Hedgehog 'on' state (Homo sapiens)

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33, 59, 100, 1203, 18, 20, 24, 48...1, 61, 1234, 9, 20, 33, 47...6120, 33, 47, 79, 93...6, 8, 28, 33, 40...27, 76, 78, 104, 119...12, 33, 44, 50, 65...3, 20, 75, 79, 80, 93...1, 25, 27, 29, 33...25, 68, 72, 97, 12412, 20, 32, 36, 59...7, 63, 11112, 44, 50, 65, 70...27, 341, 53, 61, 62, 12328, 40, 56, 57, 81...12, 23, 59, 65, 9876, 78, 11925, 68, 72, 9720, 33, 35, 39, 45...26, 28, 40, 58, 89...7, 1117, 63, 11132, 67, 73, 103, 116...33, 49, 73, 116, 1211, 53, 61, 62, 108...20, 39, 45, 93, 110...76, 782, 14, 19, 22, 76...30, 52, 54, 74, 86...1, 10, 33, 41, 53...11, 16, 17, 20, 21, 31...5, 4620, 75, 79, 93, 12812, 65, 987, 63, 111nucleoplasmendocytic vesicle lumenciliumcytosolSHH(34-?) ub-PTCH1:SMURFKIF3A ADRBK1 SPOP:CUL3:RBX1PSMD13 PSMA5 2p-GLI:GLI1 geneub-2p-GLI3 ITCH NUMBPSMB2 PSMD9 2p-GLI3 UBB(1-76) KIF7PSME1 UBB(77-152) pS588,S590, T593,S595-SMOdimer:CSNK1A1SPOP CSNK1A1 PSMC2 SMURF2p-GLI1 ITCH HHIP gene UBC(77-152) HHIP gene,PTCH2gene,BOC gene2p-GLI1 ADPITCH GLI3 PTCH1 ub-2p-GLI2 p-GLI3 PSMD11 SHH(34-?) 2p-GLI:PTCH1 gene2p-GLI2 BOC EFCAB7 GLI2 BOC gene UBC(1-76) GPR161SMO IHH PTCH1 PSMB6 26S proteasomeGLI1 2p-GLI3 PTCH2 gene GLI3 PSMD6 PSMB7 PSMB9 PSMC6 CSNK1A1DHH(33-?) CUL3 GLI:SUFUSMURF2 UBC(457-532) SUFU PSMB1 UBC(381-456) PSMD13 IQCE:EFCAB7:EVC2:EVCUBB(153-228) SMO UBC(457-532) EVC PSME4 PSME3 GLI2 GLI2 Hh-Npp:GAS1:PTCHEVC2 UBC(609-684) SMURF1 UBC(1-76) PSMC3 UBC(229-304) GLI1:NUMB:ITCHIHH ADPSHFM1 ITCHPSMD7 UBC(381-456) PSMB6 PSMB8 ARRB2 SPOPL PSMF1 GLI1 PSMD10 IHH GLI1PSMC3 PTCH1 geneub-2p-GLI2,3:SPOP:CUL3:RBX1PSME1 SPOPL p-GLI3 PSMB8 SMO 2p-GLI1,2,3PSMD14 pS588, S590, T593, S595, S611, S615, S616-SMO GAS1 EVC2 GLI1 gene ADRBK1DHH(33-?) UBC(77-152) CDC73unknown kinasePSMD5 UBA52(1-76) PSMD3 PSMB9 ATPUBC(77-152) GLI1,2,3PSMD10 p-GLI1 PSMC4 PSMC1 BOC PSMD4 UBC(229-304) ARRB2 UBB(153-228) HHIP gene p-GLI1,2,32p-GLI1 PSMD6 p-GLI1,2,3EVC PSME2 HHIPADPPSMB4 Hh-NppRBX1 GLI1 pS588,S590,T593,S595-SMOdimer:CSNK1A1:ADRBK1PSMF1 SUFU SUFUp6S, T-SMO dimerARRB2p-GLI2 2p-GLI1UBB(77-152) pS588, S590, T593, S595-SMO ATPUBC(305-380) UBC(153-228) SPOPL ATPPTCH1 IHH PSMD1 PSMD7 ARRB1 BOC:PTCH1NUMB