Joubert syndrome (Homo sapiens)

From WikiPathways

Revision as of 05:34, 21 July 2024 by Egonw (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search
243655292120NodeCiliary traffickingTransition zone35Basal body / centrioleTMEM17553513, 2913, 293253513, 292013, 2913, 2952, 292113, 291432432932232024335152115221, 8172128211718183418, 24155527, 332641241724, 272210716, 3334Nodes6LegendAxonemeTMEM67TMEM216Ciliary membraneWntKIAA0586GDPDVL3RAB3IPSUFUATF4CEP97MYO5ARHOAMYO6ARR3FLNAPIBF1BBS4TCTN3ARL2PtdIns4PNBSTMEM138GDPKAT5PARP1PCM1CEP120PCNTRP2PDE6BBBS9ATMRHEBDVL1BBS5GDPBBS7PtdIns(3,4,5)P3UNC119NPHP4SHHGMPPtdIns(4,5)P2TCTN1PtdIns(3,4)P2CPLANE1ANKS6NPHP3MTORNINTTC8CSPP1TMEM231ARMC9ARL13BINVSCCP110CEP104PDE6AZNF423cGMPNEK8GTPCETN1CETN2BBS1TMEM237MRE11BBS2PDE6GCalmodulinTCTN2B9D1RAD50OFD1INPP5ECEP41NPHP1AHI1INPP5EPDE6DARL13B21B9D2CC2D2AMKS1PDE6DGTPRHEBPDE6D15ARL3UNC119NucleusZNF423PDE6DRAB8AGTPCEP290CEP164DVL1CEP290Non JS-associated gene product or proteinJS-associated gene or gene productMetabolitePathwayMIM-interaction: conversionMIM-interaction: bindingMIM-interaction: activationMIM-interaction: catalysisMIM-interaction: inhibitionLinks two identical nodesEdgesGTPARL3CEP164OFD1WntRAB8ARPGRIP1LNodeNodeNodePhosphoinositides metabolism


Description

Joubert syndrome (JS) is a rare hereditary disorder that is classified as a ciliopathy, and is caused by mutations occurring in genes essential for the development and proper functioning of primary cellular cilia. These hair-like structures located on the cell membrane are responsible for detecting and relaying external signals to the interior of the cell. The defining JS feature is the molar tooth sign (MTS), which is the particular manner in which a characteristic malformation of midbrain appears in radiological imaging, and which causes delays in both intellectual and motor development. A visual representation of the pathways underlying JS pathogenesis was synthesized, which might provide a more complete understanding of the disease, possibly aiding in better diagnosis and more successful treatment.

Data collection on the genes, pathways and interactions involved was done through a literature search in combination supported by online databases such as OMIM, STRING and GeneMANIA. The pathway was created using PathVisio version 3.3.0. Nodes were annotated using the appropriate Ensembl, ChEBI, or Uniprot-TrEMBL identifiers and standardized MIM notation was used to visualize the interactions between them.

A final pathway containing 88 unique nodes and 71 interactions was created. The pathway highlights three functional or structural areas of the primary cilium that appear to play important roles in JS pathogenesis, namely the basal body or centriole, the transition zone and ciliary trafficking. Furthermore, two specific complexes seem to be of particular interest; the B9 ciliary complex and the centriolar satellite contain eight and three JS-associated protein respectively. Lastly, the ARL13B-PDE6D-INPP5E signaling network ensures the proper functioning of INPP5E, and enzyme that converts lipid ciliary membrane components. All three proteins have been found to be mutated in JS patients.

