Q13635 · PTC1_HUMAN

  • Protein
    Protein patched homolog 1
  • Gene
    PTCH1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

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's proteins signal. Seems to have a tumor suppressor function, as inactivation of this protein is probably a necessary, if not sufficient step for tumorigenesis.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentapical part of cell
Cellular Componentaxonal growth cone
Cellular Componentcaveola
Cellular Componentciliary membrane
Cellular Componentdendritic growth cone
Cellular Componentendocytic vesicle membrane
Cellular Componentintracellular membrane-bounded organelle
Cellular Componentmidbody
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Molecular Functioncholesterol binding
Molecular Functioncyclin binding
Molecular Functionhedgehog family protein binding
Molecular Functionhedgehog receptor activity
Molecular Functionheparin binding
Molecular Functionpatched binding
Molecular Functionprotein-containing complex binding
Molecular Functionsmoothened binding
Biological Processanimal organ morphogenesis
Biological Processbrain development
Biological Processbranching involved in ureteric bud morphogenesis
Biological Processcell differentiation involved in kidney development
Biological Processcell fate determination
Biological Processcell proliferation involved in metanephros development
Biological Processcellular response to cholesterol
Biological Processcommissural neuron axon guidance
Biological Processdorsal/ventral neural tube patterning
Biological Processdorsal/ventral pattern formation
Biological Processembryonic limb morphogenesis
Biological Processembryonic organ development
Biological Processepidermal cell fate specification
Biological Processglucose homeostasis
Biological Processheart morphogenesis
Biological Processhindlimb morphogenesis
Biological Processin utero embryonic development
Biological Processkeratinocyte proliferation
Biological Processlimb morphogenesis
Biological Processliver regeneration
Biological Processmammary gland duct morphogenesis
Biological Processmammary gland epithelial cell differentiation
Biological Processmetanephric collecting duct development
Biological Processnegative regulation of cell division
Biological Processnegative regulation of DNA-binding transcription factor activity
Biological Processnegative regulation of keratinocyte proliferation
Biological Processnegative regulation of multicellular organism growth
Biological Processnegative regulation of osteoblast differentiation
Biological Processnegative regulation of smoothened signaling pathway
Biological Processnegative regulation of stem cell proliferation
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processneural plate axis specification
Biological Processneural tube closure
Biological Processneural tube patterning
Biological Processpharyngeal system development
Biological Processpositive regulation of cholesterol efflux
Biological Processpositive regulation of DNA-templated transcription
Biological Processpositive regulation of epidermal cell differentiation
Biological Processprostate gland development
Biological Processprotein localization to plasma membrane
Biological Processprotein processing
Biological Processregulation of mitotic cell cycle
Biological Processregulation of protein localization
Biological Processregulation of smoothened signaling pathway
Biological Processresponse to chlorate
Biological Processresponse to estradiol
Biological Processresponse to mechanical stimulus
Biological Processresponse to retinoic acid
Biological Processresponse to xenobiotic stimulus
Biological Processsmooth muscle tissue development
Biological Processsmoothened signaling pathway
Biological Processsomite development
Biological Processspermatid development
Biological Processspinal cord motor neuron differentiation
Biological Processstem cell proliferation

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 2.A.6.6.13the resistance-nodulation-cell division (rnd) superfamily

Names & Taxonomy

Protein names

  • Recommended name
    Protein patched homolog 1
  • Short names
    PTC; PTC1

Gene names

    • Name
      PTCH1
    • Synonyms
      PTCH

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q13635
  • Secondary accessions
    • A3KBI9
    • E9PEJ8
    • Q13463
    • Q5R1U7
    • Q5R1U9