DHH(33-?) SPOP PSMD2 EVC2:EVC2p-GLI1 GLI3 EVC 2p-GLI3 Hh-Npp:HHIPEFCAB7 PSMA7 Hh-Npp:CDON:PTCHub-PTCH1 ADPUBB(77-152) GLI1 UBA52(1-76) 2p-GLI2 PTCH1:SMURFPSMA2 SHH(34-?) CDON GAS1PSMA3 2p-GLI3 PSMA2 DZIP1EFCAB7:IQCEPSMA6 PSMA8 SUFUPSMD4 PSMB5 PSMA6 SMURF1 PSMA7 NUMB UBC(229-304) IQCE UBC(533-608) ADRBK1 CSNK1A1 UBC(1-76) ULK3 UBC(305-380) 26S proteasomePSMA5 2p-GLI1 PSMD8 SHH(34-?) pS588, S590, T593, S595, S611, S615, S616-SMO UBC(609-684) PSMD12 PSMB1 NUMB:ITCHUb2p-GLI2,3PSMB10 PSMD11 PSMC2 Hh-Npp:BOC:PTCH1IHH PSMB3 PSMD5 DHH(33-?) PTCH1 CDC73:2p-GLIARRB1 GLI2 UBC(381-456) 2p-GLI3 SMO dimer:ARRB:KIF3APSMC5 CDC73 UbSMURF1 SMURF2 PSMA1 pS588, S590, T593, S595-SMO p6S, T-SMOdimer:EVC2:EVCSMO dimerPSMB5 UBC(533-608) ULK3PSMD2 PSMC5 PSMC1 pS588, S590, T593, S595, S611, S615, S616-SMO PTCH1 2p-GLI2 PSMD9 p-GLI1 CUL3 NUMB PSMB10 2p-GLI2 UBB(1-76) UBC(609-684) ULK3:SUFUp-GLI2 ub-PTCH1UBA52(1-76) SHFM1 CDONub-GLI1:NUMB:ITCHUBC(457-532) ATPUBB(153-228) HHIP UBB(1-76) 2p-GLI:SPOP:CUL3:RBX1PSMD1 SHH(34-?) PSME3 GPR161PTCH1 gene PSMD3 PSMA4 RPS27A(1-76) PSMA4 UBC(153-228) UBC(153-228) SMO dimerPSMB2 2p-GLI3 GLI1 p6S,T-SMOdimer:CSNK1A1:ADRBK1EVC2 PSMB11 KIF3APSMC4 PSMA3 GLI1,2,3GLI1 genePSMB7 PSME2 SMURF2 PSMB3 PTCH12p-GLI1:HHIPgene,PTCH2 gene,BOCgeneUBC(305-380) DHH(33-?) RPS27A(1-76) IQCE p-GLI2 2p-GLI2 BOC gene PSMD12 ub-PTCH1CUL3 ub-GLI1 SMO dimer:CSNK1A1UbRBX1 GLI:SUFUUBC(533-608) SMO RBX1 PTCH2 gene GAS8CSNK1A1 GLI3 PSMD14 PSMB4 SPOP CSNK1A1 PSMC6 PSMD8 SUFU PSMA1 RPS27A(1-76) 1568115, 55275136915, 5513251315


Hedgehog is a secreted morphogen that has evolutionarily conserved roles in body organization by regulating the activity of the Ci/Gli transcription factor family. In Drosophila in the absence of Hh signaling, full-length Ci is partially degraded by the proteasome to generate a truncated repressor form that translocates to the nucleus to represses Hh-responsive genes. Binding of Hh ligand to the Patched (PTC) receptor allows the 7-pass transmembrane protein Smoothened (SMO) to be activated in an unknown manner, disrupting the partial proteolysis of Ci and allowing the full length activator form to accumulate (reviewed in Ingham et al, 2011; Briscoe and Therond, 2013).
While many of the core components of Hh signaling are conserved from flies to humans, the pathways do show points of significant divergence. Notably, the human genome encodes three Ci homologues, GLI1, 2 and 3 that each play slightly different roles in regulating Hh responsive genes. GLI3 is the primary repressor of Hh signaling in vertebrates, and is converted to the truncated GLI3R repressor form in the absence of Hh. GLI2 is a potent activator of transcription in the presence of Hh but contributes only minimally to the repression function. While a minor fraction of GLI2 protein is processed into the repressor form in the absence of Hh, the majority is either fully degraded by the proteasome or sequestered in the full-length form in the cytosol by protein-protein interactions. GLI1 lacks the repression domain and appears to be an obligate transcriptional activator (reviewed in Briscoe and Therond, 2013).
Vertebrate but not fly Hh signaling also depends on the movement of pathway components through the primary cilium. The primary cilium is a non-motile microtubule based structure whose construction and maintenance depends on intraflagellar transport (IFT). Anterograde IFT moves molecules from the ciliary base along the axoneme to the ciliary tip in a manner that requires the microtubule-plus-end directed kinesin KIF3 motor complex and the IFT-B protein complex, while retrograde IFT back to the ciliary base depends on the minus-end directed dynein motor and the IFT-A complex. Genetic screens have identified a number of cilia-related proteins that are required both to maintain Hh in the 'off' state and to transduce the signal when the pathway is activated (reviewed in Hui and Angers, 2011; Goetz and Anderson, 2010). View original pathway at:Reactome.


Pathway is converted from Reactome ID: 5632684
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Reactome Author: Rothfels, Karen

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  90. Milenkovic L, Scott MP, Rohatgi R.; ''Lateral transport of Smoothened from the plasma membrane to the membrane of the cilium.''; PubMed Europe PMC
  91. Jin Z, Mei W, Strack S, Jia J, Yang J.; ''The antagonistic action of B56-containing protein phosphatase 2As and casein kinase 2 controls the phosphorylation and Gli turnover function of Daz interacting protein 1.''; PubMed Europe PMC
  92. Endoh-Yamagami S, Evangelista M, Wilson D, Wen X, Theunissen JW, Phamluong K, Davis M, Scales SJ, Solloway MJ, de Sauvage FJ, Peterson AS.; ''The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh signal transduction during development.''; PubMed Europe PMC
  93. Tukachinsky H, Lopez LV, Salic A.; ''A mechanism for vertebrate Hedgehog signaling: recruitment to cilia and dissociation of SuFu-Gli protein complexes.''; PubMed Europe PMC
  94. Szczepny A, Wagstaff KM, Dias M, Gajewska K, Wang C, Davies RG, Kaur G, Ly-Huynh J, Loveland KL, Jans DA.; ''Overlapping binding sites for importin β1 and suppressor of fused (SuFu) on glioma-associated oncogene homologue 1 (Gli1) regulate its nuclear localization.''; PubMed Europe PMC
  95. Tada M, Kanai F, Tanaka Y, Tateishi K, Ohta M, Asaoka Y, Seto M, Muroyama R, Fukai K, Imazeki F, Kawabe T, Yokosuka O, Omata M.; ''Down-regulation of hedgehog-interacting protein through genetic and epigenetic alterations in human hepatocellular carcinoma.''; PubMed Europe PMC
  96. Tojo M, Kiyosawa H, Iwatsuki K, Kaneko F.; ''Expression of a sonic hedgehog signal transducer, hedgehog-interacting protein, by human basal cell carcinoma.''; PubMed Europe PMC
