Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UMX1

- SUFU_HUMAN

UniProt

Q9UMX1 - SUFU_HUMAN

Protein

Suppressor of fused homolog

Gene

SUFU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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). Required for the proper formation of hair follicles and the control of epidermal differentiation By similarity.By similarity

    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

    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

    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

    GO - Cellular componenti

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

    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 homologPRO_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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GLI1P081519EBI-740595,EBI-308084
    Gli2Q0VGT23EBI-740595,EBI-9344284From a different organism.
    PEX26Q7Z4122EBI-740595,EBI-752057
    RCN3Q96D152EBI-740595,EBI-746283
    STK36Q9NRP73EBI-740595,EBI-863797

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    484
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UMX1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SUFU family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti336 – 3361A → P in AAD50501. (PubMed:10559945)Curated

    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. 1 PublicationVSP_013280Add
    BLAST
    Alternative sequencei433 – 4331I → L in isoform 2. 2 PublicationsVSP_013278
    Alternative sequencei434 – 48451Missing in isoform 2. 2 PublicationsVSP_013279Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 118 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