NAV1_HUMAN
ID NAV1_HUMAN Reviewed; 1877 AA.
AC Q8NEY1; A8MS88; Q5SVH1; Q5SVH2; Q5SVH3; Q5SVH7; Q5VUY9; Q8IVL2; Q96II1;
AC Q9H7V9; Q9H9S9; Q9H9T5; Q9UGI1; Q9ULK7; Q9ULR9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Neuron navigator 1;
DE AltName: Full=Pore membrane and/or filament-interacting-like protein 3;
DE AltName: Full=Steerin-1;
DE AltName: Full=Unc-53 homolog 1;
DE Short=unc53H1;
GN Name=NAV1; Synonyms=KIAA1151, KIAA1213, POMFIL3, STEERIN1;
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), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12062803; DOI=10.1016/s0378-1119(02)00567-x;
RA Coy J.F., Wiemann S., Bechmann I., Baechner D., Nitsch R., Kretz O.,
RA Christiansen H., Poustka A.;
RT "Pore membrane and/or filament interacting like protein 1 (POMFIL1) is
RT predominantly expressed in the nervous system and encodes different protein
RT isoforms.";
RL Gene 290:73-94(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-1273, AND TISSUE
RP SPECIFICITY.
RX PubMed=12079279; DOI=10.1006/geno.2002.6799;
RA Maes T., Barcelo A., Buesa C.;
RT "Neuron navigator: a human gene family with homology to unc-53, a cell
RT guidance gene from Caenorhabditis elegans.";
RL Genomics 80:21-30(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-409, AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 42-1877 (ISOFORM 1).
RX PubMed=15158073; DOI=10.1016/j.devbrainres.2004.03.004;
RA Peeters P.J., Baker A., Goris I., Daneels G., Verhasselt P.,
RA Luyten W.H.M.L., Geysen J.J.G.H., Kass S.U., Moechars D.W.E.;
RT "Sensory deficits in mice hypomorphic for a mammalian homologue of unc-
RT 53.";
RL Brain Res. Dev. Brain Res. 150:89-101(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-1877 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 707-1877 (ISOFORM 6).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 445-1205 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1161-1877 (ISOFORM 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1122-1877 (ISOFORM 3).
RC TISSUE=Skin;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; THR-159; SER-199;
RP SER-296; SER-308; SER-391; SER-452; THR-534; THR-572; SER-760; SER-808;
RP THR-1170; SER-1181 AND SER-1382, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-750, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-362; SER-452;
RP SER-808; SER-1000; THR-1006 AND SER-1265, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-142 AND SER-760, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-142; SER-194;
RP SER-199; SER-312; SER-391; SER-452; SER-474; SER-476; SER-490; SER-528;
RP SER-541; THR-544; SER-648; SER-754; SER-760; SER-797; SER-808; SER-1000 AND
RP SER-1265, AND IDENTIFICATION BY 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 [16]
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).
CC -!- FUNCTION: May be involved in neuronal migration. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with tubulin. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NEY1-3; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-11953718, EBI-742054;
CC Q8NEY1-3; Q96CN9: GCC1; NbExp=3; IntAct=EBI-11953718, EBI-746252;
CC Q8NEY1-3; Q15323: KRT31; NbExp=3; IntAct=EBI-11953718, EBI-948001;
CC Q8NEY1-3; Q96LW4: PRIMPOL; NbExp=5; IntAct=EBI-11953718, EBI-10044038;
CC Q8NEY1-3; Q7L4I2: RSRC2; NbExp=3; IntAct=EBI-11953718, EBI-953753;
CC Q8NEY1-4; Q96CN9: GCC1; NbExp=3; IntAct=EBI-10270828, EBI-746252;
CC Q8NEY1-4; Q15323: KRT31; NbExp=3; IntAct=EBI-10270828, EBI-948001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Associates with a subset of microtubule plus ends. Enriched in
CC neuronal growth cones (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8NEY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEY1-2; Sequence=VSP_025256;
CC Name=3;
CC IsoId=Q8NEY1-3; Sequence=VSP_025259;
CC Name=4;
CC IsoId=Q8NEY1-4; Sequence=VSP_025255, VSP_025259;
CC Name=5;
CC IsoId=Q8NEY1-5; Sequence=VSP_025253, VSP_025254, VSP_025259;
CC Name=6;
CC IsoId=Q8NEY1-6; Sequence=VSP_025256, VSP_025257, VSP_025258;
CC Name=7;
CC IsoId=Q8NEY1-7; Sequence=VSP_025255, VSP_025256, VSP_025259;
CC -!- TISSUE SPECIFICITY: Broadly expressed at low levels. Expressed at high
CC levels in heart, skeletal muscle and placenta.
