GenomeNet

Database: UniProt
Entry: Q96PY6
LinkDB: Q96PY6
Original site: Q96PY6 
ID   NEK1_HUMAN              Reviewed;        1258 AA.
AC   Q96PY6; G5E9Z3; Q05DG5; Q14CB7; Q5H9T1; Q6PIB8; Q96SS2; Q9H6P7; Q9Y594;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   29-SEP-2021, entry version 192.
DE   RecName: Full=Serine/threonine-protein kinase Nek1;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:20230784};
DE   AltName: Full=Never in mitosis A-related kinase 1;
DE            Short=NimA-related protein kinase 1;
DE   AltName: Full=Renal carcinoma antigen NY-REN-55;
GN   Name=NEK1; Synonyms=KIAA1901;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXI. The
RT   complete sequences of 60 new cDNA clones from brain which code for large
RT   proteins.";
RL   DNA Res. 8:179-187(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT GLY-724.
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Bone marrow, and 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-1258 (ISOFORM 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 865-1258.
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 [MRNA] OF 444-1258 (ISOFORM 2), AND IDENTIFICATION AS A
RP   RENAL CANCER ANTIGEN.
RC   TISSUE=Renal cell carcinoma;
RX   PubMed=10508479;
RX   DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA   Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA   Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA   Old L.J.;
RT   "Antigens recognized by autologous antibody in patients with renal-cell
RT   carcinoma.";
RL   Int. J. Cancer 83:456-464(1999).
RN   [8]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15604234; DOI=10.1158/0008-5472.can-04-2243;
RA   Polci R., Peng A., Chen P.L., Riley D.J., Chen Y.;
RT   "NIMA-related protein kinase 1 is involved early in the ionizing radiation-
RT   induced DNA damage response.";
RL   Cancer Res. 64:8800-8803(2004).
RN   [9]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=18843199; DOI=10.4161/cc.7.20.6815;
RA   Chen Y., Chen P.L., Chen C.F., Jiang X., Riley D.J.;
RT   "Never-in-mitosis related kinase 1 functions in DNA damage response and
RT   checkpoint control.";
RL   Cell Cycle 7:3194-3201(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414; SER-418; SER-428;
RP   SER-653; SER-798; SER-834; SER-868 AND SER-881, AND IDENTIFICATION BY MASS
RP   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   [13]
RP   FUNCTION IN PHOSPHORYLATION OF VDAC1, AND CATALYTIC ACTIVITY.
RX   PubMed=20230784; DOI=10.1016/j.bbrc.2010.03.077;
RA   Chen Y., Gaczynska M., Osmulski P., Polci R., Riley D.J.;
RT   "Phosphorylation by Nek1 regulates opening and closing of voltage dependent
RT   anion channel 1.";
RL   Biochem. Biophys. Res. Commun. 394:798-803(2010).
RN   [14]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN
RP   DIGENIC SHORT-RIB THORACIC DYSPLASIA 3/6 WITH POLYDACTYLY.
RX   PubMed=21211617; DOI=10.1016/j.ajhg.2010.12.004;
RA   Thiel C., Kessler K., Giessl A., Dimmler A., Shalev S.A., von der Haar S.,
RA   Zenker M., Zahnleiter D., Stoess H., Beinder E., Abou Jamra R., Ekici A.B.,
RA   Schroeder-Kress N., Aigner T., Kirchner T., Reis A., Brandstaetter J.H.,
RA   Rauch A.;
RT   "NEK1 mutations cause short-rib polydactyly syndrome type majewski.";
RL   Am. J. Hum. Genet. 88:106-114(2011).
RN   [15]
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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-428; THR-661;
RP   SER-664; SER-868; SER-881 AND SER-1052, AND IDENTIFICATION BY MASS
RP   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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052, AND IDENTIFICATION BY
RP   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   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP   CFAP410 AND SPATA7 BY MASS SPECTROMETRY, AND INTERACTION WITH CFAP410.
RX   PubMed=26167768; DOI=10.1038/ncb3201;
RG   UK10K Consortium;
RG   University of Washington Center for Mendelian Genomics;
RA   Wheway G., Schmidts M., Mans D.A., Szymanska K., Nguyen T.M., Racher H.,
RA   Phelps I.G., Toedt G., Kennedy J., Wunderlich K.A., Sorusch N.,
RA   Abdelhamed Z.A., Natarajan S., Herridge W., van Reeuwijk J., Horn N.,
RA   Boldt K., Parry D.A., Letteboer S.J., Roosing S., Adams M., Bell S.M.,
RA   Bond J., Higgins J., Morrison E.E., Tomlinson D.C., Slaats G.G.,
RA   van Dam T.J., Huang L., Kessler K., Giessl A., Logan C.V., Boyle E.A.,
RA   Shendure J., Anazi S., Aldahmesh M., Al Hazzaa S., Hegele R.A., Ober C.,
RA   Frosk P., Mhanni A.A., Chodirker B.N., Chudley A.E., Lamont R.,
RA   Bernier F.P., Beaulieu C.L., Gordon P., Pon R.T., Donahue C.,
RA   Barkovich A.J., Wolf L., Toomes C., Thiel C.T., Boycott K.M., McKibbin M.,
RA   Inglehearn C.F., Stewart F., Omran H., Huynen M.A., Sergouniotis P.I.,
RA   Alkuraya F.S., Parboosingh J.S., Innes A.M., Willoughby C.E., Giles R.H.,
RA   Webster A.R., Ueffing M., Blacque O., Gleeson J.G., Wolfrum U.,
RA   Beales P.L., Gibson T., Doherty D., Mitchison H.M., Roepman R.,
RA   Johnson C.A.;
RT   "An siRNA-based functional genomics screen for the identification of
RT   regulators of ciliogenesis and ciliopathy genes.";
RL   Nat. Cell Biol. 17:1074-1087(2015).