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Kong AM, Speed CJ, O'Malley CJ, Layton MJ, Meehan T, Loveland KL, Cheema S, Ooms LM, Mitchell CA; ''Cloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi network.''; J Biol Chem, 2000 PubMed Europe PMC Scholia
  2. Tuz K, Hsiao YC, Juárez O, Shi B, Harmon EY, Phelps IG, Lennartz MR, Glass IA, Doherty D, Ferland RJ; ''The Joubert syndrome-associated missense mutation (V443D) in the Abelson-helper integration site 1 (AHI1) protein alters its localization and protein-protein interactions.''; J Biol Chem, 2013 PubMed Europe PMC Scholia
  3. Tong SJ, Wall AA, Hung Y, Luo L, Stow JL; ''Guanine nucleotide exchange factors activate Rab8a for Toll-like receptor signalling.''; Small GTPases, 2019 PubMed Europe PMC Scholia
  4. Veltel S, Gasper R, Eisenacher E, Wittinghofer A; ''The retinitis pigmentosa 2 gene product is a GTPase-activating protein for Arf-like 3.''; Nat Struct Mol Biol, 2008 PubMed Europe PMC Scholia
  5. Chaki M, Airik R, Ghosh AK, Giles RH, Chen R, Slaats GG, Wang H, Hurd TW, Zhou W, Cluckey A, Gee HY, Ramaswami G, Hong CJ, Hamilton BA, Cervenka I, Ganji RS, Bryja V, Arts HH, van Reeuwijk J, Oud MM, Letteboer SJ, Roepman R, Husson H, Ibraghimov-Beskrovnaya O, Yasunaga T, Walz G, Eley L, Sayer JA, Schermer B, Liebau MC, Benzing T, Le Corre S, Drummond I, Janssen S, Allen SJ, Natarajan S, O'Toole JF, Attanasio M, Saunier S, Antignac C, Koenekoop RK, Ren H, Lopez I, Nayir A, Stoetzel C, Dollfus H, Massoudi R, Gleeson JG, Andreoli SP, Doherty DG, Lindstrad A, Golzio C, Katsanis N, Pape L, Abboud EB, Al-Rajhi AA, Lewis RA, Omran H, Lee EY, Wang S, Sekiguchi JM, Saunders R, Johnson CA, Garner E, Vanselow K, Andersen JS, Shlomai J, Nurnberg G, Nurnberg P, Levy S, Smogorzewska A, Otto EA, Hildebrandt F; ''Exome capture reveals ZNF423 and CEP164 mutations, linking renal ciliopathies to DNA damage response signaling.''; Cell, 2012 PubMed Europe PMC Scholia
  6. Gorden NT, Arts HH, Parisi MA, Coene KL, Letteboer SJ, van Beersum SE, Mans DA, Hikida A, Eckert M, Knutzen D, Alswaid AF, Ozyurek H, Dibooglu S, Otto EA, Liu Y, Davis EE, Hutter CM, Bammler TK, Farin FM, Dorschner M, Topçu M, Zackai EH, Rosenthal P, Owens KN, Katsanis N, Vincent JB, Hildebrandt F, Rubel EW, Raible DW, Knoers NV, Chance PF, Roepman R, Moens CB, Glass IA, Doherty D; ''CC2D2A is mutated in Joubert syndrome and interacts with the ciliopathy-associated basal body protein CEP290.''; Am J Hum Genet, 2008 PubMed Europe PMC Scholia
  7. Florio SK, Prusti RK, Beavo JA; ''Solubilization of membrane-bound rod phosphodiesterase by the rod phosphodiesterase recombinant delta subunit.''; J Biol Chem, 1996 PubMed Europe PMC Scholia
  8. Kisseleva MV, Wilson MP, Majerus PW; ''The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase.''; J Biol Chem, 2000 PubMed Europe PMC Scholia
  9. Huang L, Szymanska K, Jensen VL, Janecke AR, Innes AM, Davis EE, Frosk P, Li C, Willer JR, Chodirker BN, Greenberg CR, McLeod DR, Bernier FP, Chudley AE, Müller T, Shboul M, Logan CV, Loucks CM, Beaulieu CL, Bowie RV, Bell SM, Adkins J, Zuniga FI, Ross KD, Wang J, Ban MR, Becker C, Nürnberg P, Douglas S, Craft CM, Akimenko MA, Hegele RA, Ober C, Utermann G, Bolz HJ, Bulman DE, Katsanis N, Blacque OE, Doherty D, Parboosingh JS, Leroux MR, Johnson CA, Boycott KM; ''TMEM237 is mutated in individuals with a Joubert syndrome related disorder and expands the role of the TMEM family at the ciliary transition zone.''; Am J Hum Genet, 2011 PubMed Europe PMC Scholia
