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Q9H237

- PORCN_HUMAN

UniProt

Q9H237 - PORCN_HUMAN

Protein

Protein-cysteine N-palmitoyltransferase porcupine

Gene

PORCN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    protein-cysteine N-palmitoyltransferase that modulates the processing of Wnt proteins by mediating serine palmitoylation of Wnt family members.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei341 – 3411Sequence Analysis

    GO - Molecular functioni

    1. transferase activity Source: UniProtKB-KW
    2. transferase activity, transferring acyl groups Source: UniProtKB-KW

    GO - Biological processi

    1. glycoprotein metabolic process Source: Ensembl
    2. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-cysteine N-palmitoyltransferase porcupine (EC:2.3.1.-)
    Alternative name(s):
    Protein MG61
    Gene namesi
    Name:PORCN
    Synonyms:MG61, PORC, PPN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17652. PORCN.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: Ensembl
    2. integral component of endoplasmic reticulum membrane Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Focal dermal hypoplasia (FODH) [MIM:305600]: A rare congenital ectomesodermal disorder characterized by a combination of skin defects, skeletal abnormalities, and ocular anomalies. Affected individuals have patchy dermal hypoplasia, often in a distribution pattern following the Blaschko lines, and areas of subcutaneous fat herniation or deposition of fat into the dermis. In addition, sparse and brittle hair, hypoplastic nails and papillomas have been described. Skeletal abnormalities usually comprise syndactyly, ectrodactyly, and brachydactyly, and in some cases osteopathia striata has been seen. Patients frequently have ocular anomalies, including microphthalmia/ anophthalmia, coloboma, pigmentary and vascularization defects of the retina. Dental abnormalities are often present.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601G → R in FODH. 1 Publication
    VAR_035089
    Natural varianti136 – 1361S → F in FODH. 1 Publication
    VAR_058899
    Natural varianti168 – 1681G → R in FODH. 2 Publications
    VAR_058900
    Natural varianti252 – 2521H → Y in FODH. 1 Publication
    VAR_065189
    Natural varianti258 – 2581V → E in FODH. 1 Publication
    VAR_058902
    Natural varianti297 – 2971S → L in FODH. 1 Publication
    VAR_065190
    Natural varianti331 – 3311L → R in FODH. 1 Publication
    VAR_065191
    Natural varianti341 – 3411H → L in FODH. 1 Publication
    VAR_058903
    Natural varianti361 – 3611E → V in FODH. 1 Publication
    VAR_065192
    Natural varianti365 – 3651R → G in FODH. 2 Publications
    VAR_035090
    Natural varianti365 – 3651R → Q in FODH. 5 Publications
    VAR_058904
    Natural varianti374 – 3741A → P in FODH. 1 Publication
    VAR_066061
    Natural varianti385 – 3851C → R in FODH. 1 Publication
    VAR_058905
    Natural varianti385 – 3851C → Y in FODH. 1 Publication
    VAR_065193
    Natural varianti439 – 4391W → R in FODH. 1 Publication
    VAR_058906

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi187 – 1871C → A: Drastic loss of palmitoylation. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi305600. phenotype.
    Orphaneti2092. Focal dermal hypoplasia.
    PharmGKBiPA134906089.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Protein-cysteine N-palmitoyltransferase porcupinePRO_0000213137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi187 – 1871S-palmitoyl cysteine1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiQ9H237.
    PaxDbiQ9H237.
    PRIDEiQ9H237.

    PTM databases

    PhosphoSiteiQ9H237.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in fetal brain, brain, amygdala, caudate nucleus, cerebellum, hippocampus, pituitary, thalamus, heart, skeletal muscle and testis. Isoform 4 is expressed in amygdala, corpus callosum, hippocampus, spinal cord, kidney, liver, lung, spleen, uterus, testis. Isoform 2 and isoform 3 are expressed in substantia negra, spinal cord, heart and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9H237.
    BgeeiQ9H237.
    CleanExiHS_PORCN.
    GenevestigatoriQ9H237.

    Organism-specific databases

    HPAiHPA049215.

    Interactioni

    Subunit structurei

    Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6, WNT7A and WNT7B.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000322304.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H237.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 6628ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini88 – 958CytoplasmicSequence Analysis
    Topological domaini117 – 15236ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini174 – 19825CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini220 – 25233ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini274 – 33764CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini359 – 39638ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini418 – 46144CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei67 – 8721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei96 – 11621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei153 – 17321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei199 – 21921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei253 – 27321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei338 – 35821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei397 – 41721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 8876Leu-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG325605.
    HOGENOMiHOG000231245.
    HOVERGENiHBG061243.
    InParanoidiQ9H237.
    KOiK00181.
    OMAiLYHFFQL.
    PhylomeDBiQ9H237.
    TreeFamiTF313724.

