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Q9R1P0 (PSA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-4

EC=3.4.25.1
Alternative name(s):
Macropain subunit C9
Multicatalytic endopeptidase complex subunit C9
Proteasome component C9
Proteasome subunit L
Gene names
Name:Psma4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length261 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. Ref.7

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. Ref.5 Ref.7

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-body. Note: Colocalizes with TRIM5 in the cytoplasmic bodies. Ref.6

Tissue specificity

Detected in liver (at protein level). Ref.7

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Proteasome subunit alpha type-4
PRO_0000124105

Amino acid modifications

Modified residue131Phosphoserine By similarity
Modified residue751Phosphoserine By similarity
Modified residue1271N6-acetyllysine By similarity
Modified residue1761N6-acetyllysine By similarity

Secondary structure

........................................ 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R1P0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BB7CC8113791E13B

FASTA26129,471
        10         20         30         40         50         60 
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF 

        70         80         90        100        110        120 
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA 

       130        140        150        160        170        180 
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK 

       190        200        210        220        230        240 
EGEMTLKSAL ALAVKVLNKT MDVSKLSAEK VEIATLTRES GKTVIRVLKQ KEVEQLIKKH 

       250        260 
EEEEAKAERE KKEKEQREKD K 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure of mouse 20S proteasomes."
Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.
Immunogenetics 49:835-842(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: B10.BR.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Heart.
[3]"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].
[4]Lubec G., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 55-64.
Tissue: Brain.
[5]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
[6]"TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., Luban J., Campbell E.M.
Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF060093 mRNA. Translation: AAD50538.1.
AK085937 mRNA. Translation: BAC39573.1.
AK168150 mRNA. Translation: BAE40115.1.
BC001982 mRNA. Translation: AAH01982.1.
CCDSCCDS40643.1.
RefSeqNP_036096.1. NM_011966.3.
XP_006511261.1. XM_006511198.1.
UniGeneMm.30270.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90B/P/d/r1-261[»]
3UNEX-ray3.20B/P/d/r1-261[»]
3UNFX-ray2.90B/P1-261[»]
3UNHX-ray3.20B/P1-261[»]
ProteinModelPortalQ9R1P0.
SMRQ9R1P0. Positions 2-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204992. 2 interactions.
IntActQ9R1P0. 6 interactions.
MINTMINT-1850528.

Protein family/group databases

MEROPST01.973.

PTM databases

PhosphoSiteQ9R1P0.

Proteomic databases

MaxQBQ9R1P0.
PaxDbQ9R1P0.
PRIDEQ9R1P0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301.
GeneID26441.
KEGGmmu:26441.
UCSCuc009pru.1. mouse.

Organism-specific databases

CTD5685.
MGIMGI:1347060. Psma4.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074827.
HOGENOMHOG000091085.
HOVERGENHBG003005.
InParanoidQ9R1P0.
KOK02728.
OMAKQEYKDD.
OrthoDBEOG7F512J.
PhylomeDBQ9R1P0.
TreeFamTF106209.

Gene expression databases

ArrayExpressQ9R1P0.
BgeeQ9R1P0.
GenevestigatorQ9R1P0.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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

ChiTaRSPSMA4. mouse.
NextBio304521.
PROQ9R1P0.
SOURCESearch...

Entry information

Entry namePSA4_MOUSE
AccessionPrimary (citable) accession number: Q9R1P0
Secondary accession number(s): Q3THT1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 121 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot