SUFU
entrez
51684
canonical
uniprot
Q9UMX1
canonical
ensembl
ENSG00000107882
resolver
ensp
ENSP00000358915
resolver
ensp
ENSP00000358918
resolver
ensp
ENSP00000563234
resolver
ensp
ENSP00000563235
resolver
ensp
ENSP00000599577
resolver
ensp
ENSP00000663719
resolver
genesymbol
SUFU
resolver
hgnc
HGNC:16466
resolver
uniprot
A0A223LX15
resolver
uniprot
Q7LCP7
resolver
uniprot
Q9NT90
resolver
uniprot
Q9NZ07
resolver
uniprot
Q9UHK2
resolver
uniprot
Q9UHM8
resolver
uniprot
Q9UMY0
resolver
uniprot_entry
A0A223LX15_HUMAN
resolver
uniprot_entry
SUFU_HUMAN
resolver
uniprot_sec
Q7LCP7
resolver
uniprot_sec
Q9NT90
resolver
uniprot_sec
Q9NZ07
resolver
uniprot_sec
Q9UHK2
resolver
uniprot_sec
Q9UHM8
resolver
uniprot_sec
Q9UMY0
resolver
amino_acid_sequence
MAELRPSGAPGPTAPPAPGPTAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNVGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICIGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINPQRQNGLAHDRAPSRKDSLESDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH
uniprot
proteins
disease_involvement
DISEASE: Medulloblastoma (MDB) [MIM:155255]: Malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. {ECO:0000269|PubMed:12068298}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Joubert syndrome 32 (JBTS32) [MIM:617757]: A form of Joubert syndrome, a disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy, renal disease, liver fibrosis, and polydactyly. JBTS32 inheritance is autosomal recessive. {ECO:0000269|PubMed:28965847}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Basal cell nevus syndrome 2 (BCNS2) [MIM:620343]: A form of basal cell nevus syndrome, a disease characterized by nevoid basal cell carcinomas and developmental abnormalities such as rib and craniofacial alterations, polydactyly, syndactyly, and spina bifida. In addition, the patients suffer from a multitude of tumors like fibromas of the ovaries and heart, cysts of the skin, jaws and mesentery, as well as medulloblastomas and meningiomas. {ECO:0000269|PubMed:19533801}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Negative regulator in the hedgehog/smoothened signaling pathway that acts by sequestering the GLI (GI1, GLI2 and GLI3) transcription factors in the cytoplasm (PubMed:10559945, PubMed:10564661, PubMed:10806483, PubMed:12068298, PubMed:12975309, PubMed:15367681, PubMed:22365972, PubMed:24217340, PubMed:24311597, PubMed:27234298, PubMed:28965847, PubMed:35831023). When smoothened signaling is initiated, GLI transcription factors dissociate from SUFU, translocate to the nucleus and activate expression of target genes (PubMed:24311597, PubMed:28965847, PubMed:35831023). In absence of smoothened signaling, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of full-length GLI3 into transcription repressor GLI3R: SUFU participates to GLI3 processing by promoting recruitment of GSK3B to GLI3 (PubMed:24311597, PubMed:28965847). May also act as a negative regulator of beta-catenin signaling (By similarity). Required for normal embryonic development (By similarity). Required for the proper formation of hair follicles and the control of epidermal differentiation (By similarity). {ECO:0000250|UniProtKB:Q9Z0P7, ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:10564661, ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:12068298, ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:15367681, ECO:0000269|PubMed:22365972, ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:27234298, ECO:0000269|PubMed:28965847, ECO:0000269|PubMed:35831023}.
uniprot
proteins
mass_dalton
53947
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="E->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 111; /note="D->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 128; /note="T->A,D: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 147; /note="Y->R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-159 and R-380."; /evidence="ECO:0000269|PubMed:24217340"; MUTAGEN 152; /note="E->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 159; /note="D->A: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 159; /note="D->R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-380."; /evidence="ECO:0000269|PubMed:24217340"; MUTAGEN 181; /note="E->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 221; /note="E->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 257; /note="K->R: Abolishes ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:27234298"; MUTAGEN 262; /note="D->A: No effect on down-regulation of GLI1 activity."; /evidence="ECO:0000269|PubMed:15367681"; MUTAGEN 342..346; /note="SRKDS->ARKDA: Increased interaction with FBXL17 and ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:27234298"; MUTAGEN 342..346; /note="SRKDS->DRKDD: Phosphomimetic mutant; decreased interaction with FBXL17 and ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:27234298"; MUTAGEN 380; /note="L->R: Impairs interaction with GLI1 and GLI2. Abolishes interaction with GLI1 and GLI2; when associated with R-147 and R-159."; /evidence="ECO:0000269|PubMed:24217340
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated at Lys-257 by the SCF(FBXL17) complex, leading to its subsequent degradation and allowing the release of GLI1 for proper hedgehog/smoothened signal transduction (PubMed:27234298). Ubiquitination is impaired by phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353 (PubMed:27234298). {ECO:0000269|PubMed:27234298}.; PTM: Phosphorylation at Ser-342, Ser-346, Ser-352 and Thr-353 prevents ubiquitination by the SCF(FBXL17) complex. {ECO:0000269|PubMed:27234298}.
uniprot
proteins
protein_family
SUFU family
uniprot
proteins
pubmed
10559945
uniprot
proteins
pubmed
10564661
uniprot
proteins
pubmed
10806483
uniprot
proteins
pubmed
11252182
uniprot
proteins
pubmed
12068298
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15367681
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19533801
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20643644
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22365972
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24217340
uniprot
proteins
pubmed
24311597
uniprot
proteins
pubmed
27234298
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28965847
uniprot
proteins
pubmed
35831023
uniprot
proteins
pubmed
38529886
uniprot
proteins
sequence_length
484
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:28965847}. Nucleus {ECO:0000269|PubMed:10559945, ECO:0000269|PubMed:28965847}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9Z0P7}. Note=Recruited to cilia in response to smoothened signaling, leading to dissociation from GLI (GI1, GLI2 and GLI3) transcription factors. {ECO:0000250|UniProtKB:Q9Z0P7}.
uniprot
proteins