protease." Realini C., Dubiel W., Pratt G., Ferrell K., Rechsteiner M. J. Biol. Chem. 269:20727-20732(1994) [PubMed: 8051173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood.
[3]	"Organization of the genes encoding the human proteasome activators PA28alpha and beta." McCusker D., Wilson M., Trowsdale J. Immunogenetics 49:438-445(1999) [PubMed: 10199920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[6]	"Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes." Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M. J. Immunol. 160:4923-4935(1998) [PubMed: 9590240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-118.
[7]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-35; 191-197 AND 199-209. Tissue: Keratinocyte.
[8]	"The proteasome 11S regulator subunit REG alpha (PA28 alpha) is a heptamer." Johnston S.C., Whitby F.G., Realini C., Rechsteiner M., Hill C.P. Protein Sci. 6:2469-2473(1997) [PubMed: 9385652] [Abstract] Cited for: SUBUNIT.
[9]	"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: 17323924] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], INTERACTION WITH PROTEASOME. Tissue: Embryonic kidney.
[10]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Structure of the proteasome activator REGalpha (PA28alpha)." Knowlton J.R., Johnston S.C., Whitby F.G., Realini C., Zhang Z., Rechsteiner M., Hill C.P. Nature 390:639-643(1997) [PubMed: 9403698] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L07633 mRNA. Translation: AAA16521.1.
U10360 Genomic DNA. Translation: AAA53230.1.
AF078829 Genomic DNA. Translation: AAF02217.1.
BT019337 mRNA. Translation: AAV38144.1.
BC000352 mRNA. Translation: AAH00352.1.
BC007503 mRNA. Translation: AAH07503.1.
AB007137 Genomic DNA. Translation: BAA28836.1.

IPI

IPI00479722.

PIR

A54859.

RefSeq

NP_006254.1. NM_006263.2.
NP_788955.1. NM_176783.1.

UniGene

Hs.75348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AVO	X-ray	2.80	A/C/E/G/I/K/M	4-63	[»]
			B/D/F/H/J/L/N	104-242	[»]

ProteinModelPortal

Q06323.

SMR

Q06323. Positions 4-63, 104-242.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q06323. 12 interactions.

STRING

Q06323.

Polymorphism databases

DMDM

1170519.

2D gel databases

SWISS-2DPAGE

Q06323.

Aarhus/Ghent-2DPAGE

5111. IEF.

DOSAC-COBS-2DPAGE

Q06323.

OGP

Q06323.

PHCI-2DPAGE

Q06323.

Proteomic databases

PRIDE

Q06323.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000206451; ENSP00000206451; ENSG00000092010.

GeneID

5720.

KEGG

hsa:5720.

UCSC

uc001wmg.1. human.

Organism-specific databases

CTD

5720.

GeneCards

GC14P024605.

H-InvDB

HIX0202077.

HGNC

HGNC:9568. PSME1.

HPA

HPA006632.

MIM

600654. gene.

neXtProt

NX_Q06323.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17779.

HOVERGEN

HBG053745.

OrthoDB

EOG42V8H5.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6185. HIV Infection.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q06323.

Bgee

Q06323.

CleanEx

HS_PSME1.

Genevestigator

Q06323.

GermOnline

ENSG00000092010. Homo sapiens.

Family and domain databases

InterPro

IPR003185. Proteasome_activ_REG_asu.
IPR009077. Proteasome_activ_REG_asu/bsu.
IPR003186. Proteasome_activ_REG_bsu.
[Graphical view]

Gene3D

G3DSA:1.20.5.120. PA28_alpha-like. 1 hit.
G3DSA:1.20.120.180. PA28_beta. 1 hit.

K06696.

PANTHER

PTHR10660. Proteasome_activ_REG_asu/bsu. 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

NextBio

22232.

SOURCE

Search...

Entry information

Entry name

PSME1_HUMAN

Accession

Primary (citable) accession number: Q06323
Secondary accession number(s): Q9UEF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 115 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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents