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Q9UMX1 (SUFU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Suppressor of fused homolog

Short name=SUFUH
Gene names
Name:SUFU
ORF Names:UNQ650/PRO1280
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.2 Ref.3 Ref.9 Ref.14

Subunit structure

May form homodimers. Part of a DNA-bound corepressor complex containing SAP18, GLI1 and SIN3. Part of a complex containing CTNNB1. Binds BTRC, GLI2, GLI3, SAP18 and STK36. Binds both free and DNA-bound GLI1. Interacts with KIF7. Interacts with GLI3FL and this interaction regulates the formation of either repressor or activator forms of GLI3. Its association with GLI3FL is regulated by Hh signaling and dissociation of the SUFU-GLI3 interaction requires the presence of the ciliary motor KIF3A By similarity. Interacts with ULK3; inactivating the protein kinase activity of ULK3. Interacts with RAB23. Ref.1 Ref.2 Ref.9 Ref.12 Ref.14 Ref.15

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.2 Ref.14.

Tissue specificity

Ubiquitous in adult tissues. Detected in osteoblasts of the perichondrium in the developing limb of 12-week old embryos. Isoform 1 is detected in fetal brain, lung, kidney and testis. Isoform 2 is detected in fetal testis, and at much lower levels in fetal brain, lung and kidney. Ref.1 Ref.2

Involvement in disease

Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the SUFU family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytoplasmic sequestering of transcription factor

Inferred from electronic annotation. Source: Ensembl

heart looping

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

negative regulation of osteoblast differentiation

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of smoothened signaling pathway

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription factor import into nucleus

Traceable author statement PubMed 11001584. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: MGI

neural tube closure

Inferred from electronic annotation. Source: Ensembl

proteolysis

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

signal transduction

Traceable author statement Ref.2. Source: ProtInc

skeletal system development

Traceable author statement Ref.2. Source: ProtInc

skin development

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway involved in spinal cord motor neuron cell fate specification

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway involved in ventral spinal cord interneuron specification

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9. Source: UniProtKB

primary cilium

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein binding

Inferred from physical interaction Ref.9PubMed 16189514PubMed 22439934Ref.1. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

signal transducer activity

Traceable author statement Ref.2Ref.1. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UMX1-1)

Also known as: Su(fu)484;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.
Isoform 2 (identifier: Q9UMX1-2)

Also known as: Su(fu)433;

The sequence of this isoform differs from the canonical sequence as follows:
     433-433: I → L
     434-484: Missing.
Isoform 3 (identifier: Q9UMX1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     433-484: ILLTEEFVEK...PDVVFDSPLH → VRRPFFFSLL...LMDSGPGACV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Suppressor of fused homolog
PRO_0000072302

Amino acid modifications

Modified residue3031N6-acetyllysine Ref.11
Modified residue4811Phosphoserine Ref.10

Natural variations

Alternative sequence433 – 48452ILLTE…DSPLH → VRRPFFFSLLPFIDFLAHPS SSPLAALDGTPSWGAGHECL MDSGPGACV in isoform 3.
VSP_013280
Alternative sequence4331I → L in isoform 2.
VSP_013278
Alternative sequence434 – 48451Missing in isoform 2.
VSP_013279
Natural variant151P → L. Ref.3
Corresponds to variant rs28942088 [ dbSNP | Ensembl ].
VAR_021566
Natural variant3401A → S. Ref.3
Corresponds to variant rs34135067 [ dbSNP | Ensembl ].
VAR_021567

Experimental info

Mutagenesis1061E → A: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis1111D → A: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis1281T → A or D: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis1521E → A: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis1591D → A: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding. Ref.15
Mutagenesis1811E → A: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis2211E → A: No effect on down-regulation of GLI1 activity. Ref.15
Mutagenesis2621D → A: No effect on down-regulation of GLI1 activity. Ref.15
Sequence conflict3361A → P in AAD50501. Ref.2

Secondary structure

.......................................................................... 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Su(fu)484) [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: 4A9CD1CF75FC179A

FASTA48453,947
        10         20         30         40         50         60 
MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN PLQVTAIVKY 

        70         80         90        100        110        120 
WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG DNRVHEFTGT DGPSGFGFEL 

       130        140        150        160        170        180 
TFRLKRETGE SAPPTWPAEL MQGLARYVFQ SENTFCSGDH VSWHSPLDNS ESRIQHMLLT 