  10. Sato T, Umetsu A, Tamanoi F; ''Characterization of the Rheb-mTOR signaling pathway in mammalian cells: constitutive active mutants of Rheb and mTOR.''; Methods Enzymol, 2008 PubMed Europe PMC Scholia
  11. Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC; ''The complex of Arl2-GTP and PDE delta: from structure to function.''; EMBO J, 2002 PubMed Europe PMC Scholia
  12. Hsiao YC, Tong ZJ, Westfall JE, Ault JG, Page-McCaw PS, Ferland RJ; ''Ahi1, whose human ortholog is mutated in Joubert syndrome, is required for Rab8a localization, ciliogenesis and vesicle trafficking.''; Hum Mol Genet, 2009 PubMed Europe PMC Scholia
  13. Li C, Jensen VL, Park K, Kennedy J, Garcia-Gonzalo FR, Romani M, De Mori R, Bruel AL, Gaillard D, Doray B, Lopez E, Rivière JB, Faivre L, Thauvin-Robinet C, Reiter JF, Blacque OE, Valente EM, Leroux MR; ''MKS5 and CEP290 Dependent Assembly Pathway of the Ciliary Transition Zone.''; PLoS Biol, 2016 PubMed Europe PMC Scholia
  14. Sayer JA, Otto EA, O'Toole JF, Nurnberg G, Kennedy MA, Becker C, Hennies HC, Helou J, Attanasio M, Fausett BV, Utsch B, Khanna H, Liu Y, Drummond I, Kawakami I, Kusakabe T, Tsuda M, Ma L, Lee H, Larson RG, Allen SJ, Wilkinson CJ, Nigg EA, Shou C, Lillo C, Williams DS, Hoppe B, Kemper MJ, Neuhaus T, Parisi MA, Glass IA, Petry M, Kispert A, Gloy J, Ganner A, Walz G, Zhu X, Goldman D, Nurnberg P, Swaroop A, Leroux MR, Hildebrandt F; ''The centrosomal protein nephrocystin-6 is mutated in Joubert syndrome and activates transcription factor ATF4.''; Nat Genet, 2006 PubMed Europe PMC Scholia
  15. Ismail SA, Chen YX, Rusinova A, Chandra A, Bierbaum M, Gremer L, Triola G, Waldmann H, Bastiaens PI, Wittinghofer A; ''Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo.''; Nat Chem Biol, 2011 PubMed Europe PMC Scholia
  16. Kim JC, Badano JL, Sibold S, Esmail MA, Hill J, Hoskins BE, Leitch CC, Venner K, Ansley SJ, Ross AJ, Leroux MR, Katsanis N, Beales PL; ''The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression.''; Nat Genet, 2004 PubMed Europe PMC Scholia
  17. Dammermann A, Merdes A; ''Assembly of centrosomal proteins and microtubule organization depends on PCM-1.''; J Cell Biol, 2002 PubMed Europe PMC Scholia
  18. Tsang WY, Spektor A, Luciano DJ, Indjeian VB, Chen Z, Salisbury JL, Sánchez I, Dynlacht BD; ''CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability.''; Mol Biol Cell, 2006 PubMed Europe PMC Scholia
  19. Wright KJ, Baye LM, Olivier-Mason A, Mukhopadhyay S, Sang L, Kwong M, Wang W, Pretorius PR, Sheffield VC, Sengupta P, Slusarski DC, Jackson PK; ''An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3to the primary cilium.''; Genes Dev, 2011 PubMed Europe PMC Scholia
  20. Adams M, Simms RJ, Abdelhamed Z, Dawe HR, Szymanska K, Logan CV, Wheway G, Pitt E, Gull K, Knowles MA, Blair E, Cross SH, Sayer JA, Johnson CA; ''A meckelin-filamin A interaction mediates ciliogenesis.''; Hum Mol Genet, 2012 PubMed Europe PMC Scholia
