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Q9Z2S7

- T22D3_MOUSE

UniProt

Q9Z2S7 - T22D3_MOUSE

Protein

TSC22 domain family protein 3

Gene

Tsc22d3

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

    Protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro, suppresses AP1 and NFKB1 DNA-binding activities By similarity. Isoform 1 and isoform 4 inhibit myogenic differentiation and mediate anti-myogenic effects of glucocorticoids by binding and regulating MYOD1 and HDAC1 transcriptional activity resulting in reduced expression of MYOG.By similarity1 Publication

    GO - Molecular functioni

    1. MRF binding Source: MGI
    2. sequence-specific DNA binding transcription factor activity Source: InterPro

    GO - Biological processi

    1. body fluid secretion Source: Ensembl
    2. negative regulation of activation-induced cell death of T cells Source: MGI
    3. negative regulation of skeletal muscle tissue development Source: MGI
    4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    5. response to osmotic stress Source: MGI

    Enzyme and pathway databases

    ReactomeiREACT_196640. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TSC22 domain family protein 3
    Alternative name(s):
    Glucocorticoid-induced leucine zipper protein
    TSC22-related-inducible leucine zipper 3
    Short name:
    Tilz3
    Gene namesi
    Name:Tsc22d3
    Synonyms:Dsip1, Dsipi, Gilz
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1196284. Tsc22d3.

    Subcellular locationi

    Isoform 1 : Cytoplasm. Nucleus
    Note: Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 1 localizes to the cytoplasm, but in differentiating myoblasts, isoform 1 is localized to the nucleus.
    Isoform 4 : Cytoplasm. Nucleus
    Note: Localization depends on differentiation status of myoblasts. In undifferentiated myoblasts, isoform 4 localizes to the cytoplasm, but in differentiating myoblasts, isoform 4 is localized to the nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137TSC22 domain family protein 3PRO_0000219371Add
    BLAST

    Post-translational modificationi

    Isoform 3 is phosphorylated on Ser-30 and Ser-40.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z2S7.
    PaxDbiQ9Z2S7.
    PRIDEiQ9Z2S7.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00265379.

    PTM databases

    PhosphoSiteiQ9Z2S7.

    Expressioni

    Tissue specificityi

    Constitutively expressed in lung, intestine, kidney and liver, most probably by resident cells from the macrophage lineage. Expression inversely correlates with T-cell activation, being higher in resting cells and lower in cells activated by TCR/CD3 triggering. Isoform 1 and isoform 4 are expressed in spleen and skeletal muscle (at protein level). Isoform 1 is expressed in thymus, lymph nodes, bone marrow, spleen, lung and skeletal muscle.3 Publications

    Developmental stagei

    Isoform 1 and isoform 4 are expressed in differentiating myoblasts at a time of myotube formation.1 Publication

    Inductioni

    By glucocorticoids in lymphoid cells and upon IL4, IL10, IL13 or glucocorticoid treatment in monocyte/macrophage cells. Transiently induced by IL2 deprivation in T-cells. Isoform 1 and isoform 4 expression is up-regulated by the synthetic glucocorticoid dexamethasone in differentiating myoblasts.4 Publications

    Gene expression databases

    ArrayExpressiQ9Z2S7.
    BgeeiQ9Z2S7.
    CleanExiMM_TSC22D3.
    GenevestigatoriQ9Z2S7.

    Interactioni

    Subunit structurei

    Can form homodimers, however it is likely to function as a monomer. Interacts with AP1 and NFKB1 By similarity. Isoform 1 and isoform 4 interact with MYOD1. Isoform 1 interacts with HDAC1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi199919. 7 interactions.
    DIPiDIP-48844N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2S7.
    SMRiQ9Z2S7. Positions 58-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6060AP1-bindingAdd
    BLAST
    Regioni76 – 9722Leucine-zipperAdd
    BLAST

    Domaini

    The leucine-zipper is involved in homodimerization.

    Sequence similaritiesi

    Belongs to the TSC-22/Dip/Bun family.Curated

    Phylogenomic databases

    eggNOGiNOG329226.
    GeneTreeiENSGT00530000063062.
    HOVERGENiHBG075918.
    InParanoidiB1AVF3.
    OMAiYQLHNFN.
    OrthoDBiEOG7RZ5PT.
    PhylomeDBiQ9Z2S7.
    TreeFamiTF329224.

