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NAV2_HUMAN
ID   NAV2_HUMAN              Reviewed;        2488 AA.
AC   Q8IVL1; A6NEC1; Q8IVK3; Q8IVK4; Q8IVK5; Q8IVK6; Q8IVK7; Q8IVK8; Q8NHC9;
AC   Q8NHD0; Q8TDE9; Q8TDF0; Q8TEB3; Q96B30; Q9NUZ6; Q9NVM7; Q9P2C8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Neuron navigator 2;
DE            EC=3.6.4.12;
DE   AltName: Full=Helicase APC down-regulated 1;
DE   AltName: Full=Pore membrane and/or filament-interacting-like protein 2;
DE   AltName: Full=Retinoic acid inducible in neuroblastoma 1;
DE   AltName: Full=Steerin-2;
DE   AltName: Full=Unc-53 homolog 2;
DE            Short=unc53H2;
GN   Name=NAV2; Synonyms=HELAD1, KIAA1419, POMFIL2, RAINB1, STEERIN2;
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] (ISOFORMS 2 AND 3), INDUCTION BY ATRA, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT ALA-1077.
RX   PubMed=11904404; DOI=10.1073/pnas.052017399;
RA   Merrill R.A., Plum L.A., Kaiser M.E., Clagett-Dame M.;
RT   "A mammalian homolog of unc-53 is regulated by all-trans retinoic acid in
RT   neuroblastoma cells and embryos.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:3422-3427(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION,
RP   FUNCTION AS A HELICASE, INDUCTION, TISSUE SPECIFICITY, AND VARIANTS LYS-109
RP   AND ALA-1077.
RX   PubMed=12214280; DOI=10.1038/sj.onc.1205751;
RA   Ishiguro H., Shimokawa T., Tsunoda T., Tanaka T., Fujii Y., Nakamura Y.,
RA   Furukawa Y.;
RT   "Isolation of HELAD1, a novel human helicase gene up-regulated in
RT   colorectal carcinomas.";
RL   Oncogene 21:6387-6394(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 8; 9; 10; 11; 12 AND 13), FUNCTION,
RP   AND VARIANTS LYS-109 AND ALA-1077.
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-1077.
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [5]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [6]
RP   SEQUENCE REVISION.
RA   Ohara O.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7), AND VARIANTS
RP   ASP-1041; ALA-1077 AND ILE-2374.
RC   TISSUE=Placenta;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND VARIANT ALA-1077.
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   [10]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
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   [11]
RP   ALTERNATIVE SPLICING, AND TISSUE 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1977, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1480; SER-1484; SER-1488 AND
RP   SER-1977, AND IDENTIFICATION BY MASS SPECTROMETRY [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   [14]
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   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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).
RN   [17]
RP   STRUCTURE BY NMR OF 90-197.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the CH domain from human neuron navigator 2.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Possesses 3' to 5' helicase activity and exonuclease
CC       activity. Involved in neuronal development, specifically in the
CC       development of different sensory organs. {ECO:0000269|PubMed:12214280,
CC       ECO:0000269|PubMed:15158073}.
