Full text data of SNAP29
SNAP29
[Confidence: low (only semi-automatic identification from reviews)]
Synaptosomal-associated protein 29; SNAP-29 (Soluble 29 kDa NSF attachment protein; Vesicle-membrane fusion protein SNAP-29)
Synaptosomal-associated protein 29; SNAP-29 (Soluble 29 kDa NSF attachment protein; Vesicle-membrane fusion protein SNAP-29)
UniProt
O95721
ID SNP29_HUMAN Reviewed; 258 AA.
AC O95721;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Synaptosomal-associated protein 29;
DE Short=SNAP-29;
DE AltName: Full=Soluble 29 kDa NSF attachment protein;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=SNAP29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
RA Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA Scheller R.H.;
RT "Three novel proteins of the syntaxin/SNAP-25 family.";
RL J. Biol. Chem. 273:34171-34179(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schardt A., Kraemer E.-M., Werner H., Nave K.-A.;
RT "Genomic organization of the human SNAP29 gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN CEDNIK.
RX PubMed=15968592; DOI=10.1086/432556;
RA Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D.,
RA Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H.,
RA O'brien T.J., Bercovich D., Shalev S., Geiger D., Bergman R.,
RA Horowitz M., Mandel H.;
RT "A mutation in SNAP29, coding for a SNARE protein involved in
RT intracellular trafficking, causes a novel neurocutaneous syndrome
RT characterized by cerebral dysgenesis, neuropathy, ichthyosis, and
RT palmoplantar keratoderma.";
RL Am. J. Hum. Genet. 77:242-251(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH VAMP8 AND STX17.
RX PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA Itakura E., Kishi-Itakura C., Mizushima N.;
RT "The hairpin-type tail-anchored SNARE syntaxin 17 targets to
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: SNAREs, Soluble N-ethylmaleimide-sensitive factor-
CC attachment protein receptors, are essential proteins for fusion of
CC cellular membranes. SNAREs localized on opposing membranes
CC assemble to form a trans-SNARE complex, an extended, parallel four
CC alpha-helical bundle that drives membrane fusion. SNAP29 is a
CC SNARE involved in autophagy through the direct control of
CC autophagosome membrane fusion with the lysososome membrane.
CC Probably involved in multiple membrane trafficking steps.
CC -!- SUBUNIT: Interacts with multiple syntaxins including STX6 (By
CC similarity). Forms a SNARE complex, composed of VAMP8, SNAP29 and
CC STX17, involved in fusion of autophagosome with lysosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Cell junction, synapse, synaptosome. Note=Appears to be
CC mostly membrane-bound, probably via interaction with syntaxins,
CC but a significant portion is cytoplasmic.
CC -!- TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung,
CC placenta, skeletal muscle, spleen and pancreas.
CC -!- DISEASE: Cerebral dysgenesis, neuropathy, ichthyosis, and
CC palmoplantar keratoderma syndrome (CEDNIK) [MIM:609528]: A
CC neurocutaneous syndrome characterized by cerebral dysgenesis,
CC neuropathy, ichthyosis and palmoplantar keratoderma. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF115436; AAD11436.1; -; mRNA.
DR EMBL; AF278704; AAF91421.1; -; Genomic_DNA.
DR EMBL; CR456582; CAG30468.1; -; mRNA.
DR EMBL; BT007357; AAP36021.1; -; mRNA.
DR EMBL; BC009715; AAH09715.1; -; mRNA.
DR RefSeq; NP_004773.1; NM_004782.3.
DR UniGene; Hs.108002; -.
DR ProteinModelPortal; O95721; -.
DR SMR; O95721; 54-110, 203-255.
DR DIP; DIP-56475N; -.
DR IntAct; O95721; 13.
DR MINT; MINT-3003155; -.
DR STRING; 9606.ENSP00000215730; -.
DR PhosphoSite; O95721; -.
DR PaxDb; O95721; -.
DR PeptideAtlas; O95721; -.
DR PRIDE; O95721; -.
DR DNASU; 9342; -.
DR Ensembl; ENST00000215730; ENSP00000215730; ENSG00000099940.
DR GeneID; 9342; -.
DR KEGG; hsa:9342; -.
DR UCSC; uc011ahw.2; human.
DR CTD; 9342; -.
DR GeneCards; GC22P021213; -.
DR HGNC; HGNC:11133; SNAP29.
DR HPA; HPA031823; -.
DR MIM; 604202; gene.
DR MIM; 609528; phenotype.
DR neXtProt; NX_O95721; -.
DR Orphanet; 66631; CEDNIK syndrome.
DR PharmGKB; PA35981; -.
DR eggNOG; NOG244202; -.
DR HOGENOM; HOG000046806; -.
DR HOVERGEN; HBG057045; -.
DR InParanoid; O95721; -.
DR KO; K08509; -.
DR OMA; AYPRSYN; -.
DR OrthoDB; EOG7FNC8G; -.
DR PhylomeDB; O95721; -.
DR GeneWiki; SNAP29; -.
DR GenomeRNAi; 9342; -.
DR NextBio; 34991; -.
DR PRO; PR:O95721; -.
DR ArrayExpress; O95721; -.
DR Bgee; O95721; -.
DR CleanEx; HS_SNAP29; -.
DR Genevestigator; O95721; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0005484; F:SNAP receptor activity; TAS:ProtInc.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR000928; SNAP-25.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cell junction; Coiled coil; Complete proteome; Cytoplasm;
KW Ichthyosis; Membrane; Palmoplantar keratoderma; Protein transport;
KW Reference proteome; Synapse; Synaptosome; Transport.
FT CHAIN 1 258 Synaptosomal-associated protein 29.
FT /FTId=PRO_0000213601.
FT DOMAIN 196 258 t-SNARE coiled-coil homology.
FT COILED 76 107 Potential.
SQ SEQUENCE 258 AA; 28970 MW; 7E1CDBA22D6F5A3C CRC64;
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
NYFKSKPVET PPEQNGTLTS QPNNRLKEAI STSKEQEAKY QASHPNLRKL DDTDPVPRGA
GSAMSTDAYP KNPHLRAYHQ KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
VDKLDVNIKS TERKVRQL
//
ID SNP29_HUMAN Reviewed; 258 AA.
AC O95721;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Synaptosomal-associated protein 29;
DE Short=SNAP-29;
DE AltName: Full=Soluble 29 kDa NSF attachment protein;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=SNAP29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
RA Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA Scheller R.H.;
RT "Three novel proteins of the syntaxin/SNAP-25 family.";
RL J. Biol. Chem. 273:34171-34179(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schardt A., Kraemer E.-M., Werner H., Nave K.-A.;
RT "Genomic organization of the human SNAP29 gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN CEDNIK.
RX PubMed=15968592; DOI=10.1086/432556;
RA Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D.,
RA Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H.,
RA O'brien T.J., Bercovich D., Shalev S., Geiger D., Bergman R.,
RA Horowitz M., Mandel H.;
RT "A mutation in SNAP29, coding for a SNARE protein involved in
RT intracellular trafficking, causes a novel neurocutaneous syndrome
RT characterized by cerebral dysgenesis, neuropathy, ichthyosis, and
RT palmoplantar keratoderma.";
RL Am. J. Hum. Genet. 77:242-251(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH VAMP8 AND STX17.
RX PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA Itakura E., Kishi-Itakura C., Mizushima N.;
RT "The hairpin-type tail-anchored SNARE syntaxin 17 targets to
RT autophagosomes for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
CC -!- FUNCTION: SNAREs, Soluble N-ethylmaleimide-sensitive factor-
CC attachment protein receptors, are essential proteins for fusion of
CC cellular membranes. SNAREs localized on opposing membranes
CC assemble to form a trans-SNARE complex, an extended, parallel four
CC alpha-helical bundle that drives membrane fusion. SNAP29 is a
CC SNARE involved in autophagy through the direct control of
CC autophagosome membrane fusion with the lysososome membrane.
CC Probably involved in multiple membrane trafficking steps.
CC -!- SUBUNIT: Interacts with multiple syntaxins including STX6 (By
CC similarity). Forms a SNARE complex, composed of VAMP8, SNAP29 and
CC STX17, involved in fusion of autophagosome with lysosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Cell junction, synapse, synaptosome. Note=Appears to be
CC mostly membrane-bound, probably via interaction with syntaxins,
CC but a significant portion is cytoplasmic.
CC -!- TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung,
CC placenta, skeletal muscle, spleen and pancreas.
CC -!- DISEASE: Cerebral dysgenesis, neuropathy, ichthyosis, and
CC palmoplantar keratoderma syndrome (CEDNIK) [MIM:609528]: A
CC neurocutaneous syndrome characterized by cerebral dysgenesis,
CC neuropathy, ichthyosis and palmoplantar keratoderma. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF115436; AAD11436.1; -; mRNA.
DR EMBL; AF278704; AAF91421.1; -; Genomic_DNA.
DR EMBL; CR456582; CAG30468.1; -; mRNA.
DR EMBL; BT007357; AAP36021.1; -; mRNA.
DR EMBL; BC009715; AAH09715.1; -; mRNA.
DR RefSeq; NP_004773.1; NM_004782.3.
DR UniGene; Hs.108002; -.
DR ProteinModelPortal; O95721; -.
DR SMR; O95721; 54-110, 203-255.
DR DIP; DIP-56475N; -.
DR IntAct; O95721; 13.
DR MINT; MINT-3003155; -.
DR STRING; 9606.ENSP00000215730; -.
DR PhosphoSite; O95721; -.
DR PaxDb; O95721; -.
DR PeptideAtlas; O95721; -.
DR PRIDE; O95721; -.
DR DNASU; 9342; -.
DR Ensembl; ENST00000215730; ENSP00000215730; ENSG00000099940.
DR GeneID; 9342; -.
DR KEGG; hsa:9342; -.
DR UCSC; uc011ahw.2; human.
DR CTD; 9342; -.
DR GeneCards; GC22P021213; -.
DR HGNC; HGNC:11133; SNAP29.
DR HPA; HPA031823; -.
