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Q01147

- CREB1_MOUSE

UniProt

Q01147 - CREB1_MOUSE

Protein

Cyclic AMP-responsive element-binding protein 1

Gene

Creb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters. Transcription activation is enhanced by the TORC coactivators which act independently of Ser-133 phosphorylation. Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei314 – 3141Required for binding TORCsBy similarity

    GO - Molecular functioni

    1. cAMP response element binding Source: Ensembl
    2. DNA binding Source: MGI
    3. protein binding Source: IntAct
    4. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
    5. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    7. sequence-specific DNA binding Source: MGI
    8. sequence-specific DNA binding transcription factor activity Source: MGI

    GO - Biological processi

    1. axonogenesis Source: MGI
    2. cellular response to growth factor stimulus Source: BHF-UCL
    3. cellular response to zinc ion Source: MGI
    4. circadian rhythm Source: UniProtKB
    5. lactation Source: MGI
    6. lung epithelium development Source: MGI
    7. lung saccule development Source: MGI
    8. mammary gland development Source: MGI
    9. memory Source: MGI
    10. negative regulation of transcription by competitive promoter binding Source: Ensembl
    11. pituitary gland development Source: MGI
    12. positive regulation of fat cell differentiation Source: UniProtKB
    13. positive regulation of hormone secretion Source: MGI
    14. positive regulation of lipid biosynthetic process Source: UniProtKB
    15. positive regulation of multicellular organism growth Source: MGI
    16. positive regulation of osteoclast differentiation Source: MGI
    17. positive regulation of transcription, DNA-templated Source: UniProtKB
    18. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    19. protein phosphorylation Source: MGI
    20. protein stabilization Source: UniProtKB
    21. regulation of cell size Source: MGI
    22. regulation of transcription, DNA-templated Source: MGI
    23. response to drug Source: MGI
    24. response to glucagon Source: UniProtKB
    25. response to organic substance Source: MGI
    26. secretory granule organization Source: MGI
    27. Type I pneumocyte differentiation Source: MGI

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Biological rhythms, Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_213852. PKA-mediated phosphorylation of CREB.
    REACT_215503. CREB phosphorylation through the activation of CaMKK.
    REACT_216520. CaMK IV-mediated phosphorylation of CREB.
    REACT_218211. AKT phosphorylates targets in the nucleus.
    REACT_224314. CREB phosphorylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic AMP-responsive element-binding protein 1
    Short name:
    CREB-1
    Short name:
    cAMP-responsive element-binding protein 1
    Gene namesi
    Name:Creb1
    Synonyms:Creb-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:88494. Creb1.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nuclear chromatin Source: BHF-UCL
    2. nuclear euchromatin Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi133 – 1331S → A: Loss of phosphorylation by RPS6KA4 and RPS6KA5. 2 Publications
    Mutagenesisi137 – 1382IL → AA: Abolishes CREBBP binding. 1 Publication
    Mutagenesisi142 – 1421S → A: Attenuates light-induced phase shifts of locomotion and expression of c-Fos and mPer1 in the SCN. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341Cyclic AMP-responsive element-binding protein 1PRO_0000076598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei133 – 1331Phosphoserine; by CaMK1, CaMK2, CaMK4, PKB/AKT1 or PKB/AKT2, RPS6KA3, RPS6KA4, RPS6KA5 and SGK14 PublicationsPROSITE-ProRule annotation
    Modified residuei142 – 1421Phosphoserine; by CaMK2PROSITE-ProRule annotation
    Modified residuei271 – 2711Phosphoserine; by HIPK2PROSITE-ProRule annotation
    Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
    Cross-linki304 – 304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