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=3.6.4.12;
CC   -!- INTERACTION:
CC       Q8IVL1; Q7Z6V5: ADAT2; NbExp=3; IntAct=EBI-741200, EBI-2809203;
CC       Q8IVL1; Q5T655: CFAP58; NbExp=3; IntAct=EBI-741200, EBI-10245749;
CC       Q8IVL1; Q9UNL4: ING4; NbExp=3; IntAct=EBI-741200, EBI-2866661;
CC       Q8IVL1; Q8WYH8: ING5; NbExp=4; IntAct=EBI-741200, EBI-488533;
CC       Q8IVL1; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-741200, EBI-399246;
CC       Q8IVL1; O75928: PIAS2; NbExp=4; IntAct=EBI-741200, EBI-348555;
CC       Q8IVL1; Q96T37: RBM15; NbExp=3; IntAct=EBI-741200, EBI-2514922;
CC       Q8IVL1; Q8NDT2: RBM15B; NbExp=3; IntAct=EBI-741200, EBI-726721;
CC       Q8IVL1; Q8NDT2-2: RBM15B; NbExp=3; IntAct=EBI-741200, EBI-10269922;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12214280}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=Additional isoforms may exist.;
CC       Name=1;
CC         IsoId=Q8IVL1-1; Sequence=Displayed;
CC       Name=2; Synonyms=RAINB1d;
CC         IsoId=Q8IVL1-2; Sequence=VSP_021934, VSP_021937;
CC       Name=3; Synonyms=HELAD1L;
CC         IsoId=Q8IVL1-3; Sequence=VSP_021934, VSP_021937, VSP_021938;
CC       Name=4; Synonyms=HELAD1S;
CC         IsoId=Q8IVL1-4; Sequence=VSP_021927, VSP_021934, VSP_021937,
CC                                  VSP_021938;
CC       Name=5;
CC         IsoId=Q8IVL1-5; Sequence=VSP_021926, VSP_021935, VSP_021936,
CC                                  VSP_021937, VSP_021938;
CC       Name=6;
CC         IsoId=Q8IVL1-6; Sequence=VSP_021925, VSP_021937, VSP_021938;
CC       Name=7;
CC         IsoId=Q8IVL1-7; Sequence=VSP_021924;
CC       Name=8;
CC         IsoId=Q8IVL1-8; Sequence=VSP_021932;
CC       Name=9;
CC         IsoId=Q8IVL1-9; Sequence=VSP_021933;
CC       Name=10;
CC         IsoId=Q8IVL1-10; Sequence=VSP_021928;
CC       Name=11;
CC         IsoId=Q8IVL1-11; Sequence=VSP_021929;
CC       Name=12;
CC         IsoId=Q8IVL1-12; Sequence=VSP_021930;
CC       Name=13;
CC         IsoId=Q8IVL1-13; Sequence=VSP_021931;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain, kidney and liver.
CC       Also expressed in the thyroid, mammary gland, spinal cord, heart,
CC       placenta and lung. Abundantly expressed in colon cancers.
CC       {ECO:0000269|PubMed:11904404, ECO:0000269|PubMed:12062803,
CC       ECO:0000269|PubMed:12079279, ECO:0000269|PubMed:12214280}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the nervous system of
CC       developing embryos. Also expressed in fetal heart, liver and kidney.
CC       {ECO:0000269|PubMed:11904404}.
CC   -!- INDUCTION: By all-trans retinoic acid (ATRA). Up-regulated in
CC       colorectal carcinomas. {ECO:0000269|PubMed:11904404,
CC       ECO:0000269|PubMed:12214280}.
CC   -!- SIMILARITY: Belongs to the Nav/unc-53 family. {ECO:0000305}.
CC   -!- CAUTION: PubMed:15158073 experiments have been carried out in mouse.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92657.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB85038.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF466143; AAL96479.1; -; mRNA.
DR   EMBL; AF466144; AAL96480.1; -; mRNA.
DR   EMBL; AB063115; BAC00853.1; -; mRNA.
DR   EMBL; AB063116; BAC00854.1; -; mRNA.
DR   EMBL; AJ488102; CAD32471.1; -; mRNA.
DR   EMBL; AJ488203; CAD32556.1; -; mRNA.
DR   EMBL; AJ488204; CAD32557.1; -; mRNA.
DR   EMBL; AJ488205; CAD32558.1; -; mRNA.
DR   EMBL; AJ488206; CAD32559.1; -; mRNA.
DR   EMBL; AJ488207; CAD32560.1; -; mRNA.
DR   EMBL; AJ488208; CAD32561.1; -; mRNA.
DR   EMBL; AB037840; BAA92657.3; ALT_INIT; mRNA.
DR   EMBL; AK001495; BAA91723.1; -; mRNA.
DR   EMBL; AK001892; BAA91965.1; -; mRNA.
DR   EMBL; AK074287; BAB85038.1; ALT_FRAME; mRNA.
DR   EMBL; AC009549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC015684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC023950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016054; AAH16054.1; -; mRNA.
