Q9UMX1 (SUFU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Suppressor of fused homolog
Short name=SUFUH

Gene names

Name:	SUFU
ORF Names:	UNQ650/PRO1280

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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. Ref.1 Ref.2 Ref.9 Ref.12 Ref.13
Subcellular location	Cytoplasm. Nucleus Ref.1 Ref.2.
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	Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.
Sequence similarities	Belongs to the SUFU family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of osteoblast differentiation Traceable author statement. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Traceable author statement. Source: BHF-UCL negative regulation of smoothened signaling pathway Traceable author statement. Source: BHF-UCL negative regulation of transcription factor import into nucleus Traceable author statement. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: MGI proteolysis Traceable author statement. Source: ProtInc skeletal system development Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay Ref.9. Source: UniProtKB nucleus Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.1Ref.9. Source: IntAct protein kinase binding Inferred from physical interaction Ref.12. Source: UniProtKB signal transducer activity Traceable author statement. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GLI1	P08151	2	EBI-740615,EBI-308084
PEX26	Q7Z412	2	EBI-740595,EBI-752057
RCN3	Q96D15	2	EBI-740595,EBI-746283
STK36	Q9NRP7	2	EBI-740595,EBI-863797

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 484

484

Suppressor of fused homolog

PRO_0000072302

Amino acid modifications

Modified residue

303

1

N6-acetyllysine Ref.11

Modified residue

481

1

Phosphoserine Ref.10

Natural variations

Alternative sequence

433 – 484

52

ILLTE…DSPLH → VRRPFFFSLLPFIDFLAHPS SSPLAALDGTPSWGAGHECL MDSGPGACV in isoform 3.

VSP_013280

Alternative sequence

433

1

I → L in isoform 2.

VSP_013278

Alternative sequence

434 – 484

51

Missing in isoform 2.

VSP_013279

Natural variant

15

1

P → L. Ref.3
Corresponds to variant rs28942088 [ dbSNP | Ensembl ].

VAR_021566

Natural variant

340

1

A → S. Ref.3
Corresponds to variant rs34135067 [ dbSNP | Ensembl ].

VAR_021567

Experimental info

Mutagenesis

106

1

E → A: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

111

1

D → A: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

128

1

T → A or D: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

152

1

E → A: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

159

1

D → A: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding. Ref.13

Mutagenesis

181

1

E → A: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

221

1

E → A: No effect on down-regulation of GLI1 activity. Ref.13

Mutagenesis

262

1

D → A: No effect on down-regulation of GLI1 activity. Ref.13

Sequence conflict

336

1

A → P in AAD50501. Ref.2

Secondary structure

1

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484

Helix Strand Turn

Details...

Helix

32 – 44

13

Beta strand

52 – 55

4

Helix

60 – 62

3

Beta strand

69 – 76

8

Turn

80 – 83

4

Beta strand

87 – 96

10

Beta strand

101 – 105

5

Turn

109 – 111

3

Beta strand

112 – 125

14

Helix

136 – 151

16

Beta strand

169 – 171

3

Beta strand

176 – 181

6

Beta strand

188 – 190

3

Beta strand

193 – 203

11

Helix

205 – 213

9

Helix

216 – 225

10

Helix

227 – 229

3

Turn

231 – 234

4

Helix

244 – 247

4

Helix

251 – 260

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Su(fu)484) [UniParc]. Last modified April 12, 2005. Version 2. Checksum: 4A9CD1CF75FC179A	FASTA	484	53,947
	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
	Isoform 2 (Su(fu)433) [UniParc]. Checksum: 40CF1CDD5F526102	FASTA	433	47,932
	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 EHPYAAHGPW LQL
	Isoform 3 [UniParc]. Checksum: 7B312507FF653923	FASTA	481	52,977
	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 LQVRRPFFFS LLPFIDFLAH PSSSPLAALD GTPSWGAGHE CLMDSGPGAC V

References

	« Hide 'large scale' referencesShow '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: 10564661] [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: 10559945] [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: 12068298] [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. , 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: 12975309] [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. , 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: 15164054] [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: 15489334] [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: 11252182] [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: 17974005] [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: 10806483] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-303, MASS SPECTROMETRY.
[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: 20643644] [Abstract] Cited for: INTERACTION WITH ULK3.
[13]	"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: 15367681] [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 , 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.

IPI

IPI00099179.
IPI00556458.
IPI00556521.

PIR

T46409.

RefSeq

NP_001171604.1. NM_001178133.1.
NP_057253.2. NM_016169.3.

UniGene

Hs.404089.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M1L	X-ray	2.65	A/B/C/D	27-262	[»]

ProteinModelPortal

Q9UMX1.

SMR

Q9UMX1. Positions 27-262.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UMX1. 16 interactions.

MINT

MINT-1441707.

STRING

Q9UMX1.

PTM databases

PhosphoSite

Q9UMX1.

Polymorphism databases

DMDM

62511179.

Proteomic databases

PRIDE

Q9UMX1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369902; ENSP00000358918; ENSG00000107882.

GeneID

51684.

KEGG

hsa:51684.

UCSC

uc001kvx.2. human.
uc001kvy.1. human.

Organism-specific databases

CTD

51684.

GeneCards

GC10P104253.

H-InvDB

HIX0009163.

HGNC

HGNC:16466. SUFU.

HPA

HPA008700.

MIM

155255. phenotype.
607035. gene.

neXtProt

NX_Q9UMX1.

Orphanet

251858. Medulloblastoma with extensive nodularity.

PharmGKB

PA38146.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000009747.

HOVERGEN

HBG061539.

InParanoid

Q9UMX1.

OMA

RHGRHFT.

OrthoDB

EOG49S666.

PhylomeDB

Q9UMX1.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.

Gene expression databases

ArrayExpress

Q9UMX1.

Bgee

Q9UMX1.

CleanEx

HS_SUFU.

Genevestigator

Q9UMX1.

GermOnline

ENSG00000107882. Homo sapiens.

Family and domain databases

InterPro

IPR007768. SUFU-like.
IPR024314. SUFU_C.
IPR020941. SUFU_domain.
IPR016591. Suppressor_of_fused_protein.
[Graphical view]

KO

K06229.

PANTHER

PTHR10928. SUFU. 1 hit.

Pfam

PF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view]

PIRSF

PIRSF011844. Suppressor_of_fused_protein. 1 hit.

ProtoNet

Search...

Other

NextBio

55686.

SOURCE

Search...

Entry information

Entry name

SUFU_HUMAN

Accession

Primary (citable) accession number: Q9UMX1
Secondary accession number(s): Q7LCP7 , Q9NT90, Q9NZ07, Q9UHK2, Q9UHM8, Q9UMY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	April 12, 2005
Last modified:	January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.