CC {ECO:0000269|PubMed:12062803, ECO:0000269|PubMed:12079279}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain and heart.
CC {ECO:0000269|PubMed:12062803}.
CC -!- SIMILARITY: Belongs to the Nav/unc-53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07523.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14136.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14142.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14865.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY043013; AAL05591.1; -; mRNA.
DR EMBL; AC092800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ251973; CAB66088.1; -; Genomic_DNA.
DR EMBL; AJ488101; CAD32470.1; -; mRNA.
DR EMBL; AB032977; BAA86465.3; -; mRNA.
DR EMBL; AB033039; BAA86527.1; -; mRNA.
DR EMBL; AK022622; BAB14136.1; ALT_INIT; mRNA.
DR EMBL; AK022631; BAB14142.1; ALT_INIT; mRNA.
DR EMBL; AK024265; BAB14865.1; ALT_INIT; mRNA.
DR EMBL; BC007523; AAH07523.1; ALT_INIT; mRNA.
DR CCDS; CCDS1414.2; -. [Q8NEY1-1]
DR CCDS; CCDS53456.1; -. [Q8NEY1-5]
DR RefSeq; NP_001161210.1; NM_001167738.1. [Q8NEY1-5]
DR RefSeq; NP_065176.3; NM_020443.4. [Q8NEY1-1]
DR RefSeq; XP_011508399.1; XM_011510097.1.
DR RefSeq; XP_011508400.1; XM_011510098.1.
DR RefSeq; XP_011508404.1; XM_011510102.1.
DR RefSeq; XP_016858240.1; XM_017002751.1.
DR AlphaFoldDB; Q8NEY1; -.
DR BioGRID; 124605; 132.
DR IntAct; Q8NEY1; 31.
DR MINT; Q8NEY1; -.
DR STRING; 9606.ENSP00000356265; -.
DR CarbonylDB; Q8NEY1; -.
DR GlyGen; Q8NEY1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NEY1; -.
DR PhosphoSitePlus; Q8NEY1; -.
DR BioMuta; NAV1; -.
DR DMDM; 147704557; -.
DR EPD; Q8NEY1; -.
DR jPOST; Q8NEY1; -.
DR MassIVE; Q8NEY1; -.
DR MaxQB; Q8NEY1; -.
DR PaxDb; Q8NEY1; -.
DR PeptideAtlas; Q8NEY1; -.
DR PRIDE; Q8NEY1; -.
DR ProteomicsDB; 73230; -. [Q8NEY1-1]
DR ProteomicsDB; 73231; -. [Q8NEY1-2]
DR ProteomicsDB; 73232; -. [Q8NEY1-3]
DR ProteomicsDB; 73233; -. [Q8NEY1-4]
DR ProteomicsDB; 73234; -. [Q8NEY1-5]
DR ProteomicsDB; 73235; -. [Q8NEY1-6]
DR ProteomicsDB; 73236; -. [Q8NEY1-7]
DR Antibodypedia; 3226; 79 antibodies from 22 providers.
DR DNASU; 89796; -.
DR Ensembl; ENST00000367295.5; ENSP00000356264.1; ENSG00000134369.16. [Q8NEY1-5]
DR Ensembl; ENST00000367296.8; ENSP00000356265.4; ENSG00000134369.16. [Q8NEY1-1]
DR GeneID; 89796; -.
DR KEGG; hsa:89796; -.
DR UCSC; uc001gwx.4; human. [Q8NEY1-1]
DR CTD; 89796; -.
DR DisGeNET; 89796; -.
DR GeneCards; NAV1; -.