DR   CCDS; CCDS44552.1; -. [Q8IVL1-5]
DR   CCDS; CCDS53612.1; -. [Q8IVL1-4]
DR   CCDS; CCDS58126.1; -. [Q8IVL1-1]
DR   CCDS; CCDS7850.1; -. [Q8IVL1-3]
DR   CCDS; CCDS7851.2; -. [Q8IVL1-2]
DR   RefSeq; NP_001104488.1; NM_001111018.1. [Q8IVL1-4]
DR   RefSeq; NP_001104489.1; NM_001111019.2. [Q8IVL1-5]
DR   RefSeq; NP_001231892.1; NM_001244963.1. [Q8IVL1-1]
DR   RefSeq; NP_660093.2; NM_145117.4. [Q8IVL1-3]
DR   RefSeq; NP_892009.3; NM_182964.5. [Q8IVL1-2]
DR   RefSeq; XP_006718431.1; XM_006718368.3. [Q8IVL1-5]
DR   RefSeq; XP_011518754.1; XM_011520452.2.
DR   PDB; 2YRN; NMR; -; A=90-197.
DR   PDBsum; 2YRN; -.
DR   AlphaFoldDB; Q8IVL1; -.
DR   SMR; Q8IVL1; -.
DR   BioGRID; 124606; 29.
DR   IntAct; Q8IVL1; 13.
DR   MINT; Q8IVL1; -.
DR   STRING; 9606.ENSP00000379396; -.
DR   CarbonylDB; Q8IVL1; -.
DR   GlyConnect; 1961; 13 N-Linked glycans (7 sites).
DR   GlyGen; Q8IVL1; 8 sites, 15 N-linked glycans (7 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8IVL1; -.
DR   PhosphoSitePlus; Q8IVL1; -.
DR   BioMuta; NAV2; -.
DR   DMDM; 308153582; -.
DR   EPD; Q8IVL1; -.
DR   jPOST; Q8IVL1; -.
DR   MassIVE; Q8IVL1; -.
DR   MaxQB; Q8IVL1; -.
DR   PaxDb; Q8IVL1; -.
DR   PeptideAtlas; Q8IVL1; -.
DR   PRIDE; Q8IVL1; -.
DR   ProteomicsDB; 70724; -. [Q8IVL1-1]
DR   ProteomicsDB; 70725; -. [Q8IVL1-10]
DR   ProteomicsDB; 70726; -. [Q8IVL1-11]
DR   ProteomicsDB; 70727; -. [Q8IVL1-12]
DR   ProteomicsDB; 70728; -. [Q8IVL1-13]
DR   ProteomicsDB; 70729; -. [Q8IVL1-2]
DR   ProteomicsDB; 70730; -. [Q8IVL1-3]
DR   ProteomicsDB; 70731; -. [Q8IVL1-4]
DR   ProteomicsDB; 70732; -. [Q8IVL1-5]
DR   ProteomicsDB; 70733; -. [Q8IVL1-6]
DR   ProteomicsDB; 70734; -. [Q8IVL1-7]
DR   ProteomicsDB; 70735; -. [Q8IVL1-8]
DR   ProteomicsDB; 70736; -. [Q8IVL1-9]
DR   Antibodypedia; 2148; 105 antibodies from 25 providers.
DR   DNASU; 89797; -.
DR   Ensembl; ENST00000349880.9; ENSP00000309577.6; ENSG00000166833.23. [Q8IVL1-3]
DR   Ensembl; ENST00000360655.8; ENSP00000353871.4; ENSG00000166833.23. [Q8IVL1-4]
DR   Ensembl; ENST00000396085.6; ENSP00000379394.1; ENSG00000166833.23. [Q8IVL1-2]
DR   Ensembl; ENST00000396087.7; ENSP00000379396.3; ENSG00000166833.23. [Q8IVL1-1]
DR   Ensembl; ENST00000533917.5; ENSP00000437316.1; ENSG00000166833.23. [Q8IVL1-5]
DR   GeneID; 89797; -.
DR   KEGG; hsa:89797; -.
DR   MANE-Select; ENST00000349880.9; ENSP00000309577.6; NM_145117.5; NP_660093.2. [Q8IVL1-3]
DR   UCSC; uc001mpp.4; human. [Q8IVL1-1]
DR   CTD; 89797; -.
DR   DisGeNET; 89797; -.
DR   GeneCards; NAV2; -.
DR   HGNC; HGNC:15997; NAV2.
DR   HPA; ENSG00000166833; Tissue enhanced (brain, heart muscle).
DR   MIM; 607026; gene.
DR   neXtProt; NX_Q8IVL1; -.
DR   OpenTargets; ENSG00000166833; -.
DR   PharmGKB; PA31452; -.
DR   VEuPathDB; HostDB:ENSG00000166833; -.
