Full text data of NAPB
NAPB
(SNAPB)
[Confidence: low (only semi-automatic identification from reviews)]
Beta-soluble NSF attachment protein; SNAP-beta (N-ethylmaleimide-sensitive factor attachment protein beta)
Beta-soluble NSF attachment protein; SNAP-beta (N-ethylmaleimide-sensitive factor attachment protein beta)
UniProt
Q9H115
ID SNAB_HUMAN Reviewed; 298 AA.
AC Q9H115; Q4G187; Q5JXF9; Q8N3C4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Beta-soluble NSF attachment protein;
DE Short=SNAP-beta;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein beta;
GN Name=NAPB; Synonyms=SNAPB;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-298.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus (By similarity).
CC -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction
CC between GRIA2 and PRKCABP, leading to the internalization of GRIA2
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity).
CC -!- SIMILARITY: Belongs to the SNAP family.
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; AL096677; CAI20156.1; -; Genomic_DNA.
DR EMBL; BC060840; AAH60840.1; -; mRNA.
DR EMBL; AL834445; CAD39105.1; -; mRNA.
DR RefSeq; NP_071363.1; NM_022080.2.
DR UniGene; Hs.269471; -.
DR ProteinModelPortal; Q9H115; -.
DR SMR; Q9H115; 9-288.
DR IntAct; Q9H115; 2.
DR STRING; 9606.ENSP00000366225; -.
DR PhosphoSite; Q9H115; -.
DR DMDM; 18202933; -.
DR PaxDb; Q9H115; -.
DR PRIDE; Q9H115; -.
DR DNASU; 63908; -.
DR Ensembl; ENST00000377026; ENSP00000366225; ENSG00000125814.
DR GeneID; 63908; -.
DR KEGG; hsa:63908; -.
DR UCSC; uc002wta.3; human.
DR CTD; 63908; -.
DR GeneCards; GC20M023355; -.
DR HGNC; HGNC:15751; NAPB.
DR HPA; CAB037227; -.
DR MIM; 611270; gene.
DR neXtProt; NX_Q9H115; -.
DR PharmGKB; PA31444; -.
DR eggNOG; NOG245914; -.
DR HOGENOM; HOG000165015; -.
DR HOVERGEN; HBG001325; -.
DR InParanoid; Q9H115; -.
DR OMA; SIAEMYE; -.
DR OrthoDB; EOG7FNC80; -.
DR PhylomeDB; Q9H115; -.
DR ChiTaRS; NAPB; human.
DR GeneWiki; NAPB; -.
DR GenomeRNAi; 63908; -.
DR NextBio; 65622; -.
DR PRO; PR:Q9H115; -.
DR ArrayExpress; Q9H115; -.
DR Bgee; Q9H115; -.
DR CleanEx; HS_NAPB; -.
DR Genevestigator; Q9H115; -.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IEA:Ensembl.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
PE 1: Evidence at protein level;
KW Complete proteome; ER-Golgi transport; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 298 Beta-soluble NSF attachment protein.
FT /FTId=PRO_0000219060.
FT VARIANT 61 61 A -> T (in dbSNP:rs6036399).
FT /FTId=VAR_052026.
SQ SEQUENCE 298 AA; 33557 MW; 5B7BE0FB84BABD83 CRC64;
MDNAGKEREA VQLMAEAEKR VKASHSFLRG LFGGNTRIEE ACEMYTRAAN MFKMAKNWSA
AGNAFCQAAK LHMQLQSKHD SATSFVDAGN AYKKADPQEA INCLNAAIDI YTDMGRFTIA
AKHHITIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAA YAAQLEQYQK
AIEIYEQVGA NTMDNPLLKY SAKDYFFKAA LCHFIVDELN AKLALEKYEE MFPAFTDSRE
CKLLKKLLEA HEEQNSEAYT EAVKEFDSIS RLDQWLTTML LRIKKSIQGD GEGDGDLK
//
ID SNAB_HUMAN Reviewed; 298 AA.
AC Q9H115; Q4G187; Q5JXF9; Q8N3C4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-AUG-2001, sequence version 2.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Beta-soluble NSF attachment protein;
DE Short=SNAP-beta;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein beta;
GN Name=NAPB; Synonyms=SNAPB;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-298.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus (By similarity).
CC -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction
CC between GRIA2 and PRKCABP, leading to the internalization of GRIA2
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC similarity).
CC -!- SIMILARITY: Belongs to the SNAP family.
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; AL096677; CAI20156.1; -; Genomic_DNA.
DR EMBL; BC060840; AAH60840.1; -; mRNA.
DR EMBL; AL834445; CAD39105.1; -; mRNA.
DR RefSeq; NP_071363.1; NM_022080.2.
DR UniGene; Hs.269471; -.
DR ProteinModelPortal; Q9H115; -.
DR SMR; Q9H115; 9-288.
DR IntAct; Q9H115; 2.
DR STRING; 9606.ENSP00000366225; -.
DR PhosphoSite; Q9H115; -.
DR DMDM; 18202933; -.