DR MIM; 604202; gene.
DR MIM; 609528; phenotype.
DR neXtProt; NX_O95721; -.
DR Orphanet; 66631; CEDNIK syndrome.
DR PharmGKB; PA35981; -.
DR eggNOG; NOG244202; -.
DR HOGENOM; HOG000046806; -.
DR HOVERGEN; HBG057045; -.
DR InParanoid; O95721; -.
DR KO; K08509; -.
DR OMA; AYPRSYN; -.
DR OrthoDB; EOG7FNC8G; -.
DR PhylomeDB; O95721; -.
DR GeneWiki; SNAP29; -.
DR GenomeRNAi; 9342; -.
DR NextBio; 34991; -.
DR PRO; PR:O95721; -.
DR ArrayExpress; O95721; -.
DR Bgee; O95721; -.
DR CleanEx; HS_SNAP29; -.
DR Genevestigator; O95721; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0005484; F:SNAP receptor activity; TAS:ProtInc.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR000928; SNAP-25.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cell junction; Coiled coil; Complete proteome; Cytoplasm;
KW Ichthyosis; Membrane; Palmoplantar keratoderma; Protein transport;
KW Reference proteome; Synapse; Synaptosome; Transport.
FT CHAIN 1 258 Synaptosomal-associated protein 29.
FT /FTId=PRO_0000213601.
FT DOMAIN 196 258 t-SNARE coiled-coil homology.
FT COILED 76 107 Potential.
SQ SEQUENCE 258 AA; 28970 MW; 7E1CDBA22D6F5A3C CRC64;
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
NYFKSKPVET PPEQNGTLTS QPNNRLKEAI STSKEQEAKY QASHPNLRKL DDTDPVPRGA
GSAMSTDAYP KNPHLRAYHQ KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
VDKLDVNIKS TERKVRQL
//
MIM
604202
*RECORD*
*FIELD* NO
604202
*FIELD* TI
*604202 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 29-KD; SNAP29
*FIELD* TX
DESCRIPTION
Intracellular membrane traffic appears to be regulated in part by
read moreSNAREs, SNAP (soluble N-ethylmaleimide-sensitive factor-attachment
protein; see SNAP-alpha, 603215) receptors, through the formation of
complexes between SNAREs on vesicle and target membranes. In the nerve
terminal, the core fusion complex is a parallel bundle of 4 helices
formed from the coiled-coil domains of 3 proteins. Two helices are
contributed by the SNAP25 (600322) plasma membrane protein, and 1 helix
each comes from a vesicle SNARE, or VAMP, and a target membrane SNARE,
or syntaxin. Dissociation of the core complex is mediated by recruitment
of the NSF (601633) ATPase chaperone and SNAP-alpha to the complex,
followed by ATP hydrolysis, thereby allowing the components to recycle
for another round of membrane fusion (summary by Steegmaier et al.,
1998).
CLONING
By carrying out a yeast 2-hybrid screen with syntaxin-3 (600876) as
bait, Steegmaier et al. (1998) isolated a partial cDNA encoding a
protein with homology to SNAP25 and SNAP23 (602534). They used the
partial cDNA to screen a brain library and recovered a cDNA
corresponding to the complete coding sequence of the gene, which they
called SNAP29 based on the predicted molecular weight of the encoded
product. The deduced 258-amino acid SNAP29 protein is 17% identical to
SNAP25 and SNAP23. Like SNAP23 and SNAP25, SNAP29 contains 2 predicted
coiled-coil regions that can participate in the formation of the core
complex. However, SNAP29 lacks the palmitoylated membrane-attachment
domain found in the other 2 proteins and has a distinct localization
pattern. Immunofluorescence studies of epitope-tagged SNAP29 indicated
that it localized predominantly to intracellular membrane structures,
whereas SNAP25 and SNAP23 are primarily localized to the plasma
membrane. Northern blot analysis revealed that SNAP29 is expressed
ubiquitously as a major 1.4-kb mRNA and 3 less abundant transcripts.
MAPPING
Gross (2013) mapped the SNAP29 gene to chromosome 22q11.21 based on an
alignment of the SNAP29 sequence (GenBank GENBANK AF115436) with the
genomic sequence (GRCh37).
GENE FUNCTION
Steegmaier et al. (1998) found that in vitro SNAP29 bound to a broader
range of syntaxin fusion proteins than did SNAP25 or SNAP23. Steegmaier
et al. (1998) proposed that SNAP29 is bound to membrane structures via
its interaction with multiple syntaxins, and that it is capable of
participating in various intracellular transport steps, interacting with
different syntaxins and VAMPs specifically localized to distinct
membrane compartments.
Through several in vitro and in vivo binding assays, Hohenstein and
Roche (2001) confirmed that SNAP29 binds to plasma membrane syntaxins as
well as to syntaxins present on many different internal membranes. By
coimmunoprecipitation studies, they also found that the association
between syntaxin-6 and SNAP29 is enhanced in cells coexpressing VAMP.