DR HGNC; HGNC:15989; NAV1.
DR HPA; ENSG00000134369; Low tissue specificity.
DR MIM; 611628; gene.
DR neXtProt; NX_Q8NEY1; -.
DR OpenTargets; ENSG00000134369; -.
DR PharmGKB; PA31451; -.
DR VEuPathDB; HostDB:ENSG00000134369; -.
DR eggNOG; ENOG502QSUE; Eukaryota.
DR GeneTree; ENSGT00940000156637; -.
DR InParanoid; Q8NEY1; -.
DR OMA; DPACDLY; -.
DR OrthoDB; 21830at2759; -.
DR PhylomeDB; Q8NEY1; -.
DR TreeFam; TF329881; -.
DR PathwayCommons; Q8NEY1; -.
DR SignaLink; Q8NEY1; -.
DR BioGRID-ORCS; 89796; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; NAV1; human.
DR GeneWiki; NAV1; -.
DR GenomeRNAi; 89796; -.
DR Pharos; Q8NEY1; Tbio.
DR PRO; PR:Q8NEY1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NEY1; protein.
DR Bgee; ENSG00000134369; Expressed in endothelial cell and 190 other tissues.
DR ExpressionAtlas; Q8NEY1; baseline and differential.
DR Genevisible; Q8NEY1; HS.
DR GO; GO:0043194; C:axon initial segment; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR039041; Nav/unc-53.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12784; PTHR12784; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Methylation; Microtubule;
KW Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1877
FT /note="Neuron navigator 1"
FT /id="PRO_0000286974"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1810..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..280
FT /evidence="ECO:0000255"
FT COILED 731..756
FT /evidence="ECO:0000255"
FT COILED 1072..1163
FT /evidence="ECO:0000255"
FT COILED 1303..1362
FT /evidence="ECO:0000255"
FT COMPBIAS 193..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..914
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 544
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CH77"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1006
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..389
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_025253"
FT VAR_SEQ 390..409
FT /note="MSDSDLMGKTMTEDDDITTG -> MLHLPLPRSGRTVNFPRS (in
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_025254"
FT VAR_SEQ 999..1055
FT /note="Missing (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_025255"
FT VAR_SEQ 1074..1081
FT /note="Missing (in isoform 2, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10574461,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_025256"
FT VAR_SEQ 1173..1198
FT /note="ELRIKRQNSSDSISSLNSITSHSSIG -> GRTSSHRLRGNREQESKSITDF
FT YLGP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_025257"
FT VAR_SEQ 1199..1877
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:10574461"
FT /id="VSP_025258"
FT VAR_SEQ 1214..1216
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025259"
FT VARIANT 937
FT /note="Q -> H (in dbSNP:rs16849342)"
FT /id="VAR_032245"
FT VARIANT 1273
FT /note="S -> L (in dbSNP:rs2820289)"
FT /evidence="ECO:0000269|PubMed:12079279"
FT /id="VAR_032246"
