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Q9UMX1

- SUFU_HUMAN

UniProt

Q9UMX1 - SUFU_HUMAN

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Protein
Suppressor of fused homolog
Gene
SUFU, UNQ650/PRO1280
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).5 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein kinase binding Source: UniProtKB
  3. signal transducer activity Source: ProtInc
  4. transcription corepressor activity Source: UniProtKB
  5. transcription factor binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. cytoplasmic sequestering of transcription factor Source: Ensembl
  2. heart looping Source: Ensembl
  3. multicellular organismal development Source: ProtInc
  4. negative regulation of osteoblast differentiation Source: BHF-UCL
  5. negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  6. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  7. negative regulation of smoothened signaling pathway Source: BHF-UCL
  8. negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: Ensembl
  9. negative regulation of transcription factor import into nucleus Source: BHF-UCL
  10. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  11. neural tube closure Source: Ensembl
  12. proteolysis Source: ProtInc
  13. regulation of transcription, DNA-templated Source: UniProtKB
  14. signal transduction Source: ProtInc
  15. skeletal system development Source: ProtInc
  16. skin development Source: Ensembl
  17. smoothened signaling pathway involved in spinal cord motor neuron cell fate specification Source: Ensembl
  18. smoothened signaling pathway involved in ventral spinal cord interneuron specification Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

SignaLinkiQ9UMX1.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of fused homolog
Short name:
SUFUH
Gene namesi
Name:SUFU
ORF Names:UNQ650/PRO1280
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:16466. SUFU.

Subcellular locationi

Cytoplasm. Nucleus 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. primary cilium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061E → A: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi111 – 1111D → A: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi128 – 1281T → A or D: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi152 – 1521E → A: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi159 – 1591D → A: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding. 1 Publication
Mutagenesisi181 – 1811E → A: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi221 – 2211E → A: No effect on down-regulation of GLI1 activity. 1 Publication
Mutagenesisi262 – 2621D → A: No effect on down-regulation of GLI1 activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

MIMi155255. phenotype.
Orphaneti251863. Desmoplastic/nodular medulloblastoma.
263662. Familial multiple meningioma.
251858. Medulloblastoma with extensive nodularity.
PharmGKBiPA38146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Suppressor of fused homolog
PRO_0000072302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031N6-acetyllysine1 Publication
Modified residuei481 – 4811Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UMX1.
PaxDbiQ9UMX1.
PRIDEiQ9UMX1.

PTM databases

PhosphoSiteiQ9UMX1.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9UMX1.
CleanExiHS_SUFU.
GenevestigatoriQ9UMX1.

Organism-specific databases

HPAiHPA008700.

Interactioni

Subunit structurei

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 RAB23.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GLI1P081518EBI-740595,EBI-308084
Gli2Q0VGT23EBI-740595,EBI-9344284From a different organism.
PEX26Q7Z4122EBI-740595,EBI-752057
RCN3Q96D152EBI-740595,EBI-746283
STK36Q9NRP72EBI-740595,EBI-863797

Protein-protein interaction databases

BioGridi119676. 21 interactions.
IntActiQ9UMX1. 14 interactions.
MINTiMINT-1441707.
STRINGi9606.ENSP00000358918.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293
Helixi32 – 4413
Beta strandi52 – 554
Helixi60 – 623
Beta strandi69 – 768
Helixi80 – 823
Beta strandi87 – 9610
Beta strandi101 – 1055
Beta strandi110 – 12516
Helixi136 – 15116
Beta strandi160 – 1623
Beta strandi169 – 1713
Beta strandi176 – 1816
Beta strandi188 – 1903
Beta strandi193 – 20311
Helixi205 – 2139
Helixi216 – 2249
Helixi227 – 2293
Turni230 – 2345
Helixi244 – 2474
Helixi250 – 26213
Beta strandi266 – 27611
Beta strandi363 – 3675
Beta strandi369 – 3735
Helixi375 – 3784
Helixi381 – 3877
Helixi389 – 3913
Beta strandi395 – 4039
Beta strandi405 – 4095
Beta strandi420 – 4223
Beta strandi424 – 4274
Beta strandi430 – 4345
Helixi437 – 44610
Turni447 – 4493
Beta strandi460 – 4645
Helixi465 – 4673
Beta strandi469 – 4735
Helixi476 – 4794

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9UMX1.
SMRiQ9UMX1. Positions 1-481.

