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Q62141

- SIN3B_MOUSE

UniProt

Q62141 - SIN3B_MOUSE

Protein

Paired amphipathic helix protein Sin3b

Gene

Sin3b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional repressor. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Interacts with MAD-MAX heterodimers by binding to MAD. The heterodimer then represses transcription by tethering SIN3B to DNA. Also forms a complex with FOXK1 which represses transcription.2 Publications

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. protein binding Source: UniProtKB
    3. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cardiac muscle tissue development Source: UniProtKB
    2. negative regulation of cell cycle Source: UniProtKB
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. rhythmic process Source: UniProtKB-KW
    5. skeletal muscle tissue development Source: UniProtKB
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Paired amphipathic helix protein Sin3b
    Alternative name(s):
    Histone deacetylase complex subunit Sin3b
    Transcriptional corepressor Sin3b
    Gene namesi
    Name:Sin3b
    Synonyms:Kiaa0700
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:107158. Sin3b.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. autosome Source: MGI
    2. cytoplasm Source: MGI
    3. nucleus Source: UniProtKB
    4. X chromosome Source: MGI
    5. XY body Source: UniProtKB
    6. Y chromosome Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10981098Paired amphipathic helix protein Sin3bPRO_0000121540Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by RNF220 that leads to proteasomal degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ62141.
    PRIDEiQ62141.

    PTM databases

    PhosphoSiteiQ62141.

    Expressioni

    Gene expression databases

    ArrayExpressiQ62141.
    BgeeiQ62141.
    CleanExiMM_SIN3B.
    GenevestigatoriQ62141.

    Interactioni

    Subunit structurei

    Interacts with FOXK1/MNF, MXI, MAD, NCOR1 and SAP30. Interaction with SUDS3 enhances the interaction with HDAC1 to form a complex. Interacts with CRY1, HCFC1, MAD3, MAD4, MAEL, REST, RNF220 and SETDB1.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Foxk1P4212811EBI-591466,EBI-878270
    Rnf220Q6PDX65EBI-591450,EBI-2795840
    Suds3Q8BR655EBI-591450,EBI-591431

    Protein-protein interaction databases

    BioGridi203257. 16 interactions.
    DIPiDIP-470N.
    IntActiQ62141. 6 interactions.
    MINTiMINT-1510576.

    Structurei

    Secondary structure

    1
    1098
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 4710
    Turni48 – 503
    Helixi52 – 6615
    Helixi72 – 8211
    Helixi83 – 853
    Helixi87 – 9610
    Beta strandi99 – 1013
    Helixi152 – 16716
    Turni168 – 1703
    Helixi172 – 18716
    Beta strandi191 – 1933
    Helixi202 – 21211
    Turni213 – 2153
    Helixi217 – 22610
    Helixi229 – 2313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E91NMR-A148-232[»]
    1PD7NMR-A148-232[»]
    2CR7NMR-A32-98[»]
    2CZYNMR-A31-107[»]
    2F05NMR-A148-252[»]
    ProteinModelPortaliQ62141.
    SMRiQ62141. Positions 31-107, 148-232, 292-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62141.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 10071PAH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 23086PAH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 36078PAH 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 299299Interaction with CRY1Add
    BLAST
    Regioni52 – 9847Interaction with RESTAdd
    BLAST
    Regioni275 – 499225Interaction with NCOR1Add
    BLAST
    Regioni383 – 550168Interaction with SUDS3 and HDAC1Add
    BLAST

    Sequence similaritiesi

    Contains 3 PAH (paired amphipathic helix) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5602.
    GeneTreeiENSGT00390000007239.
    HOGENOMiHOG000230688.
    HOVERGENiHBG060425.
    InParanoidiQ62141.
    OMAiSEPHMVF.
    OrthoDBiEOG7SV0TV.
    PhylomeDBiQ62141.
    TreeFamiTF106187.

    Family and domain databases

    Gene3Di1.20.1160.11. 3 hits.
    InterProiIPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view]
    PfamiPF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view]
    SMARTiSM00761. HDAC_interact. 1 hit.
    [Graphical view]
    SUPFAMiSSF47762. SSF47762. 3 hits.
    PROSITEiPS51477. PAH. 3 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: Q62141-4) [UniParc]FASTAAdd to Basket

    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

    MAHAGSGGSA GRGFGGSRWG RSGSGGHEKL PVHVEDALTY LDQVKIRFGS     50
    DPATYNGFLE IMKEFKSQSI DTPGVIRRVS QLFHEHPDLI VGFNAFLPLG 100
    YRIDIPKNGK LNIQSPLSSQ DNSHSHGDCG EDFKQMSYKE DRGQVPLESD 150
    SVEFNNAISY VNKIKTRFLD HPEIYRSFLE ILHTYQKEQL HTKGRPFRGM 200
    SEEEVFTEVA NLFRGQEDLL SEFGQFLPEA KRSLFTGNGS CEMNSGQKNE 250
    EKSLEHNKKR SRPSLLRPVS APAKKKMKLR GTKDLSIAAV GKYGTLQEFS 300
    FFDKVRRVLK SQEVYENFLR CIALFNQELV SGSELLQLVS PFLGKFPELF 350
    AQFKSFLGVK ELSFAPPMSD RSGDGISREI DYASCKRIGS SYRALPKTYQ 400
    QPKCSGRTAI CKEVLNDTWV SFPSWSEDST FVSSKKTPYE EQLHRCEDER 450
    FELDVVLETN LATIRVLESV QKKLSRMAPE DQEKLRLDDC LGGTSEVIQR 500
    RAIHRIYGDK APEVIESLKR NPATAVPVVL KRLKAKEEEW REAQQGFNKI 550
    WREQYEKAYL KSLDHQAVNF KQNDTKALRS KSLLNEIESV YDEHQEQHSE 600
    GRSAPSSEPH LIFVYEDRQI LEDAAALISY YVKRQPAIQK EDQGTIRQLL 650
    HRFLPSLFFS QQCPGTSDDS ADERDRDRDS AEPERRRPTD EKPPADASPE 700
    PPKVLDDVYS LFFANNNWYF FLRLHQTLCA RLLKIYRQAQ KQLLEHRREQ 750
    EREQLLCEGR REKAADPAME LRLKQPSEVE LEEYYPAFLD MVRSLLEGSI 800
    DPTQYEDTLR EMFTIHAYIG FTMDKLVQNI ARQLHHLVSD DVCLKVVELY 850
    LNEQQRGAAG GNLSSRCVRA ARETSYQWKA ERCMADENCF KVMFLQRRGQ 900
    VIMTIELLDT EEAQTEDPVE VQHLARYVEQ YVGSEGASSS STEGFLLKPV 950
    FLQRNLKKFR RWQCEQVRAM RGEAKSSWKR LMGVESACDV DCRFRLGTHK 1000
    MVFIVNSEDY MYRRGTLCRA KQVQPLVLLR HHRHFEEWHG RWLEDNVTVA 1050
    AAGLVQDWLM GEEEEDMVPC KTLCETAHVH GLPVTRYRVQ YSRRPASP 1098

    Note: No experimental confirmation available.

    Length:1,098
    Mass (Da):126,405
    Last modified:June 21, 2005 - v2
    Checksum:iA73F6DFC11EBA256
    GO
    Isoform 1 (identifier: Q62141-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         955-1098: Missing.

    Show »
    Length:954
    Mass (Da):109,393
    Checksum:i31F4BE14523EA213
    GO
    Isoform 2 (identifier: Q62141-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         275-293: KKMKLRGTKDLSIAAVGKY → VGLQLKCAVVWFGYCTAEE
         294-954: Missing.
         955-1098: Missing.

    Show »
    Length:293
    Mass (Da):32,846
    Checksum:i11A75E8F67C818AE
    GO
    Isoform 3 (identifier: Q62141-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         275-302: KKMKLRGTKDLSIAAVGKYGTLQEFSFF → VLVHVWVLPAHGRSGVEAQAAGEPEARA
         303-954: Missing.
         955-1098: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:302
    Mass (Da):33,637
    Checksum:i421131CCD87C88F8
    GO

    Sequence cautioni

    The sequence BAD32283.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301A → G in AAC04821. (PubMed:10620510)Curated
    Sequence conflicti233 – 2331S → P in AAC04821. (PubMed:10620510)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei275 – 30228KKMKL…EFSFF → VLVHVWVLPAHGRSGVEAQA AGEPEARA in isoform 3. 1 PublicationVSP_008227Add
    BLAST
    Alternative sequencei275 – 29319KKMKL…AVGKY → VGLQLKCAVVWFGYCTAEE in isoform 2. 2 PublicationsVSP_008225Add
    BLAST
    Alternative sequencei294 – 954661Missing in isoform 2. 2 PublicationsVSP_008226Add
    BLAST
    Alternative sequencei303 – 954652Missing in isoform 3. 1 PublicationVSP_008228Add
    BLAST
    Alternative sequencei955 – 1098144Missing in isoform 1, isoform 2 and isoform 3. 3 PublicationsVSP_014187Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38622 mRNA. Translation: AAA69774.1.
    AF038848 mRNA. Translation: AAC04821.1.
    AK173005 mRNA. Translation: BAD32283.1. Different initiation.
    BC020049 mRNA. Translation: AAH20049.1.
    BC021160 mRNA. Translation: AAH21160.1.
    CCDSiCCDS52598.1. [Q62141-2]
    CCDS52599.1. [Q62141-4]
    PIRiI61714.
    RefSeqiNP_001106719.1. NM_001113248.2. [Q62141-2]
    NP_033214.2. NM_009188.4. [Q62141-4]
    UniGeneiMm.2137.

