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P60901 (PSA6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-6

EC=3.4.25.1
Alternative name(s):
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain
Gene names
Name:Psma6
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

Interacts with ALKBH4 By similarity. 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.

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-body By similarity. Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity.

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

proteolysis involved in cellular protein catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasmic mRNA processing body

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

myofibril

Inferred from direct assay PubMed 15561103. Source: BHF-UCL

nuclear matrix

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

polysome

Inferred from sequence or structural similarity. Source: BHF-UCL

proteasome core complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome core complex, alpha-subunit complex

Inferred from sequence or structural similarity. Source: BHF-UCL

sarcomere

Inferred from direct assay PubMed 15561103. Source: BHF-UCL

   Molecular_functionRNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

threonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Proteasome subunit alpha type-6
PRO_0000124132

Amino acid modifications

Modified residue1021N6-acetyllysine By similarity
Modified residue1041N6-acetyllysine By similarity
Modified residue1591Phosphotyrosine By similarity
Glycosylation51O-linked (GlcNAc) By similarity
Cross-link59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P60901 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 94D1FD3C0A7CC72A

FASTA24627,399
        10         20         30         40         50         60 
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL 

        70         80         90        100        110        120 
LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD 

       130        140        150        160        170        180 
ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE 

       190        200        210        220        230        240 
KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV 


ALAERD 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNAs for rat proteasomes: deduced primary structures of four other subunits."
Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K., Ichihara A.
J. Biochem. 112:530-534(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Pituitary.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-21; 60-71; 154-164 AND 229-246, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10755 mRNA. Translation: BAA01587.1.
BC062232 mRNA. Translation: AAH62232.1.
PIRJX0230.
RefSeqNP_058979.1. NM_017283.3.
UniGeneRn.107278.

3D structure databases

ProteinModelPortalP60901.
SMRP60901. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248294. 2 interactions.
IntActP60901. 1 interaction.

Protein family/group databases

MEROPST01.971.

PTM databases

PhosphoSiteP60901.

2D gel databases

World-2DPAGE0004:P60901.

Proteomic databases

PaxDbP60901.
PRIDEP60901.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009666; ENSRNOP00000009666; ENSRNOG00000007114.
GeneID29673.
KEGGrno:29673.
UCSCRGD:61849. rat.

Organism-specific databases

CTD5687.
RGD61849. Psma6.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074807.
HOGENOMHOG000091084.
HOVERGENHBG107363.
InParanoidP60901.
KOK02730.
OMAMSRTSYD.
OrthoDBEOG70PBZH.
PhylomeDBP60901.
TreeFamTF106210.

Gene expression databases

GenevestigatorP60901.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio22090.
PROP60901.

Entry information

Entry namePSA6_RAT
AccessionPrimary (citable) accession number: P60901
Secondary accession number(s): P34062
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries