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Q9HAU4

- SMUF2_HUMAN

UniProt

Q9HAU4 - SMUF2_HUMAN

Protein

E3 ubiquitin-protein ligase SMURF2

Gene

SMURF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD1 and SMAD7 in order to trigger their ubiquitination and proteasome-dependent degradation. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with SCYE1. Forms a stable complex with the TGF-beta receptor-mediated phosphorylated SMAD2 and SMAD3. In this way, SMAD2 may recruit substrates, such as SNON, for ubiquitin-mediated degradation. Enhances the inhibitory activity of SMAD7 and reduces the transcriptional activity of SMAD2. Coexpression of SMURF2 with SMAD1 results in considerable decrease in steady-state level of SMAD1 protein and a smaller decrease of SMAD2 level.2 Publications

    Enzyme regulationi

    Activated by NDFIP1- and NDFIP2-binding.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei716 – 7161Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. SMAD binding Source: BHF-UCL
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. BMP signaling pathway Source: Reactome
    2. gene expression Source: Reactome
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    5. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    7. regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
    8. transcription, DNA-templated Source: Reactome
    9. transcription initiation from RNA polymerase II promoter Source: Reactome
    10. transforming growth factor beta receptor signaling pathway Source: RefGenome
    11. ubiquitin-dependent protein catabolic process Source: UniProtKB
    12. ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_12034. Signaling by BMP.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_200766. degradation of AXIN.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9HAU4.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase SMURF2 (EC:6.3.2.-)
    Short name:
    hSMURF2
    Alternative name(s):
    SMAD ubiquitination regulatory factor 2
    SMAD-specific E3 ubiquitin-protein ligase 2
    Gene namesi
    Name:SMURF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:16809. SMURF2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication. Cell membrane 1 Publication. Membrane raft 1 Publication
    Note: Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. cytosol Source: Reactome
    3. membrane raft Source: UniProtKB-SubCell
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: UniProtKB-SubCell
    7. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291F → A: Increases autoubiquitination; when associated with A-30. 2 Publications
    Mutagenesisi30 – 301F → A: Increases autoubiquitination; when associated with A-29. 2 Publications
    Mutagenesisi56 – 561T → A: Increases autoubiquitination; when associated with A-57. 2 Publications
    Mutagenesisi57 – 571L → A: Increases autoubiquitination; when associated with A-56. 2 Publications
    Mutagenesisi251 – 28434Missing: Abolishes interaction with SMAD2 and SMAD7. 1 PublicationAdd
    BLAST
    Mutagenesisi297 – 33034Missing: Abolishes interaction with SMAD7. 1 PublicationAdd
    BLAST
    Mutagenesisi535 – 5351W → A: Loss of catalytic activity. 2 Publications
    Mutagenesisi535 – 5351W → D: Loss of catalytic activity. 2 Publications
    Mutagenesisi547 – 5471H → A: Partial loss of catalytic activity. 2 Publications
    Mutagenesisi547 – 5471H → F or I: Activates autocatalytic activity. 2 Publications
    Mutagenesisi581 – 5811Y → A: Loss of catalytic activity. 2 Publications
    Mutagenesisi716 – 7161C → A: Increases Smad7-bound TGF-beta receptors in membrane rafts. 4 Publications
    Mutagenesisi716 – 7161C → G: Loss of activity. Loss of ability to ubiquitinate SMAD1 and SMAD2 and no down-regulation of SMAD1 and SMAD2 protein levels. 4 Publications

    Organism-specific databases

    PharmGKBiPA134985524.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 748748E3 ubiquitin-protein ligase SMURF2PRO_0000120329Add
    BLAST

    Post-translational modificationi

    Auto-ubiquitinated and ubiquitinated in the presence of RNF11 and UBE2D1. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9HAU4.
    PaxDbiQ9HAU4.
    PRIDEiQ9HAU4.

    PTM databases

    PhosphoSiteiQ9HAU4.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiQ9HAU4.
    BgeeiQ9HAU4.
    CleanExiHS_SMURF2.
    GenevestigatoriQ9HAU4.