    Genome annotation databases

    EnsembliENSMUST00000004494; ENSMUSP00000004494; ENSMUSG00000031622. [Q62141-4]
    ENSMUST00000109950; ENSMUSP00000105576; ENSMUSG00000031622. [Q62141-2]
    GeneIDi20467.
    KEGGimmu:20467.
    UCSCiuc009mgp.2. mouse. [Q62141-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L38622 mRNA. Translation: AAA69774.1 .
    AF038848 mRNA. Translation: AAC04821.1 .
    AK173005 mRNA. Translation: BAD32283.1 . Different initiation.
    BC020049 mRNA. Translation: AAH20049.1 .
    BC021160 mRNA. Translation: AAH21160.1 .
    CCDSi CCDS52598.1. [Q62141-2 ]
    CCDS52599.1. [Q62141-4 ]
    PIRi I61714.
    RefSeqi NP_001106719.1. NM_001113248.2. [Q62141-2 ]
    NP_033214.2. NM_009188.4. [Q62141-4 ]
    UniGenei Mm.2137.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E91 NMR - A 148-232 [» ]
    1PD7 NMR - A 148-232 [» ]
    2CR7 NMR - A 32-98 [» ]
    2CZY NMR - A 31-107 [» ]
    2F05 NMR - A 148-252 [» ]
    ProteinModelPortali Q62141.
    SMRi Q62141. Positions 31-107, 148-232, 292-361.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203257. 16 interactions.
    DIPi DIP-470N.
    IntActi Q62141. 6 interactions.
    MINTi MINT-1510576.

    PTM databases

    PhosphoSitei Q62141.

    Proteomic databases

    PaxDbi Q62141.
    PRIDEi Q62141.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004494 ; ENSMUSP00000004494 ; ENSMUSG00000031622 . [Q62141-4 ]
    ENSMUST00000109950 ; ENSMUSP00000105576 ; ENSMUSG00000031622 . [Q62141-2 ]
    GeneIDi 20467.
    KEGGi mmu:20467.
    UCSCi uc009mgp.2. mouse. [Q62141-4 ]

    Organism-specific databases

    CTDi 23309.
    MGIi MGI:107158. Sin3b.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5602.
    GeneTreei ENSGT00390000007239.
    HOGENOMi HOG000230688.
    HOVERGENi HBG060425.
    InParanoidi Q62141.
    OMAi SEPHMVF.
    OrthoDBi EOG7SV0TV.
    PhylomeDBi Q62141.
    TreeFami TF106187.

    Miscellaneous databases

    EvolutionaryTracei Q62141.
    NextBioi 298571.
    PROi Q62141.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62141.
    Bgeei Q62141.
    CleanExi MM_SIN3B.
    Genevestigatori Q62141.

    Family and domain databases

    Gene3Di 1.20.1160.11. 3 hits.
    InterProi IPR013194. HDAC_interact.
    IPR003822. PAH.
    [Graphical view ]
    Pfami PF02671. PAH. 3 hits.
    PF08295. Sin3_corepress. 1 hit.
    [Graphical view ]
    SMARTi SM00761. HDAC_interact. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47762. SSF47762. 3 hits.
    PROSITEi PS51477. PAH. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3."
      Ayer D.E., Lawrence Q.A., Eisenman R.N.
      Cell 80:767-776(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
      Tissue: Embryonic kidney.
    2. "The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian Sin3B."
      Yang Q., Kong Y., Rothermel B., Garry D.J., Bassel-Duby R., Williams R.S.
      Biochem. J. 345:335-343(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH FOXK1.
      Tissue: Heart.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    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] (ISOFORMS 2 AND 3).
      Tissue: Mammary gland and Salivary gland.
    5. "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation."
      Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E., Copeland N.G., Jenkins N.A., Eisenman R.N.
      EMBO J. 14:5646-5659(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAD3 AND MAD4.
    6. Cited for: INTERACTION WITH NCOR1.
    7. "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors."
      Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N.
      Mol. Cell 2:33-42(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAP30.
    8. "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex."
      Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.
      Mol. Cell. Biol. 22:2743-2750(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUDS3 AND HDAC1.
    9. "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."
      Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.
      Biochem. J. 369:651-657(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1.
    10. "Circadian and light-induced transcription of clock gene Per1 depends on histone acetylation and deacetylation."
      Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.
      Mol. Cell. Biol. 24:6278-6287(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CRY1.
    11. "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed chromatin and microRNA pathway?"
      Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A., Cooke H.J.
      Hum. Mol. Genet. 15:2324-2334(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAEL.
    12. "RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination."
      Kong Q., Zeng W., Wu J., Hu W., Li C., Mao B.
      Biochem. Biophys. Res. Commun. 393:708-713(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF220, SUBCELLULAR LOCATION, UBIQUITINATION.
    13. Cited for: STRUCTURE BY NMR OF 148-232 IN COMPLEX WITH MAD1.
    14. "The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix."
      Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.
      J. Mol. Biol. 354:903-915(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 31-107 IN COMPLEX WITH REST, INTERACTION WITH REST.
    15. "Solution structure of the first PAH domain of the mouse transcriptional repressor SIN3B."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 32-100.

    Entry informationi

    Entry nameiSIN3B_MOUSE
    AccessioniPrimary (citable) accession number: Q62141
    Secondary accession number(s): O54976
    , Q6A013, Q8VCB8, Q8VDZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 143 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

    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