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-100Cytoplasmic
Transmembrane101-121Helical
Topological domain122-436Extracellular
Transmembrane437-457Helical
Topological domain458-472Cytoplasmic
Transmembrane473-493Helical
Topological domain494-501Extracellular
Transmembrane502-522Helical
Topological domain523-547Cytoplasmic
Transmembrane548-568Helical
Topological domain569-577Extracellular
Transmembrane578-598Helical
Topological domain599-748Cytoplasmic
Transmembrane749-769Helical
Topological domain770-1027Extracellular
Transmembrane1028-1048Helical
Topological domain1049-1055Cytoplasmic
Transmembrane1056-1076Helical
Topological domain1077-1083Extracellular
Transmembrane1084-1104Helical
Topological domain1105-1121Cytoplasmic
Transmembrane1122-1141Helical
Topological domain1142-1154Extracellular
Transmembrane1155-1175Helical
Topological domain1176-1447Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Basal cell nevus syndrome 1 (BCNS1)

  • Note
    • The disease may be caused by variants affecting the gene represented in this entry
  • Description
    A form of basal cell nevus syndrome, a 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 fibromas of the ovaries and heart, cysts of the skin, jaws and mesentery, as well as medulloblastomas and meningiomas. BCNS1 inheritance is autosomal dominant.
  • See also
    MIM:109400
Natural variants in BCNS1
Variant IDPosition(s)ChangeDescription
VAR_007843175L>Pin BCNS1; dbSNP:rs2118541066
VAR_020845230T>Pin BCNS1; dbSNP:rs2118464571
VAR_007844376F>Sin BCNS1
VAR_020846505-506FL>LRin BCNS1
VAR_010974509G>Rin BCNS1; uncertain significance; dbSNP:rs2118285458
VAR_010975509G>Vin BCNS1; dbSNP:rs1060502268
VAR_010976513D>Yin BCNS1
VAR_007845815I>IPNIin BCNS1
VAR_010977816missingin BCNS1
VAR_0109791069G>Rin BCNS1; dbSNP:rs2136649648
VAR_0078461083V>VVin BCNS1
VAR_0078471114R>Win BCNS1 and BCC; dbSNP:rs587776689
VAR_0109801132S>Pin BCNS1; dbSNP:rs878853856
VAR_0109811132S>Yin BCNS1
VAR_0109841438E>Din BCNS1

Basal cell carcinoma (BCC)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. BCC is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter.
  • See also
    MIM:605462
Natural variants in BCC
Variant IDPosition(s)ChangeDescription
VAR_0078471114R>Win BCNS1 and BCC; dbSNP:rs587776689

Holoprosencephaly 7 (HPE7)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability.
  • See also
    MIM:610828
Natural variants in HPE7
Variant IDPosition(s)ChangeDescription
VAR_032952393A>Tin HPE7; dbSNP:rs199476091
VAR_032953443A>Gin HPE7; dbSNP:rs878853845
VAR_032954728T>Min HPE7; dbSNP:rs115556836
VAR_032955751V>Gin HPE7
VAR_032956827S>Gin HPE7; dbSNP:rs199476092
VAR_032957908V>Gin HPE7; dbSNP:rs199476093
VAR_0329581052T>Min HPE7; dbSNP:rs138911275

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_007843175in BCNS1; dbSNP:rs2118541066
Natural variantVAR_020845230in BCNS1; dbSNP:rs2118464571
Natural variantVAR_007844376in BCNS1
Natural variantVAR_032952393in HPE7; dbSNP:rs199476091
Natural variantVAR_032953443in HPE7; dbSNP:rs878853845
Natural variantVAR_020846505-506in BCNS1
Natural variantVAR_010974509in BCNS1; uncertain significance; dbSNP:rs2118285458
Natural variantVAR_010975509in BCNS1; dbSNP:rs1060502268
Natural variantVAR_010976513in BCNS1
Natural variantVAR_032954728in HPE7; dbSNP:rs115556836
Natural variantVAR_032955751in HPE7
Natural variantVAR_007845815in BCNS1
Natural variantVAR_010977816in BCNS1
Natural variantVAR_032956827in HPE7; dbSNP:rs199476092
Natural variantVAR_010978829in squamous cell carcinoma; dbSNP:rs201125580
Natural variantVAR_032957908in HPE7; dbSNP:rs199476093
Natural variantVAR_0329581052in HPE7; dbSNP:rs138911275
Natural variantVAR_0109791069in BCNS1; dbSNP:rs2136649648
Natural variantVAR_0078461083in BCNS1
Natural variantVAR_0078471114in BCNS1 and BCC; dbSNP:rs587776689
Natural variantVAR_0109801132in BCNS1; dbSNP:rs878853856
Natural variantVAR_0109811132in BCNS1
Natural variantVAR_0204401195in dbSNP:rs2236405
Natural variantVAR_0109821242in squamous cell carcinoma; dbSNP:rs779417284
Natural variantVAR_0208471282in dbSNP:rs2227968
Natural variantVAR_0109831315in dbSNP:rs357564
Natural variantVAR_0109841438in BCNS1