DR PaxDb; Q9H115; -.
DR PRIDE; Q9H115; -.
DR DNASU; 63908; -.
DR Ensembl; ENST00000377026; ENSP00000366225; ENSG00000125814.
DR GeneID; 63908; -.
DR KEGG; hsa:63908; -.
DR UCSC; uc002wta.3; human.
DR CTD; 63908; -.
DR GeneCards; GC20M023355; -.
DR HGNC; HGNC:15751; NAPB.
DR HPA; CAB037227; -.
DR MIM; 611270; gene.
DR neXtProt; NX_Q9H115; -.
DR PharmGKB; PA31444; -.
DR eggNOG; NOG245914; -.
DR HOGENOM; HOG000165015; -.
DR HOVERGEN; HBG001325; -.
DR InParanoid; Q9H115; -.
DR OMA; SIAEMYE; -.
DR OrthoDB; EOG7FNC80; -.
DR PhylomeDB; Q9H115; -.
DR ChiTaRS; NAPB; human.
DR GeneWiki; NAPB; -.
DR GenomeRNAi; 63908; -.
DR NextBio; 65622; -.
DR PRO; PR:Q9H115; -.
DR ArrayExpress; Q9H115; -.
DR Bgee; Q9H115; -.
DR CleanEx; HS_NAPB; -.
DR Genevestigator; Q9H115; -.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IEA:Ensembl.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
PE 1: Evidence at protein level;
KW Complete proteome; ER-Golgi transport; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 298 Beta-soluble NSF attachment protein.
FT /FTId=PRO_0000219060.
FT VARIANT 61 61 A -> T (in dbSNP:rs6036399).
FT /FTId=VAR_052026.
SQ SEQUENCE 298 AA; 33557 MW; 5B7BE0FB84BABD83 CRC64;
MDNAGKEREA VQLMAEAEKR VKASHSFLRG LFGGNTRIEE ACEMYTRAAN MFKMAKNWSA
AGNAFCQAAK LHMQLQSKHD SATSFVDAGN AYKKADPQEA INCLNAAIDI YTDMGRFTIA
AKHHITIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAA YAAQLEQYQK
AIEIYEQVGA NTMDNPLLKY SAKDYFFKAA LCHFIVDELN AKLALEKYEE MFPAFTDSRE
CKLLKKLLEA HEEQNSEAYT EAVKEFDSIS RLDQWLTTML LRIKKSIQGD GEGDGDLK
//
MIM
611270
*RECORD*
*FIELD* NO
611270
*FIELD* TI
*611270 N-ETHYLMALEIMIDE-SENSITIVE FACTOR ATTACHMENT PROTEIN, BETA; NAPB
;;SOLUBLE NSF-ATTACHMENT PROTEIN, BETA; SNAPB;;
read moreSNAP, BETA
*FIELD* TX
CLONING
Whiteheart et al. (1993) cloned beta-Snap from bovine brain and
identified the mouse homolog. The deduced bovine protein contains 2
coiled-coil domains and 5 putative casein kinase II (see CSNK2A1;
115440) phosphorylation sites. Northern blot analysis of mouse tissues
detected beta-Snap expression in brain only. Whiteheart et al. (1993)
stated that highest concentration of beta-Snap in mouse brain is in
areas of high neuron density.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAPB
gene to chromosome 20 (TMAP RH11675).
*FIELD* RF
1. Whiteheart, S. W.; Griff, I. C.; Brunner, M.; Clary, D. O.; Mayer,
T.; Buhrow, S. A.; Rothman, J. E.: SNAP family of NSF attachment
proteins includes a brain-specific isoform. Nature 362: 353-355,
1993.
*FIELD* CD
Patricia A. Hartz: 7/30/2007
*FIELD* ED
mgross: 07/30/2007
*RECORD*
*FIELD* NO
611270
*FIELD* TI
*611270 N-ETHYLMALEIMIDE-SENSITIVE FACTOR ATTACHMENT PROTEIN, BETA; NAPB
;;SOLUBLE NSF-ATTACHMENT PROTEIN, BETA; SNAPB;;
read moreSNAP, BETA
*FIELD* TX
CLONING
Whiteheart et al. (1993) cloned beta-Snap from bovine brain and
identified the mouse homolog. The deduced bovine protein contains 2
coiled-coil domains and 5 putative casein kinase II (see CSNK2A1;
115440) phosphorylation sites. Northern blot analysis of mouse tissues
detected beta-Snap expression in brain only. Whiteheart et al. (1993)
stated that highest concentration of beta-Snap in mouse brain is in
areas of high neuron density.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAPB
gene to chromosome 20 (TMAP RH11675).
*FIELD* RF
1. Whiteheart, S. W.; Griff, I. C.; Brunner, M.; Clary, D. O.; Mayer,
T.; Buhrow, S. A.; Rothman, J. E.: SNAP family of NSF attachment
proteins includes a brain-specific isoform. Nature 362: 353-355,
1993.
*FIELD* CD
Patricia A. Hartz: 7/30/2007
*FIELD* ED
mgross: 07/30/2007