       190        200        210        220        230        240 
EDPQMQPVQT PFGVVTFLQI VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR 

       250        260        270        280        290        300 
GETIFEIDPH LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDDEDSRS ICIGTQPRRL 

       310        320        330        340        350        360 
SGKDTEQIRE TLRRGLEINS KPVLPPINPQ RQNGLAHDRA PSRKDSLESD SSTAIIPHEL 

       370        380        390        400        410        420 
IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI TGDMAITFVS TGVEGAFATE 

       430        440        450        460        470        480 
EHPYAAHGPW LQILLTEEFV EKMLEDLEDL TSPEEFKLPK EYSWPEKKLK VSILPDVVFD 


SPLH 

« Hide

Isoform 2 (Su(fu)433) [UniParc].

Checksum: 40CF1CDD5F526102
Show »

FASTA43347,932
Isoform 3 [UniParc].

Checksum: 7B312507FF653923
Show »

FASTA48152,977

References

« Hide 'large scale' references
[1]"Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli."
Stone D.M., Murone M., Luoh S.-M., Ye W., Armanini M.P., Gurney A., Phillips H., Brush J., Goddard A., deSauvage F.J., Rosenthal A.
J. Cell Sci. 112:4437-4448(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION WITH GLI1; GLI2; GLI3 AND BTRC, HOMODIMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Fetal kidney, Fetal lung and Fetal testis.
[2]"Mammalian suppressor-of-fused modulates nuclear-cytoplasmic shuttling of Gli-1."
Kogerman P., Grimm T., Kogerman L., Krause D., Unden A.B., Sandstedt B., Toftgaard R., Zaphiropoulos P.G.
Nat. Cell Biol. 1:312-319(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GLI1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Mutations in SUFU predispose to medulloblastoma."
Taylor M.D., Liu L., Raffel C., Hui C.-C., Mainprize T.G., Zhang X., Agatep R., Chiappa S., Gao L., Lowrance A., Hao A., Goldstein A.M., Stavrou T., Scherer S.W., Dura W.T., Wainwright B., Squire J.A., Rutka J.T., Hogg D.
Nat. Genet. 31:306-310(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANTS LEU-15 AND SER-340, ROLE IN THE DEVELOPMENT OF MEDULLOBLASTOMA.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Muscle.
[7]"Suppressor of fused gene involved in hedgehog signal transduction in Drosophila melanogaster is conserved in mammals."
Delattre M., Briand S., Paces-Fessy M., Blanchet-Tournier M.-F.
Dev. Genes Evol. 209:294-300(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-484 (ISOFORM 1).
Tissue: Neuron.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-484 (ISOFORM 1).
Tissue: Testis.
[9]"Gli regulation by the opposing activities of fused and suppressor of fused."
Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., Grey C., Rosenthal A., de Sauvage F.J.
Nat. Cell Biol. 2:310-312(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STK36.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Dual function of UNC-51-like kinase 3 (Ulk3) in the Sonic hedgehog signaling pathway."
Maloverjan A., Piirsoo M., Kasak L., Peil L., Osterlund T., Kogerman P.
J. Biol. Chem. 285:30079-30090(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ULK3.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Rab23 negatively regulates Gli1 transcriptional factor in a Su(Fu)-dependent manner."
Chi S., Xie G., Liu H., Chen K., Zhang X., Li C., Xie J.
Cell. Signal. 24:1222-1228(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB23, FUNCTION, SUBCELLULAR LOCATION.
[15]"Suppressor of fused regulates Gli activity through a dual binding mechanism."
Merchant M., Vajdos F.F., Ultsch M., Maun H.R., Wendt U., Cannon J., Desmarais W., Lazarus R.A., de Vos A.M., de Sauvage F.J.
Mol. Cell. Biol. 24:8627-8641(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 27-268, INTERACTION WITH GLI1, MUTAGENESIS OF GLU-106; ASP-111; THR-128; GLU-152; ASP-159; GLU-181; GLU-221 AND ASP-262.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144231 mRNA. Translation: AAF23890.1.
AF159447 mRNA. Translation: AAF23893.1.
AF222345 mRNA. Translation: AAF35866.1.
AF175770 mRNA. Translation: AAD50501.1.
AY081829 expand/collapse EMBL AC list , AY081818, AY081819, AY081820, AY081822, AY081824, AY081825, AY081821, AY081823, AY081826, AY081828, AY081827 Genomic DNA. Translation: AAM08947.1.
AY358550 mRNA. Translation: AAQ88914.1.
AL121928, AL391121, AL157386 Genomic DNA. Translation: CAI12525.1.
AL121928, AL157386, AL391121 Genomic DNA. Translation: CAI12526.1.
AL157386, AL391121, AL121928 Genomic DNA. Translation: CAI39614.1.
AL157386, AL121928, AL391121 Genomic DNA. Translation: CAI39615.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40864.1.
AL391121, AL121928, AL157386 Genomic DNA. Translation: CAI40865.1.
BC013291 mRNA. Translation: AAH13291.1.
AF172319 mRNA. Translation: AAD51655.1.
AL137465 mRNA. Translation: CAB70752.1.
CCDSCCDS53571.1. [Q9UMX1-2]
CCDS7537.1. [Q9UMX1-1]
PIRT46409.
RefSeqNP_001171604.1. NM_001178133.1. [Q9UMX1-2]
NP_057253.2. NM_016169.3. [Q9UMX1-1]
UniGeneHs.404089.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M1LX-ray2.65A/B/C/D27-262[»]
4BL8X-ray3.04A/B32-483[»]
4BL9X-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLAX-ray3.50A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLBX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4BLDX-ray2.80A/B/C/D32-278[»]
A/B/C/D361-483[»]
4KM8X-ray2.26A1-484[»]
4KM9X-ray3.19A1-484[»]
4KMDX-ray1.70A1-484[»]
4KMHX-ray3.04A/B1-484[»]
ProteinModelPortalQ9UMX1.
SMRQ9UMX1. Positions 1-481.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119676. 21 interactions.
IntActQ9UMX1. 13 interactions.
MINTMINT-1441707.
STRING9606.ENSP00000358918.