Rotem-Yehudar et al. (2001) found evidence for a role of SNAP29 in the
endocytosis of IGF1 receptors (IGF1R; 147370). They found that EHD1
(605888) and SNAP29 interact directly with each other and are present in
complexes with IGF1R. Following IGF1 induction, EHD1 and IGF1R
colocalize intracellularly. Immunoprecipitation of rat tissues also
suggested interaction of SNAP29 with AP2A1 (601026).
MOLECULAR GENETICS
In affected patients with CEDNIK syndrome (609528), Sprecher et al.
(2005) identified a homozygous mutation in the SNAP29 gene
(604202.0001).
In a Pakistani brother and sister with CEDNIK syndrome, Fuchs-Telem et
al. (2011) identified homozygosity for a 1-bp insertion in the SNAP29
gene (604202.0002).
*FIELD* AV
.0001
CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
SNAP29, 1-BP DEL, 220G
In affected patients with CEDNIK syndrome (609528), Sprecher et al.
(2005) identified a 1-bp deletion (220delG) in the SNAP29 gene,
resulting in premature termination of the protein. The mutation was not
identified in 200 control chromosomes. RT-PCR showed significantly
reduced SNAP29 expression in the skin of affected individuals. Sprecher
et al. (2005) concluded that SNAP29 is essential for proper vesicle
trafficking in neuroectodermal differentiation.
.0002
CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
SNAP29, 1-BP INS, 486A
In a Pakistani brother and sister with CEDNIK syndrome (609528),
Fuchs-Telem et al. (2011) identified homozygosity for a 1-bp insertion
(c.486insA) in the SNAP29 gene, causing a frameshift predicted to result
in premature termination. The mutation was not found in 200 control
chromosomes; DNA from other family members was not available. Premature
termination was confirmed by Western blot analysis, and transfection
studies in HeLa cells demonstrated complete loss of the wildtype
distribution pattern with the mutant construct. In addition, histologic
features typical for CEDNIK syndrome were replicated in 3-dimensional
primary human keratinocyte organotypic cell cultures downregulated for
SNAP29.
*FIELD* RF
1. Fuchs-Telem, D.; Stewart, H.; Rapaport, D.; Nousbeck, J.; Gat,
A.; Gini, M.; Lugassy, Y.; Emmert, S.; Eckl, K.; Hennies, H. C.; Sarig,
O.; Goldsher, D.; Meilik, B.; Ishida-Yamamoto, A. I.; Horowitz, M.;
Sprecher, E.: CEDNIK syndrome results from loss-of-function mutations
in SNAP29. Brit. J. Derm. 164: 610-616, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/9/2013.
3. Hohenstein, A. C.; Roche, P. A.: SNAP-29 is a promiscuous syntaxin-binding
SNARE. Biochem. Biophys. Res. Commun. 285: 167-171, 2001.
4. Rotem-Yehudar, R.; Galperin, E.; Horowitz, M.: Association of
insulin-like growth factor 1 receptor with EHD1 and SNAP29. J. Biol.
Chem. 276: 33054-33060, 2001.
5. Sprecher, E.; Ishida-Yamamoto, A.; Mizrahi-Koren, M.; Rapaport,
D.; Goldsher, D.; Indelman, M.; Topaz, O.; Chefetz, I.; Keren, H.;
O'Brien, T. J.; Bercovich, D.; Shalev, S.; Geiger, D.; Bergman, R.;
Horowitz, M.; Mandel, H.: A mutation in SNAP29, coding for a SNARE
protein involved in intracellular trafficking, causes a novel neurocutaneous
syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis,
and palmoplantar keratoderma. Am. J. Hum. Genet. 77: 242-251, 2005.
6. Steegmaier, M.; Yang, B.; Yoo, J.-S.; Huang, B.; Shen, M.; Yu,
S.; Luo, Y.; Scheller, R. H.: Three novel proteins of the syntaxin/SNAP-25
family. J. Biol. Chem. 273: 34171-34179, 1998.
*FIELD* CN
Matthew B. Gross - updated: 5/9/2013
Marla J. F. O'Neill - updated: 5/8/2013
Cassandra L. Kniffin - updated: 8/9/2005
Patricia A. Hartz - updated: 4/29/2002
*FIELD* CD
Rebekah S. Rasooly: 9/29/1999
*FIELD* ED
carol: 09/26/2013
carol: 6/21/2013
mgross: 5/9/2013
carol: 5/8/2013
carol: 10/6/2010
wwang: 8/30/2005
wwang: 8/12/2005
ckniffin: 8/9/2005
carol: 4/30/2002
terry: 4/29/2002
carol: 5/18/2000
alopez: 9/29/1999
*RECORD*
*FIELD* NO
604202
*FIELD* TI
*604202 SYNAPTOSOMAL-ASSOCIATED PROTEIN, 29-KD; SNAP29
*FIELD* TX
DESCRIPTION
Intracellular membrane traffic appears to be regulated in part by
read moreSNAREs, SNAP (soluble N-ethylmaleimide-sensitive factor-attachment
protein; see SNAP-alpha, 603215) receptors, through the formation of
complexes between SNAREs on vesicle and target membranes. In the nerve
terminal, the core fusion complex is a parallel bundle of 4 helices
formed from the coiled-coil domains of 3 proteins. Two helices are
contributed by the SNAP25 (600322) plasma membrane protein, and 1 helix
each comes from a vesicle SNARE, or VAMP, and a target membrane SNARE,
or syntaxin. Dissociation of the core complex is mediated by recruitment
of the NSF (601633) ATPase chaperone and SNAP-alpha to the complex,
followed by ATP hydrolysis, thereby allowing the components to recycle
for another round of membrane fusion (summary by Steegmaier et al.,
1998).
