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P62509

- ERR3_MOUSE

UniProt

P62509 - ERR3_MOUSE

Protein

Estrogen-related receptor gamma

Gene

Esrrg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi125 – 20076Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri128 – 14821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri164 – 18825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calmodulin binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. retinoic acid receptor activity Source: InterPro
    6. RNA polymerase II regulatory region sequence-specific DNA binding Source: NTNU_SB
    7. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    8. steroid binding Source: InterPro
    9. steroid hormone receptor activity Source: InterPro
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. multicellular organismal development Source: UniProtKB
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    4. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Activator, Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Estrogen-related receptor gamma
    Alternative name(s):
    Estrogen receptor-related protein 3
    Nuclear receptor subfamily 3 group B member 3
    Gene namesi
    Name:Esrrg
    Synonyms:Err3, Kiaa0832, Nr3b3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1347056. Esrrg.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi449 – 4491L → A: Loss of transcriptional activation; when associated with A-450. 1 Publication
    Mutagenesisi450 – 4501F → A: Loss of transcriptional activation; when associated with A-449. 1 Publication
    Mutagenesisi453 – 4531M → A: Loss of transcriptional activation; when associated with A-454. 1 Publication
    Mutagenesisi454 – 4541L → A: Loss of transcriptional activation; when associated with A-453. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Estrogen-related receptor gammaPRO_0000053666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki40 – 40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei45 – 451PhosphoserineCurated

    Post-translational modificationi

    Acetylated by PCAF/KAT2 (in vitro).By similarity
    Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and represses transcriptional activity.By similarity
    Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus repressing transcriptional activity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP62509.

    PTM databases

    PhosphoSiteiP62509.

    Expressioni

    Tissue specificityi

    Highly expressed in the heart, brain and kidney and low expression in the liver.1 Publication

    Gene expression databases

    ArrayExpressiP62509.
    BgeeiP62509.
    CleanExiMM_ESRRG.
    GenevestigatoriP62509.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with NRIP1, NCOA1 and NCOR2 By similarity. Binds TLE1, PNRC1 and PNRC2 By similarity. Binds GRIP1.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CREBZFQ9NS373EBI-5274019,EBI-632965From a different organism.
    CrebzfQ91ZR33EBI-5274019,EBI-5274001

    Protein-protein interaction databases

    BioGridi204939. 4 interactions.
    IntActiP62509. 2 interactions.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi236 – 2438
    Helixi261 – 28323
    Turni287 – 2915
    Helixi294 – 31623
    Turni317 – 3193
    Beta strandi320 – 3223
    Beta strandi324 – 3274
    Beta strandi330 – 3323
    Helixi334 – 3385
    Turni339 – 3413
    Helixi343 – 35917
    Helixi363 – 37513
    Helixi385 – 40622
    Helixi413 – 4186
    Helixi421 – 44020
    Helixi448 – 4558

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S9PX-ray2.13A/B/C/D232-458[»]
    1S9QX-ray2.20A/B229-456[»]
    ProteinModelPortaliP62509.
    SMRiP62509. Positions 120-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri128 – 14821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri164 – 18825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG282629.
    GeneTreeiENSGT00730000110346.
    HOGENOMiHOG000233467.
    HOVERGENiHBG108344.
    InParanoidiP62509.
    KOiK08554.
    OMAiHVEDPRR.
    PhylomeDBiP62509.
    TreeFamiTF323751.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR027289. Oest-rel_rcp.
    IPR024178. Oest_rcpt/oest-rel_rcp.
    IPR003078. Retinoic_acid_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002527. ER-like_NR. 1 hit.
    PIRSF500939. ERR1-2-3. 1 hit.
    PRINTSiPR01292. RETNOICACIDR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 1 hit.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P62509-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT    50
    DSVNHHSPGG SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL 100
    YDDCSSTIVE DPQTKCEYML NSMPKRLCLV CGDIASGYHY GVASCEACKA 150
    FFKRTIQGNI EYSCPATNEC EITKRRRKSC QACRFMKCLK VGMLKEGVRL 200
    DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH LLVAEPEKIY 250
    AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL 300
    LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL 350
    QLVKKYKSMK LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ 400
    DYEAGQHMED PRRAGKMLMT LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF 450
    LEMLEAKV 458
    Length:458
    Mass (Da):51,306
    Last modified:July 19, 2004 - v1
    Checksum:i63D36CFD37573152
    GO
    Isoform 2 (identifier: P62509-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Show »
    Length:435
    Mass (Da):48,581
    Checksum:i63F81CDBE3A9C2D5
    GO

    Sequence cautioni

    The sequence BAC41450.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531K → N in BAC41450. (PubMed:12465718)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform 2. 2 PublicationsVSP_010766Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117254 mRNA. Translation: AAD48369.1.
    AB093266 mRNA. Translation: BAC41450.1. Different initiation.
    AK052731 mRNA. Translation: BAC35120.1.
    BC082324 mRNA. Translation: AAH82324.1.
    CCDSiCCDS15606.1. [P62509-1]
    CCDS56666.1. [P62509-2]
    RefSeqiNP_001230721.1. NM_001243792.1. [P62509-2]
    NP_036065.1. NM_011935.3. [P62509-1]
    XP_006497227.1. XM_006497164.1. [P62509-2]
    XP_006497228.1. XM_006497165.1. [P62509-2]
    XP_006497229.1. XM_006497166.1. [P62509-2]
    XP_006497230.1. XM_006497167.1. [P62509-2]
    XP_006497231.1. XM_006497168.1. [P62509-2]
    XP_006497232.1. XM_006497169.1. [P62509-2]
    XP_006497233.1. XM_006497170.1. [P62509-2]
    UniGeneiMm.388156.
    Mm.421613.
    Mm.89989.