RN   [19]
RP   VARIANTS [LARGE SCALE ANALYSIS] PHE-10; LYS-25; VAL-76; PRO-294; GLY-355;
RP   VAL-463; THR-598; GLY-724; ASN-745; GLU-883 AND ASN-1180.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [20]
RP   VARIANTS SRTD6 ARG-145 AND SER-253.
RX   PubMed=22499340; DOI=10.1136/jmedgenet-2011-100717;
RA   El Hokayem J., Huber C., Couve A., Aziza J., Baujat G., Bouvier R.,
RA   Cavalcanti D.P., Collins F.A., Cordier M.P., Delezoide A.L., Gonzales M.,
RA   Johnson D., Le Merrer M., Levy-Mozziconacci A., Loget P.,
RA   Martin-Coignard D., Martinovic J., Mortier G.R., Perez M.J., Roume J.,
RA   Scarano G., Munnich A., Cormier-Daire V.;
RT   "NEK1 and DYNC2H1 are both involved in short rib polydactyly Majewski type
RT   but not in Beemer Langer cases.";
RL   J. Med. Genet. 49:227-233(2012).
RN   [21]
RP   INVOLVEMENT IN ALS24, AND VARIANTS ALS24 784-ARG--GLU-1258 DEL AND
RP   1008-SER--GLU-1258 DEL.
RX   PubMed=26945885; DOI=10.1093/brain/aww033;
RA   Brenner D., Mueller K., Wieland T., Weydt P., Boehm S., Lule D.,
RA   Huebers A., Neuwirth C., Weber M., Borck G., Wahlqvist M., Danzer K.M.,
RA   Volk A.E., Meitinger T., Strom T.M., Otto M., Kassubek J., Ludolph A.C.,
RA   Andersen P.M., Weishaupt J.H.;
RT   "NEK1 mutations in familial amyotrophic lateral sclerosis.";
RL   Brain 139:E28-E28(2016).
RN   [22]
RP   INVOLVEMENT IN ALS24, AND VARIANTS ALS24 HIS-261 AND 550-ARG--GLU-1258 DEL.
RX   PubMed=27455347; DOI=10.1038/ng.3626;
RA   Kenna K.P., van Doormaal P.T., Dekker A.M., Ticozzi N., Kenna B.J.,
RA   Diekstra F.P., van Rheenen W., van Eijk K.R., Jones A.R., Keagle P.,
RA   Shatunov A., Sproviero W., Smith B.N., van Es M.A., Topp S.D., Kenna A.,
RA   Miller J.W., Fallini C., Tiloca C., McLaughlin R.L., Vance C., Troakes C.,
RA   Colombrita C., Mora G., Calvo A., Verde F., Al-Sarraj S., King A.,
RA   Calini D., de Belleroche J., Baas F., van der Kooi A.J., de Visser M.,
RA   Ten Asbroek A.L., Sapp P.C., McKenna-Yasek D., Polak M., Asress S.,
RA   Munoz-Blanco J.L., Strom T.M., Meitinger T., Morrison K.E., Lauria G.,
RA   Williams K.L., Leigh P.N., Nicholson G.A., Blair I.P., Leblond C.S.,
RA   Dion P.A., Rouleau G.A., Pall H., Shaw P.J., Turner M.R., Talbot K.,
RA   Taroni F., Boylan K.B., Van Blitterswijk M., Rademakers R.,
RA   Esteban-Perez J., Garcia-Redondo A., Van Damme P., Robberecht W., Chio A.,
RA   Gellera C., Drepper C., Sendtner M., Ratti A., Glass J.D., Mora J.S.,
RA   Basak N.A., Hardiman O., Ludolph A.C., Andersen P.M., Weishaupt J.H.,
RA   Brown R.H. Jr., Al-Chalabi A., Silani V., Shaw C.E., van den Berg L.H.,
RA   Veldink J.H., Landers J.E.;
RT   "NEK1 variants confer susceptibility to amyotrophic lateral sclerosis.";
RL   Nat. Genet. 48:1037-1042(2016).