FT VARIANT 1290
FT /note="H -> D (in dbSNP:rs2292822)"
FT /id="VAR_032247"
FT VARIANT 1527
FT /note="V -> I (in dbSNP:rs16849379)"
FT /id="VAR_032248"
FT CONFLICT 267..269
FT /note="DLR -> FLW (in Ref. 5; BAA86465)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="S -> R (in Ref. 2; AAL05591)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="C -> R (in Ref. 6; BAB14142)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="S -> P (in Ref. 6; BAB14142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="S -> L (in Ref. 6; BAB14142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="N -> S (in Ref. 6; BAB14142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1793
FT /note="E -> K (in Ref. 6; BAB14865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1877 AA; 202472 MW; B18C9AC9DC8D9CF2 CRC64;
MLGSSVKSVQ PEVELSSGGG DEGADEPRGA GRKAAAADGR GMLPKRAKAP GGGGGMAKAS
AAELKVFKSG SVDSRVPGGP PASNLRKQKS LTNLSFLTDS EKKLQLYEPE WSDDMAKAPK
GLGKVGSKGR EAPLMSKTLS KSEHSLFQAK GSPAGGAKTP LAPLAPNLGK PSRIPRGPYA
EVKPLSKAPE AAVSEDGKSD DELLSSKAKA QKSSGPVPSA KGQEERAFLK VDPELVVTVL
GDLEQLLFSQ MLDPESQRKR TVQNVLDLRQ NLEETMSSLR GSQVTHSSLE MTCYDSDDAN
PRSVSSLSNR SSPLSWRYGQ SSPRLQAGDA PSVGGSCRSE GTPAWYMHGE RAHYSHTMPM
RSPSKLSHIS RLELVESLDS DEVDLKSGYM SDSDLMGKTM TEDDDITTGW DESSSISSGL
SDASDNLSSE EFNASSSLNS LPSTPTASRR NSTIVLRTDS EKRSLAESGL SWFSESEEKA
PKKLEYDSGS LKMEPGTSKW RRERPESCDD SSKGGELKKP ISLGHPGSLK KGKTPPVAVT
SPITHTAQSA LKVAGKPEGK ATDKGKLAVK NTGLQRSSSD AGRDRLSDAK KPPSGIARPS
TSGSFGYKKP PPATGTATVM QTGGSATLSK IQKSSGIPVK PVNGRKTSLD VSNSAEPGFL
APGARSNIQY RSLPRPAKSS SMSVTGGRGG PRPVSSSIDP SLLSTKQGGL TPSRLKEPTK
VASGRTTPAP VNQTDREKEK AKAKAVALDS DNISLKSIGS PESTPKNQAS HPTATKLAEL
PPTPLRATAK SFVKPPSLAN LDKVNSNSLD LPSSSDTTHA SKVPDLHATS SASGGPLPSC
FTPSPAPILN INSASFSQGL ELMSGFSVPK ETRMYPKLSG LHRSMESLQM PMSLPSAFPS
STPVPTPPAP PAAPTEEETE ELTWSGSPRA GQLDSNQRDR NTLPKKGLRY QLQSQEETKE
RRHSHTIGGL PESDDQSELP SPPALPMSLS AKGQLTNIVS PTAATTPRIT RSNSIPTHEA
AFELYSGSQM GSTLSLAERP KGMIRSGSFR DPTDDVHGSV LSLASSASST YSSAEERMQS
EQIRKLRREL ESSQEKVATL TSQLSANANL VAAFEQSLVN MTSRLRHLAE TAEEKDTELL
DLRETIDFLK KKNSEAQAVI QGALNASETT PKELRIKRQN SSDSISSLNS ITSHSSIGSS
KDADAKKKKK KSWVYELRSS FNKAFSIKKG PKSASSYSDI EEIATPDSSA PSSPKLQHGS
TETASPSIKS STSSSVGTDV TEGPAHPAPH TRLFHANEEE EPEKKEVSEL RSELWEKEMK
LTDIRLEALN SAHQLDQLRE TMHNMQLEVD LLKAENDRLK VAPGPSSGST PGQVPGSSAL
SSPRRSLGLA LTHSFGPSLA DTDLSPMDGI STCGPKEEVT LRVVVRMPPQ HIIKGDLKQQ
EFFLGCSKVS GKVDWKMLDE AVFQVFKDYI SKMDPASTLG LSTESIHGYS ISHVKRVLDA
EPPEMPPCRR GVNNISVSLK GLKEKCVDSL VFETLIPKPM MQHYISLLLK HRRLVLSGPS
GTGKTYLTNR LAEYLVERSG REVTEGIVST FNMHQQSCKD LQLYLSNLAN QIDRETGIGD
VPLVILLDDL SEAGSISELV NGALTCKYHK CPYIIGTTNQ PVKMTPNHGL HLSFRMLTFS
NNVEPANGFL VRYLRRKLVE SDSDINANKE ELLRVLDWVP KLWYHLHTFL EKHSTSDFLI
GPCFFLSCPI GIEDFRTWFI DLWNNSIIPY LQEGAKDGIK VHGQKAAWED PVEWVRDTLP
WPSAQQDQSK LYHLPPPTVG PHSIASPPED RTVKDSTPSS LDSDPLMAML LKLQEAANYI
ESPDRETILD PNLQATL