  21. Humbert MC, Weihbrecht K, Searby CC, Li Y, Pope RM, Sheffield VC, Seo S; ''ARL13B, PDE6D, and CEP164 form a functional network for INPP5E ciliary targeting.''; Proc Natl Acad Sci U S A, 2012 PubMed Europe PMC Scholia
  22. Cote RH; ''Characteristics of photoreceptor PDE (PDE6): similarities and differences to PDE5.''; Int J Impot Res, 2004 PubMed Europe PMC Scholia
  23. Valente EM, Logan CV, Mougou-Zerelli S, Lee JH, Silhavy JL, Brancati F, Iannicelli M, Travaglini L, Romani S, Illi B, Adams M, Szymanska K, Mazzotta A, Lee JE, Tolentino JC, Swistun D, Salpietro CD, Fede C, Gabriel S, Russ C, Cibulskis K, Sougnez C, Hildebrandt F, Otto EA, Held S, Diplas BH, Davis EE, Mikula M, Strom CM, Ben-Zeev B, Lev D, Sagie TL, Michelson M, Yaron Y, Krause A, Boltshauser E, Elkhartoufi N, Roume J, Shalev S, Munnich A, Saunier S, Inglehearn C, Saad A, Alkindy A, Thomas S, Vekemans M, Dallapiccola B, Katsanis N, Johnson CA, Attié-Bitach T, Gleeson JG; ''Mutations in TMEM216 perturb ciliogenesis and cause Joubert, Meckel and related syndromes.''; Nat Genet, 2010 PubMed Europe PMC Scholia
  24. Tsang WY, Bossard C, Khanna H, Peränen J, Swaroop A, Malhotra V, Dynlacht BD; ''CP110 suppresses primary cilia formation through its interaction with CEP290, a protein deficient in human ciliary disease.''; Dev Cell, 2008 PubMed Europe PMC Scholia
  25. Wang C, Li J, Meng Q, Wang B; ''Three Tctn proteins are functionally conserved in the regulation of neural tube patterning and Gli3 processing but not ciliogenesis and Hedgehog signaling in the mouse.''; Dev Biol, 2017 PubMed Europe PMC Scholia
  26. Garcia-Gonzalo FR, Phua SC, Roberson EC, Garcia G 3rd, Abedin M, Schurmans S, Inoue T, Reiter JF; ''Phosphoinositides Regulate Ciliary Protein Trafficking to Modulate Hedgehog Signaling.''; Dev Cell, 2015 PubMed Europe PMC Scholia
  27. Kim J, Krishnaswami SR, Gleeson JG; ''CEP290 interacts with the centriolar satellite component PCM-1 and is required for Rab8 localization to the primary cilium.''; Hum Mol Genet, 2008 PubMed Europe PMC Scholia
  28. Nachury MV, Loktev AV, Zhang Q, Westlake CJ, Peränen J, Merdes A, Slusarski DC, Scheller RH, Bazan JF, Sheffield VC, Jackson PK; ''A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis.''; Cell, 2007 PubMed Europe PMC Scholia
  29. Williams CL, Li C, Kida K, Inglis PN, Mohan S, Semenec L, Bialas NJ, Stupay RM, Chen N, Blacque OE, Yoder BK, Leroux MR; ''MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis.''; J Cell Biol, 2011 PubMed Europe PMC Scholia
  30. Ku MC, Stewart S, Hata A; ''Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target genes.''; Biochem Biophys Res Commun, 2003 PubMed Europe PMC Scholia
  31. Chih B, Liu P, Chinn Y, Chalouni C, Komuves LG, Hass PE, Sandoval W, Peterson AS; ''A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain.''; Nat Cell Biol, 2011 PubMed Europe PMC Scholia
  32. Zuniga FI, Craft CM; ''Deciphering the structure and function of Als2cr4 in the mouse retina.''; Invest Ophthalmol Vis Sci, 2010 PubMed Europe PMC Scholia
  33. Lopes CA, Prosser SL, Romio L, Hirst RA, O'Callaghan C, Woolf AS, Fry AM; ''Centriolar satellites are assembly points for proteins implicated in human ciliopathies, including oral-facial-digital syndrome 1.''; J Cell Sci, 2011 PubMed Europe PMC Scholia
