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Protein

E3 ubiquitin-protein ligase SMURF2

Gene

SMURF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. SMAD binding Source: BHF-UCL
  4. 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: CACAO
  6. positive regulation of canonical Wnt signaling pathway Source: Reactome
  7. positive regulation of trophoblast cell migration Source: CACAO
  8. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: GO_Central
  9. regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  10. transcription, DNA-templated Source: Reactome
  11. transcription initiation from RNA polymerase II promoter Source: Reactome
  12. transforming growth factor beta receptor signaling pathway Source: GO_Central
  13. ubiquitin-dependent protein catabolic process Source: UniProtKB
  14. ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi6.3.2.19. 2681.
ReactomeiREACT_12034. Signaling by BMP.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_263873. degradation of AXIN.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_268718. Hedgehog 'on' state.
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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:16809. SMURF2.

Subcellular locationi

  1. Nucleus 1 Publication
  2. Cytoplasm 1 Publication
  3. Cell membrane 1 Publication
  4. Membrane raft 1 Publication

  5. Note: Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  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
Complete GO annotation...

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. 1 Publication
Mutagenesisi30 – 301F → A: Increases autoubiquitination; when associated with A-29. 1 Publication
Mutagenesisi56 – 561T → A: Increases autoubiquitination; when associated with A-57. 1 Publication
Mutagenesisi57 – 571L → A: Increases autoubiquitination; when associated with A-56. 1 Publication
Mutagenesisi251 – 28434Missing : Abolishes interaction with SMAD2 and SMAD7. 2 PublicationsAdd
BLAST
Mutagenesisi297 – 33034Missing : Abolishes interaction with SMAD7. 1 PublicationAdd
BLAST
Mutagenesisi535 – 5351W → A: Loss of catalytic activity. 1 Publication
Mutagenesisi535 – 5351W → D: Loss of catalytic activity. 1 Publication
Mutagenesisi547 – 5471H → A: Partial loss of catalytic activity. 1 Publication
Mutagenesisi547 – 5471H → F or I: Activates autocatalytic activity. 1 Publication
Mutagenesisi581 – 5811Y → A: Loss of catalytic activity. 1 Publication
Mutagenesisi716 – 7161C → A: Increases Smad7-bound TGF-beta receptors in membrane rafts. 3 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. 3 Publications

Organism-specific databases

PharmGKBiPA134985524.

Polymorphism and mutation databases

BioMutaiSMURF2.
DMDMi17865624.

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

BgeeiQ9HAU4.
CleanExiHS_SMURF2.
ExpressionAtlasiQ9HAU4. baseline and differential.
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
SMAD3P840225EBI-396727,EBI-347161
UBBP0CG474EBI-396727,EBI-413034

Protein-protein interaction databases

BioGridi122265. 119 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 – 2312Combined sources
Beta strandi35 – 417Combined sources
Turni42 – 443Combined sources
Beta strandi48 – 503Combined sources
Beta strandi60 – 6910Combined sources
Beta strandi75 – 817Combined sources
Helixi82 – 876Combined sources
Beta strandi93 – 997Combined sources
Helixi101 – 11010Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi258 – 2625Combined sources
Turni263 – 2653Combined sources
Beta strandi266 – 2716Combined sources
Turni272 – 2754Combined sources
Beta strandi276 – 2805Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi286 – 2883Combined sources
Helixi293 – 2953Combined sources
Beta strandi301 – 3077Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi313 – 3175Combined sources
Turni318 – 3214Combined sources
Beta strandi322 – 3265Combined sources
Turni328 – 3303Combined sources
Helixi372 – 38615Combined sources
Beta strandi392 – 3976Combined sources
Helixi402 – 41110Combined sources
Helixi415 – 4195Combined sources
Beta strandi420 – 4267Combined sources
Helixi434 – 44916Combined sources
Helixi452 – 4543Combined sources
Beta strandi455 – 4606Combined sources
Beta strandi463 – 4697Combined sources
Helixi473 – 4753Combined sources
Helixi479 – 49517Combined sources
Helixi506 – 5127Combined sources
Helixi522 – 5254Combined sources
Helixi527 – 53812Combined sources
Turni542 – 5443Combined sources
Beta strandi549 – 5557Combined sources
Beta strandi558 – 5658Combined sources
Turni574 – 5774Combined sources
Helixi578 – 59013Combined sources
Turni591 – 5944Combined sources
Helixi595 – 60814Combined sources
Helixi611 – 6144Combined sources
Helixi619 – 6279Combined sources
Beta strandi629 – 6313Combined sources
Helixi634 – 6396Combined sources
Beta strandi641 – 6466Combined sources
Helixi651 – 66212Combined sources
Helixi665 – 67612Combined sources
Beta strandi679 – 6813Combined sources
Helixi686 – 6883Combined sources
Beta strandi698 – 7025Combined sources
Beta strandi712 – 7143Combined sources
Helixi715 – 7173Combined sources
Beta strandi719 – 7224Combined sources
Helixi728 – 73912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9HAU4.
KOiK04678.
OMAiKIDIHDW.
PhylomeDBiQ9HAU4.
TreeFamiTF323658.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
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