    Post-translational modificationi

    Phosphorylation of Ser-133 allows CREBBP binding. Stimulated by phosphorylation. Phosphorylated Ser-142 can be detected in the suprachiasmatic nucleus (SCN), the amygdala, the cortex, and the hippocampus but not in the striatum nor in the cerebellum. In the SCN, phosphorylation of Ser-142 and Ser-133 are stimulated by light exposure and submitted to circadian oscillations. In the retina, only phosphorylation of Ser-133 can be detected upon light exposure. Phosphorylation of both Ser-133 and Ser-142 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-133. CaMK4 is much more potent than CAMK2 in activating CREB. Phosphorylated by CaMK2 on Ser-142. Phosphorylation of Ser-142 blocks CREB-mediated transcription even when Ser-133 is phosphorylated. Phosphorylated by CaMK1. Phosphorylation of Ser-271 by HIPK2 in response to genotoxic stress promotes CREB1 activity, facilitating the recruitment of the coactivator CBP By similarity. Phosphorylated at Ser-133 by RPS6KA3, RPS6KA4 and RPS6KA5 in response to mitogenic or stress stimuli. CREBL2 positively regulates phosphorylation at Ser-133 thereby stimulating CREB1 transcriptional activity. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion.By similarity4 Publications
    Sumoylated with SUMO1. Sumoylation on Lys-304, but not on Lys-285, is required for nuclear localization of this protein. Sumoylation is enhanced under hypoxia, promoting nuclear localization and stabilization By similarity.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ01147.
    PaxDbiQ01147.
    PRIDEiQ01147.

    PTM databases

    PhosphoSiteiQ01147.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ01147.
    BgeeiQ01147.
    CleanExiMM_CREB1.
    GenevestigatoriQ01147.

    Interactioni

    Subunit structurei

    Interacts with PPRC1. Binds DNA as a dimer. This dimer is stabilized by magnesium ions. Interacts, through the bZIP domain, with the coactivators TORC1/CRTC1, TORC2/CRTC2 and TORC3/CRTC3. Interacts (phosphorylated form) with TOX3 By similarity. When phosphorylated on Ser-133, binds CREBBP. Interacts with ARRB1. Binds to HIPK2 By similarity. Interacts with SGK1 By similarity. Interacts with CREBL2; regulates CREB1 phosphorylation, stability and transcriptional activity.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CrebbpP454812EBI-2291098,EBI-296306
    Crebl2Q32M004EBI-2291098,EBI-5314489
    EP300Q094722EBI-2291098,EBI-447295From a different organism.
    Ncor1Q609745EBI-2291098,EBI-349004

    Protein-protein interaction databases

    BioGridi198873. 13 interactions.
    IntActiQ01147. 9 interactions.
    MINTiMINT-263062.

    Structurei

    Secondary structure

    1
    341
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi286 – 33348

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DH3X-ray3.00A/C285-339[»]
    ProteinModelPortaliQ01147.
    SMRiQ01147. Positions 116-149, 285-339.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01147.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 16060KIDPROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 34159bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni284 – 30926Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni311 – 33222Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation
    Contains 1 KID (kinase-inducible) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG300199.
    HOGENOMiHOG000007365.
    HOVERGENiHBG011077.
    InParanoidiQ01147.
    KOiK05870.
    OMAiQXISTIA.
    OrthoDBiEOG72G18D.
    PhylomeDBiQ01147.
    TreeFamiTF106464.

    Family and domain databases

    InterProiIPR004827. bZIP.
    IPR003102. Coactivator_CBP_pKID.
    IPR001630. Leuzip_CREB.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    PF02173. pKID. 1 hit.
    [Graphical view]
    PRINTSiPR00041. LEUZIPPRCREB.
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    PS50953. KID. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: At least 6 isoforms are produced.

