SNAB_HUMAN
ID SNAB_HUMAN Reviewed; 298 AA.
AC Q9H115; B4DK44; Q4G0M0; Q4G187; Q5JXF9; Q8N3C4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 163.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-298 (ISOFORM 1/2).
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between
CC GRIA2 and PRKCABP, leading to the internalization of GRIA2.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9H115; P20292: ALOX5AP; NbExp=3; IntAct=EBI-3921185, EBI-3904621;
CC Q9H115; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-3921185, EBI-714543;
CC Q9H115; O15155: BET1; NbExp=3; IntAct=EBI-3921185, EBI-749204;
CC Q9H115; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-3921185, EBI-1045797;
CC Q9H115; Q8IUN9: CLEC10A; NbExp=5; IntAct=EBI-3921185, EBI-2873246;
CC Q9H115; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-3921185, EBI-6942903;
CC Q9H115; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-3921185, EBI-12831978;
CC Q9H115; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3921185, EBI-18304435;
CC Q9H115; O95377: GJB5; NbExp=3; IntAct=EBI-3921185, EBI-3909454;
CC Q9H115; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3921185, EBI-18053395;
CC Q9H115; Q9UGI6-2: KCNN3; NbExp=3; IntAct=EBI-3921185, EBI-17888181;
CC Q9H115; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-3921185, EBI-17490413;
CC Q9H115; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-3921185, EBI-949945;
CC Q9H115; O00560: SDCBP; NbExp=3; IntAct=EBI-3921185, EBI-727004;
CC Q9H115; O15389: SIGLEC5; NbExp=3; IntAct=EBI-3921185, EBI-750381;
CC Q9H115; A8K287: SNAP23; NbExp=3; IntAct=EBI-3921185, EBI-10188497;
CC Q9H115; O00161: SNAP23; NbExp=3; IntAct=EBI-3921185, EBI-745000;
CC Q9H115; O95721: SNAP29; NbExp=8; IntAct=EBI-3921185, EBI-490676;
CC Q9H115; O14662: STX16; NbExp=3; IntAct=EBI-3921185, EBI-2853548;
CC Q9H115; O14662-5: STX16; NbExp=3; IntAct=EBI-3921185, EBI-9089968;
CC Q9H115; Q8N4C7: STX19; NbExp=3; IntAct=EBI-3921185, EBI-8484990;
CC Q9H115; Q16623: STX1A; NbExp=4; IntAct=EBI-3921185, EBI-712466;
CC Q9H115; P61266: STX1B; NbExp=5; IntAct=EBI-3921185, EBI-9071709;
CC Q9H115; P32856-2: STX2; NbExp=3; IntAct=EBI-3921185, EBI-11956649;
CC Q9H115; Q13277: STX3; NbExp=8; IntAct=EBI-3921185, EBI-1394295;
CC Q9H115; Q12846: STX4; NbExp=6; IntAct=EBI-3921185, EBI-744942;
CC Q9H115; Q13190: STX5; NbExp=9; IntAct=EBI-3921185, EBI-714206;
CC Q9H115; O43752: STX6; NbExp=4; IntAct=EBI-3921185, EBI-2695795;
CC Q9H115; P21579: SYT1; NbExp=3; IntAct=EBI-3921185, EBI-524909;
CC Q9H115; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-3921185, EBI-8032987;
CC Q9H115; O14948: TFEC; NbExp=3; IntAct=EBI-3921185, EBI-3916574;
CC Q9H115; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-3921185, EBI-7238458;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H115-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H115-2; Sequence=VSP_055278;
CC Name=3;
CC IsoId=Q9H115-3; Sequence=VSP_055276, VSP_055277;
CC -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR EMBL; AK296385; BAG59056.1; -; mRNA.
DR EMBL; AL096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10152.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10156.1; -; Genomic_DNA.
DR EMBL; BC047426; AAH47426.1; -; mRNA.
DR EMBL; BC060840; AAH60840.1; -; mRNA.
DR EMBL; AL834445; CAD39105.1; -; mRNA.
DR CCDS; CCDS13152.1; -. [Q9H115-1]
DR CCDS; CCDS63241.1; -. [Q9H115-3]
DR CCDS; CCDS63242.1; -. [Q9H115-2]
DR RefSeq; NP_001269947.1; NM_001283018.1.
DR RefSeq; NP_001269949.1; NM_001283020.1. [Q9H115-2]
DR RefSeq; NP_001269955.1; NM_001283026.1. [Q9H115-3]
DR RefSeq; NP_071363.1; NM_022080.2. [Q9H115-1]
DR AlphaFoldDB; Q9H115; -.
DR SMR; Q9H115; -.
DR BioGRID; 121983; 47.
DR CORUM; Q9H115; -.
DR IntAct; Q9H115; 41.
DR MINT; Q9H115; -.
DR STRING; 9606.ENSP00000482826; -.
DR GlyGen; Q9H115; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H115; -.
DR PhosphoSitePlus; Q9H115; -.
DR BioMuta; NAPB; -.
DR DMDM; 18202933; -.
DR EPD; Q9H115; -.
DR jPOST; Q9H115; -.
DR MassIVE; Q9H115; -.
DR MaxQB; Q9H115; -.
DR PaxDb; Q9H115; -.
DR PeptideAtlas; Q9H115; -.
DR PRIDE; Q9H115; -.
DR ProteomicsDB; 4427; -.
DR ProteomicsDB; 62109; -.
DR ProteomicsDB; 80352; -. [Q9H115-1]
DR Antibodypedia; 42862; 105 antibodies from 19 providers.
DR DNASU; 63908; -.
DR Ensembl; ENST00000377026.4; ENSP00000366225.4; ENSG00000125814.17. [Q9H115-1]
DR Ensembl; ENST00000398425.7; ENSP00000381459.3; ENSG00000125814.17. [Q9H115-3]
DR Ensembl; ENST00000432543.6; ENSP00000413600.2; ENSG00000125814.17. [Q9H115-2]
DR GeneID; 63908; -.
DR KEGG; hsa:63908; -.
DR MANE-Select; ENST00000377026.4; ENSP00000366225.4; NM_022080.3; NP_071363.1.
DR UCSC; uc002wta.4; human. [Q9H115-1]
DR CTD; 63908; -.
DR DisGeNET; 63908; -.
DR GeneCards; NAPB; -.
DR HGNC; HGNC:15751; NAPB.
DR HPA; ENSG00000125814; Group enriched (brain, retina).
DR MalaCards; NAPB; -.
DR MIM; 611270; gene.
DR neXtProt; NX_Q9H115; -.
DR OpenTargets; ENSG00000125814; -.
DR PharmGKB; PA31444; -.
DR VEuPathDB; HostDB:ENSG00000125814; -.
DR eggNOG; KOG1586; Eukaryota.
DR GeneTree; ENSGT00390000005826; -.
DR HOGENOM; CLU_046329_1_1_1; -.
DR InParanoid; Q9H115; -.
DR OMA; WSVKEYL; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; Q9H115; -.
DR TreeFam; TF316547; -.
DR PathwayCommons; Q9H115; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q9H115; -.
DR BioGRID-ORCS; 63908; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; NAPB; human.
DR GeneWiki; NAPB; -.
DR GenomeRNAi; 63908; -.
DR Pharos; Q9H115; Tdark.
DR PRO; PR:Q9H115; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H115; protein.
DR Bgee; ENSG00000125814; Expressed in middle temporal gyrus and 181 other tissues.
DR ExpressionAtlas; Q9H115; baseline and differential.
DR Genevisible; Q9H115; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IBA:GO_Central.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0035494; P:SNARE complex disassembly; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..298
FT /note="Beta-soluble NSF attachment protein"
FT /id="PRO_0000219060"
FT VAR_SEQ 1..20
FT /note="MDNAGKEREAVQLMAEAEKR -> MTLLPALWMLEMLTKRQIPK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055276"
FT VAR_SEQ 21..114
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055277"
FT VAR_SEQ 60..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055278"
FT VARIANT 61
FT /note="A -> T (in dbSNP:rs6036399)"
FT /id="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