  97. Caparrós-Martín JA, Valencia M, Reytor E, Pacheco M, Fernandez M, Perez-Aytes A, Gean E, Lapunzina P, Peters H, Goodship JA, Ruiz-Perez VL.; ''The ciliary Evc/Evc2 complex interacts with Smo and controls Hedgehog pathway activity in chondrocytes by regulating Sufu/Gli3 dissociation and Gli3 trafficking in primary cilia.''; PubMed Europe PMC
  98. Vokes SA, Ji H, Wong WH, McMahon AP.; ''A genome-scale analysis of the cis-regulatory circuitry underlying sonic hedgehog-mediated patterning of the mammalian limb.''; PubMed Europe PMC
  99. McLellan JS, Zheng X, Hauk G, Ghirlando R, Beachy PA, Leahy DJ.; ''The mode of Hedgehog binding to Ihog homologues is not conserved across different phyla.''; PubMed Europe PMC
  100. Ingham PW, Nakano Y, Seger C.; ''Mechanisms and functions of Hedgehog signalling across the metazoa.''; PubMed Europe PMC
  101. Ogden SK, Ascano M, Stegman MA, Suber LM, Hooper JE, Robbins DJ.; ''Identification of a functional interaction between the transmembrane protein Smoothened and the kinesin-related protein Costal2.''; PubMed Europe PMC
  102. Bosanac I, Maun HR, Scales SJ, Wen X, Lingel A, Bazan JF, de Sauvage FJ, Hymowitz SG, Lazarus RA.; ''The structure of SHH in complex with HHIP reveals a recognition role for the Shh pseudo active site in signaling.''; PubMed Europe PMC
  103. Varjosalo M, Björklund M, Cheng F, Syvänen H, Kivioja T, Kilpinen S, Sun Z, Kallioniemi O, Stunnenberg HG, He WW, Ojala P, Taipale J.; ''Application of active and kinase-deficient kinome collection for identification of kinases regulating hedgehog signaling.''; PubMed Europe PMC
  104. Denef N, Neubüser D, Perez L, Cohen SM.; ''Hedgehog induces opposite changes in turnover and subcellular localization of patched and smoothened.''; PubMed Europe PMC
  105. Wang Y, Zhou Z, Walsh CT, McMahon AP.; ''Selective translocation of intracellular Smoothened to the primary cilium in response to Hedgehog pathway modulation.''; PubMed Europe PMC
  106. Sanchez-Arrones L, Cardozo M, Nieto-Lopez F, Bovolenta P.; ''Cdon and Boc: Two transmembrane proteins implicated in cell-cell communication.''; PubMed Europe PMC
  107. Kim J, Kato M, Beachy PA.; ''Gli2 trafficking links Hedgehog-dependent activation of Smoothened in the primary cilium to transcriptional activation in the nucleus.''; PubMed Europe PMC
  108. Wilson CW, Chen MH, Chuang PT.; ''Smoothened adopts multiple active and inactive conformations capable of trafficking to the primary cilium.''; PubMed Europe PMC
  109. Beachy PA, Hymowitz SG, Lazarus RA, Leahy DJ, Siebold C.; ''Interactions between Hedgehog proteins and their binding partners come into view.''; PubMed Europe PMC
  110. Mukhopadhyay S, Rohatgi R.; ''G-protein-coupled receptors, Hedgehog signaling and primary cilia.''; PubMed Europe PMC
  111. Di Marcotullio L, Ferretti E, Greco A, De Smaele E, Po A, Sico MA, Alimandi M, Giannini G, Maroder M, Screpanti I, Gulino A.; ''Numb is a suppressor of Hedgehog signalling and targets Gli1 for Itch-dependent ubiquitination.''; PubMed Europe PMC
  112. Evron T, Philipp M, Lu J, Meloni AR, Burkhalter M, Chen W, Caron MG.; ''Growth Arrest Specific 8 (Gas8) and G protein-coupled receptor kinase 2 (GRK2) cooperate in the control of Smoothened signaling.''; PubMed Europe PMC
  113. Zhang Q, Zhang L, Wang B, Ou CY, Chien CT, Jiang J.; ''A hedgehog-induced BTB protein modulates hedgehog signaling by degrading Ci/Gli transcription factor.''; PubMed Europe PMC
  114. Glazer AM, Wilkinson AW, Backer CB, Lapan SW, Gutzman JH, Cheeseman IM, Reddien PW.; ''The Zn finger protein Iguana impacts Hedgehog signaling by promoting ciliogenesis.''; PubMed Europe PMC