    Interactioni

    Subunit structurei

    Interacts (via WW domains) with SMAD1. Interacts (via WW domains) with SMAD2 (via PY-motif). Interacts (via WW domains) with SMAD3 (via PY-motif). Interacts with SMAD6. Interacts with SMAD7 (via PY-motif) and TGFBR1; SMAD7 recruits SMURF2 to the TGF-beta receptor and regulates its degradation. Does not interact with SMAD4; SMAD4 lacks a PY-motif. Interacts with AIMP1. Interacts with STAMBP and RNF11. Interacts with NDFIP1 and NDFIP2 Probable; this interaction activates the E3 ubiquitin-protein ligase.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-396727,EBI-396727
    Q9WMX22EBI-396727,EBI-6863741From a different organism.
    FBXL15Q9H4693EBI-396727,EBI-6144096
    RNF11Q9Y3C55EBI-396727,EBI-396669
    SMAD2Q157965EBI-396727,EBI-1040141
    SMAD3P840227EBI-396727,EBI-347161
    UBBP0CG474EBI-396727,EBI-413034

    Protein-protein interaction databases

    BioGridi122265. 117 interactions.
    DIPiDIP-33061N.
    IntActiQ9HAU4. 65 interactions.
    MINTiMINT-1180022.
    STRINGi9606.ENSP00000262435.

    Structurei

    Secondary structure

    1
    748
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 2312
    Beta strandi35 – 417
    Turni42 – 443
    Beta strandi48 – 503
    Beta strandi60 – 6910
    Beta strandi75 – 817
    Helixi82 – 876
    Beta strandi93 – 997
    Helixi101 – 11010
    Beta strandi113 – 1153
    Beta strandi131 – 1388
    Beta strandi258 – 2625
    Turni263 – 2653
    Beta strandi266 – 2716
    Turni272 – 2754
    Beta strandi276 – 2805
    Beta strandi282 – 2843
    Beta strandi286 – 2883
    Helixi293 – 2953
    Beta strandi301 – 3077
    Beta strandi309 – 3113
    Beta strandi313 – 3175
    Turni318 – 3214
    Beta strandi322 – 3265
    Turni328 – 3303
    Helixi372 – 38615
    Beta strandi392 – 3976
    Helixi402 – 41110
    Helixi415 – 4195
    Beta strandi420 – 4267
    Helixi434 – 44916
    Helixi452 – 4543
    Beta strandi455 – 4606
    Beta strandi463 – 4697
    Helixi473 – 4753
    Helixi479 – 49517
    Helixi506 – 5127
    Helixi522 – 5254
    Helixi527 – 53812
    Turni542 – 5443
    Beta strandi549 – 5557
    Beta strandi558 – 5658
    Turni574 – 5774
    Helixi578 – 59013
    Turni591 – 5944
    Helixi595 – 60814
    Helixi611 – 6144
    Helixi619 – 6279
    Beta strandi629 – 6313
    Helixi634 – 6396
    Beta strandi641 – 6466
    Helixi651 – 66212
    Helixi665 – 67612
    Beta strandi679 – 6813
    Helixi686 – 6883
    Beta strandi698 – 7025
    Beta strandi712 – 7143
    Helixi715 – 7173
    Beta strandi719 – 7224
    Helixi728 – 73912

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZVDX-ray2.10A369-748[»]
    2DJYNMR-A297-333[»]
    2JQZNMR-A10-140[»]
    2KXQNMR-A250-333[»]
    2LTZNMR-A297-333[»]
    ProteinModelPortaliQ9HAU4.
    SMRiQ9HAU4. Positions 10-140, 159-192, 249-745.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HAU4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9898C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini157 – 19034WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini251 – 28434WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini297 – 33034WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 748335HECTPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The second and third WW domains are responsible for interaction with the PY-motif of R-SMAD (SMAD1, SMAD2 and SMAD3).
    The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain.