    Family and domain databases

    InterProiIPR004299. MBOAT_fam.
    [Graphical view]
    PfamiPF03062. MBOAT. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H237-1) [UniParc]FASTAAdd to Basket

    Also known as: D

    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.

    « Hide

    MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY    50
    LKHASTVAGG FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS 100
    VTILIYLLMG EMHMVDTVTW HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP 150
    SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV QGRPLSCRWL QKVARSLALA 200
    LLCLVLSTCV GPYLFPYFIP LNGDRLLRNK KRKARGTMVR WLRAYESAVS 250
    FHFSNYFVGF LSEATATLAG AGFTEEKDHL EWDLTVSKPL NVELPRSMVE 300
    VVTSWNLPMS YWLNNYVFKN ALRLGTFSAV LVTYAASALL HGFSFHLAAV 350
    LLSLAFITYV EHVLRKRLAR ILSACVLSKR CPPDCSHQHR LGLGVRALNL 400
    LFGALAIFHL AYLGSLFDVD VDDTTEEQGY GMAYTVHKWS ELSWASHWVT 450
    FGCWIFYRLI G 461
    Length:461
    Mass (Da):52,318
    Last modified:October 17, 2006 - v2
    Checksum:i000624825E507385
    GO
    Isoform 2 (identifier: Q9H237-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         235-239: Missing.

    Show »
    Length:456
    Mass (Da):51,773
    Checksum:iBF22FF1836BC9397
    GO
    Isoform 3 (identifier: Q9H237-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         229-235: NKKRKAR → K

    Show »
    Length:455
    Mass (Da):51,564
    Checksum:i21532BA9B4D19F4A
    GO
    Isoform 4 (identifier: Q9H237-4) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         229-240: NKKRKARGTMVR → K

    Show »
    Length:450
    Mass (Da):51,019
    Checksum:i7ECE3021794835EB
    GO
    Isoform 5 (identifier: Q9H237-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: Missing.
         229-240: NKKRKARGTMVR → K

    Note: No experimental confirmation available.

    Show »
    Length:379
    Mass (Da):42,878
    Checksum:i562081CACFEDA645
    GO

    Sequence cautioni

    The sequence AAA74510.1 differs from that shown. Reason: The sequence differs from that shown upstream of position 63 for unknown reasons.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421L → P in AAG39631. (PubMed:12034504)Curated
    Sequence conflicti179 – 1791A → T in AAG39628. (PubMed:12034504)Curated
    Sequence conflicti179 – 1791A → T in AAG39630. (PubMed:12034504)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601G → R in FODH. 1 Publication
    VAR_035089
    Natural varianti136 – 1361S → F in FODH. 1 Publication
    VAR_058899
    Natural varianti168 – 1681G → R in FODH. 2 Publications
    VAR_058900
    Natural varianti228 – 2281R → C in a patient with focal dermal hypoplasia also carrying a frameshift mutation; uncertain pathological significance. 1 Publication
    VAR_058901
    Natural varianti252 – 2521H → Y in FODH. 1 Publication
    VAR_065189
    Natural varianti258 – 2581V → E in FODH. 1 Publication
    VAR_058902
    Natural varianti297 – 2971S → L in FODH. 1 Publication
    VAR_065190
    Natural varianti331 – 3311L → R in FODH. 1 Publication
    VAR_065191
    Natural varianti341 – 3411H → L in FODH. 1 Publication
    VAR_058903
    Natural varianti361 – 3611E → V in FODH. 1 Publication
    VAR_065192
    Natural varianti365 – 3651R → G in FODH. 2 Publications
    VAR_035090
    Natural varianti365 – 3651R → Q in FODH. 5 Publications
    VAR_058904
    Natural varianti374 – 3741A → P in FODH. 1 Publication
    VAR_066061
    Natural varianti385 – 3851C → R in FODH. 1 Publication
    VAR_058905
    Natural varianti385 – 3851C → Y in FODH. 1 Publication
    VAR_065193
    Natural varianti439 – 4391W → R in FODH. 1 Publication
    VAR_058906

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7171Missing in isoform 5. 1 PublicationVSP_055419Add
    BLAST
    Alternative sequencei229 – 24012NKKRK…GTMVR → K in isoform 4 and isoform 5. 2 PublicationsVSP_015886Add
    BLAST
    Alternative sequencei229 – 2357NKKRKAR → K in isoform 3. 1 PublicationVSP_015887
    Alternative sequencei235 – 2395Missing in isoform 2. 2 PublicationsVSP_015888

