Full text data of NSF
NSF
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Vesicle-fusing ATPase; 3.6.4.6 (N-ethylmaleimide-sensitive fusion protein; NEM-sensitive fusion protein; Vesicular-fusion protein NSF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Vesicle-fusing ATPase; 3.6.4.6 (N-ethylmaleimide-sensitive fusion protein; NEM-sensitive fusion protein; Vesicular-fusion protein NSF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00006451
IPI00006451 Vesicular-fusion protein NSF ATP binding, nucleoside triphosphate activity, nucleotide binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00006451 Vesicular-fusion protein NSF ATP binding, nucleoside triphosphate activity, nucleotide binding soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P46459
ID NSF_HUMAN Reviewed; 744 AA.
AC P46459; A8K2D9; Q8N6D7; Q9UKZ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Vesicle-fusing ATPase;
DE EC=3.6.4.6;
DE AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE Short=NEM-sensitive fusion protein;
DE AltName: Full=Vesicular-fusion protein NSF;
GN Name=NSF;
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;
RA Hong R., Moriyama Y., Mori H., Futai M., Yamamoto A., Tashiro Y.,
RA Fukui T., Tagaya M.;
RT "Structure and localization of a brain N-ethylmaleimide-sensitive
RT factor involved in vesicular transport.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bui T.D., Lu L., Hong W.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Zhang R., Liu Z., Wu M.;
RT "The regulation of hNSF gene expression.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 [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).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the
CC fusion of transport vesicles within the Golgi cisternae. Is also
CC required for transport from the endoplasmic reticulum to the Golgi
CC stack. Seem to function as a fusion protein required for the
CC delivery of cargo proteins to all compartments of the Golgi stack
CC independent of vesicle origin. Interaction with AMPAR subunit
CC GRIA2 leads to influence GRIA2 membrane cycling (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2.
CC Interacts with GRIA2. Interacts with PLK2, leading to disrupt the
CC interaction with GRIA2. Interacts with MUSK; may regulate MUSK
CC endocytosis and activity (By similarity). Interacts with CDK16 (By
CC similarity).
CC -!- INTERACTION:
CC Q9UBS5:GABBR1; NbExp=3; IntAct=EBI-712251, EBI-724156;
CC O75899:GABBR2; NbExp=4; IntAct=EBI-712251, EBI-715469;
CC P42262:GRIA2; NbExp=2; IntAct=EBI-712251, EBI-3909876;
CC P54920:NAPA; NbExp=2; IntAct=EBI-712251, EBI-749652;
CC P43378:PTPN9; NbExp=2; IntAct=EBI-712251, EBI-742898;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization
CC (By similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17411.1; Type=Erroneous initiation;
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DR EMBL; U03985; AAA17411.1; ALT_INIT; mRNA.
DR EMBL; AF135168; AAF70545.1; -; mRNA.
DR EMBL; AF102846; AAF04745.2; -; mRNA.
DR EMBL; AK290204; BAF82893.1; -; mRNA.
DR EMBL; AC004098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030613; AAH30613.1; -; mRNA.
DR PIR; G01234; G01234.
DR RefSeq; NP_006169.2; NM_006178.3.
DR UniGene; Hs.431279; -.
DR ProteinModelPortal; P46459; -.
DR SMR; P46459; 1-201, 220-742.
DR DIP; DIP-389N; -.
DR IntAct; P46459; 37.
DR MINT; MINT-1369243; -.
DR STRING; 9606.ENSP00000381293; -.
DR ChEMBL; CHEMBL2311231; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; P46459; -.
DR DMDM; 257051048; -.
DR UCD-2DPAGE; P46459; -.
DR PaxDb; P46459; -.
DR PRIDE; P46459; -.
DR Ensembl; ENST00000398238; ENSP00000381293; ENSG00000073969.
DR GeneID; 4905; -.
DR KEGG; hsa:4905; -.
DR UCSC; uc002iku.3; human.
DR CTD; 4905; -.
DR GeneCards; GC17P044668; -.
DR H-InvDB; HIX0013914; -.
DR H-InvDB; HIX0013915; -.
DR HGNC; HGNC:8016; NSF.
DR HPA; CAB009324; -.
DR HPA; CAB013645; -.
DR HPA; HPA003154; -.
DR MIM; 601633; gene.
DR neXtProt; NX_P46459; -.
DR PharmGKB; PA31793; -.
DR eggNOG; COG0464; -.
DR HOGENOM; HOG000198544; -.
DR HOVERGEN; HBG000324; -.
DR InParanoid; P46459; -.
DR KO; K06027; -.
DR OMA; FKDKERS; -.
DR OrthoDB; EOG7P8P7F; -.
DR PhylomeDB; P46459; -.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; NSF; human.
DR GeneWiki; N-ethylmaleimide_sensitive_fusion_protein; -.
DR GenomeRNAi; 4905; -.
DR NextBio; 18875; -.
DR PMAP-CutDB; P46459; -.
DR PRO; PR:P46459; -.
DR ArrayExpress; P46459; -.
DR Bgee; P46459; -.
DR CleanEx; HS_NSF; -.
DR Genevestigator; P46459; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042623; F:ATPase activity, coupled; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; TAS:UniProtKB.
DR GO; GO:0045026; P:plasma membrane fusion; TAS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009010; Asp_de-COase-like_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 744 Vesicle-fusing ATPase.
FT /FTId=PRO_0000084563.
FT NP_BIND 505 510 ATP (By similarity).
FT NP_BIND 545 552 ATP (By similarity).
FT METAL 550 550 Magnesium (By similarity).
FT MOD_RES 259 259 Phosphotyrosine (By similarity).
FT MOD_RES 569 569 Phosphoserine; by CDK16 (By similarity).
FT VARIANT 476 476 T -> M (in dbSNP:rs155733).
FT /FTId=VAR_029580.
FT CONFLICT 22 22 A -> S (in Ref. 1; AAA17411 and 2;
FT AAF70545).
FT CONFLICT 25 25 N -> S (in Ref. 4; BAF82893).
FT CONFLICT 107 107 I -> N (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 130 130 F -> Y (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 154 154 A -> S (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 237 237 S -> F (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 251 251 K -> I (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 427 427 K -> R (in Ref. 4; BAF82893).
FT CONFLICT 571 571 D -> E (in Ref. 3; AAF04745).
FT CONFLICT 639 639 K -> M (in Ref. 4; BAF82893).
FT CONFLICT 686 686 F -> L (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
SQ SEQUENCE 744 AA; 82594 MW; BF545A2A0C7EC2F7 CRC64;
MAGRSMQAAR CPTDELSLTN CAVVNEKDFQ SGQHVIVRTS PNHRYTFTLK THPSVVPGSI
AFSLPQRKWA GLSIGQEIEV SLYTFDKAKQ CIGTMTIEID FLQKKSIDSN PYDTDKMAAE
FIQQFNNQAF SVGQQLVFSF NEKLFGLLVK DIEAMDPSIL KGEPATGKRQ KIEVGLVVGN
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
DPEYRVRKFL ALLREEGASP LDFD
//
ID NSF_HUMAN Reviewed; 744 AA.
AC P46459; A8K2D9; Q8N6D7; Q9UKZ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 3.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Vesicle-fusing ATPase;
DE EC=3.6.4.6;
DE AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE Short=NEM-sensitive fusion protein;
DE AltName: Full=Vesicular-fusion protein NSF;
GN Name=NSF;
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;
RA Hong R., Moriyama Y., Mori H., Futai M., Yamamoto A., Tashiro Y.,
RA Fukui T., Tagaya M.;
RT "Structure and localization of a brain N-ethylmaleimide-sensitive
RT factor involved in vesicular transport.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bui T.D., Lu L., Hong W.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Zhang R., Liu Z., Wu M.;
RT "The regulation of hNSF gene expression.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 [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).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the
CC fusion of transport vesicles within the Golgi cisternae. Is also
CC required for transport from the endoplasmic reticulum to the Golgi
CC stack. Seem to function as a fusion protein required for the
CC delivery of cargo proteins to all compartments of the Golgi stack
CC independent of vesicle origin. Interaction with AMPAR subunit
CC GRIA2 leads to influence GRIA2 membrane cycling (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2.
CC Interacts with GRIA2. Interacts with PLK2, leading to disrupt the
CC interaction with GRIA2. Interacts with MUSK; may regulate MUSK
CC endocytosis and activity (By similarity). Interacts with CDK16 (By
CC similarity).
CC -!- INTERACTION:
CC Q9UBS5:GABBR1; NbExp=3; IntAct=EBI-712251, EBI-724156;
CC O75899:GABBR2; NbExp=4; IntAct=EBI-712251, EBI-715469;
CC P42262:GRIA2; NbExp=2; IntAct=EBI-712251, EBI-3909876;
CC P54920:NAPA; NbExp=2; IntAct=EBI-712251, EBI-749652;
CC P43378:PTPN9; NbExp=2; IntAct=EBI-712251, EBI-742898;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization
CC (By similarity).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17411.1; Type=Erroneous initiation;
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DR EMBL; U03985; AAA17411.1; ALT_INIT; mRNA.
DR EMBL; AF135168; AAF70545.1; -; mRNA.
DR EMBL; AF102846; AAF04745.2; -; mRNA.
DR EMBL; AK290204; BAF82893.1; -; mRNA.
DR EMBL; AC004098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC217780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030613; AAH30613.1; -; mRNA.
DR PIR; G01234; G01234.
DR RefSeq; NP_006169.2; NM_006178.3.
DR UniGene; Hs.431279; -.
DR ProteinModelPortal; P46459; -.
DR SMR; P46459; 1-201, 220-742.
DR DIP; DIP-389N; -.
DR IntAct; P46459; 37.
DR MINT; MINT-1369243; -.
DR STRING; 9606.ENSP00000381293; -.
DR ChEMBL; CHEMBL2311231; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR PhosphoSite; P46459; -.
DR DMDM; 257051048; -.
DR UCD-2DPAGE; P46459; -.
DR PaxDb; P46459; -.
DR PRIDE; P46459; -.
DR Ensembl; ENST00000398238; ENSP00000381293; ENSG00000073969.
DR GeneID; 4905; -.
DR KEGG; hsa:4905; -.
DR UCSC; uc002iku.3; human.
DR CTD; 4905; -.
DR GeneCards; GC17P044668; -.
DR H-InvDB; HIX0013914; -.
DR H-InvDB; HIX0013915; -.
DR HGNC; HGNC:8016; NSF.
DR HPA; CAB009324; -.
DR HPA; CAB013645; -.
DR HPA; HPA003154; -.
DR MIM; 601633; gene.
DR neXtProt; NX_P46459; -.
DR PharmGKB; PA31793; -.
DR eggNOG; COG0464; -.
DR HOGENOM; HOG000198544; -.
DR HOVERGEN; HBG000324; -.
DR InParanoid; P46459; -.
DR KO; K06027; -.
DR OMA; FKDKERS; -.
DR OrthoDB; EOG7P8P7F; -.
DR PhylomeDB; P46459; -.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; NSF; human.
DR GeneWiki; N-ethylmaleimide_sensitive_fusion_protein; -.
DR GenomeRNAi; 4905; -.
DR NextBio; 18875; -.
DR PMAP-CutDB; P46459; -.
DR PRO; PR:P46459; -.
DR ArrayExpress; P46459; -.
DR Bgee; P46459; -.
DR CleanEx; HS_NSF; -.
DR Genevestigator; P46459; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042623; F:ATPase activity, coupled; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; TAS:UniProtKB.
DR GO; GO:0045026; P:plasma membrane fusion; TAS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009010; Asp_de-COase-like_dom.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1 744 Vesicle-fusing ATPase.
FT /FTId=PRO_0000084563.
FT NP_BIND 505 510 ATP (By similarity).
FT NP_BIND 545 552 ATP (By similarity).
FT METAL 550 550 Magnesium (By similarity).
FT MOD_RES 259 259 Phosphotyrosine (By similarity).
FT MOD_RES 569 569 Phosphoserine; by CDK16 (By similarity).
FT VARIANT 476 476 T -> M (in dbSNP:rs155733).
FT /FTId=VAR_029580.
FT CONFLICT 22 22 A -> S (in Ref. 1; AAA17411 and 2;
FT AAF70545).
FT CONFLICT 25 25 N -> S (in Ref. 4; BAF82893).
FT CONFLICT 107 107 I -> N (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 130 130 F -> Y (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 154 154 A -> S (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 237 237 S -> F (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 251 251 K -> I (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
FT CONFLICT 427 427 K -> R (in Ref. 4; BAF82893).
FT CONFLICT 571 571 D -> E (in Ref. 3; AAF04745).
FT CONFLICT 639 639 K -> M (in Ref. 4; BAF82893).
FT CONFLICT 686 686 F -> L (in Ref. 1; AAA17411, 2; AAF70545
FT and 3; AAF04745).
SQ SEQUENCE 744 AA; 82594 MW; BF545A2A0C7EC2F7 CRC64;
MAGRSMQAAR CPTDELSLTN CAVVNEKDFQ SGQHVIVRTS PNHRYTFTLK THPSVVPGSI
AFSLPQRKWA GLSIGQEIEV SLYTFDKAKQ CIGTMTIEID FLQKKSIDSN PYDTDKMAAE
FIQQFNNQAF SVGQQLVFSF NEKLFGLLVK DIEAMDPSIL KGEPATGKRQ KIEVGLVVGN
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
DPEYRVRKFL ALLREEGASP LDFD
//
MIM
601633
*RECORD*
*FIELD* NO
601633
*FIELD* TI
*601633 N-ETHYLMALEIMIDE-SENSITIVE FACTOR; NSF
*FIELD* TX
CLONING
Mammalian N-ethylmaleimide-sensitive protein was first described by
read moreGlick and Rothman (1987) as the protein that restored the ability of
Golgi membranes that had been inactivated with the reagent
N-ethylmaleimide to re-engage in vesicular transport. The NSF gene was
subsequently cloned from Chinese hamster cells by Block et al. (1988)
and Wilson et al. (1989). NSF is a member of the AAA (ATPases associated
with diverse cellular activities) gene family. Hoyle et al. (1996)
stated that the genes are most related throughout the approximately
200-amino acid domain (the AAA domain) that binds ATP; however, the
family is notable not only for its conservation but also for diverse
functions of its proteins in eukaryotic cells. The family can be
subdivided into those with either 1 or 2 ATP-binding domains. NSF is a
2-domain member of the AAA family. Valosin-containing protein (601023),
which is also involved in membrane fusion, is another 2-AAA domain
protein.
GENE FUNCTION
The process of vesicle targeting and fusion in the secretory and
endocytic pathways has been described by the SNAREs hypothesis (Rothman,
1994). This proposes that vesicles dock with specific target membranes
by binding to membrane-specific SNAREs (soluble
N-ethylmaleimide-sensitive factors attachment protein receptors) (see
604026). Hoyle et al. (1996) noted that targeting specificity is also
affected by the Rabs, a group of small soluble GTPases. After the
vesicle has bound to the target membrane, the SNARE multimer is joined
by the soluble SNAP proteins and N-ethylmaleimide-sensitive factor
(NSF). The resulting large complex is thought to allow membrane fusion
and the ATPase activity of the NSF appears to be essential for the
process. Hoyle et al. (1996) stated that while many of different SNAREs,
Rabs, and SNAPs are involved in membrane fusion, there is only 1 NSF,
and the SNARE hypothesis describes NSF-dependent fusion.
By use of microarray expression profiling of prefrontal cortex from
matched pairs of patients with schizophrenia (181500) and control
subjects and hierarchical data analysis, Mirnics et al. (2000) found
that transcripts encoding proteins involved in the regulation of
presynaptic function were decreased in all subjects with schizophrenia.
Genes of presynaptic function showed a different combination of
decreased expression across subjects. Over 250 other gene groups did not
show altered expression. Selected presynaptic function gene microarray
observations were verified by in situ hybridization. Two of the most
consistently changed transcripts in the presynaptic functional gene
group, N-ethylmaleimide-sensitive factor and synapsin-2 (600755), were
decreased in 10 of 10 and 9 of 10 subjects with schizophrenia,
respectively. The combined data suggested that subjects with
schizophrenia share a common abnormality in presynaptic function.
MAPPING
By PCR amplification in a human monochromosomal somatic cell hybrid
mapping panel, Hoyle et al. (1996) mapped the NSF gene to human
chromosome 17. To determine a regional mapping position for NSF and to
confirm their cell hybrid results, they isolated NSF-containing human
cosmids for fluorescence in situ hybridization (FISH) mapping. The
results showed that the gene mapped to 17q21-q22. They mapped the mouse
homolog, Nsf, to mouse chromosome 11 by analysis of DNA from
interspecific backcrosses. Hoyle et al. (1996) noted that there are
neurologic disorders mapping in that region of chromosome 17, such as
DDBAC (600274) and PPND (600274), which may be allelic disorders. They
noted that NSF is preferentially expressed in the mammalian nervous
system. An aberrant Nsf gene in Drosophila results in defective synaptic
transmission.
*FIELD* RF
1. Block, M. R.; Glick, B. S.; Wilcox, C. A.; Wieland, F. T.; Rothman,
J. E.: Purification of an N-ethylmaleimide-sensitive protein catalyzing
vesicular transport. Proc. Nat. Acad. Sci. 85: 7852-7856, 1988.
2. Glick, B. S.; Rothman, J. E.: Possible role for fatty acyl-coenzyme
A in intracellular protein transport. Nature 326: 309-312, 1987.
3. Hoyle, J.; Phelan, J. P.; Bermingham, N.; Fisher, E. M. C.: Localization
of human and mouse N-ethylmaleimide-sensitive factor (NSF) gene: a
two-domain member of the AAA family that is involved in membrane fusion. Mammalian
Genome 7: 850-852, 1996.
4. Mirnics, K.; Middleton, F. A.; Marquez, A.; Lewis, D. A.; Levitt,
P.: Molecular characterization of schizophrenia viewed by microarray
analysis of gene expression in prefrontal cortex. Neuron 28: 53-67,
2000.
5. Rothman, J. E.: Mechanisms of intracellular protein transport. Nature 372:
55-63, 1994.
6. Wilson, D. W.; Wilcox, C. A.; Flynn, G. C.; Chen, E.; Kuang, W.-J.;
Henzel, W. J.; Block, M. R.; Ullrich, A.; Rothman, J. E.: A fusion
protein required for vesicle-mediated transport in both mammalian
cells and yeast. Nature 339: 355-359, 1989.
*FIELD* CD
Victor A. McKusick: 1/16/1997
*FIELD* ED
terry: 05/20/2010
alopez: 7/15/2009
terry: 7/9/2009
cwells: 1/23/2001
cwells: 1/19/2001
jamie: 1/16/1997
*RECORD*
*FIELD* NO
601633
*FIELD* TI
*601633 N-ETHYLMALEIMIDE-SENSITIVE FACTOR; NSF
*FIELD* TX
CLONING
Mammalian N-ethylmaleimide-sensitive protein was first described by
read moreGlick and Rothman (1987) as the protein that restored the ability of
Golgi membranes that had been inactivated with the reagent
N-ethylmaleimide to re-engage in vesicular transport. The NSF gene was
subsequently cloned from Chinese hamster cells by Block et al. (1988)
and Wilson et al. (1989). NSF is a member of the AAA (ATPases associated
with diverse cellular activities) gene family. Hoyle et al. (1996)
stated that the genes are most related throughout the approximately
200-amino acid domain (the AAA domain) that binds ATP; however, the
family is notable not only for its conservation but also for diverse
functions of its proteins in eukaryotic cells. The family can be
subdivided into those with either 1 or 2 ATP-binding domains. NSF is a
2-domain member of the AAA family. Valosin-containing protein (601023),
which is also involved in membrane fusion, is another 2-AAA domain
protein.
GENE FUNCTION
The process of vesicle targeting and fusion in the secretory and
endocytic pathways has been described by the SNAREs hypothesis (Rothman,
1994). This proposes that vesicles dock with specific target membranes
by binding to membrane-specific SNAREs (soluble
N-ethylmaleimide-sensitive factors attachment protein receptors) (see
604026). Hoyle et al. (1996) noted that targeting specificity is also
affected by the Rabs, a group of small soluble GTPases. After the
vesicle has bound to the target membrane, the SNARE multimer is joined
by the soluble SNAP proteins and N-ethylmaleimide-sensitive factor
(NSF). The resulting large complex is thought to allow membrane fusion
and the ATPase activity of the NSF appears to be essential for the
process. Hoyle et al. (1996) stated that while many of different SNAREs,
Rabs, and SNAPs are involved in membrane fusion, there is only 1 NSF,
and the SNARE hypothesis describes NSF-dependent fusion.
By use of microarray expression profiling of prefrontal cortex from
matched pairs of patients with schizophrenia (181500) and control
subjects and hierarchical data analysis, Mirnics et al. (2000) found
that transcripts encoding proteins involved in the regulation of
presynaptic function were decreased in all subjects with schizophrenia.
Genes of presynaptic function showed a different combination of
decreased expression across subjects. Over 250 other gene groups did not
show altered expression. Selected presynaptic function gene microarray
observations were verified by in situ hybridization. Two of the most
consistently changed transcripts in the presynaptic functional gene
group, N-ethylmaleimide-sensitive factor and synapsin-2 (600755), were
decreased in 10 of 10 and 9 of 10 subjects with schizophrenia,
respectively. The combined data suggested that subjects with
schizophrenia share a common abnormality in presynaptic function.
MAPPING
By PCR amplification in a human monochromosomal somatic cell hybrid
mapping panel, Hoyle et al. (1996) mapped the NSF gene to human
chromosome 17. To determine a regional mapping position for NSF and to
confirm their cell hybrid results, they isolated NSF-containing human
cosmids for fluorescence in situ hybridization (FISH) mapping. The
results showed that the gene mapped to 17q21-q22. They mapped the mouse
homolog, Nsf, to mouse chromosome 11 by analysis of DNA from
interspecific backcrosses. Hoyle et al. (1996) noted that there are
neurologic disorders mapping in that region of chromosome 17, such as
DDBAC (600274) and PPND (600274), which may be allelic disorders. They
noted that NSF is preferentially expressed in the mammalian nervous
system. An aberrant Nsf gene in Drosophila results in defective synaptic
transmission.
*FIELD* RF
1. Block, M. R.; Glick, B. S.; Wilcox, C. A.; Wieland, F. T.; Rothman,
J. E.: Purification of an N-ethylmaleimide-sensitive protein catalyzing
vesicular transport. Proc. Nat. Acad. Sci. 85: 7852-7856, 1988.
2. Glick, B. S.; Rothman, J. E.: Possible role for fatty acyl-coenzyme
A in intracellular protein transport. Nature 326: 309-312, 1987.
3. Hoyle, J.; Phelan, J. P.; Bermingham, N.; Fisher, E. M. C.: Localization
of human and mouse N-ethylmaleimide-sensitive factor (NSF) gene: a
two-domain member of the AAA family that is involved in membrane fusion. Mammalian
Genome 7: 850-852, 1996.
4. Mirnics, K.; Middleton, F. A.; Marquez, A.; Lewis, D. A.; Levitt,
P.: Molecular characterization of schizophrenia viewed by microarray
analysis of gene expression in prefrontal cortex. Neuron 28: 53-67,
2000.
5. Rothman, J. E.: Mechanisms of intracellular protein transport. Nature 372:
55-63, 1994.
6. Wilson, D. W.; Wilcox, C. A.; Flynn, G. C.; Chen, E.; Kuang, W.-J.;
Henzel, W. J.; Block, M. R.; Ullrich, A.; Rothman, J. E.: A fusion
protein required for vesicle-mediated transport in both mammalian
cells and yeast. Nature 339: 355-359, 1989.
*FIELD* CD
Victor A. McKusick: 1/16/1997
*FIELD* ED
terry: 05/20/2010
alopez: 7/15/2009
terry: 7/9/2009
cwells: 1/23/2001
cwells: 1/19/2001
jamie: 1/16/1997