  115. Stone DM, Murone M, Luoh S, Ye W, Armanini MP, Gurney A, Phillips H, Brush J, Goddard A, de Sauvage FJ, Rosenthal A.; ''Characterization of the human suppressor of fused, a negative regulator of the zinc-finger transcription factor Gli.''; PubMed Europe PMC
  116. Maloverjan A, Piirsoo M, Michelson P, Kogerman P, Osterlund T.; ''Identification of a novel serine/threonine kinase ULK3 as a positive regulator of Hedgehog pathway.''; PubMed Europe PMC
  117. Chuang PT, McMahon AP.; ''Vertebrate Hedgehog signalling modulated by induction of a Hedgehog-binding protein.''; PubMed Europe PMC
  118. Varjosalo M, Li SP, Taipale J.; ''Divergence of hedgehog signal transduction mechanism between Drosophila and mammals.''; PubMed Europe PMC
  119. Rohatgi R, Milenkovic L, Scott MP.; ''Patched1 regulates hedgehog signaling at the primary cilium.''; PubMed Europe PMC
  120. Goetz SC, Anderson KV.; ''The primary cilium: a signalling centre during vertebrate development.''; PubMed Europe PMC
  121. Maloverjan A, Piirsoo M, Kasak L, Peil L, Østerlund T, Kogerman P.; ''Dual function of UNC-51-like kinase 3 (Ulk3) in the Sonic hedgehog signaling pathway.''; PubMed Europe PMC
  122. Mao B, Wu W, Davidson G, Marhold J, Li M, Mechler BM, Delius H, Hoppe D, Stannek P, Walter C, Glinka A, Niehrs C.; ''Kremen proteins are Dickkopf receptors that regulate Wnt/beta-catenin signalling.''; PubMed Europe PMC
  123. Chen Y, Li S, Tong C, Zhao Y, Wang B, Liu Y, Jia J, Jiang J.; ''G protein-coupled receptor kinase 2 promotes high-level Hedgehog signaling by regulating the active state of Smo through kinase-dependent and kinase-independent mechanisms in Drosophila.''; PubMed Europe PMC
  124. Yang C, Chen W, Chen Y, Jiang J.; ''Smoothened transduces Hedgehog signal by forming a complex with Evc/Evc2.''; PubMed Europe PMC
  125. Jia J, Kolterud A, Zeng H, Hoover A, Teglund S, Toftgård R, Liu A.; ''Suppressor of Fused inhibits mammalian Hedgehog signaling in the absence of cilia.''; PubMed Europe PMC
  126. Corbit KC, Aanstad P, Singla V, Norman AR, Stainier DY, Reiter JF.; ''Vertebrate Smoothened functions at the primary cilium.''; PubMed Europe PMC
  127. Wang C, Low WC, Liu A, Wang B.; ''Centrosomal protein DZIP1 regulates Hedgehog signaling by promoting cytoplasmic retention of transcription factor GLI3 and affecting ciliogenesis.''; PubMed Europe PMC
  128. Chen MH, Wilson CW, Li YJ, Law KK, Lu CS, Gacayan R, Zhang X, Hui CC, Chuang PT.; ''Cilium-independent regulation of Gli protein function by Sufu in Hedgehog signaling is evolutionarily conserved.''; PubMed Europe PMC


View all...
101461view11:32, 1 November 2018ReactomeTeamreactome version 66
100999view21:11, 31 October 2018ReactomeTeamreactome version 65
100535view19:45, 31 October 2018ReactomeTeamreactome version 64
100082view16:30, 31 October 2018ReactomeTeamreactome version 63
99633view15:02, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99239view12:44, 31 October 2018ReactomeTeamreactome version 62
94028view13:52, 16 August 2017ReactomeTeamreactome version 61
93650view11:29, 9 August 2017ReactomeTeamreactome version 61
87140view18:52, 18 July 2016MkutmonOntology Term : 'Hedgehog signaling pathway' added !
86766view09:25, 11 July 2016ReactomeTeamreactome version 56
85681view02:23, 5 June 2016AlexanderPicoQuick edit to datanode annotation or property
83588view07:53, 26 November 2015EgonwAdded missing ENSG parts of the Ensembl IDs.
83259view10:34, 18 November 2015ReactomeTeamVersion54
81371view12:54, 21 August 2015ReactomeTeamNew pathway

External references


View all...