CLONING
By carrying out a yeast 2-hybrid screen with syntaxin-3 (600876) as
bait, Steegmaier et al. (1998) isolated a partial cDNA encoding a
protein with homology to SNAP25 and SNAP23 (602534). They used the
partial cDNA to screen a brain library and recovered a cDNA
corresponding to the complete coding sequence of the gene, which they
called SNAP29 based on the predicted molecular weight of the encoded
product. The deduced 258-amino acid SNAP29 protein is 17% identical to
SNAP25 and SNAP23. Like SNAP23 and SNAP25, SNAP29 contains 2 predicted
coiled-coil regions that can participate in the formation of the core
complex. However, SNAP29 lacks the palmitoylated membrane-attachment
domain found in the other 2 proteins and has a distinct localization
pattern. Immunofluorescence studies of epitope-tagged SNAP29 indicated
that it localized predominantly to intracellular membrane structures,
whereas SNAP25 and SNAP23 are primarily localized to the plasma
membrane. Northern blot analysis revealed that SNAP29 is expressed
ubiquitously as a major 1.4-kb mRNA and 3 less abundant transcripts.
MAPPING
Gross (2013) mapped the SNAP29 gene to chromosome 22q11.21 based on an
alignment of the SNAP29 sequence (GenBank GENBANK AF115436) with the
genomic sequence (GRCh37).
GENE FUNCTION
Steegmaier et al. (1998) found that in vitro SNAP29 bound to a broader
range of syntaxin fusion proteins than did SNAP25 or SNAP23. Steegmaier
et al. (1998) proposed that SNAP29 is bound to membrane structures via
its interaction with multiple syntaxins, and that it is capable of
participating in various intracellular transport steps, interacting with
different syntaxins and VAMPs specifically localized to distinct
membrane compartments.
Through several in vitro and in vivo binding assays, Hohenstein and
Roche (2001) confirmed that SNAP29 binds to plasma membrane syntaxins as
well as to syntaxins present on many different internal membranes. By
coimmunoprecipitation studies, they also found that the association
between syntaxin-6 and SNAP29 is enhanced in cells coexpressing VAMP.
Rotem-Yehudar et al. (2001) found evidence for a role of SNAP29 in the
endocytosis of IGF1 receptors (IGF1R; 147370). They found that EHD1
(605888) and SNAP29 interact directly with each other and are present in
complexes with IGF1R. Following IGF1 induction, EHD1 and IGF1R
colocalize intracellularly. Immunoprecipitation of rat tissues also
suggested interaction of SNAP29 with AP2A1 (601026).
MOLECULAR GENETICS
In affected patients with CEDNIK syndrome (609528), Sprecher et al.
(2005) identified a homozygous mutation in the SNAP29 gene
(604202.0001).
In a Pakistani brother and sister with CEDNIK syndrome, Fuchs-Telem et
al. (2011) identified homozygosity for a 1-bp insertion in the SNAP29
gene (604202.0002).
*FIELD* AV
.0001
CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
SNAP29, 1-BP DEL, 220G
In affected patients with CEDNIK syndrome (609528), Sprecher et al.
(2005) identified a 1-bp deletion (220delG) in the SNAP29 gene,
resulting in premature termination of the protein. The mutation was not
identified in 200 control chromosomes. RT-PCR showed significantly
reduced SNAP29 expression in the skin of affected individuals. Sprecher
et al. (2005) concluded that SNAP29 is essential for proper vesicle
trafficking in neuroectodermal differentiation.
.0002
CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
SNAP29, 1-BP INS, 486A
In a Pakistani brother and sister with CEDNIK syndrome (609528),
Fuchs-Telem et al. (2011) identified homozygosity for a 1-bp insertion
(c.486insA) in the SNAP29 gene, causing a frameshift predicted to result
in premature termination. The mutation was not found in 200 control
chromosomes; DNA from other family members was not available. Premature
termination was confirmed by Western blot analysis, and transfection
studies in HeLa cells demonstrated complete loss of the wildtype
distribution pattern with the mutant construct. In addition, histologic
features typical for CEDNIK syndrome were replicated in 3-dimensional
primary human keratinocyte organotypic cell cultures downregulated for
SNAP29.
*FIELD* RF
1. Fuchs-Telem, D.; Stewart, H.; Rapaport, D.; Nousbeck, J.; Gat,
A.; Gini, M.; Lugassy, Y.; Emmert, S.; Eckl, K.; Hennies, H. C.; Sarig,
O.; Goldsher, D.; Meilik, B.; Ishida-Yamamoto, A. I.; Horowitz, M.;
Sprecher, E.: CEDNIK syndrome results from loss-of-function mutations
in SNAP29. Brit. J. Derm. 164: 610-616, 2011.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 5/9/2013.