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 5,686 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00002059641-1447UniProtProtein patched homolog 1
Glycosylation141UniProtN-linked (GlcNAc...) asparagine
Glycosylation312UniProtN-linked (GlcNAc...) asparagine
Glycosylation349UniProtN-linked (GlcNAc...) asparagine
Glycosylation414UniProtN-linked (GlcNAc...) asparagine
Glycosylation875UniProtN-linked (GlcNAc...) asparagine
Glycosylation1000UniProtN-linked (GlcNAc...) asparagine
Modified residue1195UniProtPhosphothreonine
Modified residue (large scale data)1195PRIDEPhosphothreonine
Modified residue1197UniProtPhosphoserine
Modified residue (large scale data)1197PRIDEPhosphoserine
Cross-link1426UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modification

Glycosylation is necessary for SHH binding.
In the absence of Hh ligands, ubiquitination by ITCH at Lys-1426 promotes endocytosis and both proteasomal and lysosomal degradation.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In the adult, expressed in brain, lung, liver, heart, placenta, skeletal muscle, pancreas and kidney. Expressed in tumor cells but not in normal skin.

Developmental stage

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.

Gene expression databases

Organism-specific databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-43Disordered
Domain438-598SSD
Region1189-1234Disordered
Compositional bias1193-1207Pro residues
Compositional bias1214-1234Polar residues
Region1270-1360Disordered

Sequence similarities

Belongs to the patched family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (4)
  • Sequence status
    Complete

This entry describes 4 isoforms produced by Alternative splicing.

Q13635-1

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.

  • Name
    L
  • Synonyms
    1B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,447
  • Mass (Da)
    160,545
  • Last updated
    2007-10-23 v2
  • Checksum
    F2937247BC812F85
MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRRAAAPDRDYLHRPSYCDAAFALEQISKGKATGRKAPLWLRAKFQRLLFKLGCYIQKNCGKFLVVGLLIFGAFAVGLKAANLETNVEELWVEVGGRVSRELNYTRQKIGEEAMFNPQLMIQTPKEEGANVLTTEALLQHLDSALQASRVHVYMYNRQWKLEHLCYKSGELITETGYMDQIIEYLYPCLIITPLDCFWEGAKLQSGTAYLLGKPPLRWTNFDPLEFLEELKKINYQVDSWEEMLNKAEVGHGYMDRPCLNPADPDCPATAPNKNSTKPLDMALVLNGGCHGLSRKYMHWQEELIVGGTVKNSTGKLVSAHALQTMFQLMTPKQMYEHFKGYEYVSHINWNEDKAAAILEAWQRTYVEVVHQSVAQNSTQKVLSFTTTTLDDILKSFSDVSVIRVASGYLLMLAYACLTMLRWDCSKSQGAVGLAGVLLVALSVAAGLGLCSLIGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQNKRIPFEDRTGECLKRTGASVALTSISNVTAFFMAALIPIPALRAFSLQAAVVVVFNFAMVLLIFPAILSMDLYRREDRRLDIFCCFTSPCVSRVIQVEPQAYTDTHDNTRYSPPPPYSSHSFAHETQITMQSTVQLRTEYDPHTHVYYTTAEPRSEISVQPVTVTQDTLSCQSPESTSSTRDLLSQFSDSSLHCLEPPCTKWTLSSFAEKHYAPFLLKPKAKVVVIFLFLGLLGVSLYGTTRVRDGLDLTDIVPRETREYDFIAAQFKYFSFYNMYIVTQKADYPNIQHLLYDLHRSFSNVKYVMLEENKQLPKMWLHYFRDWLQGLQDAFDSDWETGKIMPNNYKNGSDDGVLAYKLLVQTGSRDKPIDISQLTKQRLVDADGIINPSAFYIYLTAWVSNDPVAYAASQANIRPHRPEWVHDKADYMPETRLRIPAAEPIEYAQFPFYLNGLRDTSDFVEAIEKVRTICSNYTSLGLSSYPNGYPFLFWEQYIGLRHWLLLFISVVLACTFLVCAVFLLNPWTAGIIVMVLALMTVELFGMMGLIGIKLSAVPVVILIASVGIGVEFTVHVALAFLTAIGDKNRRAVLALEHMFAPVLDGAVSTLLGVLMLAGSEFDFIVRYFFAVLAILTILGVLNGLVLLPVLLSFFGPYPEVSPANGLNRLPTPSPEPPPSVVRFAMPPGHTHSGSDSSDSEYSSQTTVSGLSEELRHYEAQQGAGGPAHQVIVEATENPVFAHSTVVHPESRHHPPSNPRQQPHLDSGSLPPGRQGQQPRRDPPREGLWPPPYRPRRDAFEISTEGHSGPSNRARWGPRGARSHNPRNPASTAMGSSVPGYCQPITTVTASASVTVAVHPPPVPGPGRNPRGGLCPGYPETDHGLFEDPHVPFHVRCERRDSKVEVIELQDVECEERPRGSSSN

