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Q9HAU4

- SMUF2_HUMAN

UniProt

Q9HAU4 - SMUF2_HUMAN

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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

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: 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
Complete GO annotation...

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. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: UniProtKB-KW
  6. 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.

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
SMAD3P840227EBI-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 – 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, 159-188, 249-742.
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.
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

        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:
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, 159-188, 249-742.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122265. 119 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.
GeneTreei ENSGT00760000118966.
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

Bgeei Q9HAU4.
CleanExi HS_SMURF2.
ExpressionAtlasi Q9HAU4. baseline and differential.
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

« 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: October 29, 2014
This is version 143 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