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317058 mRNA. Translation: AAG39628.1.
    AF317059 mRNA. Translation: AAG39629.1.
    AF317060 mRNA. Translation: AAG39630.1.
    AF317061 mRNA. Translation: AAG39631.1.
    AK314745 mRNA. Translation: BAG37285.1.
    AK316378 mRNA. Translation: BAH14749.1.
    AF196972 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50780.1.
    BC019080 mRNA. Translation: AAH19080.1.
    L08239 mRNA. Translation: AAA74510.1. Sequence problems.
    CCDSiCCDS14296.1. [Q9H237-4]
    CCDS14297.1. [Q9H237-2]
    CCDS14298.1. [Q9H237-3]
    CCDS14299.1. [Q9H237-1]
    RefSeqiNP_001269096.1. NM_001282167.1.
    NP_073736.2. NM_022825.3. [Q9H237-4]
    NP_982299.1. NM_203473.2. [Q9H237-2]
    NP_982300.1. NM_203474.1. [Q9H237-3]
    NP_982301.1. NM_203475.2. [Q9H237-1]
    XP_006724609.1. XM_006724546.1. [Q9H237-1]
    UniGeneiHs.386453.

    Genome annotation databases

    EnsembliENST00000326194; ENSP00000322304; ENSG00000102312. [Q9H237-1]
    ENST00000355092; ENSP00000347207; ENSG00000102312. [Q9H237-3]
    ENST00000355961; ENSP00000348233; ENSG00000102312. [Q9H237-2]
    ENST00000359882; ENSP00000352946; ENSG00000102312. [Q9H237-3]
    ENST00000361988; ENSP00000354978; ENSG00000102312. [Q9H237-4]
    ENST00000367574; ENSP00000356546; ENSG00000102312. [Q9H237-5]
    ENST00000537758; ENSP00000446401; ENSG00000102312. [Q9H237-1]
    GeneIDi64840.
    KEGGihsa:64840.
    UCSCiuc004djr.1. human. [Q9H237-2]
    uc004djs.1. human. [Q9H237-4]
    uc004djv.1. human. [Q9H237-1]
    uc004djw.1. human. [Q9H237-3]

    Polymorphism databases

    DMDMi116242723.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Leiden Open Variation Database

    Porcupine homolog (Drosophila) (PORCN)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF317058 mRNA. Translation: AAG39628.1 .
    AF317059 mRNA. Translation: AAG39629.1 .
    AF317060 mRNA. Translation: AAG39630.1 .
    AF317061 mRNA. Translation: AAG39631.1 .
    AK314745 mRNA. Translation: BAG37285.1 .
    AK316378 mRNA. Translation: BAH14749.1 .
    AF196972 Genomic DNA. No translation available.
    CH471224 Genomic DNA. Translation: EAW50780.1 .
    BC019080 mRNA. Translation: AAH19080.1 .
    L08239 mRNA. Translation: AAA74510.1 . Sequence problems.
    CCDSi CCDS14296.1. [Q9H237-4 ]
    CCDS14297.1. [Q9H237-2 ]
    CCDS14298.1. [Q9H237-3 ]
    CCDS14299.1. [Q9H237-1 ]
    RefSeqi NP_001269096.1. NM_001282167.1.
    NP_073736.2. NM_022825.3. [Q9H237-4 ]
    NP_982299.1. NM_203473.2. [Q9H237-2 ]
    NP_982300.1. NM_203474.1. [Q9H237-3 ]
    NP_982301.1. NM_203475.2. [Q9H237-1 ]
    XP_006724609.1. XM_006724546.1. [Q9H237-1 ]
    UniGenei Hs.386453.

    3D structure databases

    ProteinModelPortali Q9H237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000322304.

    Chemistry

    ChEMBLi CHEMBL1255163.

    PTM databases

    PhosphoSitei Q9H237.

    Polymorphism databases

    DMDMi 116242723.

    Proteomic databases

    MaxQBi Q9H237.
    PaxDbi Q9H237.
    PRIDEi Q9H237.

