Smurf2 E3 ubiquitin-protein ligase SMURF2

• Overview
• Annotations

UniProt Data

Enzyme Annotations (1)

• EC:2.3.2.26 HECT-type E3 ubiquitin transferase.
  S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.

GO Annotations

Cellular component (3)

• GO:0000151 Ubiquitin ligase complex
  A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.
• GO:0005829 Cytosol
  The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
• GO:0016607 Nuclear speck
  A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.

Molecular function (5)

• GO:0004842 Ubiquitin-protein transferase activity
  Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
• GO:0005515 Protein binding
  Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
• GO:0042802 Identical protein binding
  Interacting selectively and non-covalently with an identical protein or proteins.
• GO:0046332 SMAD binding
  Interacting selectively and non-covalently with a SMAD signaling protein.
• GO:0061630 Ubiquitin protein ligase activity
  Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.

Biological process (4)

• GO:0006511 Ubiquitin-dependent protein catabolic process
  The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
• GO:0030512 Negative regulation of transforming growth factor beta receptor signaling pathway
  Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway.
• GO:0030579 Ubiquitin-dependent SMAD protein catabolic process
  The chemical reactions and pathways resulting in the breakdown of SMAD signaling proteins by ubiquitination and targeting to the proteasome.
• GO:1901165 Positive regulation of trophoblast cell migration
  Any process that activates or increases the frequency, rate or extent of trophoblast cell migration.

Protein Sequence

>A2A5Z6
MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVW
NHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLP
DGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRN
YMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNN
RTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVPLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSRE
EIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHL
SYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEII
QHELKPNGKSIPVTEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVSDWKVN
TRLKHCTPDSNVVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRI
DIPPYESYEKLYEKLLTAIEETCGFAVE