Miscellaneous databases

EvolutionaryTraceiQ9UMX1.

Family & Domainsi

Sequence similaritiesi

Belongs to the SUFU family.

Phylogenomic databases

eggNOGiNOG72477.
HOVERGENiHBG061539.
InParanoidiQ9UMX1.
KOiK06229.
OMAiGDTAITF.
OrthoDBiEOG7RV9FV.
PhylomeDBiQ9UMX1.
TreeFamiTF324548.

Family and domain databases

InterProiIPR020941. SUFU-like_domain.
IPR024314. SUFU_C.
IPR007768. Suppressor_of_fused.
IPR016591. Suppressor_of_fused_euk.
[Graphical view]
PANTHERiPTHR10928. PTHR10928. 1 hit.
PfamiPF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view]
PIRSFiPIRSF011844. Suppressor_of_fused_protein. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UMX1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAELRPSGAP GPTAPPAPGP TAPPAFASLF PPGLHAIYGE CRRLYPDQPN    50
PLQVTAIVKY WLGGPDPLDY VSMYRNVGSP SANIPEHWHY ISFGLSDLYG 100
DNRVHEFTGT DGPSGFGFEL TFRLKRETGE SAPPTWPAEL MQGLARYVFQ 150
SENTFCSGDH VSWHSPLDNS ESRIQHMLLT EDPQMQPVQT PFGVVTFLQI 200
VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR GETIFEIDPH 250
LQERVDKGIE TDGSNLSGVS AKCAWDDLSR PPEDDEDSRS ICIGTQPRRL 300
SGKDTEQIRE TLRRGLEINS KPVLPPINPQ RQNGLAHDRA PSRKDSLESD 350
SSTAIIPHEL IRTRQLESVH LKFNQESGAL IPLCLRGRLL HGRHFTYKSI 400
TGDMAITFVS TGVEGAFATE EHPYAAHGPW LQILLTEEFV EKMLEDLEDL 450
TSPEEFKLPK EYSWPEKKLK VSILPDVVFD SPLH 484

Note: Major isoform.

Length:484
Mass (Da):53,947
Last modified:April 12, 2005 - v2
Checksum:i4A9CD1CF75FC179A
GO
Isoform 2 (identifier: Q9UMX1-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:433
Mass (Da):47,932
Checksum:i40CF1CDD5F526102
GO
Isoform 3 (identifier: Q9UMX1-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:481
Mass (Da):52,977
Checksum:i7B312507FF653923
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151P → L.1 Publication
Corresponds to variant rs28942088 [ dbSNP | Ensembl ].
VAR_021566
Natural varianti340 – 3401A → S.1 Publication
Corresponds to variant rs34135067 [ dbSNP | Ensembl ].
VAR_021567

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei433 – 48452ILLTE…DSPLH → VRRPFFFSLLPFIDFLAHPS SSPLAALDGTPSWGAGHECL MDSGPGACV in isoform 3.
VSP_013280Add
BLAST
Alternative sequencei433 – 4331I → L in isoform 2.
VSP_013278
Alternative sequencei434 – 48451Missing in isoform 2.
VSP_013279Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3361A → P in AAD50501. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53571.1. [Q9UMX1-2]
CCDS7537.1. [Q9UMX1-1]
PIRiT46409.
RefSeqiNP_001171604.1. NM_001178133.1. [Q9UMX1-2]
NP_057253.2. NM_016169.3. [Q9UMX1-1]
UniGeneiHs.404089.

Genome annotation databases

EnsembliENST00000369899; ENSP00000358915; ENSG00000107882. [Q9UMX1-2]
ENST00000369902; ENSP00000358918; ENSG00000107882. [Q9UMX1-1]
ENST00000423559; ENSP00000411597; ENSG00000107882. [Q9UMX1-3]
GeneIDi51684.
KEGGihsa:51684.
UCSCiuc001kvw.2. human. [Q9UMX1-3]
uc001kvx.3. human. [Q9UMX1-2]
uc001kvy.2. human. [Q9UMX1-1]