3. Hohenstein, A. C.; Roche, P. A.: SNAP-29 is a promiscuous syntaxin-binding
SNARE. Biochem. Biophys. Res. Commun. 285: 167-171, 2001.
4. Rotem-Yehudar, R.; Galperin, E.; Horowitz, M.: Association of
insulin-like growth factor 1 receptor with EHD1 and SNAP29. J. Biol.
Chem. 276: 33054-33060, 2001.
5. Sprecher, E.; Ishida-Yamamoto, A.; Mizrahi-Koren, M.; Rapaport,
D.; Goldsher, D.; Indelman, M.; Topaz, O.; Chefetz, I.; Keren, H.;
O'Brien, T. J.; Bercovich, D.; Shalev, S.; Geiger, D.; Bergman, R.;
Horowitz, M.; Mandel, H.: A mutation in SNAP29, coding for a SNARE
protein involved in intracellular trafficking, causes a novel neurocutaneous
syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis,
and palmoplantar keratoderma. Am. J. Hum. Genet. 77: 242-251, 2005.
6. Steegmaier, M.; Yang, B.; Yoo, J.-S.; Huang, B.; Shen, M.; Yu,
S.; Luo, Y.; Scheller, R. H.: Three novel proteins of the syntaxin/SNAP-25
family. J. Biol. Chem. 273: 34171-34179, 1998.
*FIELD* CN
Matthew B. Gross - updated: 5/9/2013
Marla J. F. O'Neill - updated: 5/8/2013
Cassandra L. Kniffin - updated: 8/9/2005
Patricia A. Hartz - updated: 4/29/2002
*FIELD* CD
Rebekah S. Rasooly: 9/29/1999
*FIELD* ED
carol: 09/26/2013
carol: 6/21/2013
mgross: 5/9/2013
carol: 5/8/2013
carol: 10/6/2010
wwang: 8/30/2005
wwang: 8/12/2005
ckniffin: 8/9/2005
carol: 4/30/2002
terry: 4/29/2002
carol: 5/18/2000
alopez: 9/29/1999
MIM
609528
*RECORD*
*FIELD* NO
609528
*FIELD* TI
#609528 CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
read more;;CEDNIK SYNDROME
*FIELD* TX
A number sign (#) is used with this entry because cerebral dysgenesis,
neuropathy, ichthyosis, and palmoplantar keratoderma syndrome (CEDNIK
syndrome) is caused by homozygous mutation in the SNAP29 gene (604202)
on chromosome 22q11.
DESCRIPTION
CEDNIK (cerebral dysgenesis, neuropathy, ichthyosis, and keratoderma)
syndrome refers to a unique constellation of clinical manifestations
including microcephaly, severe neurologic impairment, psychomotor
retardation, failure to thrive, and facial dysmorphism, as well as
palmoplantar keratoderma and late-onset ichthyosis. Brain magnetic
resonance imaging (MRI) shows various degrees of cerebral dysgenesis
including absence of corpus callosum and cortical dysplasia. The
syndrome has been found to be uniformly fatal between the ages of 5 and
12 years (Fuchs-Telem et al., 2011).
CLINICAL FEATURES
Sprecher et al. (2005) described a clinical syndrome in 7 individuals
from 2 unrelated consanguineous Arab Muslim families living in northern
Israel. After a normal birth, the patients presented during the first 4
months of life with failure to thrive, roving eye movements, and poor
head and trunk control. All patients had progressive microcephaly and
facial dysmorphism consisting of elongated facies, downward-slanting
palpebral fissures, mild hypertelorism, and flat, broad nasal root.
Palmoplantar keratosis and ichthyosis appeared between 5 and 11 months
of age. By 8 to 15 months, major developmental milestones were not
achieved, and all patients had severe psychomotor retardation. Other
features included hypoplastic optic discs and sensorineural deafness.
MRI showed defects of the corpus callosum and cortical dysplasia with
pachygyria and polimicrogyria. Skin biopsy showed clear vesicles in the
spinous, granular, and stratum corneum layers, with retained
glucosylceramides, suggesting abnormal lamellar granule maturation.
Sprecher et al. (2005) concluded that this neurocutaneous syndrome
results from abnormal vesicle trafficking, vesicle maturation, and
vesicle fusion.
Fuchs-Telem et al. (2011) reported a brother and sister from a
consanguineous Pakistani family who both required neonatal tube feeding
and had dysmorphic facies with small fontanels, long pointed nose, and
small chin, as well as ichthyosis, palmoplantar keratoderma, hearing
loss, and severe developmental delay. Brain MRI revealed a small corpus
callosum in both sibs as well as other abnormalities, including
ventricular asymmetry and frontal cortical dysplasia in the sister and
perisylvian polymicrogyria with extensive cortical malformation in the
brother.
MAPPING
By linkage analysis of families with CEDNIK syndrome, Sprecher et al.