    Isoform 1 (identifier: Q01147-1) [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

    MTMESGADNQ QSGDAAVTEA ENQQMTVQAQ PQIATLAQVS MPAAHATSSA    50
    PTVTLVQLPN GQTVQVHGVI QAAQPSVIQS PQVQTVQSSC KDLKRLFSGT 100
    QISTIAESED SQESVDSVTD SQKRREILSR RPSYRKILND LSSDAPGVPR 150
    IEEEKSEEET SAPAITTVTV PTPIYQTSSG QYIAITQGGA IQLANNGTDG 200
    VQGLQTLTMT NAAATQPGTT ILQYAQTTDG QQILVPSNQV VVQAASGDVQ 250
    TYQIRTAPTS TIAPGVVMAS SPALPTQPAE EAARKREVRL MKNREAAREC 300
    RRKKKEYVKC LENRVAVLEN QNKTLIEELK ALKDLYCHKS D 341
    Length:341
    Mass (Da):36,674
    Last modified:June 1, 1994 - v1
    Checksum:iCF2958DE9174968A
    GO
    Isoform 2 (identifier: Q01147-2) [UniParc]FASTAAdd to Basket

    Also known as: CREB-delta

    The sequence of this isoform differs from the canonical sequence as follows:
         88-101: Missing.

    Show »
    Length:327
    Mass (Da):35,122
    Checksum:i00D1F26B00D48442
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei88 – 10114Missing in isoform 2. CuratedVSP_000597Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67719
    , X67721, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47953.1.
    X67719
    , X67721, X67722, X67724, X67725, X67726, X67727, X67728 Genomic DNA. Translation: CAA47954.1.
    M95106 mRNA. Translation: AAA37456.1.
    CCDSiCCDS15004.1. [Q01147-1]
    CCDS15005.1. [Q01147-2]
    PIRiS20955.
    S42699.
    RefSeqiNP_034082.1. NM_009952.2. [Q01147-1]
    NP_598589.2. NM_133828.2. [Q01147-2]
    XP_006495713.1. XM_006495650.1. [Q01147-1]
    XP_006495714.1. XM_006495651.1. [Q01147-2]
    UniGeneiMm.422634.

    Genome annotation databases

    EnsembliENSMUST00000049932; ENSMUSP00000059973; ENSMUSG00000025958. [Q01147-1]
    ENSMUST00000087366; ENSMUSP00000084624; ENSMUSG00000025958. [Q01147-2]
    GeneIDi12912.
    KEGGimmu:12912.
    UCSCiuc007bgr.1. mouse. [Q01147-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X67719
    , X67721 , X67724 , X67725 , X67726 , X67727 , X67728 Genomic DNA. Translation: CAA47953.1 .
    X67719
    , X67721 , X67722 , X67724 , X67725 , X67726 , X67727 , X67728 Genomic DNA. Translation: CAA47954.1 .
    M95106 mRNA. Translation: AAA37456.1 .
    CCDSi CCDS15004.1. [Q01147-1 ]
    CCDS15005.1. [Q01147-2 ]
    PIRi S20955.
    S42699.
    RefSeqi NP_034082.1. NM_009952.2. [Q01147-1 ]
    NP_598589.2. NM_133828.2. [Q01147-2 ]
    XP_006495713.1. XM_006495650.1. [Q01147-1 ]
    XP_006495714.1. XM_006495651.1. [Q01147-2 ]
    UniGenei Mm.422634.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DH3 X-ray 3.00 A/C 285-339 [» ]
    ProteinModelPortali Q01147.
    SMRi Q01147. Positions 116-149, 285-339.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198873. 13 interactions.
    IntActi Q01147. 9 interactions.
    MINTi MINT-263062.

    PTM databases

    PhosphoSitei Q01147.

    Proteomic databases

    MaxQBi Q01147.
    PaxDbi Q01147.
    PRIDEi Q01147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049932 ; ENSMUSP00000059973 ; ENSMUSG00000025958 . [Q01147-1 ]
    ENSMUST00000087366 ; ENSMUSP00000084624 ; ENSMUSG00000025958 . [Q01147-2 ]
    GeneIDi 12912.
    KEGGi mmu:12912.
    UCSCi uc007bgr.1. mouse. [Q01147-1 ]

    Organism-specific databases

    CTDi 1385.
    MGIi MGI:88494. Creb1.

