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Q9QUM9 (PSA6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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-6

EC=3.4.25.1
Alternative name(s):
Macropain iota chain
Multicatalytic endopeptidase complex iota chain
Proteasome iota chain
Gene names
Name:Psma6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.12

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. Ref.7 Ref.12

Subcellular location

Cytoplasm. Nucleus. CytoplasmP-body. Note: Colocalizes with TRIM5 in the cytoplasmic bodies. Ref.9

Tissue specificity

Detected in liver (at protein level). Ref.12

Induction

Up-regulated in liver tumor tissues (at protein level). Ref.6

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 term3D-structure
Complete 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

skeletal muscle tissue development

Non-traceable author statement PubMed 10852819. Source: BHF-UCL

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 10852819. Source: BHF-UCL

cytoplasmic mRNA processing body

Inferred from direct assay Ref.9. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

myofibril

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

nuclear matrix

Inferred from direct assay PubMed 10852819. Source: BHF-UCL

polysome

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

proteasome core complex

Inferred from direct assay Ref.7. Source: UniProtKB

proteasome core complex, alpha-subunit complex

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

sarcomere

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

   Molecular_functionRNA binding

Inferred from direct assay PubMed 10852819. 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_0000124131

Amino acid modifications

Modified residue1021N6-acetyllysine By similarity
Modified residue1041N6-acetyllysine Ref.11
Modified residue1591Phosphotyrosine Ref.8
Glycosylation51O-linked (GlcNAc) Ref.10
Cross-link59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1331P → T in BAE36518. Ref.3

Secondary structure

...................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QUM9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6DF57BE87FA48D32

FASTA24627,372
        10         20         30         40         50         60 
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL 

        70         80         90        100        110        120 
LDSSTVTHLF KITESIGCVM 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]"Sequence of mouse prosomal subunit iota."
Thomson S.A., Fechheimer M.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Carcinoma.
[2]"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.
[3]"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 NOD.
Tissue: Bone marrow and Thymus.
[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].
Strain: C57BL/6.
Tissue: Eye.
[5]Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 60-71; 105-116; 118-132 AND 229-245, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Brain and Hippocampus.
[6]"The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"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.
[8]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[9]"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.
[10]"Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag."
Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A., Siele D., Kloetzel P.M., Janek K.
Mol. Cell. Proteomics 11:467-477(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-5.
Tissue: Brain and Spleen.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"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
U60288 mRNA. Translation: AAF21459.1.
AF060087 mRNA. Translation: AAD50532.1.
AK088143 mRNA. Translation: BAC40169.1.
AK152915 mRNA. Translation: BAE31592.1.
AK161662 mRNA. Translation: BAE36518.1.
BC086685 mRNA. Translation: AAH86685.1.
CCDSCCDS25917.1.
RefSeqNP_036098.1. NM_011968.3.
UniGeneMm.30210.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90G/U/i/w1-246[»]
3UNEX-ray3.20G/U/i/w1-246[»]
3UNFX-ray2.90G/U1-246[»]
3UNHX-ray3.20G/U1-246[»]
ProteinModelPortalQ9QUM9.
SMRQ9QUM9. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204994. 2 interactions.
IntActQ9QUM9. 6 interactions.
MINTMINT-1856833.

Protein family/group databases

MEROPST01.971.

PTM databases

PhosphoSiteQ9QUM9.

2D gel databases

COMPLUYEAST-2DPAGEQ9QUM9.
REPRODUCTION-2DPAGEQ9QUM9.

Proteomic databases

MaxQBQ9QUM9.
PaxDbQ9QUM9.
PRIDEQ9QUM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021412; ENSMUSP00000021412; ENSMUSG00000021024.
GeneID26443.
KEGGmmu:26443.
UCSCuc007noq.2. mouse.

Organism-specific databases

CTD5687.
MGIMGI:1347006. Psma6.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074807.
HOGENOMHOG000091084.
HOVERGENHBG107363.
InParanoidQ9QUM9.
KOK02730.
OMAMSRTSYD.
PhylomeDBQ9QUM9.
TreeFamTF106210.

Gene expression databases

ArrayExpressQ9QUM9.
BgeeQ9QUM9.
GenevestigatorQ9QUM9.

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

ChiTaRSPSMA6. mouse.
NextBio304529.
PROQ9QUM9.
SOURCESearch...

Entry information

Entry namePSA6_MOUSE
AccessionPrimary (citable) accession number: Q9QUM9
Secondary accession number(s): Q0VGS3, Q3TT07, Q3U6Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 123 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