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SNAB_MOUSE
ID   SNAB_MOUSE              Reviewed;         298 AA.
AC   P28663;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Beta-soluble NSF attachment protein;
DE            Short=SNAP-beta;
DE   AltName: Full=Brain protein I47;
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein beta;
GN   Name=Napb; Synonyms=Snapb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-298.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in mouse
RT   brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 123-140; 209-222 AND 228-239, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=8455721; DOI=10.1038/362353a0;
RA   Whiteheart S.W., Griff I.C., Brunner M., Clary D.O., Mayer T., Buhrow S.A.,
RA   Rothman J.E.;
RT   "SNAP family of NSF attachment proteins includes a brain-specific
RT   isoform.";
RL   Nature 362:353-355(1993).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between
CC       GRIA2 and PRKCABP, leading to the internalization of GRIA2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Cerebral cortex, cerebellar cortex, hippocampus,
CC       and dentate gyrus, weakly expressed in the putamen, the thalamus and
CC       the brain stem. {ECO:0000269|PubMed:8455721}.
CC   -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR   EMBL; AK083184; BAC38798.1; -; mRNA.
DR   EMBL; BC038362; AAH38362.1; -; mRNA.
DR   EMBL; BC049874; AAH49874.1; -; mRNA.
DR   EMBL; X61455; CAA43695.1; -; mRNA.
DR   CCDS; CCDS16842.1; -.
DR   PIR; S16869; S16869.
DR   RefSeq; NP_062606.1; NM_019632.3.
DR   AlphaFoldDB; P28663; -.
DR   SMR; P28663; -.
DR   BioGRID; 201693; 16.
DR   IntAct; P28663; 5.
DR   MINT; P28663; -.
DR   STRING; 10090.ENSMUSP00000028926; -.
DR   iPTMnet; P28663; -.
DR   PhosphoSitePlus; P28663; -.
DR   SwissPalm; P28663; -.
DR   jPOST; P28663; -.
DR   MaxQB; P28663; -.
DR   PaxDb; P28663; -.
DR   PeptideAtlas; P28663; -.
DR   PRIDE; P28663; -.
DR   ProteomicsDB; 261284; -.
DR   Antibodypedia; 42862; 105 antibodies from 19 providers.
DR   DNASU; 17957; -.
DR   Ensembl; ENSMUST00000028926; ENSMUSP00000028926; ENSMUSG00000027438.
DR   GeneID; 17957; -.
DR   KEGG; mmu:17957; -.
DR   UCSC; uc008mti.1; mouse.
DR   CTD; 63908; -.
DR   MGI; MGI:104562; Napb.
DR   VEuPathDB; HostDB:ENSMUSG00000027438; -.
DR   eggNOG; KOG1586; Eukaryota.
DR   GeneTree; ENSGT00390000005826; -.
DR   HOGENOM; CLU_046329_0_1_1; -.
DR   InParanoid; P28663; -.
DR   OMA; WSVKEYL; -.
DR   OrthoDB; 1191204at2759; -.
DR   PhylomeDB; P28663; -.
DR   TreeFam; TF316547; -.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR   Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   BioGRID-ORCS; 17957; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Napb; mouse.
DR   PRO; PR:P28663; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P28663; protein.
DR   Bgee; ENSMUSG00000027438; Expressed in pontine nuclear group and 214 other tissues.
DR   ExpressionAtlas; P28663; baseline and differential.
DR   Genevisible; P28663; MM.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI.
DR   GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR   GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0032984; P:protein-containing complex disassembly; ISO:MGI.
DR   GO; GO:0043462; P:regulation of ATP-dependent activity; ISO:MGI.
DR   GO; GO:0002090; P:regulation of receptor internalization; ISO:MGI.
DR   GO; GO:0010807; P:regulation of synaptic vesicle priming; IDA:SynGO.
DR   GO; GO:0035494; P:SNARE complex disassembly; IGI:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IGI:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IC:SynGO.
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   Direct protein sequencing; ER-Golgi transport; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..298
FT                   /note="Beta-soluble NSF attachment protein"
FT                   /id="PRO_0000219061"
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
 
 
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