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 3 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    HOGENOMiHOG000208451.
    HOVERGENiHBG004134.
    InParanoidiQ9HAU4.
    KOiK04678.
    OMAiNQAARPF.
    PhylomeDBiQ9HAU4.
    TreeFamiTF323658.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9HAU4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNPGGRRNG PVKLRLTVLC AKNLVKKDFF RLPDPFAKVV VDGSGQCHST    50
    DTVKNTLDPK WNQHYDLYIG KSDSVTISVW NHKKIHKKQG AGFLGCVRLL 100
    SNAINRLKDT GYQRLDLCKL GPNDNDTVRG QIVVSLQSRD RIGTGGQVVD 150
    CSRLFDNDLP DGWEERRTAS GRIQYLNHIT RTTQWERPTR PASEYSSPGR 200
    PLSCFVDENT PISGTNGATC GQSSDPRLAE RRVRSQRHRN YMSRTHLHTP 250
    PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLSN INCEELGPLP 300
    PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNR QNQLKDQQQQ 350
    QVVSLCPDDT ECLTVPRYKR DLVQKLKILR QELSQQQPQA GHCRIEVSRE 400
    EIFEESYRQV MKMRPKDLWK RLMIKFRGEE GLDYGGVARE WLYLLSHEML 450
    NPYYGLFQYS RDDIYTLQIN PDSAVNPEHL SYFHFVGRIM GMAVFHGHYI 500
    DGGFTLPFYK QLLGKSITLD DMELVDPDLH NSLVWILEND ITGVLDHTFC 550
    VEHNAYGEII QHELKPNGKS IPVNEENKKE YVRLYVNWRF LRGIEAQFLA 600
    LQKGFNEVIP QHLLKTFDEK ELELIICGLG KIDVNDWKVN TRLKHCTPDS 650
    NIVKWFWKAV EFFDEERRAR LLQFVTGSSR VPLQGFKALQ GAAGPRLFTI 700
    HQIDACTNNL PKAHTCFNRI DIPPYESYEK LYEKLLTAIE ETCGFAVE 748
    Length:748
    Mass (Da):86,196
    Last modified:March 1, 2001 - v1
    Checksum:i3042B443A3755762
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61G → R in AAG45422. (PubMed:11016919)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF310676 mRNA. Translation: AAG45422.1.
    AF301463 mRNA. Translation: AAG25641.1.
    AY014180 mRNA. Translation: AAG50421.1.
    BC093876 mRNA. Translation: AAH93876.1.
    BC111945 mRNA. Translation: AAI11946.1.
    CCDSiCCDS32707.1.
    RefSeqiNP_073576.1. NM_022739.3.
    UniGeneiHs.515011.

    Genome annotation databases

    EnsembliENST00000262435; ENSP00000262435; ENSG00000108854.
    GeneIDi64750.
    KEGGihsa:64750.
    UCSCiuc002jep.1. human.

    Polymorphism databases

    DMDMi17865624.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF310676 mRNA. Translation: AAG45422.1 .
    AF301463 mRNA. Translation: AAG25641.1 .
    AY014180 mRNA. Translation: AAG50421.1 .
    BC093876 mRNA. Translation: AAH93876.1 .
    BC111945 mRNA. Translation: AAI11946.1 .
    CCDSi CCDS32707.1.
    RefSeqi NP_073576.1. NM_022739.3.
    UniGenei Hs.515011.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZVD X-ray 2.10 A 369-748 [» ]
    2DJY NMR - A 297-333 [» ]
    2JQZ NMR - A 10-140 [» ]
    2KXQ NMR - A 250-333 [» ]
    2LTZ NMR - A 297-333 [» ]
    ProteinModelPortali Q9HAU4.
    SMRi Q9HAU4. Positions 10-140, 159-192, 249-745.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122265. 117 interactions.
    DIPi DIP-33061N.
    IntActi Q9HAU4. 65 interactions.
    MINTi MINT-1180022.
    STRINGi 9606.ENSP00000262435.

    PTM databases

    PhosphoSitei Q9HAU4.

    Polymorphism databases

    DMDMi 17865624.