NameTypeDatabase referenceComment
26S proteasomeComplexR-HSA-177750 (Reactome)
26S proteasomeComplexR-HSA-68819 (Reactome)
2p-GLI1 ProteinP08151 (Uniprot-TrEMBL)
2p-GLI1,2,3ComplexR-HSA-5635077 (Reactome)

gene,PTCH2 gene,BOC

ComplexR-HSA-5635078 (Reactome)
2p-GLI1ProteinP08151 (Uniprot-TrEMBL)
2p-GLI2 ProteinP10070 (Uniprot-TrEMBL)
2p-GLI2,3ComplexR-HSA-5635080 (Reactome)
2p-GLI3 ProteinP10071 (Uniprot-TrEMBL)
2p-GLI:GLI1 geneComplexR-HSA-5635082 (Reactome)
2p-GLI:PTCH1 geneComplexR-HSA-5635085 (Reactome)
2p-GLI:SPOP:CUL3:RBX1ComplexR-HSA-5635087 (Reactome)
ADPMetaboliteCHEBI:16761 (ChEBI)
ADRBK1 ProteinP25098 (Uniprot-TrEMBL)
ADRBK1ProteinP25098 (Uniprot-TrEMBL)
ARRB1 ProteinP49407 (Uniprot-TrEMBL)
ARRB2 ProteinP32121 (Uniprot-TrEMBL)
ARRBComplexR-HSA-1911410 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
BOC ProteinQ9BWV1 (Uniprot-TrEMBL)
BOC gene ProteinENSG00000144857 (Ensembl)
BOC:PTCH1ComplexR-HSA-5632584 (Reactome)
CDC73 ProteinQ6P1J9 (Uniprot-TrEMBL)
CDC73:2p-GLIComplexR-HSA-5635076 (Reactome)
CDC73ProteinQ6P1J9 (Uniprot-TrEMBL)
CDON ProteinQ4KMG0 (Uniprot-TrEMBL)
CDONProteinQ4KMG0 (Uniprot-TrEMBL)
CSNK1A1 ProteinP48729 (Uniprot-TrEMBL)
CSNK1A1ProteinP48729 (Uniprot-TrEMBL)
CUL3 ProteinQ13618 (Uniprot-TrEMBL)
DHH(33-?) ProteinO43323 (Uniprot-TrEMBL)
DZIP1ProteinQ86YF9 (Uniprot-TrEMBL)
EFCAB7 ProteinA8K855 (Uniprot-TrEMBL)
EFCAB7:IQCEComplexR-HSA-5633045 (Reactome)
EVC ProteinP57679 (Uniprot-TrEMBL)
EVC2 ProteinQ86UK5 (Uniprot-TrEMBL)
EVC2:EVCComplexR-HSA-5633041 (Reactome)
GAS1 ProteinP54826 (Uniprot-TrEMBL)
GAS1ProteinP54826 (Uniprot-TrEMBL)
GAS8ProteinO95995 (Uniprot-TrEMBL)
GLI1 ProteinP08151 (Uniprot-TrEMBL)
GLI1 gene ProteinENSG00000111087 (Ensembl)
GLI1 geneGeneProductENSG00000111087 (Ensembl)
GLI1,2,3ComplexR-HSA-5610616 (Reactome)
GLI1,2,3ComplexR-HSA-5621782 (Reactome)
GLI1:NUMB:ITCHComplexR-HSA-5635832 (Reactome)
GLI1ProteinP08151 (Uniprot-TrEMBL)
GLI2 ProteinP10070 (Uniprot-TrEMBL)
GLI3 ProteinP10071 (Uniprot-TrEMBL)
GLI:SUFUComplexR-HSA-5621780 (Reactome)
GLI:SUFUComplexR-HSA-5621783 (Reactome)
GPR161ProteinQ8N6U8 (Uniprot-TrEMBL)
HHIP ProteinQ96QV1 (Uniprot-TrEMBL)
HHIP gene ProteinENSG00000164161 (Ensembl)
HHIP gene,PTCH2 gene,BOC geneComplexR-HSA-5635070 (Reactome)
HHIPProteinQ96QV1 (Uniprot-TrEMBL)