DR   eggNOG; ENOG502QPT3; Eukaryota.
DR   GeneTree; ENSGT00940000155663; -.
DR   HOGENOM; CLU_001002_1_1_1; -.
DR   InParanoid; Q8IVL1; -.
DR   OMA; SSIYSTX; -.
DR   OrthoDB; 21830at2759; -.
DR   PhylomeDB; Q8IVL1; -.
DR   TreeFam; TF329881; -.
DR   PathwayCommons; Q8IVL1; -.
DR   SignaLink; Q8IVL1; -.
DR   SIGNOR; Q8IVL1; -.
DR   BioGRID-ORCS; 89797; 11 hits in 1078 CRISPR screens.
DR   ChiTaRS; NAV2; human.
DR   EvolutionaryTrace; Q8IVL1; -.
DR   GeneWiki; NAV2; -.
DR   GenomeRNAi; 89797; -.
DR   Pharos; Q8IVL1; Tbio.
DR   PRO; PR:Q8IVL1; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8IVL1; protein.
DR   Bgee; ENSG00000166833; Expressed in blood vessel layer and 199 other tissues.
DR   ExpressionAtlas; Q8IVL1; baseline and differential.
DR   Genevisible; Q8IVL1; HS.
DR   GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR   GO; GO:0021563; P:glossopharyngeal nerve development; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0022008; P:neurogenesis; IEA:InterPro.
DR   GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR   GO; GO:0003025; P:regulation of systemic arterial blood pressure by baroreceptor feedback; IEA:Ensembl.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   GO; GO:0021564; P:vagus nerve development; IEA:Ensembl.
DR   CDD; cd00014; CH; 1.
DR   Gene3D; 1.10.418.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR039041; Nav/unc-53.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12784; PTHR12784; 1.
DR   Pfam; PF00307; CH; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Coiled coil; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..2488
FT                   /note="Neuron navigator 2"
FT                   /id="PRO_0000267198"
FT   DOMAIN          85..192
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REGION          194..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          706..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1295..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1355..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1440..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1473..1560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1591..1629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1790..1887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1951..1985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2423..2488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          498..531
FT                   /evidence="ECO:0000255"
FT   COILED          743..771
FT                   /evidence="ECO:0000255"
FT   COILED          1686..1773
FT                   /evidence="ECO:0000255"
FT   COILED          1897..1964
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        214..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1047
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1125..1148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1295..1309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1473..1490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1496..1512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1541..1560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1591..1620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1790..1818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1819..1834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1858..1887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1958..1985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2455..2470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2157..2164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1977
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..1896
FT                   /note="Missing (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021924"
FT   VAR_SEQ         1..1578
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021925"
FT   VAR_SEQ         1..937
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021926"
FT   VAR_SEQ         1..89
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDTQ -> MESVSESSQQQKRKPVIH