    Proteomic databases

    MaxQBi Q9HAU4.
    PaxDbi Q9HAU4.
    PRIDEi Q9HAU4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262435 ; ENSP00000262435 ; ENSG00000108854 .
    GeneIDi 64750.
    KEGGi hsa:64750.
    UCSCi uc002jep.1. human.

    Organism-specific databases

    CTDi 64750.
    GeneCardsi GC17M062540.
    HGNCi HGNC:16809. SMURF2.
    MIMi 605532. gene.
    neXtProti NX_Q9HAU4.
    PharmGKBi PA134985524.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000208451.
    HOVERGENi HBG004134.
    InParanoidi Q9HAU4.
    KOi K04678.
    OMAi NQAARPF.
    PhylomeDBi Q9HAU4.
    TreeFami TF323658.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_12034. Signaling by BMP.
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_200766. degradation of AXIN.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9HAU4.

    Miscellaneous databases

    ChiTaRSi SMURF2. human.
    EvolutionaryTracei Q9HAU4.
    GeneWikii SMURF2.
    GenomeRNAii 64750.
    NextBioi 66708.
    PROi Q9HAU4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAU4.
    Bgeei Q9HAU4.
    CleanExi HS_SMURF2.
    Genevestigatori Q9HAU4.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 3 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF-beta receptor for degradation."
      Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L.
      Mol. Cell 6:1365-1375(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF 251-PRO--VAL-284 AND 297-GLY--LEU-330, INTERACTION WITH SMAD7 AND TGFBR1.
    2. "Smurf2 Is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling."
      Lin X., Liang M., Feng X.-H.
      J. Biol. Chem. 275:36818-36822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF 251-PRO--VAL-284 AND CYS-716.
    3. "Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase."
      Zhang Y., Chang C., Gehling D.J., Hemmati-Brivanlou A., Derynck R.
      Proc. Natl. Acad. Sci. U.S.A. 98:974-979(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-716.
    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].
      Tissue: Brain.
    5. "TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation."
      Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L.
      Nat. Cell Biol. 3:587-595(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3 AND SNON.
    6. "Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover."
      Di Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L.
      Nat. Cell Biol. 5:410-421(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-716.
    7. Erratum
      Di Guglielmo G.M., Le Roy C., Goodfellow A.F., Wrana J.L.
      Nat. Cell Biol. 5:680-680(2003)
    8. "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase."
      Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.
      Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF11.
    9. "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein."
      Li H., Seth A.K.
      Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAMBP AND RNF11.
    10. "AIMP1/p43 downregulates TGF-beta signaling via stabilization of smurf2."
      Lee Y.S., Han J.M., Son S.H., Choi J.W., Jeon E.J., Bae S.-C., Park Y.I., Kim S.
      Biochem. Biophys. Res. Commun. 371:395-400(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIMP1.
    11. "Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins."
      Mund T., Pelham H.R.
      EMBO Rep. 10:501-507(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION BY NDFIP1 AND NDFIP2, AUTOUBIQUITINATION.
    12. "SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
      Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
      EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    13. "Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain."
      Ogunjimi A.A., Briant D.J., Pece-Barbara N., Le Roy C., Di Guglielmo G.M., Kavsak P., Rasmussen R.K., Seet B.T., Sicheri F., Wrana J.L.
      Mol. Cell 19:297-308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 369-748, INTERACTION WITH SMAD7, MUTAGENESIS OF TRP-535; HIS-547 AND TYR-581.
    14. "An expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2."
      Chong P.A., Lin H., Wrana J.L., Forman-Kay J.D.
      J. Biol. Chem. 281:17069-17075(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 297-333 IN COMPLEX WITH SMAD7.
    15. "Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain."
      Wiesner S., Ogunjimi A.A., Wang H.R., Rotin D., Sicheri F., Wrana J.L., Forman-Kay J.D.
      Cell 130:651-662(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 10-140, AUTOINHIBITION BY C2 DOMAIN, MUTAGENESIS OF PHE-29; PHE-30; THR-56 AND LEU-57.

    Entry informationi

    Entry nameiSMUF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAU4
    Secondary accession number(s): Q52LL1, Q9H260
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3