Hh-Npp:BOC:PTCH1ComplexR-HSA-5632588 (Reactome)
Hh-Npp:CDON:PTCHComplexR-HSA-5632590 (Reactome)
Hh-Npp:GAS1:PTCHComplexR-HSA-5632592 (Reactome)
Hh-Npp:HHIPComplexR-HSA-445447 (Reactome)
Hh-NppComplexR-HSA-5362783 (Reactome)
IHH ProteinQ14623 (Uniprot-TrEMBL)
IQCE ProteinQ6IPM2 (Uniprot-TrEMBL)
IQCE:EFCAB7:EVC2:EVCComplexR-HSA-5633050 (Reactome)
ITCH ProteinQ96J02 (Uniprot-TrEMBL)
ITCHProteinQ96J02 (Uniprot-TrEMBL)
KIF3A ProteinQ9Y496 (Uniprot-TrEMBL)
KIF3AProteinQ9Y496 (Uniprot-TrEMBL)
KIF7ProteinQ2M1P5 (Uniprot-TrEMBL)
NUMB ProteinP49757 (Uniprot-TrEMBL)
NUMB:ITCHComplexR-HSA-5610562 (Reactome)
NUMBProteinP49757 (Uniprot-TrEMBL)
PSMA1 ProteinP25786 (Uniprot-TrEMBL)
PSMA2 ProteinP25787 (Uniprot-TrEMBL)
PSMA3 ProteinP25788 (Uniprot-TrEMBL)
PSMA4 ProteinP25789 (Uniprot-TrEMBL)
PSMA5 ProteinP28066 (Uniprot-TrEMBL)
PSMA6 ProteinP60900 (Uniprot-TrEMBL)
PSMA7 ProteinO14818 (Uniprot-TrEMBL)
PSMA8 ProteinQ8TAA3 (Uniprot-TrEMBL)
PSMB1 ProteinP20618 (Uniprot-TrEMBL)
PSMB10 ProteinP40306 (Uniprot-TrEMBL)
PSMB11 ProteinA5LHX3 (Uniprot-TrEMBL)
PSMB2 ProteinP49721 (Uniprot-TrEMBL)
PSMB3 ProteinP49720 (Uniprot-TrEMBL)
PSMB4 ProteinP28070 (Uniprot-TrEMBL)
PSMB5 ProteinP28074 (Uniprot-TrEMBL)
PSMB6 ProteinP28072 (Uniprot-TrEMBL)
PSMB7 ProteinQ99436 (Uniprot-TrEMBL)
PSMB8 ProteinP28062 (Uniprot-TrEMBL)
PSMB9 ProteinP28065 (Uniprot-TrEMBL)
PSMC1 ProteinP62191 (Uniprot-TrEMBL)
PSMC2 ProteinP35998 (Uniprot-TrEMBL)
PSMC3 ProteinP17980 (Uniprot-TrEMBL)
PSMC4 ProteinP43686 (Uniprot-TrEMBL)
PSMC5 ProteinP62195 (Uniprot-TrEMBL)
PSMC6 ProteinP62333 (Uniprot-TrEMBL)
PSMD1 ProteinQ99460 (Uniprot-TrEMBL)
PSMD10 ProteinO75832 (Uniprot-TrEMBL)
PSMD11 ProteinO00231 (Uniprot-TrEMBL)
PSMD12 ProteinO00232 (Uniprot-TrEMBL)
PSMD13 ProteinQ9UNM6 (Uniprot-TrEMBL)
PSMD14 ProteinO00487 (Uniprot-TrEMBL)
PSMD2 ProteinQ13200 (Uniprot-TrEMBL)
PSMD3 ProteinO43242 (Uniprot-TrEMBL)
PSMD4 ProteinP55036 (Uniprot-TrEMBL)
PSMD5 ProteinQ16401 (Uniprot-TrEMBL)
PSMD6 ProteinQ15008 (Uniprot-TrEMBL)
PSMD7 ProteinP51665 (Uniprot-TrEMBL)
PSMD8 ProteinP48556 (Uniprot-TrEMBL)
PSMD9 ProteinO00233 (Uniprot-TrEMBL)
PSME1 ProteinQ06323 (Uniprot-TrEMBL)
PSME2 ProteinQ9UL46 (Uniprot-TrEMBL)
PSME3 ProteinP61289 (Uniprot-TrEMBL)
PSME4 ProteinQ14997 (Uniprot-TrEMBL)
PSMF1 ProteinQ92530 (Uniprot-TrEMBL)
PTCH1 ProteinQ13635 (Uniprot-TrEMBL)