    Family and domain databases

    InterProiIPR000580. TSC-22_Dip_Bun.
    [Graphical view]
    PANTHERiPTHR12348. PTHR12348. 1 hit.
    PfamiPF01166. TSC22. 1 hit.
    [Graphical view]
    ProDomiPD007152. TSC-22_Dip_Bun. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    PROSITEiPS01289. TSC22. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z2S7-1) [UniParc]FASTAAdd to Basket

    Also known as: Tilz3b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAL    50
    DNKIEQAMDL VKNHLMYAVR EEVEVLKEQI RELLEKNSQL ERENTLLKTL 100
    ASPEQLEKFQ SRLSPEEPAP EAPETPETPE APGGSAV 137
    Length:137
    Mass (Da):15,177
    Last modified:February 1, 2005 - v2
    Checksum:iA11D7B69037F111E
    GO
    Isoform 2 (identifier: Q9Z2S7-2) [UniParc]FASTAAdd to Basket

    Also known as: Tilz3a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-57: Missing.

    Show »
    Length:80
    Mass (Da):9,040
    Checksum:i2174BA0EC92DDCFC
    GO
    Isoform 3 (identifier: Q9Z2S7-3) [UniParc]FASTAAdd to Basket

    Also known as: Tilz3c

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: MNTEMYQTPM...GDVVSVKLDN → MAQPKTECRS...TMLSILLFFH

    Show »
    Length:201
    Mass (Da):22,565
    Checksum:iB12F0480154A20DE
    GO
    Isoform 4 (identifier: Q9Z2S7-4) [UniParc]FASTAAdd to Basket

    Also known as: Long Gilz, L-Gilz

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: MNTEMYQTPM...GDVVSVKLDN → MESQKASSAG...TMLSILLFFH

    Show »
    Length:234
    Mass (Da):25,778
    Checksum:iC7CEDB07D24D4185
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221I → T in AAD01789. (PubMed:9430225)Curated
    Sequence conflicti33 – 331V → L in AAG41221. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5757Missing in isoform 2. 2 PublicationsVSP_012690Add
    BLAST
    Alternative sequencei1 – 4040MNTEM…VKLDN → MAQPKTECRSPVGLDCCNCC LDLANRCELQKEKSGESPGS PFVSNFRQLQEKLVFENLNT DKLNNIMRQDSMEPVVRDPC YLINEGICNRNIDQTMLSIL LFFH in isoform 3. 1 PublicationVSP_012691Add
    BLAST
    Alternative sequencei1 – 4040MNTEM…VKLDN → MESQKASSAGAHLPAAPDLP EQAAAAAASKPEKMAQPKTE CRSPVGLDCCNCCLDLANRC ELQKEKSGESPGSPFVSNFR QLQEKLVFENLNTDKLNNIM RQDSMEPVVRDPCYLINEGI CNRNIDQTMLSILLFFH in isoform 4. 1 PublicationVSP_055016Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024519 mRNA. Translation: AAD01789.1.
    EU818782 mRNA. Translation: ACJ09091.1.
    AF201287 mRNA. Translation: AAG41220.1.
    AF201288 mRNA. Translation: AAG41221.1.
    AF201289 mRNA. Translation: AAG41222.1.
    AK083389 mRNA. Translation: BAC38897.1.
    AK144196 mRNA. Translation: BAE25761.1.
    AL683809 Genomic DNA. Translation: CAM24436.1.
    BC028813 mRNA. Translation: AAH28813.1.
    CCDSiCCDS30440.1. [Q9Z2S7-1]
    CCDS41150.1. [Q9Z2S7-3]
    RefSeqiNP_001070832.1. NM_001077364.1. [Q9Z2S7-3]
    NP_034416.3. NM_010286.3. [Q9Z2S7-1]
    XP_006528562.1. XM_006528499.1. [Q9Z2S7-3]
    XP_006528563.1. XM_006528500.1. [Q9Z2S7-3]
    XP_006528564.1. XM_006528501.1. [Q9Z2S7-1]
    XP_006528565.1. XM_006528502.1. [Q9Z2S7-2]
    XP_006528566.1. XM_006528503.1. [Q9Z2S7-2]
    XP_006528567.1. XM_006528504.1. [Q9Z2S7-3]
    XP_006528568.1. XM_006528505.1. [Q9Z2S7-3]
    UniGeneiMm.22216.

