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Protein

Suppressor of fused homolog

Gene

Sufu

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 3 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).UniRule annotation

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_327126. Hedgehog 'on' state.
REACT_342405. Hedgehog 'off' state.
REACT_357442. Degradation of GLI1 by the proteasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of fused homologUniRule annotation
Gene namesi
Name:SufuImported
ORF Names:rCG_57679Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1559462. Sufu.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation, NucleusUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026987.

Family & Domainsi

Sequence similaritiesi

Belongs to the SUFU family.UniRule annotation

Phylogenomic databases

eggNOGiNOG72477.
GeneTreeiENSGT00390000009747.
HOGENOMiHOG000007864.
HOVERGENiHBG061539.
KOiK06229.
OMAiGDTAITF.
OrthoDBiEOG7RV9FV.
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.

Sequencei

Sequence statusi: Complete.

Q4V8C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELRPSVAP GPAAPPASGP SAPPAFASLF PPGLHAIYGE CRRLYPDQPN
60 70 80 90 100
PLQVTAIVKY WLGGPDPLDY VSMYRNMGSP SANIPEHWHY ISFGLSDLYG
110 120 130 140 150
DNRVHEFTGT DGPSGFGFEL TFRLKRETGE SAPPTWPAEL MQGLARYVFQ
160 170 180 190 200
SENTFCSGDH VSWHSPLDNS ESRIQHMLLT EDPQMQPVQT PFGVVTFLQI
210 220 230 240 250
VGVCTEELHS AQQWNGQGIL ELLRTVPIAG GPWLITDMRR GETIFEIDPH
260 270 280 290 300
LQQERVDKGI ETDGSNLSGV SAKCAWDDLS RPPEDDEDSR SICLGTQPRR
310 320 330 340 350
LSGKDTEQIR ETLRRGLEIN SKPVLPPINS QRQNGLTYDR APSRKDSLGS
360 370 380 390 400
DISTAVIPHE LIRTRQLESV HLKFNQESGA LIPLCLRGRL LHGRHFTYKS
410 420 430 440 450
ITGDMAITFV STGVEGAFAT EEHPYAAHGP WLQILLTEEF VEKMLEDLED
460 470 480
LTSPEEFKLP KEYSWPEKKL KVSILPDVVF DSPLH
Length:485
Mass (Da):54,081
Last modified:July 5, 2005 - v1
Checksum:iE4E70580C797155D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC097694 Genomic DNA. No translation available.
BC097447 mRNA. Translation: AAH97447.1.
CH473986 Genomic DNA. Translation: EDL94350.1.
RefSeqiNP_001020070.1. NM_001024899.1.
UniGeneiRn.211670.

Genome annotation databases

EnsembliENSRNOT00000026987; ENSRNOP00000026987; ENSRNOG00000019807.
GeneIDi361769.
KEGGirno:361769.
UCSCiRGD:1559462. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC097694 Genomic DNA. No translation available.
BC097447 mRNA. Translation: AAH97447.1.
CH473986 Genomic DNA. Translation: EDL94350.1.
RefSeqiNP_001020070.1. NM_001024899.1.
UniGeneiRn.211670.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026987; ENSRNOP00000026987; ENSRNOG00000019807.
GeneIDi361769.
KEGGirno:361769.
UCSCiRGD:1559462. rat.

Organism-specific databases

CTDi51684.
RGDi1559462. Sufu.

Phylogenomic databases

eggNOGiNOG72477.
GeneTreeiENSGT00390000009747.
HOGENOMiHOG000007864.
HOVERGENiHBG061539.
KOiK06229.
OMAiGDTAITF.
OrthoDBiEOG7RV9FV.
TreeFamiTF324548.

Enzyme and pathway databases

ReactomeiREACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_327126. Hedgehog 'on' state.
REACT_342405. Hedgehog 'off' state.
REACT_357442. Degradation of GLI1 by the proteasome.

Miscellaneous databases

NextBioi677549.
PROiQ4V8C6.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: TestisImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ4V8C6_RAT
AccessioniPrimary (citable) accession number: Q4V8C6
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2005
Last sequence update: July 5, 2005
Last modified: July 22, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.