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Protein Page:
SMURF2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SMURF2 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. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Ligase; Ubiquitin conjugating system; EC 6.3.2.19; EC 6.3.2.-
Chromosomal Location of Human Ortholog: 17q22-q23
Cellular Component: cytoplasm; cytosol; lipid raft; nucleoplasm; nucleus; plasma membrane; ubiquitin ligase complex
Molecular Function: identical protein binding; ligase activity; protein binding; SMAD binding; transforming growth factor beta receptor binding; ubiquitin-protein ligase activity
Biological Process: BMP signaling pathway; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of transforming growth factor beta receptor signaling pathway; protein polyubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of transforming growth factor beta receptor signaling pathway; ubiquitin-dependent protein catabolic process; ubiquitin-dependent SMAD protein catabolic process; Wnt receptor signaling pathway, planar cell polarity pathway
Reference #:  Q9HAU4 (UniProtKB)
Alt. Names/Synonyms: DKFZp686F0270; E3 ubiquitin ligase SMURF2; E3 ubiquitin-protein ligase SMURF2; hSMURF2; MGC138150; SMAD specific E3 ubiquitin protein ligase 2; SMAD ubiquitination regulatory factor 2; SMAD-specific E3 ubiquitin-protein ligase 2; SMUF2; SMURF2
Gene Symbols: SMURF2
Molecular weight: 86,196 Da
Basal Isoelectric point: 8.18  Predict pI for various phosphorylation states
CST Pathways:  TGF-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SMURF2

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 K26‑sm LCAKNLVkKDFFRLP
1 0 K38‑ub RLPDPFAkVVVDGsG
0 2 S44‑p AkVVVDGsGQCHSTD
0 1 T168‑p DGWEERRtAsGRIQY
0 1 S170‑p WEERRtAsGRIQYLN
0 2 S203‑p SSPGRPLsCFVDENT
0 1 T249‑p MSRTHLHtPPDLPEG
0 1 K345 LNRQNQLKDQQQQQV
1 0 K369‑sm CLTVPRYkRDLVQkL
1 0 K375‑ub YkRDLVQkLkILRQE
1 0 K377‑ub RDLVQkLkILRQELS
1 0 K412‑ub ESYRQVMkMRPKDLW
0 3 Y434‑p RGEEGLDyGGVAREW
0 1 Y499‑p MAVFHGHyIDGGFTL
1 0 K578‑ub IPVNEENkkEYVRLY
1 0 K579‑ub PVNEENkkEYVRLYV
0 1 K615 VIPQHLLKTFDEKEL
1 0 K638‑ub KIDVNDWkVNTRLKH
1 0 K734‑ub SYEKLYEkLLTAIEE
  mouse

 
K26 LCAKNLVKKDFFRLP
K38 RLPDPFAKVVVDGsG
S44‑p AKVVVDGsGQCHSTD
T168 DGWEERRTASGRIQY
S170 WEERRTASGRIQYLN
S203 SSPGRPLSCFVDENT
T249 MSRTHLHTPPDLPEG
K345‑ub LNRQNQLkDQQQQQV
K369 CLTVPRYKRDLVQKL
K375 YKRDLVQKLKILRQE
K377 RDLVQKLKILRQELS
K412 ESYRQVMKMRPKDLW
Y434 RGEEGLDYGGVAREW
Y499 MAVFHGHYIDGGFTL
K578 IPVTEENKKEYVRLY
K579 PVTEENKKEYVRLYV
K615‑ub VIPQHLLkTFDEKEL
K638 KIDVSDWKVNTRLKH
K734 SYEKLYEKLLTAIEE
  rat

 
K26 LCAKNLVKKDFFRLP
K38 RLPDPFAKVVVDGSG
S44 AKVVVDGSGQCHSTD
T168 DGWEERRTASGRIQY
S170 WEERRTASGRIQYLN
S203 SSPGRPLSCFVDENT
T249 MSRTHLHTPPDLPEG
K345 LNRQNQLKDQQQQQV
K369 CLTVPRYKRDLVQKL
K375 YKRDLVQKLKILRQE
K377 RDLVQKLKILRQELS
K412 ESYRQVMKMRPKDLW
Y434‑p RGEEGLDyGGVAREW
Y499 MAVFHGHYIDGGFTL
K578 IPVTEENKKEYVRLY
K579 PVTEENKKEYVRLYV
K615 VIPQHLLKTFDEKEL
K638 KIDVSDWKANTRLKH
K734 SYEKLYEKLLTAIEE
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