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Q9QUM9

- PSA6_MOUSE

UniProt

Q9QUM9 - PSA6_MOUSE

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
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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.

    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: 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. mitochondrion 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

    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

    ArrayExpressiQ9QUM9.
    BgeeiQ9QUM9.
    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 – 123
    Helixi23 – 3210
    Helixi33 – 353
    Beta strandi38 – 436
    Beta strandi45 – 539
    Turni63 – 653
    Beta strandi69 – 713
    Beta strandi73 – 8210
    Helixi84 – 10522
    Helixi111 – 12717
    Beta strandi128 – 1314
    Beta strandi135 – 14410
    Turni145 – 1473
    Beta strandi148 – 1547
    Beta strandi156 – 1583
    Beta strandi160 – 16910
    Helixi172 – 18413
    Helixi191 – 20616
    Turni212 – 2143
    Beta strandi215 – 2239
    Helixi232 – 24211

    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.

    Q9QUM9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI    50
    VTQKKVPDKL LDSSTVTHLF KITESIGCVM TGMTADSRSQ VQRARYEAAN 100
    WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ 150
    VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT 200
    CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD 246
    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.

    Protein family/group databases

    MEROPSi T01.971.

    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

    ArrayExpressi Q9QUM9.
    Bgeei Q9QUM9.
    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

    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 1, 2014
    This is version 125 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