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Q9QUM9

- PSA6_MOUSE

UniProt

Q9QUM9 - PSA6_MOUSE

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Protein

Proteasome subunit alpha type-6

Gene

Psma6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. RNA binding Source: BHF-UCL
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. positive regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  2. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
  3. skeletal muscle tissue development Source: BHF-UCL
  4. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Psma6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1347006. Psma6.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. CytoplasmP-body 1 Publication
Note: Colocalizes with TRIM5 in the cytoplasmic bodies.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytoplasmic mRNA processing body Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: Ensembl
  5. myofibril Source: BHF-UCL
  6. nuclear matrix Source: BHF-UCL
  7. polysome Source: BHF-UCL
  8. proteasome core complex Source: UniProtKB
  9. proteasome core complex, alpha-subunit complex Source: BHF-UCL
  10. sarcomere Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246Proteasome subunit alpha type-6PRO_0000124131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi5 – 51O-linked (GlcNAc)1 Publication
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei102 – 1021N6-acetyllysineBy similarity
Modified residuei104 – 1041N6-acetyllysine1 Publication
Modified residuei159 – 1591Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9QUM9.
PaxDbiQ9QUM9.
PRIDEiQ9QUM9.

2D gel databases

COMPLUYEAST-2DPAGEQ9QUM9.
REPRODUCTION-2DPAGEQ9QUM9.

PTM databases

PhosphoSiteiQ9QUM9.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues (at protein level).1 Publication

Gene expression databases

BgeeiQ9QUM9.
ExpressionAtlasiQ9QUM9. baseline and differential.
GenevestigatoriQ9QUM9.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi204994. 2 interactions.
IntActiQ9QUM9. 6 interactions.
MINTiMINT-1856833.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123Combined sources
Helixi23 – 3210Combined sources
Helixi33 – 353Combined sources
Beta strandi38 – 436Combined sources
Beta strandi45 – 539Combined sources
Turni63 – 653Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 8210Combined sources
Helixi84 – 10522Combined sources
Helixi111 – 12717Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi135 – 14410Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1547Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi160 – 16910Combined sources
Helixi172 – 18413Combined sources
Helixi191 – 20616Combined sources
Turni212 – 2143Combined sources
Beta strandi215 – 2239Combined sources
Helixi232 – 24211Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9QUM9.
SMRiQ9QUM9. Positions 2-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074807.
HOGENOMiHOG000091084.
HOVERGENiHBG107363.
InParanoidiQ9QUM9.
KOiK02730.
OMAiMSRTSYD.
PhylomeDBiQ9QUM9.
TreeFamiTF106210.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QUM9 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI
60 70 80 90 100
VTQKKVPDKL LDSSTVTHLF KITESIGCVM TGMTADSRSQ VQRARYEAAN
110 120 130 140 150
WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ
160 170 180 190 200
VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT
210 220 230 240
CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD
Length:246
Mass (Da):27,372
Last modified:May 1, 2000 - v1
Checksum:i6DF57BE87FA48D32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331P → T in BAE36518. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS25917.1.
RefSeqiNP_036098.1. NM_011968.3.
UniGeneiMm.30210.

Genome annotation databases

EnsembliENSMUST00000021412; ENSMUSP00000021412; ENSMUSG00000021024.
GeneIDi26443.
KEGGimmu:26443.
UCSCiuc007noq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS25917.1.
RefSeqi NP_036098.1. NM_011968.3.
UniGenei Mm.30210.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 G/U/i/w 1-246 [» ]
3UNE X-ray 3.20 G/U/i/w 1-246 [» ]
3UNF X-ray 2.90 G/U 1-246 [» ]
3UNH X-ray 3.20 G/U 1-246 [» ]
ProteinModelPortali Q9QUM9.
SMRi Q9QUM9. Positions 2-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204994. 2 interactions.
IntActi Q9QUM9. 6 interactions.
MINTi MINT-1856833.

PTM databases

PhosphoSitei Q9QUM9.

2D gel databases

COMPLUYEAST-2DPAGE Q9QUM9.
REPRODUCTION-2DPAGE Q9QUM9.

Proteomic databases

MaxQBi Q9QUM9.
PaxDbi Q9QUM9.
PRIDEi Q9QUM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021412 ; ENSMUSP00000021412 ; ENSMUSG00000021024 .
GeneIDi 26443.
KEGGi mmu:26443.
UCSCi uc007noq.2. mouse.

Organism-specific databases

CTDi 5687.
MGIi MGI:1347006. Psma6.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074807.
HOGENOMi HOG000091084.
HOVERGENi HBG107363.
InParanoidi Q9QUM9.
KOi K02730.
OMAi MSRTSYD.
PhylomeDBi Q9QUM9.
TreeFami TF106210.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

ChiTaRSi PSMA6. mouse.
NextBioi 304529.
PROi Q9QUM9.
SOURCEi Search...

Gene expression databases

Bgeei Q9QUM9.
ExpressionAtlasi Q9QUM9. baseline and differential.
Genevestigatori Q9QUM9.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.

Entry informationi

Entry nameiPSA6_MOUSE
AccessioniPrimary (citable) accession number: Q9QUM9
Secondary accession number(s): Q0VGS3, Q3TT07, Q3U6Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3