Chemistry

ChEMBLCHEMBL5390.

PTM databases

PhosphoSiteQ9UMX1.

Polymorphism databases

DMDM62511179.

Proteomic databases

MaxQBQ9UMX1.
PaxDbQ9UMX1.
PRIDEQ9UMX1.

Protocols and materials databases

DNASU51684.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369899; ENSP00000358915; ENSG00000107882. [Q9UMX1-2]
ENST00000369902; ENSP00000358918; ENSG00000107882. [Q9UMX1-1]
ENST00000423559; ENSP00000411597; ENSG00000107882. [Q9UMX1-3]
GeneID51684.
KEGGhsa:51684.
UCSCuc001kvw.2. human. [Q9UMX1-3]
uc001kvx.3. human. [Q9UMX1-2]
uc001kvy.2. human. [Q9UMX1-1]

Organism-specific databases

CTD51684.
GeneCardsGC10P104253.
HGNCHGNC:16466. SUFU.
HPAHPA008700.
MIM155255. phenotype.
607035. gene.
neXtProtNX_Q9UMX1.
Orphanet251863. Desmoplastic/nodular medulloblastoma.
263662. Familial multiple meningioma.
251858. Medulloblastoma with extensive nodularity.
PharmGKBPA38146.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72477.
HOVERGENHBG061539.
InParanoidQ9UMX1.
KOK06229.
OMAGDTAITF.
OrthoDBEOG7RV9FV.
PhylomeDBQ9UMX1.
TreeFamTF324548.

Enzyme and pathway databases

SignaLinkQ9UMX1.

Gene expression databases

BgeeQ9UMX1.
CleanExHS_SUFU.
GenevestigatorQ9UMX1.

Family and domain databases

InterProIPR020941. SUFU-like_domain.
IPR024314. SUFU_C.
IPR007768. Suppressor_of_fused.
IPR016591. Suppressor_of_fused_euk.
[Graphical view]
PANTHERPTHR10928. PTHR10928. 1 hit.
PfamPF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view]
PIRSFPIRSF011844. Suppressor_of_fused_protein. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9UMX1.
GeneWikiSUFU.
GenomeRNAi51684.
NextBio55686.
PROQ9UMX1.
SOURCESearch...

Entry information

Entry nameSUFU_HUMAN
AccessionPrimary (citable) accession number: Q9UMX1
Secondary accession number(s): Q7LCP7 expand/collapse secondary AC list , Q9NT90, Q9NZ07, Q9UHK2, Q9UHM8, Q9UMY0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM