UniProt Accession

 SUFU_HUMAN; Q9UMX1; Q7LCP7; Q9NT90; Q9NZ07; Q9UHK2; Q9UHM8; Q9UMY0 

Genbank Protein ID

 AF144231; AF159447; AF222345; AF175770; AY081829; AY081818; AY081819; AY081820; AY081822; AY081824; AY081825; AY081821; AY081823; AY081826; AY081828; AY081827; AY358550; AL121928; AL391121; AL157386; AL121928; AL157386; AL391121; AL157386; AL391121; AL121928; AL157386; AL121928; AL391121; AL391121; AL121928; AL157386; AL391121; AL121928; AL157386; BC013291; AF172319; AL137465 

Genbank Nucleotide ID

 AAF23890.1; AAF23893.1; AAF35866.1; AAD50501.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAM08947.1; AAQ88914.1; CAI12525.1; CAI12525.1; CAI12525.1; CAI12526.1; CAI12526.1; CAI12526.1; CAI39614.1; CAI39614.1; CAI39614.1; CAI39615.1; CAI39615.1; CAI39615.1; CAI40864.1; CAI40864.1; CAI40864.1; CAI40865.1; CAI40865.1; CAI40865.1; AAH13291.1; AAD51655.1; CAB70752.1 

Protein Name

 Suppressor of fused homolog 

Protein Synonyms/Alias

 SUFUH 

Gene Name

 SUFU 

Gene Synonyms/Alias

 UNQ650/PRO1280 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
257	HLQERVDKGIETDGS	ubiquitination	[1, 2]
303	QPRRLSGKDTEQIRE	acetylation	[3]
321	RGLEINSKPVLPPIN	ubiquitination	[1, 2, 4, 5, 6]
344	HDRAPSRKDSLESDS	ubiquitination	[5]
457	LTSPEEFKLPKEYSW	ubiquitination	[1]
470	SWPEKKLKVSILPDV	ubiquitination	[5]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU- GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A). 

Sequence Annotation

 MOD_RES 303 303 N6-acetyllysine.
 MOD_RES 481 481 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Tumor suppressor. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 484 AA 

Protein Sequence

Gene Ontology

 GO:0005929; C:cilium; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0003714; F:transcription corepressor activity; TAS:UniProtKB.
 GO:0008134; F:transcription factor binding; IDA:MGI.
 GO:0042994; P:cytoplasmic sequestering of transcription factor; IEA:Compara.
 GO:0001947; P:heart looping; IEA:Compara.
 GO:0045668; P:negative regulation of osteoblast differentiation; TAS:BHF-UCL.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; TAS:BHF-UCL.
 GO:0045879; P:negative regulation of smoothened signaling pathway; TAS:BHF-UCL.
 GO:0042992; P:negative regulation of transcription factor import into nucleus; TAS:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
 GO:0001843; P:neural tube closure; IEA:Compara.
 GO:0006508; P:proteolysis; TAS:ProtInc.
 GO:0001501; P:skeletal system development; TAS:ProtInc.
 GO:0043588; P:skin development; IEA:Compara.
 GO:0021513; P:spinal cord dorsal/ventral patterning; IEA:Compara. 

Interpro

 IPR007768; SUFU-like.
 IPR024314; SUFU_C.
 IPR020941; SUFU_domain.
 IPR016591; Suppressor_of_fused_protein. 

Pfam

 PF05076; SUFU
 PF12470; SUFU_C 

SMART

  

PROSITE

  

PRINTS