FT                   GLEDQKR (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12214280"
FT                   /id="VSP_021927"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MSVMLWRWEQNNTTMKL
FT                   (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021928"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MESVSESSQQQKRKPVIHG
FT                   LEDQKR (in isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021929"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MQECDSKFFLPSGSNSGFT
FT                   LLSNQ (in isoform 12)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021930"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MAIDLYCGLACLWGIHEPR
FT                   (in isoform 13)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021931"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MLWPRNLT (in
FT                   isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021932"
FT   VAR_SEQ         1..88
FT                   /note="MPAILVASKMKSGLPKPVHSAAPILHVPPARAGPQPCYLKLGSKVEVSKTTY
FT                   PSQIPLKSQVLQGLQEPAGEGLPLRKSGSVENGFDT -> MAGTSAASSWGGGK (in
FT                   isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:15158073"
FT                   /id="VSP_021933"
FT   VAR_SEQ         256..278
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10718198,
FT                   ECO:0000303|PubMed:11904404, ECO:0000303|PubMed:12214280"
FT                   /id="VSP_021934"
FT   VAR_SEQ         938..945
FT                   /note="SLGLGDAD -> MLWPRNLT (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021935"
FT   VAR_SEQ         1480..1501
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021936"
FT   VAR_SEQ         1634..1666
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT                   5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:10718198,
FT                   ECO:0000303|PubMed:11904404, ECO:0000303|PubMed:12214280,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021937"
FT   VAR_SEQ         1832..1834
FT                   /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:11904404,
FT                   ECO:0000303|PubMed:12214280, ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021938"
FT   VARIANT         109
FT                   /note="R -> K (in dbSNP:rs6483617)"
FT                   /evidence="ECO:0000269|PubMed:12214280,
FT                   ECO:0000269|PubMed:15158073"
FT                   /id="VAR_029640"
FT   VARIANT         491
FT                   /note="Q -> H (in dbSNP:rs16937251)"
FT                   /id="VAR_029641"
FT   VARIANT         1041
FT                   /note="E -> D (in dbSNP:rs3802799)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_029642"
FT   VARIANT         1077
FT                   /note="P -> A (in dbSNP:rs3802800)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:11904404, ECO:0000269|PubMed:12214280,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15158073,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_029643"
FT   VARIANT         2374
FT                   /note="V -> I (in dbSNP:rs35891966)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_032252"
FT   CONFLICT        100
FT                   /note="A -> T (in Ref. 2; BAC00854 and 3; CAD32471)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        259
FT                   /note="S -> P (in Ref. 1; AAL96479/AAL96480 and 4;
FT                   BAA92657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="P -> S (in Ref. 3; CAD32471)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1046
FT                   /note="T -> M (in Ref. 7; BAB85038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1173
FT                   /note="G -> D (in Ref. 7; BAB85038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1845
FT                   /note="Missing (in Ref. 8; AAH16054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1939
FT                   /note="M -> V (in Ref. 7; BAB85038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2012
FT                   /note="E -> G (in Ref. 7; BAA91965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2053