  34. Bergmann C, Fliegauf M, Brüchle NO, Frank V, Olbrich H, Kirschner J, Schermer B, Schmedding I, Kispert A, Kränzlin B, Nürnberg G, Becker C, Grimm T, Girschick G, Lynch SA, Kelehan P, Senderek J, Neuhaus TJ, Stallmach T, Zentgraf H, Nürnberg P, Gretz N, Lo C, Lienkamp S, Schäfer T, Walz G, Benzing T, Zerres K, Omran H; ''Loss of nephrocystin-3 function can cause embryonic lethality, Meckel-Gruber-like syndrome, situs inversus, and renal-hepatic-pancreatic dysplasia.''; Am J Hum Genet, 2008 PubMed Europe PMC Scholia
  35. Garcia-Gonzalo FR, Corbit KC, Sirerol-Piquer MS, Ramaswami G, Otto EA, Noriega TR, Seol AD, Robinson JF, Bennett CL, Josifova DJ, García-Verdugo JM, Katsanis N, Hildebrandt F, Reiter JF; ''A transition zone complex regulates mammalian ciliogenesis and ciliary membrane composition.''; Nat Genet, 2011 PubMed Europe PMC Scholia
  36. ''''; , PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
134349view05:34, 21 July 2024EgonwRemoved template comments
125785view09:57, 10 March 2023DeSlConverted NIN-protein ID to reviewed UniProt
125784view09:55, 10 March 2023DeSlAdded PW node to link to more detailed molecular mechanism
125783view09:52, 10 March 2023DeSlChanged DataNodes in Legend to textLabels
120396view08:56, 30 November 2021Fehrhartboxed pathway nodes
117153view09:44, 18 May 2021EweitzModified title
105130view12:27, 9 July 2019Fehrhartconnected unconnected lines
105068view07:38, 4 July 2019EgonwReplaced secondary ChEBI identifiers with a primary identifiers.
105054view13:07, 3 July 2019AnneDBA small adjustmen was made regarding the structural organization of the pathway.
105022view16:47, 28 June 2019AnneDBModified description
104971view13:54, 27 June 2019AnneDBModified description
104969view13:51, 27 June 2019AnneDBModified description
104958view12:34, 27 June 2019AnneDBModified description
104956view11:41, 27 June 2019AnneDBA few corrections were made, in addition to replacements of interactions of unknown nature by MIM notations.
104932view14:14, 25 June 2019AnneDBModified description
104931view14:12, 25 June 2019AnneDBModified description
104922view11:40, 25 June 2019AnneDBOntology Term : 'signaling pathway' added !
104921view11:40, 25 June 2019AnneDBOntology Term : 'disease pathway' added !
104890view13:18, 23 June 2019AnneDBOntology Term : 'Joubert syndrome' added !
104889view13:14, 23 June 2019AnneDBModified description
104888view13:14, 23 June 2019AnneDBModified description
104887view13:08, 23 June 2019AnneDBModified title
104886view13:07, 23 June 2019AnneDBNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
AHI1GeneProductENSG00000135541 (Ensembl)
ANKS6GeneProductENSG00000165138 (Ensembl)
ARL13BGeneProductENSG00000169379 (Ensembl)
ARL2GeneProductENSG00000213465 (Ensembl)
ARL3GeneProductENSG00000138175 (Ensembl)
ARMC9GeneProductENSG00000135931 (Ensembl)
ARR3GeneProductENSG00000120500 (Ensembl)
ATF4GeneProductENSG00000128272 (Ensembl)
ATMGeneProductENSG00000149311 (Ensembl)
B9D1GeneProductENSG00000108641 (Ensembl)
B9D2GeneProductENSG00000123810 (Ensembl)
BBS1GeneProductENSG00000174483 (Ensembl)