(2005) mapped the disorder to a 4-Mb region on chromosome 22q11.2
(maximum multipoint lod score of 4.85 at D22S446).
MOLECULAR GENETICS
In affected patients with CEDNIK syndrome, Sprecher et al. (2005)
identified a homozygous mutation in the SNAP29 gene (604202.0001).
In a brother and sister from a consanguineous Pakistani family who had
features consistent with CEDNIK syndome, Fuchs-Telem et al. (2011)
identified homozygosity for a 1-bp insertion in the SNAP29 gene
(604202.0002) that was not found in 200 control chromosomes. DNA from
other family members was not available.
*FIELD* RF
1. Fuchs-Telem, D.; Stewart, H.; Rapaport, D.; Nousbeck, J.; Gat,
A.; Gini, M.; Lugassy, Y.; Emmert, S.; Eckl, K.; Hennies, H. C.; Sarig,
O.; Goldsher, D.; Meilik, B.; Ishida-Yamamoto, A. I.; Horowitz, M.;
Sprecher, E.: CEDNIK syndrome results from loss-of-function mutations
in SNAP29. Brit. J. Derm. 164: 610-616, 2011.
2. Sprecher, E.; Ishida-Yamamoto, A.; Mizrahi-Koren, M.; Rapaport,
D.; Goldsher, D.; Indelman, M.; Topaz, O.; Chefetz, I.; Keren, H.;
O'Brien, T. J.; Bercovich, D.; Shalev, S.; Geiger, D.; Bergman, R.;
Horowitz, M.; Mandel, H.: A mutation in SNAP29, coding for a SNARE
protein involved in intracellular trafficking, causes a novel neurocutaneous
syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis,
and palmoplantar keratoderma. Am. J. Hum. Genet. 77: 242-251, 2005.
*FIELD* CS
INHERITANCE:
Autosomal recessive
GROWTH:
[Other];
Failure to thrive
HEAD AND NECK:
[Head];
Microcephaly, progressive;
[Face];
Long face;
[Ears];
Sensorineural deafness;
[Eyes];
Downward-slanting palpebral fissures;
Hypertelorism, mild;
Hypoplastic optic discs;
[Nose];
Flat, broad nasal root
SKIN, NAILS, HAIR:
[Skin];
Palmoplantar keratoderma;
Ichthyosis;
HISTOLOGY;
Spinous, granular, and stratum corneum layers contain clear vesicles;
Abnormal lamellar granule maturation;
Abnormal distribution of glucosylceramides
NEUROLOGIC:
[Central nervous system];
Delayed psychomotor development;
Major developmental milestones are not attained;
Mental retardation, severe;
Roving eye movements (infancy);
Trunk hypotonia;
Poor head control;
MRI shows defects of the corpus callosum;
Cortical dysplasia;
Pachygyria;
Polymicrogyria;
[Peripheral nervous system];
Peripheral neuropathy;
Areflexia
MISCELLANEOUS:
Onset in first months of life
MOLECULAR BASIS:
Caused by mutations in the synaptosomal-associated protein 29kD gene
(SNAP29, 604202.0001)
*FIELD* CD
Cassandra L. Kniffin: 8/9/2005
*FIELD* ED
joanna: 12/27/2013
joanna: 9/19/2005
ckniffin: 8/9/2005
*FIELD* CN
Marla J. F. O'Neill - updated: 05/08/2013
*FIELD* CD
Cassandra L. Kniffin: 8/9/2005
*FIELD* ED
carol: 05/08/2013
carol: 10/6/2010
wwang: 8/30/2005
wwang: 8/11/2005
ckniffin: 8/9/2005
*RECORD*
*FIELD* NO
609528
*FIELD* TI
#609528 CEREBRAL DYSGENESIS, NEUROPATHY, ICHTHYOSIS, AND PALMOPLANTAR KERATODERMA
SYNDROME
read more;;CEDNIK SYNDROME
*FIELD* TX
A number sign (#) is used with this entry because cerebral dysgenesis,
neuropathy, ichthyosis, and palmoplantar keratoderma syndrome (CEDNIK
syndrome) is caused by homozygous mutation in the SNAP29 gene (604202)
on chromosome 22q11.
DESCRIPTION
CEDNIK (cerebral dysgenesis, neuropathy, ichthyosis, and keratoderma)
syndrome refers to a unique constellation of clinical manifestations
including microcephaly, severe neurologic impairment, psychomotor
retardation, failure to thrive, and facial dysmorphism, as well as
palmoplantar keratoderma and late-onset ichthyosis. Brain magnetic
resonance imaging (MRI) shows various degrees of cerebral dysgenesis
including absence of corpus callosum and cortical dysplasia. The
syndrome has been found to be uniformly fatal between the ages of 5 and
12 years (Fuchs-Telem et al., 2011).
CLINICAL FEATURES
Sprecher et al. (2005) described a clinical syndrome in 7 individuals
from 2 unrelated consanguineous Arab Muslim families living in northern
Israel. After a normal birth, the patients presented during the first 4
months of life with failure to thrive, roving eye movements, and poor
head and trunk control. All patients had progressive microcephaly and
facial dysmorphism consisting of elongated facies, downward-slanting
palpebral fissures, mild hypertelorism, and flat, broad nasal root.