PTCH1 gene ProteinENSG00000185920 (Ensembl)
PTCH1 geneGeneProductENSG00000185920 (Ensembl)
PTCH1:SMURFComplexR-HSA-5632594 (Reactome)
PTCH1ProteinQ13635 (Uniprot-TrEMBL)
PTCH2 gene ProteinENSG00000117425 (Ensembl)
RBX1 ProteinP62877 (Uniprot-TrEMBL)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
SHFM1 ProteinP60896 (Uniprot-TrEMBL)
SHH(34-?) ProteinQ15465 (Uniprot-TrEMBL)
SMO ProteinQ99835 (Uniprot-TrEMBL)
SMO dimer:ARRB:KIF3AComplexR-HSA-5632599 (Reactome)
SMO dimer:CSNK1A1ComplexR-HSA-5632602 (Reactome)
SMO dimerComplexR-HSA-5610574 (Reactome)
SMO dimerComplexR-HSA-5632597 (Reactome)
SMURF1 ProteinQ9HCE7 (Uniprot-TrEMBL)
SMURF2 ProteinQ9HAU4 (Uniprot-TrEMBL)
SMURFComplexR-HSA-173533 (Reactome)
SPOP ProteinO43791 (Uniprot-TrEMBL)
SPOP:CUL3:RBX1ComplexR-HSA-5635071 (Reactome)
SPOPL ProteinQ6IQ16 (Uniprot-TrEMBL)
SUFU ProteinQ9UMX1 (Uniprot-TrEMBL)
SUFUProteinQ9UMX1 (Uniprot-TrEMBL)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
ULK3 ProteinQ6PHR2 (Uniprot-TrEMBL)
ULK3:SUFUComplexR-HSA-5635073 (Reactome)
ULK3ProteinQ6PHR2 (Uniprot-TrEMBL)
UbComplexR-HSA-113595 (Reactome)
UbComplexR-HSA-68524 (Reactome)
p-GLI1 ProteinP08151 (Uniprot-TrEMBL)
p-GLI1,2,3ComplexR-HSA-5635089 (Reactome)
p-GLI1,2,3ComplexR-HSA-5635090 (Reactome)
p-GLI2 ProteinP10070 (Uniprot-TrEMBL)
p-GLI3 ProteinP10071 (Uniprot-TrEMBL)


ComplexR-HSA-5632615 (Reactome)
p6S, T-SMO dimer:EVC2:EVCComplexR-HSA-5633039 (Reactome)
p6S, T-SMO dimerComplexR-HSA-5632614 (Reactome)

S590, T593, S595-SMO

ComplexR-HSA-5632622 (Reactome)
pS588, S590, T593, S595, S611, S615, S616-SMO ProteinQ99835 (Uniprot-TrEMBL)
pS588, S590, T593, S595-SMO ProteinQ99835 (Uniprot-TrEMBL)
pS588,S590, T593,


ComplexR-HSA-5632624 (Reactome)
ub-2p-GLI2 ProteinP10070 (Uniprot-TrEMBL)
ub-2p-GLI2,3:SPOP:CUL3:RBX1ComplexR-HSA-5635095 (Reactome)
ub-2p-GLI3 ProteinP10071 (Uniprot-TrEMBL)
ub-GLI1 ProteinP08151 (Uniprot-TrEMBL)
ub-GLI1:NUMB:ITCHComplexR-HSA-5635836 (Reactome)
ub-PTCH1 ProteinQ13635 (Uniprot-TrEMBL)
ub-PTCH1:SMURFComplexR-HSA-5632582 (Reactome)
ub-PTCH1ProteinQ13635 (Uniprot-TrEMBL)
unknown kinaseR-HSA-5635063 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
26S proteasomemim-catalysisR-HSA-5635854 (Reactome)
26S proteasomemim-catalysisR-HSA-5635868 (Reactome)
2p-GLI1,2,3ArrowR-HSA-5635841 (Reactome)