Polymorphism databases

DMDMi62511179.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS53571.1. [Q9UMX1-2 ]
CCDS7537.1. [Q9UMX1-1 ]
PIRi T46409.
RefSeqi NP_001171604.1. NM_001178133.1. [Q9UMX1-2 ]
NP_057253.2. NM_016169.3. [Q9UMX1-1 ]
UniGenei Hs.404089.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M1L X-ray 2.65 A/B/C/D 27-262 [» ]
4BL8 X-ray 3.04 A/B 32-483 [» ]
4BL9 X-ray 2.80 A/B/C/D 32-278 [» ]
A/B/C/D 361-483 [» ]
4BLA X-ray 3.50 A/B/C/D 32-278 [» ]
A/B/C/D 361-483 [» ]
4BLB X-ray 2.80 A/B/C/D 32-278 [» ]
A/B/C/D 361-483 [» ]
4BLD X-ray 2.80 A/B/C/D 32-278 [» ]
A/B/C/D 361-483 [» ]
4KM8 X-ray 2.26 A 1-484 [» ]
4KM9 X-ray 3.19 A 1-484 [» ]
4KMD X-ray 1.70 A 1-484 [» ]
4KMH X-ray 3.04 A/B 1-484 [» ]
ProteinModelPortali Q9UMX1.
SMRi Q9UMX1. Positions 1-481.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119676. 21 interactions.
IntActi Q9UMX1. 14 interactions.
MINTi MINT-1441707.
STRINGi 9606.ENSP00000358918.

Chemistry

ChEMBLi CHEMBL5390.

PTM databases

PhosphoSitei Q9UMX1.

Polymorphism databases

DMDMi 62511179.

Proteomic databases

MaxQBi Q9UMX1.
PaxDbi Q9UMX1.
PRIDEi Q9UMX1.

Protocols and materials databases

DNASUi 51684.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369899 ; ENSP00000358915 ; ENSG00000107882 . [Q9UMX1-2 ]
ENST00000369902 ; ENSP00000358918 ; ENSG00000107882 . [Q9UMX1-1 ]
ENST00000423559 ; ENSP00000411597 ; ENSG00000107882 . [Q9UMX1-3 ]
GeneIDi 51684.
KEGGi hsa:51684.
UCSCi uc001kvw.2. human. [Q9UMX1-3 ]
uc001kvx.3. human. [Q9UMX1-2 ]
uc001kvy.2. human. [Q9UMX1-1 ]

Organism-specific databases

CTDi 51684.
GeneCardsi GC10P104253.
HGNCi HGNC:16466. SUFU.
HPAi HPA008700.
MIMi 155255. phenotype.
607035. gene.
neXtProti NX_Q9UMX1.
Orphaneti 251863. Desmoplastic/nodular medulloblastoma.
263662. Familial multiple meningioma.
251858. Medulloblastoma with extensive nodularity.
PharmGKBi PA38146.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG72477.
HOVERGENi HBG061539.
InParanoidi Q9UMX1.
KOi K06229.
OMAi GDTAITF.
OrthoDBi EOG7RV9FV.
PhylomeDBi Q9UMX1.
TreeFami TF324548.

Enzyme and pathway databases

SignaLinki Q9UMX1.

Miscellaneous databases

EvolutionaryTracei Q9UMX1.
GeneWikii SUFU.
GenomeRNAii 51684.
NextBioi 55686.
PROi Q9UMX1.
SOURCEi Search...

Gene expression databases

Bgeei Q9UMX1.
CleanExi HS_SUFU.
Genevestigatori Q9UMX1.

Family and domain databases

InterProi IPR020941. SUFU-like_domain.
IPR024314. SUFU_C.
IPR007768. Suppressor_of_fused.
IPR016591. Suppressor_of_fused_euk.
[Graphical view ]
PANTHERi PTHR10928. PTHR10928. 1 hit.
Pfami PF05076. SUFU. 1 hit.
PF12470. SUFU_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF011844. Suppressor_of_fused_protein. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, VARIANTS LEU-15 AND SER-340, ROLE IN THE DEVELOPMENT OF MEDULLOBLASTOMA.
  4. 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] [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. 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. 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. 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. 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.

Entry informationi

Entry nameiSUFU_HUMAN
AccessioniPrimary (citable) accession number: Q9UMX1
Secondary accession number(s): Q7LCP7
, Q9NT90, Q9NZ07, Q9UHK2, Q9UHM8, Q9UMY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: April 12, 2005
Last modified: September 3, 2014
This is version 117 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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