Palmoplantar keratosis and ichthyosis appeared between 5 and 11 months
of age. By 8 to 15 months, major developmental milestones were not
achieved, and all patients had severe psychomotor retardation. Other
features included hypoplastic optic discs and sensorineural deafness.
MRI showed defects of the corpus callosum and cortical dysplasia with
pachygyria and polimicrogyria. Skin biopsy showed clear vesicles in the
spinous, granular, and stratum corneum layers, with retained
glucosylceramides, suggesting abnormal lamellar granule maturation.
Sprecher et al. (2005) concluded that this neurocutaneous syndrome
results from abnormal vesicle trafficking, vesicle maturation, and
vesicle fusion.
Fuchs-Telem et al. (2011) reported a brother and sister from a
consanguineous Pakistani family who both required neonatal tube feeding
and had dysmorphic facies with small fontanels, long pointed nose, and
small chin, as well as ichthyosis, palmoplantar keratoderma, hearing
loss, and severe developmental delay. Brain MRI revealed a small corpus
callosum in both sibs as well as other abnormalities, including
ventricular asymmetry and frontal cortical dysplasia in the sister and
perisylvian polymicrogyria with extensive cortical malformation in the
brother.
MAPPING
By linkage analysis of families with CEDNIK syndrome, Sprecher et al.
(2005) mapped the disorder to a 4-Mb region on chromosome 22q11.2
(maximum multipoint lod score of 4.85 at D22S446).
MOLECULAR GENETICS
In affected patients with CEDNIK syndrome, Sprecher et al. (2005)
identified a homozygous mutation in the SNAP29 gene (604202.0001).
In a brother and sister from a consanguineous Pakistani family who had
features consistent with CEDNIK syndome, Fuchs-Telem et al. (2011)
identified homozygosity for a 1-bp insertion in the SNAP29 gene
(604202.0002) that was not found in 200 control chromosomes. DNA from
other family members was not available.
*FIELD* RF
1. Fuchs-Telem, D.; Stewart, H.; Rapaport, D.; Nousbeck, J.; Gat,
A.; Gini, M.; Lugassy, Y.; Emmert, S.; Eckl, K.; Hennies, H. C.; Sarig,
O.; Goldsher, D.; Meilik, B.; Ishida-Yamamoto, A. I.; Horowitz, M.;
Sprecher, E.: CEDNIK syndrome results from loss-of-function mutations
in SNAP29. Brit. J. Derm. 164: 610-616, 2011.
2. Sprecher, E.; Ishida-Yamamoto, A.; Mizrahi-Koren, M.; Rapaport,
D.; Goldsher, D.; Indelman, M.; Topaz, O.; Chefetz, I.; Keren, H.;
O'Brien, T. J.; Bercovich, D.; Shalev, S.; Geiger, D.; Bergman, R.;
Horowitz, M.; Mandel, H.: A mutation in SNAP29, coding for a SNARE
protein involved in intracellular trafficking, causes a novel neurocutaneous
syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis,
and palmoplantar keratoderma. Am. J. Hum. Genet. 77: 242-251, 2005.
*FIELD* CS
INHERITANCE:
Autosomal recessive
GROWTH:
[Other];
Failure to thrive
HEAD AND NECK:
[Head];
Microcephaly, progressive;
[Face];
Long face;
[Ears];
Sensorineural deafness;
[Eyes];
Downward-slanting palpebral fissures;
Hypertelorism, mild;
Hypoplastic optic discs;
[Nose];
Flat, broad nasal root
SKIN, NAILS, HAIR:
[Skin];
Palmoplantar keratoderma;
Ichthyosis;
HISTOLOGY;
Spinous, granular, and stratum corneum layers contain clear vesicles;
Abnormal lamellar granule maturation;
Abnormal distribution of glucosylceramides
NEUROLOGIC:
[Central nervous system];
Delayed psychomotor development;
Major developmental milestones are not attained;
Mental retardation, severe;
Roving eye movements (infancy);
Trunk hypotonia;
Poor head control;
MRI shows defects of the corpus callosum;
Cortical dysplasia;
Pachygyria;
Polymicrogyria;
[Peripheral nervous system];
Peripheral neuropathy;
Areflexia
MISCELLANEOUS:
Onset in first months of life
MOLECULAR BASIS:
Caused by mutations in the synaptosomal-associated protein 29kD gene
(SNAP29, 604202.0001)
*FIELD* CD
Cassandra L. Kniffin: 8/9/2005
*FIELD* ED
joanna: 12/27/2013
joanna: 9/19/2005
ckniffin: 8/9/2005
*FIELD* CN
Marla J. F. O'Neill - updated: 05/08/2013
*FIELD* CD
Cassandra L. Kniffin: 8/9/2005
*FIELD* ED
carol: 05/08/2013
carol: 10/6/2010
wwang: 8/30/2005
wwang: 8/11/2005
ckniffin: 8/9/2005