    Protocols and materials databases

    DNASUi 64840.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326194 ; ENSP00000322304 ; ENSG00000102312 . [Q9H237-1 ]
    ENST00000355092 ; ENSP00000347207 ; ENSG00000102312 . [Q9H237-3 ]
    ENST00000355961 ; ENSP00000348233 ; ENSG00000102312 . [Q9H237-2 ]
    ENST00000359882 ; ENSP00000352946 ; ENSG00000102312 . [Q9H237-3 ]
    ENST00000361988 ; ENSP00000354978 ; ENSG00000102312 . [Q9H237-4 ]
    ENST00000367574 ; ENSP00000356546 ; ENSG00000102312 . [Q9H237-5 ]
    ENST00000537758 ; ENSP00000446401 ; ENSG00000102312 . [Q9H237-1 ]
    GeneIDi 64840.
    KEGGi hsa:64840.
    UCSCi uc004djr.1. human. [Q9H237-2 ]
    uc004djs.1. human. [Q9H237-4 ]
    uc004djv.1. human. [Q9H237-1 ]
    uc004djw.1. human. [Q9H237-3 ]

    Organism-specific databases

    CTDi 64840.
    GeneCardsi GC0XP048367.
    GeneReviewsi PORCN.
    HGNCi HGNC:17652. PORCN.
    HPAi HPA049215.
    MIMi 300651. gene.
    305600. phenotype.
    neXtProti NX_Q9H237.
    Orphaneti 2092. Focal dermal hypoplasia.
    PharmGKBi PA134906089.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325605.
    HOGENOMi HOG000231245.
    HOVERGENi HBG061243.
    InParanoidi Q9H237.
    KOi K00181.
    OMAi LYHFFQL.
    PhylomeDBi Q9H237.
    TreeFami TF313724.

    Enzyme and pathway databases

    Reactomei REACT_163710. WNT ligand biogenesis and trafficking.

    Miscellaneous databases

    ChiTaRSi PORCN. human.
    GenomeRNAii 64840.
    NextBioi 66934.
    PROi Q9H237.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H237.
    Bgeei Q9H237.
    CleanExi HS_PORCN.
    Genevestigatori Q9H237.

    Family and domain databases

    InterProi IPR004299. MBOAT_fam.
    [Graphical view ]
    Pfami PF03062. MBOAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and initial characterization of the MG61/PORC gene, the human homologue of the Drosophila segment polarity gene Porcupine."
      Caricasole A., Ferraro T., Rimland J.M., Terstappen G.C.
      Gene 288:147-157(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT PROTEINS PROCESSING, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
      Tissue: Hippocampus.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Kidney.
    6. Geraghty M.T.
      Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-461 (ISOFORM 1).
      Tissue: Retina.
    7. Cited for: INVOLVEMENT IN FODH.
    8. Cited for: FUNCTION.
    9. "Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine."
      Gao X., Hannoush R.N.
      Nat. Chem. Biol. 10:61-68(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PALMITOYLATION AT CYS-187, MUTAGENESIS OF CYS-187.
    10. "Mutations in X-linked PORCN, a putative regulator of Wnt signaling, cause focal dermal hypoplasia."
      Wang X., Reid Sutton V., Omar Peraza-Llanes J., Yu Z., Rosetta R., Kou Y.-C., Eble T.N., Patel A., Thaller C., Fang P., Van den Veyver I.B.
      Nat. Genet. 39:836-838(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FODH ARG-60 AND GLY-365.
    11. "Three novel mutations in the PORCN gene underlying focal dermal hypoplasia."
      Leoyklang P., Suphapeetiporn K., Wananukul S., Shotelersuk V.
      Clin. Genet. 73:373-379(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FODH GLN-365, VARIANT CYS-228.
    12. Cited for: VARIANTS FODH ARG-331 AND GLN-365.
    13. "Goltz-Gorlin (focal dermal hypoplasia) and the microphthalmia with linear skin defects (MLS) syndrome: no evidence of genetic overlap."
      Harmsen M.B., Azzarello-Burri S., Garcia Gonzalez M.M., Gillessen-Kaesbach G., Meinecke P., Muller D., Rauch A., Rossier E., Seemanova E., Spaich C., Steiner B., Wieczorek D., Zenker M., Kutsche K.
      Eur. J. Hum. Genet. 17:1207-1215(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FODH VAL-361 AND TYR-385.
    14. Cited for: VARIANTS FODH PHE-136; ARG-168; GLU-258; LEU-341; GLN-365; GLY-365; ARG-385 AND ARG-439.
    15. Cited for: VARIANTS FODH ARG-168; LEU-297; GLN-365 AND PRO-374.
    16. Cited for: VARIANTS FODH TYR-252 AND GLN-365.

    Entry informationi

    Entry nameiPORCN_HUMAN
    AccessioniPrimary (citable) accession number: Q9H237
    Secondary accession number(s): B2RBN8
    , B7ZAR3, Q14829, Q9H234, Q9H235, Q9H236, Q9UJU7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3