FT                   /note="V -> A (in Ref. 7; BAA91723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2075
FT                   /note="L -> V (in Ref. 7; BAB85038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2296
FT                   /note="K -> E (in Ref. 7; BAA91965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2299
FT                   /note="E -> K (in Ref. 7; BAB85038)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2395
FT                   /note="M -> V (in Ref. 7; BAA91723)"
FT                   /evidence="ECO:0000305"
FT   HELIX           86..101
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   HELIX           119..128
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   HELIX           145..159
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   HELIX           169..174
FT                   /evidence="ECO:0007829|PDB:2YRN"
FT   HELIX           177..191
FT                   /evidence="ECO:0007829|PDB:2YRN"
SQ   SEQUENCE   2488 AA;  268167 MW;  0AEDD1C1469A11A8 CRC64;
     MPAILVASKM KSGLPKPVHS AAPILHVPPA RAGPQPCYLK LGSKVEVSKT TYPSQIPLKS
     QVLQGLQEPA GEGLPLRKSG SVENGFDTQI YTDWANHYLA KSGHKRLIRD LQQDVTDGVL
     LAQIIQVVAN EKIEDINGCP KNRSQMIENI DACLNFLAAK GINIQGLSAE EIRNGNLKAI
     LGLFFSLSRY KQQQQQPQKQ HLSSPLPPAV SQVAGAPSQC QAGTPQQQVP VTPQAPCQPH
     QPAPHQQSKA QAEMQSSASS KDSSQSKIIR FTLGQKKISR LPGPTARVSA AGSEAKTRGG
     STTANNRRSQ SFNNYDKSKP VTSPPPPPSS HEKEPLASSA SSHPGMSDNA PASLESGSSS
     TPTNCSTSSA IPQPGAATKP WRSKSLSVKH SATVSMLSVK PPGPEAPRPT PEAMKPAPNN
     QKSMLEKLKL FNSKGGSKAG EGPGSRDTSC ERLETLPSFE ESEELEAASR MLTTVGPASS
     SPKIALKGIA QRTFSRALTN KKSSLKGNEK EKEKQQREKD KEKSKDLAKR ASVTERLDLK
     EEPKEDPSGA AVPEMPKKSS KIASFIPKGG KLNSAKKEPM APSHSGIPKP GMKSMPGKSP
     SAPAPSKEGE RSRSGKLSSG LPQQKPQLDG RHSSSSSSLA SSEGKGPGGT TLNHSISSQT
     VSGSVGTTQT TGSNTVSVQL PQPQQQYNHP NTATVAPFLY RSQTDTEGNV TAESSSTGVS
     VEPSHFTKTG QPALEELTGE DPEARRLRTV KNIADLRQNL EETMSSLRGT QVTHSTLETT
     FDTNVTTEMS GRSILSLTGR PTPLSWRLGQ SSPRLQAGDA PSMGNGYPPR ANASRFINTE
     SGRYVYSAPL RRQLASRGSS VCHVDVSDKA GDEMDLEGIS MDAPGYMSDG DVLSKNIRTD
     DITSGYMTDG GLGLYTRRLN RLPDGMAVVR ETLQRNTSLG LGDADSWDDS SSVSSGISDT
     IDNLSTDDIN TSSSISSYAN TPASSRKNLD VQTDAEKHSQ VERNSLWSGD DVKKSDGGSD
     SGIKMEPGSK WRRNPSDVSD ESDKSTSGKK NPVISQTGSW RRGMTAQVGI TMPRTKPSAP
     AGALKTPGTG KTDDAKVSEK GRLSPKASQV KRSPSDAGRS SGDESKKPLP SSSRTPTANA
     NSFGFKKQSG SAAGLAMITA SGVTVTSRSA TLGKIPKSSA LVSRSAGRKS SMDGAQNQDD
     GYLALSSRTN LQYRSLPRPS KSNSRNGAGN RSSTSSIDSN ISSKSAGLPV PKLREPSKTA
     LGSSLPGLVN QTDKEKGISS DNESVASCNS VKVNPAAQPV SSPAQTSLQP GAKYPDVASP
     TLRRLFGGKP TKQVPIATAE NMKNSVVISN PHATMTQQGN LDSPSGSGVL SSGSSSPLYS
     KNVDLNQSPL ASSPSSAHSA PSNSLTWGTN ASSSSAVSKD GLGFQSVSSL HTSCESIDIS
     LSSGGVPSHN SSTGLIASSK DDSLTPFVRT NSVKTTLSES PLSSPAASPK FCRSTLPRKQ
     DSDPHLDRNT LPKKGLRYTP TSQLRTQEDA KEWLRSHSAG GLQDTAANSP FSSGSSVTSP
     SGTRFNFSQL ASPTTVTQMS LSNPTMLRTH SLSNADGQYD PYTDSRFRNS SMSLDEKSRT
     MSRSGSFRDG FEEESWEKSS VDNFVSRLHS SLHFSLPLFH HARYELVHGS SLSLVSSTSS
     VYSTPEEKCQ SEIRKLRREL DASQEKVSAL TTQLTANAHL VAAFEQSLGN MTIRLQSLTM
     TAEQKDSELN ELRKTIELLK KQNAAAQAAI NGVINTPELN CKGNGTAQSA DLRIRRQHSS
     DSVSSINSAT SHSSVGSNIE SDSKKKKRKN WVNELRSSFK QAFGKKKSPK SASSHSDIEE
     MTDSSLPSSP KLPHNGSTGS TPLLRNSHSN SLISECMDSE AETVMQLRNE LRDKEMKLTD
     IRLEALSSAH QLDQLREAMN RMQSEIEKLK AENDRLKSES QGSGCSRAPS QVSISASPRQ
     SMGLSQHSLN LTESTSLDML LDDTGECSAR KEGGRHVKIV VSFQEEMKWK EDSRPHLFLI
     GCIGVSGKTK WDVLDGVVRR LFKEYIIHVD PVSQLGLNSD SVLGYSIGEI KRSNTSETPE
     LLPCGYLVGE NTTISVTVKG LAENSLDSLV FESLIPKPIL QRYVSLLIEH RRIILSGPSG
     TGKTYLANRL SEYIVLREGR ELTDGVIATF NVDHKSSKEL RQYLSNLADQ CNSENNAVDM
     PLVIILDNLH HVSSLGEIFN GLLNCKYHKC PYIIGTMNQA TSSTPNLQLH HNFRWVLCAN
     HTEPVKGFLG RFLRRKLMET EISGRVRNME LVKIIDWIPK VWHHLNRFLE AHSSSDVTIG
     PRLFLSCPID VDGSRVWFTD LWNYSIIPYL LEAVREGLQL YGRRAPWEDP AKWVMDTYPW
     AASPQQHEWP PLLQLRPEDV GFDGYSMPRE GSTSKQMPPS DAEGDPLMNM LMRLQEAANY
     SSPQSYDSDS NSNSHHDDIL DSSLESTL
 
 
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