Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PTCH1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PTCH1 a multi-pass membrane protein member of the ?patched? family that acts as a receptor for sonic hedgehog (SHH), indian hedgehog (IHH) and desert hedgehog (DHH). Associates with the smoothened protein (SMO) to transduce the hedgehog protein?s signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis. Interacts with SNX17. Expressed in tumor cells but not in normal skin. In the embryo, found in all major target tissues of sonic hedgehog, such as the ventral neural tube, somites, and tissues surrounding the zone of polarizing activity of the limb bud. Defects in PTCH1 are the cause of basal cell nevus syndrome (BCNS), also known as Gorlin syndrome. BCNS is an autosomal dominant 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 basal cell carcinomas, fibromas of the ovaries and heart, cysts of the skin, jaws and mesentery, as well as medulloblastomas and meningiomas. PTCH1 defects is also the cause of holoprosencephaly, the most common structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; Cell cycle regulation; Membrane protein, integral
Cellular Component: Golgi apparatus; intracellular membrane-bound organelle; perinuclear region of cytoplasm; postsynaptic density; plasma membrane; integral to membrane; midbody; caveola
Molecular Function: heparin binding; protein binding; cyclin binding; hedgehog receptor activity; protein complex binding; cholesterol binding; patched binding; smoothened binding
Biological Process: heart morphogenesis; hindlimb morphogenesis; epidermis development; regulation of mitotic cell cycle; negative regulation of transcription from RNA polymerase II promoter; glucose homeostasis; response to chlorate; response to estradiol stimulus; regulation of protein localization; negative regulation of osteoblast differentiation; embryonic limb morphogenesis; negative regulation of epithelial cell proliferation; response to drug; smoothened signaling pathway; negative regulation of multicellular organism growth; response to retinoic acid; pharyngeal system development; negative regulation of transcription factor activity; neural tube patterning; keratinocyte proliferation; negative regulation of cell division; spinal cord motor neuron differentiation; limb morphogenesis; organ morphogenesis; dorsal/ventral pattern formation; response to mechanical stimulus; ureteric bud branching; negative regulation of smoothened signaling pathway; neural plate pattern formation; neural tube closure; protein processing; brain development; regulation of smoothened signaling pathway
Reference #:  Q13635 (UniProtKB)
Alt. Names/Synonyms: BCNS; FLJ26746; FLJ42602; HPE7; NBCCS; patched homolog 1 (Drosophila); Protein patched homolog 1; PTC; PTC1; PTCH; PTCH protein +12b; PTCH protein +4'; PTCH protein -10; PTCH1; PTCH11
Gene Symbols: PTCH1
Molecular weight: 160,545 Da
Basal Isoelectric point: 6.42  Predict pI for various phosphorylation states
CST Pathways:  Hedgehog Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PTCH1

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K163-ub QLMIQTPkEEGANVL
0 1 K269 LEFLEELKKINYQVD
0 1 S435-p DDILKSFsDVSVIRV
0 1 S463-p TMLRWDCsKSQGAVG
0 1 Y873-p GKIMPNNyKNGSDDG
0 1 Y884-p SDDGVLAyKLLVQTG
0 1 S1079 GLIGIKLSAVPVVIL
0 1 S1089 PVVILIASVGIGVEF
0 4 T1195-p NGLNRLPtPsPEPPP
0 4 S1197-p LNRLPtPsPEPPPSV
0 1 S1331-p EISTEGHsGPSNRAR
  PTCH1 iso2  
K162 QLMIQTPKEEGANVL
K268 LEFLEELKKINYQVD
S434 DDILKSFSDVSVIRV
S462 TMLRWDCSKSQGAVG
Y872 GKIMPNNYKNGSDDG
Y883 SDDGVLAYKLLVQTG
S1078 GLIGIKLSAVPVVIL
S1088 PVVILIASVGIGVEF
T1194 NGLNRLPTPSPEPPP
S1196 LNRLPTPSPEPPPSV
S1330 EISTEGHSGPSNRAR
  mouse

 
K149 QLMIQTPKEEGANVL
K255-ub LEFLEELkKINYQVD
S421 DDILKSFSDVSVIRV
S449 TMLRWDCSKSQGAVG
Y859 GRIMPNNYKNGSDDG
Y870 SDDGVLAYKLLVQTG
S1065-p GLIGIKLsAVPVVIL
S1075-p PVVILIAsVGIGVEF
T1181-p NGLNRLPtPsPEPPP
S1183-p LNRLPtPsPEPPPSV
S1317 EISTEGHSGPSNRDR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.