    Genome annotation databases

    EnsembliENSMUST00000027906; ENSMUSP00000027906; ENSMUSG00000026610. [P62509-1]
    ENSMUST00000110938; ENSMUSP00000106563; ENSMUSG00000026610. [P62509-2]
    ENSMUST00000110939; ENSMUSP00000106564; ENSMUSG00000026610. [P62509-2]
    GeneIDi26381.
    KEGGimmu:26381.
    UCSCiuc007eaa.2. mouse. [P62509-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF117254 mRNA. Translation: AAD48369.1 .
    AB093266 mRNA. Translation: BAC41450.1 . Different initiation.
    AK052731 mRNA. Translation: BAC35120.1 .
    BC082324 mRNA. Translation: AAH82324.1 .
    CCDSi CCDS15606.1. [P62509-1 ]
    CCDS56666.1. [P62509-2 ]
    RefSeqi NP_001230721.1. NM_001243792.1. [P62509-2 ]
    NP_036065.1. NM_011935.3. [P62509-1 ]
    XP_006497227.1. XM_006497164.1. [P62509-2 ]
    XP_006497228.1. XM_006497165.1. [P62509-2 ]
    XP_006497229.1. XM_006497166.1. [P62509-2 ]
    XP_006497230.1. XM_006497167.1. [P62509-2 ]
    XP_006497231.1. XM_006497168.1. [P62509-2 ]
    XP_006497232.1. XM_006497169.1. [P62509-2 ]
    XP_006497233.1. XM_006497170.1. [P62509-2 ]
    UniGenei Mm.388156.
    Mm.421613.
    Mm.89989.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S9P X-ray 2.13 A/B/C/D 232-458 [» ]
    1S9Q X-ray 2.20 A/B 229-456 [» ]
    ProteinModelPortali P62509.
    SMRi P62509. Positions 120-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204939. 4 interactions.
    IntActi P62509. 2 interactions.

    Chemistry

    BindingDBi P62509.

    PTM databases

    PhosphoSitei P62509.

    Proteomic databases

    PRIDEi P62509.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027906 ; ENSMUSP00000027906 ; ENSMUSG00000026610 . [P62509-1 ]
    ENSMUST00000110938 ; ENSMUSP00000106563 ; ENSMUSG00000026610 . [P62509-2 ]
    ENSMUST00000110939 ; ENSMUSP00000106564 ; ENSMUSG00000026610 . [P62509-2 ]
    GeneIDi 26381.
    KEGGi mmu:26381.
    UCSCi uc007eaa.2. mouse. [P62509-1 ]

    Organism-specific databases

    CTDi 2104.
    MGIi MGI:1347056. Esrrg.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG282629.
    GeneTreei ENSGT00730000110346.
    HOGENOMi HOG000233467.
    HOVERGENi HBG108344.
    InParanoidi P62509.
    KOi K08554.
    OMAi HVEDPRR.
    PhylomeDBi P62509.
    TreeFami TF323751.

    Miscellaneous databases

    NextBioi 304297.
    PROi P62509.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62509.
    Bgeei P62509.
    CleanExi MM_ESRRG.
    Genevestigatori P62509.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR027289. Oest-rel_rcp.
    IPR024178. Oest_rcpt/oest-rel_rcp.
    IPR003078. Retinoic_acid_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002527. ER-like_NR. 1 hit.
    PIRSF500939. ERR1-2-3. 1 hit.
    PRINTSi PR01292. RETNOICACIDR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Hormone-independent transcriptional activation and coactivator binding by novel orphan nuclear receptor ERR3."
      Hong H., Yang L., Stallcup M.R.
      J. Biol. Chem. 274:22618-22626(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIP1, MUTAGENESIS OF LEU-449; PHE-450; MET-453 AND LEU-454, FUNCTION, TISSUE SPECIFICITY.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
      DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Kidney.
    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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    5. "Structural basis for the deactivation of the estrogen-related receptor gamma by diethylstilbestrol or 4-hydroxytamoxifen and determinants of selectivity."
      Greschik H., Flaig R., Renaud J.-P., Moras D.
      J. Biol. Chem. 279:33639-33646(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 229-458 IN COMPLEXES WITH INVERSE AGONISTS, SUBUNIT.

    Entry informationi

    Entry nameiERR3_MOUSE
    AccessioniPrimary (citable) accession number: P62509
    Secondary accession number(s): O75454
    , O96021, Q8CHC9, Q9R1F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    No physiological activating ligand is known for this orphan receptor, but 4-hydroxytamoxifen and diethylstilbestrol act as inverse agonists and deactivate ESRRG.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3