Q13635-2

  • Name
    L'
  • Synonyms
    1Ckid
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-66: MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRRAAAPDRDYLHRPSYCDAAFALEQIS → MELLNRNRLVIVSPRCTPPKASGGPARRGFYTFRSFCKDGGGGEEEEENGGEEKDDRGDKETRSD

Q13635-3

  • Name
    M
  • Synonyms
    1C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q13635-4

  • Name
    S
  • Synonyms
    1A, 1CdeltaE2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0YHK0H0YHK0_HUMANPTCH116
F8VXL8F8VXL8_HUMANPTCH166
H3BLX7H3BLX7_HUMANPTCH1486
F8VQS6F8VQS6_HUMANPTCH192
F8VPA3F8VPA3_HUMANPTCH179
H0Y3B8H0Y3B8_HUMANPTCH1352
A0A8I5KPP5A0A8I5KPP5_HUMANPTCH1456
A0A0C4DGI4A0A0C4DGI4_HUMANPTCH1174
A0A0C4DGJ5A0A0C4DGJ5_HUMANPTCH1183

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0413691-66in isoform L'
Alternative sequenceVSP_0413712-67in isoform M
Alternative sequenceVSP_0413702-152in isoform S
Sequence conflict1109in Ref. 2; AAC50496
Sequence conflict1144in Ref. 2; AAC50496
Sequence conflict1175in Ref. 2; AAC50496
Compositional bias1193-1207Pro residues
Compositional bias1214-1234Polar residues
Sequence conflict1283in Ref. 2; AAC50496
Sequence conflict1309in Ref. 2; AAC50496
Sequence conflict1353in Ref. 2; AAC50496

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U59464
EMBL· GenBank· DDBJ
AAC50550.1
EMBL· GenBank· DDBJ
mRNA
U43148
EMBL· GenBank· DDBJ
AAC50496.1
EMBL· GenBank· DDBJ
mRNA
AL161729
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AB189436
EMBL· GenBank· DDBJ
BAD74184.1
EMBL· GenBank· DDBJ
mRNA
AB189437
EMBL· GenBank· DDBJ
BAD74185.1
EMBL· GenBank· DDBJ
mRNA
AB189438
EMBL· GenBank· DDBJ
BAD74186.1
EMBL· GenBank· DDBJ
mRNA
AB189439
EMBL· GenBank· DDBJ
BAD74187.1
EMBL· GenBank· DDBJ
mRNA
AB189440
EMBL· GenBank· DDBJ
BAD74188.1
EMBL· GenBank· DDBJ
mRNA
BC043542
EMBL· GenBank· DDBJ
AAH43542.1
EMBL· GenBank· DDBJ
mRNA
AB239329
EMBL· GenBank· DDBJ
BAF47712.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp