ID NSF_HUMAN Reviewed; 744 AA.
AC P46459; A8K2D9; B4DFA2; Q8N6D7; Q9UKZ2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 27-MAR-2024, entry version 220.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Hong R., Moriyama Y., Mori H., Futai M., Yamamoto A., Tashiro Y., Fukui T.,
RA Tagaya M.;
RT "Structure and localization of a brain N-ethylmaleimide-sensitive factor
RT involved in vesicular transport.";
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bui T.D., Lu L., Hong W.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and 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 [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., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., 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 the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT 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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP VARIANTS DEE96 THR-459 AND LEU-563, AND INVOLVEMENT IN DEE96.
RX PubMed=31675180; DOI=10.1002/acn3.50917;
RA Suzuki H., Yoshida T., Morisada N., Uehara T., Kosaki K., Sato K.,
RA Matsubara K., Takano-Shimizu T., Takenouchi T.;
RT "De novo NSF mutations cause early infantile epileptic encephalopathy.";
RL Ann. Clin. Transl. Neurol. 6:2334-2339(2019).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack independent of vesicle
CC origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2
CC membrane cycling (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18708};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P18708};
CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2. Interacts
CC with GRIA2. Interacts with PLK2, leading to disrupt the interaction
CC with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and
CC activity (By similarity). Interacts with CDK16 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P46459; Q9UBS5: GABBR1; NbExp=3; IntAct=EBI-712251, EBI-724156;
CC P46459; O75899: GABBR2; NbExp=4; IntAct=EBI-712251, EBI-715469;
CC P46459; P42262: GRIA2; NbExp=2; IntAct=EBI-712251, EBI-3909876;
CC P46459; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-712251, EBI-16439278;
CC P46459; P54920: NAPA; NbExp=3; IntAct=EBI-712251, EBI-749652;
CC P46459; P43378: PTPN9; NbExp=2; IntAct=EBI-712251, EBI-742898;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P46459-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46459-2; Sequence=VSP_056420, VSP_056421;
CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization.
CC {ECO:0000250}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 96 (DEE96)
CC [MIM:619340]: A form of epileptic encephalopathy, a heterogeneous group
CC of early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE96 is an autosomal dominant form characterized by
CC onset of seizures in the first days or weeks of life. Affected infants
CC also have hypotonia with respiratory insufficiency that may result in
CC premature death. {ECO:0000269|PubMed:31675180}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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; AK294001; BAG57363.1; -; 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 CCDS; CCDS42354.1; -. [P46459-1]
DR PIR; G01234; G01234.
DR RefSeq; NP_006169.2; NM_006178.3. [P46459-1]
DR PDB; 6KZQ; X-ray; 1.70 A; F=79-87.
DR PDBsum; 6KZQ; -.
DR AlphaFoldDB; P46459; -.
DR SMR; P46459; -.
DR BioGRID; 110960; 232.
DR IntAct; P46459; 79.
DR MINT; P46459; -.
DR STRING; 9606.ENSP00000381293; -.
DR ChEMBL; CHEMBL2311231; -.
DR DrugBank; DB01902; 1-Ethyl-Pyrrolidine-2,5-Dione.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR GlyGen; P46459; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46459; -.
DR MetOSite; P46459; -.
DR PhosphoSitePlus; P46459; -.
DR SwissPalm; P46459; -.
DR BioMuta; NSF; -.
DR DMDM; 257051048; -.
DR UCD-2DPAGE; P46459; -.
DR EPD; P46459; -.
DR jPOST; P46459; -.
DR MassIVE; P46459; -.
DR MaxQB; P46459; -.
DR PaxDb; 9606-ENSP00000381293; -.
DR PeptideAtlas; P46459; -.
DR ProteomicsDB; 4017; -.
DR ProteomicsDB; 55740; -. [P46459-1]
DR Pumba; P46459; -.
DR Antibodypedia; 1006; 326 antibodies from 37 providers.
DR DNASU; 4905; -.
DR Ensembl; ENST00000398238.8; ENSP00000381293.4; ENSG00000073969.19. [P46459-1]
DR Ensembl; ENST00000611398.3; ENSP00000478614.1; ENSG00000278174.3. [P46459-1]
DR Ensembl; ENST00000620290.2; ENSP00000481714.1; ENSG00000276262.2. [P46459-1]
DR Ensembl; ENST00000706392.1; ENSP00000516369.1; ENSG00000073969.19. [P46459-1]
DR GeneID; 4905; -.
DR KEGG; hsa:4905; -.
DR MANE-Select; ENST00000398238.8; ENSP00000381293.4; NM_006178.4; NP_006169.2.
DR UCSC; uc002iku.4; human. [P46459-1]
DR AGR; HGNC:8016; -.
DR DisGeNET; 4905; -.
DR GeneCards; NSF; -.
DR HGNC; HGNC:8016; NSF.
DR HPA; ENSG00000073969; Tissue enhanced (brain).
DR MalaCards; NSF; -.
DR MIM; 601633; gene.
DR MIM; 619340; phenotype.
DR neXtProt; NX_P46459; -.
DR OpenTargets; ENSG00000073969; -.
DR PharmGKB; PA31793; -.
DR VEuPathDB; HostDB:ENSG00000073969; -.
DR eggNOG; KOG0741; Eukaryota.
DR GeneTree; ENSGT00530000064085; -.
DR InParanoid; P46459; -.
DR OMA; CFDNEIA; -.
DR OrthoDB; 553800at2759; -.
DR PhylomeDB; P46459; -.
DR TreeFam; TF300371; -.
DR PathwayCommons; P46459; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
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; P46459; -.
DR SIGNOR; P46459; -.
DR BioGRID-ORCS; 4905; 832 hits in 1159 CRISPR screens.
DR ChiTaRS; NSF; human.
DR GeneWiki; N-ethylmaleimide_sensitive_fusion_protein; -.
DR GenomeRNAi; 4905; -.
DR Pharos; P46459; Tbio.
DR PRO; PR:P46459; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P46459; Protein.
DR Bgee; ENSG00000073969; Expressed in superior frontal gyrus and 103 other cell types or tissues.
DR ExpressionAtlas; P46459; baseline and differential.
DR Genevisible; P46459; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043198; C:dendritic shaft; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005795; C:Golgi stack; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006887; P:exocytosis; TAS:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IMP:CACAO.
DR GO; GO:0045026; P:plasma membrane fusion; TAS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:CACAO.
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:0017157; P:regulation of exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0035494; P:SNARE complex disassembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
DR CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Disease variant; Epilepsy; Hydrolase; Intellectual disability; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..744
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000084563"
FT BINDING 505..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 545..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46460"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46460"
FT MOD_RES 569
FT /note="Phosphoserine; by CDK16"
FT /evidence="ECO:0000250|UniProtKB:P46460"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056420"
FT VAR_SEQ 739..744
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056421"
FT VARIANT 459
FT /note="A -> T (in DEE96)"
FT /evidence="ECO:0000269|PubMed:31675180"
FT /id="VAR_085695"
FT VARIANT 476
FT /note="T -> M (in dbSNP:rs155733)"
FT /id="VAR_029580"
FT VARIANT 563
FT /note="P -> L (in DEE96)"
FT /evidence="ECO:0000269|PubMed:31675180"
FT /id="VAR_085696"
FT CONFLICT 22
FT /note="A -> S (in Ref. 1; AAA17411 and 2; AAF70545)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="N -> S (in Ref. 4; BAF82893)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="I -> N (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="F -> Y (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="A -> S (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="S -> F (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="K -> I (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="K -> R (in Ref. 4; BAF82893)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="D -> E (in Ref. 3; AAF04745)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="K -> M (in Ref. 4; BAF82893)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="F -> L (in Ref. 1; AAA17411, 2; AAF70545 and 3;
FT AAF04745)"
FT /evidence="ECO:0000305"
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
//
