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Protein

Proteasome subunit alpha type-6

Gene

Psma6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.

Protein family/group databases

MEROPSiT01.971.

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 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1347006. Psma6.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • myofibril Source: BHF-UCL
  • nuclear matrix Source: BHF-UCL
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • polysome Source: BHF-UCL
  • proteasome complex Source: MGI
  • proteasome core complex Source: UniProtKB
  • proteasome core complex, alpha-subunit complex Source: BHF-UCL
  • 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:
PDBei
RCSB PDBi
PDBji
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.
OMAiRMANINQ.
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.

Q9QUM9-1 [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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiT01.971.

PTM databases

PhosphoSiteiQ9QUM9.

2D gel databases

COMPLUYEAST-2DPAGEQ9QUM9.
REPRODUCTION-2DPAGEQ9QUM9.

Proteomic databases

MaxQBiQ9QUM9.
PaxDbiQ9QUM9.
PRIDEiQ9QUM9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5687.
MGIiMGI:1347006. Psma6.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.
REACT_359269. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_359387. Degradation of GLI1 by the proteasome.
REACT_360804. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

ChiTaRSiPsma6. mouse.
NextBioi304529.
PROiQ9QUM9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUM9.
ExpressionAtlasiQ9QUM9. baseline and differential.
GenevestigatoriQ9QUM9.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.