    Phylogenomic databases

    eggNOGi NOG300199.
    HOGENOMi HOG000007365.
    HOVERGENi HBG011077.
    InParanoidi Q01147.
    KOi K05870.
    OMAi QXISTIA.
    OrthoDBi EOG72G18D.
    PhylomeDBi Q01147.
    TreeFami TF106464.

    Enzyme and pathway databases

    Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198248. CREB phosphorylation through the activation of CaMKII.
    REACT_205251. Transcriptional activation of mitochondrial biogenesis.
    REACT_213852. PKA-mediated phosphorylation of CREB.
    REACT_215503. CREB phosphorylation through the activation of CaMKK.
    REACT_216520. CaMK IV-mediated phosphorylation of CREB.
    REACT_218211. AKT phosphorylates targets in the nucleus.
    REACT_224314. CREB phosphorylation.

    Miscellaneous databases

    EvolutionaryTracei Q01147.
    NextBioi 282540.
    PROi Q01147.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01147.
    Bgeei Q01147.
    CleanExi MM_CREB1.
    Genevestigatori Q01147.

    Family and domain databases

    InterProi IPR004827. bZIP.
    IPR003102. Coactivator_CBP_pKID.
    IPR001630. Leuzip_CREB.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    PF02173. pKID. 1 hit.
    [Graphical view ]
    PRINTSi PR00041. LEUZIPPRCREB.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    PS50953. KID. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Multiple mRNA isoforms of the transcription activator protein CREB: generation by alternative splicing and specific expression in primary spermatocytes."
      Ruppert S., Cole T.J., Boshart M., Schmid E., Schuetz G.
      EMBO J. 11:1503-1512(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The mouse CREB (cAMP responsive element binding protein) gene: structure, promoter analysis, and chromosomal localization."
      Cole T.J., Copeland N.G., Gilbert D.J., Jenkins N.A., Schuetz G., Ruppert R.
      Genomics 13:974-982(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    3. "Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism."
      Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., Hoeger C., Montminy M.R.
      Mol. Cell. Biol. 16:694-703(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CREBBP, PHOSPHORYLATION AT SER-133, MUTAGENESIS OF 137-ILE-LEU-138.
    4. "Phosphorylation of CREB Ser142 regulates light-induced phase shifts of the circadian clock."
      Gau D., Lemberger T., von Gall C., Kretz O., Le Minh N., Gass P., Schmid W., Schibler U., Korf H.W., Schuetz G.
      Neuron 34:245-253(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-133 AND SER-142, MUTAGENESIS OF SER-142, FUNCTION.
    5. "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor signaling."
      Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M., Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.
      Nat. Immunol. 9:1028-1036(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-133, MUTAGENESIS OF SER-133.
    6. "Cryptochrome mediates circadian regulation of cAMP signaling and hepatic gluconeogenesis."
      Zhang E.E., Liu Y., Dentin R., Pongsawakul P.Y., Liu A.C., Hirota T., Nusinow D.A., Sun X., Landais S., Kodama Y., Brenner D.A., Montminy M., Kay S.A.
      Nat. Med. 16:1152-1156(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    7. "CREBL2, interacting with CREB, induces adipogenesis in 3T3-L1 adipocytes."
      Ma X., Zhang H., Yuan L., Jing H., Thacker P., Li D.
      Biochem. J. 439:27-38(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, INTERACTION WITH CREBL2, SUBCELLULAR LOCATION.
    8. "The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding."
      Schumacher M.A., Goodman R.H., Brennan R.G.
      J. Biol. Chem. 275:35242-35247(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH THE SOMATOSTATIN CAMP RESPONSE ELEMENT (SSCRE).

    Entry informationi

    Entry nameiCREB1_MOUSE
    AccessioniPrimary (citable) accession number: Q01147
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 148 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, 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