        10         20         30         40         50
MSNPGGRRNG PVKLRLTVLC AKNLVKKDFF RLPDPFAKVV VDGSGQCHST
60 70 80 90 100
DTVKNTLDPK WNQHYDLYIG KSDSVTISVW NHKKIHKKQG AGFLGCVRLL
110 120 130 140 150
SNAINRLKDT GYQRLDLCKL GPNDNDTVRG QIVVSLQSRD RIGTGGQVVD
160 170 180 190 200
CSRLFDNDLP DGWEERRTAS GRIQYLNHIT RTTQWERPTR PASEYSSPGR
210 220 230 240 250
PLSCFVDENT PISGTNGATC GQSSDPRLAE RRVRSQRHRN YMSRTHLHTP
260 270 280 290 300
PDLPEGYEQR TTQQGQVYFL HTQTGVSTWH DPRVPRDLSN INCEELGPLP
310 320 330 340 350
PGWEIRNTAT GRVYFVDHNN RTTQFTDPRL SANLHLVLNR QNQLKDQQQQ
360 370 380 390 400
QVVSLCPDDT ECLTVPRYKR DLVQKLKILR QELSQQQPQA GHCRIEVSRE
410 420 430 440 450
EIFEESYRQV MKMRPKDLWK RLMIKFRGEE GLDYGGVARE WLYLLSHEML
460 470 480 490 500
NPYYGLFQYS RDDIYTLQIN PDSAVNPEHL SYFHFVGRIM GMAVFHGHYI
510 520 530 540 550
DGGFTLPFYK QLLGKSITLD DMELVDPDLH NSLVWILEND ITGVLDHTFC
560 570 580 590 600
VEHNAYGEII QHELKPNGKS IPVNEENKKE YVRLYVNWRF LRGIEAQFLA
610 620 630 640 650
LQKGFNEVIP QHLLKTFDEK ELELIICGLG KIDVNDWKVN TRLKHCTPDS
660 670 680 690 700
NIVKWFWKAV EFFDEERRAR LLQFVTGSSR VPLQGFKALQ GAAGPRLFTI
710 720 730 740
HQIDACTNNL PKAHTCFNRI DIPPYESYEK LYEKLLTAIE ETCGFAVE
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiSMURF2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi122265. 119 interactions.
DIPiDIP-33061N.
IntActiQ9HAU4. 65 interactions.
MINTiMINT-1180022.
STRINGi9606.ENSP00000262435.

PTM databases

PhosphoSiteiQ9HAU4.

Polymorphism and mutation databases

BioMutaiSMURF2.
DMDMi17865624.

Proteomic databases

MaxQBiQ9HAU4.
PaxDbiQ9HAU4.
PRIDEiQ9HAU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi64750.
GeneCardsiGC17M062540.
HGNCiHGNC:16809. SMURF2.
MIMi605532. gene.
neXtProtiNX_Q9HAU4.
PharmGKBiPA134985524.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5021.
GeneTreeiENSGT00760000118966.
HOGENOMiHOG000208451.
HOVERGENiHBG004134.
InParanoidiQ9HAU4.
KOiK04678.
OMAiKIDIHDW.
PhylomeDBiQ9HAU4.
TreeFamiTF323658.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
ReactomeiREACT_12034. Signaling by BMP.
REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_263873. degradation of AXIN.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_268718. Hedgehog 'on' state.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ9HAU4.

Miscellaneous databases

ChiTaRSiSMURF2. human.
EvolutionaryTraceiQ9HAU4.
GeneWikiiSMURF2.
GenomeRNAii64750.
NextBioi66708.
PROiQ9HAU4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAU4.
CleanExiHS_SMURF2.
ExpressionAtlasiQ9HAU4. baseline and differential.
GenevestigatoriQ9HAU4.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR000569. HECT.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.