BBS2GeneProductENSG00000125124 (Ensembl)
BBS4GeneProductENSG00000140463 (Ensembl)
BBS5GeneProductENSG00000163093 (Ensembl)
BBS7GeneProductENSG00000138686 (Ensembl)
BBS9GeneProductENSG00000122507 (Ensembl)
CC2D2AGeneProductENSG00000048342 (Ensembl)
CCP110GeneProductENSG00000103540 (Ensembl)
CEP104GeneProductENSG00000116198 (Ensembl)
CEP120GeneProductENSG00000168944 (Ensembl)
CEP164GeneProductENSG00000110274 (Ensembl)
CEP290GeneProductENSG00000198707 (Ensembl)
CEP41GeneProductENSG00000106477 (Ensembl)
CEP97GeneProductENSG00000182504 (Ensembl)
CETN1ProteinQ12798 (Uniprot-TrEMBL)
CETN2ProteinP41208 (Uniprot-TrEMBL)
CPLANE1GeneProductENSG00000197603 (Ensembl)
CSPP1GeneProductENSG00000104218 (Ensembl)
CalmodulinMetaboliteCHEBI:3324 (ChEBI)
DVL1GeneProductENSG00000107404 (Ensembl)
DVL3GeneProductENSG00000161202 (Ensembl)
FLNAGeneProductENSG00000196924 (Ensembl)
GDPMetaboliteCHEBI:17552 (ChEBI)
GMPMetaboliteCHEBI:16356 (ChEBI)
GTPMetaboliteCHEBI:37565 (ChEBI)
INPP5EGeneProductENSG00000148384 (Ensembl)
INVSGeneProductENSG00000119509 (Ensembl)
KAT5GeneProductENSG00000172977 (Ensembl)
KIAA0586GeneProductENSG00000100578 (Ensembl)
MKS1GeneProductENSG00000011143 (Ensembl)
MRE11GeneProductENSG00000020922 (Ensembl)
MTORGeneProductENSG00000198793 (Ensembl)
MYO5AGeneProductENSG00000197535 (Ensembl)
MYO6GeneProductENSG00000196586 (Ensembl)
NBSMetaboliteCHEBI:53174 (ChEBI)
NEK8GeneProductENSG00000160602 (Ensembl)
NINProteinQ8N4C6 (Uniprot-TrEMBL)
NPHP1GeneProductENSG00000144061 (Ensembl)
NPHP3GeneProductENSG00000113971 (Ensembl)
NPHP4GeneProductENSG00000131697 (Ensembl)
OFD1GeneProductENSG00000046651 (Ensembl)
PARP1GeneProductENSG00000143799 (Ensembl)
PCM1GeneProductENSG00000078674 (Ensembl) Component of the centriolar satellite.
PCNTProteinO95613 (Uniprot-TrEMBL)
PDE6AGeneProductENSG00000132915 (Ensembl)
PDE6BGeneProductENSG00000133256 (Ensembl)
PDE6DGeneProductENSG00000156973 (Ensembl)
PDE6GGeneProductENSG00000185527 (Ensembl)
PIBF1GeneProductENSG00000083535 (Ensembl)
Phosphoinositides metabolismPathwayWP4971 (WikiPathways)
PtdIns(3,4)P2MetaboliteCHEBI:84247 (ChEBI)
PtdIns(3,4,5)P3MetaboliteCHEBI:16618 (ChEBI)
PtdIns(4,5)P2MetaboliteCHEBI:18348 (ChEBI)
PtdIns4PMetaboliteCHEBI:17526 (ChEBI)
RAB3IPGeneProductENSG00000127328 (Ensembl)
RAB8AGeneProductENSG00000167461 (Ensembl)
RAD50GeneProductENSG00000113522 (Ensembl)
RHEBGeneProductENSG00000106615 (Ensembl)
RHOAGeneProductENSG00000067560 (Ensembl)
RP2GeneProductENSG00000102218 (Ensembl)
RPGRIP1LGeneProductENSG00000103494 (Ensembl)
SHHGeneProductENSG00000164690 (Ensembl)
SUFUGeneProductENSG00000107882 (Ensembl)
TCTN1GeneProductENSG00000204852 (Ensembl)
TCTN2GeneProductENSG00000168778 (Ensembl)
TCTN3GeneProductENSG00000119977 (Ensembl)
TMEM138GeneProductENSG00000149483 (Ensembl)
TMEM17GeneProductENSG00000186889 (Ensembl)
TMEM216GeneProductENSG00000187049 (Ensembl)
TMEM231GeneProductENSG00000205084 (Ensembl)
TMEM237GeneProductENSG00000155755 (Ensembl)
TMEM67GeneProductENSG00000164953 (Ensembl)
TTC8GeneProductENSG00000165533 (Ensembl)
UNC119GeneProductENSG00000109103 (Ensembl)
WntPathwayWP428 (WikiPathways)
ZNF423GeneProductENSG00000102935 (Ensembl)
cGMPMetaboliteCHEBI:16356 (ChEBI)

Annotated Interactions

No annotated interactions

Personal tools