    Genome annotation databases

    EnsembliENSMUST00000055738; ENSMUSP00000062589; ENSMUSG00000031431. [Q9Z2S7-1]
    ENSMUST00000112996; ENSMUSP00000108620; ENSMUSG00000031431. [Q9Z2S7-3]
    GeneIDi14605.
    KEGGimmu:14605.
    UCSCiuc009ukz.1. mouse. [Q9Z2S7-1]
    uc009ulb.1. mouse. [Q9Z2S7-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF024519 mRNA. Translation: AAD01789.1 .
    EU818782 mRNA. Translation: ACJ09091.1 .
    AF201287 mRNA. Translation: AAG41220.1 .
    AF201288 mRNA. Translation: AAG41221.1 .
    AF201289 mRNA. Translation: AAG41222.1 .
    AK083389 mRNA. Translation: BAC38897.1 .
    AK144196 mRNA. Translation: BAE25761.1 .
    AL683809 Genomic DNA. Translation: CAM24436.1 .
    BC028813 mRNA. Translation: AAH28813.1 .
    CCDSi CCDS30440.1. [Q9Z2S7-1 ]
    CCDS41150.1. [Q9Z2S7-3 ]
    RefSeqi NP_001070832.1. NM_001077364.1. [Q9Z2S7-3 ]
    NP_034416.3. NM_010286.3. [Q9Z2S7-1 ]
    XP_006528562.1. XM_006528499.1. [Q9Z2S7-3 ]
    XP_006528563.1. XM_006528500.1. [Q9Z2S7-3 ]
    XP_006528564.1. XM_006528501.1. [Q9Z2S7-1 ]
    XP_006528565.1. XM_006528502.1. [Q9Z2S7-2 ]
    XP_006528566.1. XM_006528503.1. [Q9Z2S7-2 ]
    XP_006528567.1. XM_006528504.1. [Q9Z2S7-3 ]
    XP_006528568.1. XM_006528505.1. [Q9Z2S7-3 ]
    UniGenei Mm.22216.

    3D structure databases

    ProteinModelPortali Q9Z2S7.
    SMRi Q9Z2S7. Positions 58-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199919. 7 interactions.
    DIPi DIP-48844N.

    PTM databases

    PhosphoSitei Q9Z2S7.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00265379.

    Proteomic databases

    MaxQBi Q9Z2S7.
    PaxDbi Q9Z2S7.
    PRIDEi Q9Z2S7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000055738 ; ENSMUSP00000062589 ; ENSMUSG00000031431 . [Q9Z2S7-1 ]
    ENSMUST00000112996 ; ENSMUSP00000108620 ; ENSMUSG00000031431 . [Q9Z2S7-3 ]
    GeneIDi 14605.
    KEGGi mmu:14605.
    UCSCi uc009ukz.1. mouse. [Q9Z2S7-1 ]
    uc009ulb.1. mouse. [Q9Z2S7-3 ]

    Organism-specific databases

    CTDi 1831.
    MGIi MGI:1196284. Tsc22d3.

    Phylogenomic databases

    eggNOGi NOG329226.
    GeneTreei ENSGT00530000063062.
    HOVERGENi HBG075918.
    InParanoidi B1AVF3.
    OMAi YQLHNFN.
    OrthoDBi EOG7RZ5PT.
    PhylomeDBi Q9Z2S7.
    TreeFami TF329224.

    Enzyme and pathway databases

    Reactomei REACT_196640. Stimuli-sensing channels.

    Miscellaneous databases

    NextBioi 286388.
    PROi Q9Z2S7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2S7.
    Bgeei Q9Z2S7.
    CleanExi MM_TSC22D3.
    Genevestigatori Q9Z2S7.

    Family and domain databases

    InterProi IPR000580. TSC-22_Dip_Bun.
    [Graphical view ]
    PANTHERi PTHR12348. PTHR12348. 1 hit.
    Pfami PF01166. TSC22. 1 hit.
    [Graphical view ]
    ProDomi PD007152. TSC-22_Dip_Bun. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    PROSITEi PS01289. TSC22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new dexamethasone-induced gene of the leucine zipper family protects T lymphocytes from TCR/CD3-activated cell death."
      D'Adamio F., Zollo O., Moraca R., Ayroldi E., Bruscoli S., Bartoli A., Cannarile L., Migliorati G., Riccardi C.
      Immunity 7:803-812(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION.
      Strain: C3H/HeN.
      Tissue: Thymus.
    2. "Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit myogenic differentiation and mediate anti-myogenic effects of glucocorticoids."
      Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G., Donato R., Riccardi C.
      J. Biol. Chem. 285:10385-10396(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH MYOD1 AND HDAC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Strain: DBA/2.
      Tissue: Myoblast.
    3. "Identification and characterization of a family of leucine zipper genes related to TSC22."
      Ershler M.A., Belyavsky A.V., Visser J.W.M.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    4. "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] (ISOFORM 1).
      Strain: BALB/c and C57BL/6J.
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Liver.
    7. "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappa B."
      Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O., Cannarile L., D'Adamio F., Riccardi C.
      Blood 98:743-753(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ."
      Mittelstadt P.R., Ashwell J.D.
      J. Biol. Chem. 276:29603-29610(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, INTERACTION WITH JUN AND FOS.
    9. "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10."
      Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G., Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P., Peuchmaur M., Riccardi C., Emilie D.
      Blood 101:729-738(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    10. "GILZ, a new target for the transcription factor FoxO3, protects T lymphocytes from interleukin-2 withdrawal-induced apoptosis."
      Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D., Zennaro M.-C., Bertoglio J., Pallardy M.
      Blood 104:215-223(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiT22D3_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2S7
    Secondary accession number(s): B1AVF3
    , C6EX03, Q3UNI6, Q8K160, Q9EQN0, Q9EQN1, Q9EQN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3