CC   -!- FUNCTION: Phosphorylates serines and threonines, but also appears to
CC       possess tyrosine kinase activity (PubMed:20230784). Involved in DNA
CC       damage checkpoint control and for proper DNA damage repair
CC       (PubMed:20230784). In response to injury that includes DNA damage, NEK1
CC       phosphorylates VDAC1 to limit mitochondrial cell death
CC       (PubMed:20230784). May be implicated in the control of meiosis (By
CC       similarity). Involved in cilium assembly (PubMed:21211617).
CC       {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:20230784,
CC       ECO:0000269|PubMed:21211617}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:20230784};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20230784};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Binds to CBY2 (By similarity). Found in a complex with
CC       CFAP410, NEK1 and SPATA7 (PubMed:26167768). Interacts with CFAP410
CC       (PubMed:26167768). Interacts (via Ser-1052 phosphorylated form) with
CC       14-3-3 proteins (By similarity). {ECO:0000250|UniProtKB:P51954,
CC       ECO:0000269|PubMed:26167768}.
CC   -!- INTERACTION:
CC       Q96PY6; Q99689: FEZ1; NbExp=2; IntAct=EBI-373615, EBI-396435;
CC       Q96PY6; Q9UHY8: FEZ2; NbExp=2; IntAct=EBI-373615, EBI-396453;
CC       Q96PY6; Q5S007: LRRK2; NbExp=2; IntAct=EBI-373615, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15604234,
CC       ECO:0000305|PubMed:21211617}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P51954}. Cytoplasm
CC       {ECO:0000269|PubMed:18843199}. Note=Associated with the pericentriolar
CC       material (PubMed:21211617). Localizes to centrosome during interphase
CC       and mitosis (By similarity). Translocated from cytoplasm to discrete
CC       nuclear foci at sites of DNA damage (PubMed:15604234).
CC       {ECO:0000250|UniProtKB:P51954, ECO:0000269|PubMed:15604234,
CC       ECO:0000269|PubMed:21211617}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q96PY6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96PY6-2; Sequence=VSP_004870;
CC       Name=3;
CC         IsoId=Q96PY6-3; Sequence=VSP_035439;
CC       Name=4;
CC         IsoId=Q96PY6-4; Sequence=VSP_035435, VSP_035436;
CC       Name=5;
CC         IsoId=Q96PY6-5; Sequence=VSP_035437, VSP_035438;
CC       Name=6;
CC         IsoId=Q96PY6-6; Sequence=VSP_035436, VSP_035439;
CC   -!- TISSUE SPECIFICITY: High fetal expression in the brain and kidney.
CC       {ECO:0000269|PubMed:21211617}.
CC   -!- DISEASE: Short-rib thoracic dysplasia 6 with or without polydactyly
CC       (SRTD6) [MIM:263520]: A form of short-rib thoracic dysplasia, a group
CC       of autosomal recessive ciliopathies that are characterized by a
CC       constricted thoracic cage, short ribs, shortened tubular bones, and a
CC       'trident' appearance of the acetabular roof. Polydactyly is variably
CC       present. Non-skeletal involvement can include cleft lip/palate as well
CC       as anomalies of major organs such as the brain, eye, heart, kidneys,
CC       liver, pancreas, intestines, and genitalia. Some forms of the disease
CC       are lethal in the neonatal period due to respiratory insufficiency
CC       secondary to a severely restricted thoracic cage, whereas others are
CC       compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC       syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC       Saldino syndrome, and short rib-polydactyly syndrome.
CC       {ECO:0000269|PubMed:22499340}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry. In some cases NEK1
CC       mutations result in disease phenotype in the presence of mutations in
CC       DYNC2H1 indicating digenic inheritance (digenic short rib-polydactyly
CC       syndrome 3/6 with polydactyly) (PubMed:21211617).
CC       {ECO:0000269|PubMed:21211617}.
CC   -!- DISEASE: Amyotrophic lateral sclerosis 24 (ALS24) [MIM:617892]: A form
CC       of amyotrophic lateral sclerosis, a neurodegenerative disorder
CC       affecting upper motor neurons in the brain and lower motor neurons in
CC       the brain stem and spinal cord, resulting in fatal paralysis. Sensory
CC       abnormalities are absent. The pathologic hallmarks of the disease
CC       include pallor of the corticospinal tract due to loss of motor neurons,
CC       presence of ubiquitin-positive inclusions within surviving motor
CC       neurons, and deposition of pathologic aggregates. The etiology of
CC       amyotrophic lateral sclerosis is likely to be multifactorial, involving
CC       both genetic and environmental factors. The disease is inherited in 5-
CC       10% of the cases. {ECO:0000269|PubMed:26945885,
CC       ECO:0000269|PubMed:27455347}. Note=Disease susceptibility is associated
CC       with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH15147.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAB15207.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55209.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB67794.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB067488; BAB67794.1; ALT_INIT; mRNA.
DR   EMBL; CR933642; CAI45943.1; -; mRNA.
DR   EMBL; AC116615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC084724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471056; EAX04791.1; -; Genomic_DNA.
DR   EMBL; BC015147; AAH15147.1; ALT_SEQ; mRNA.
DR   EMBL; BC037790; AAH37790.1; -; mRNA.
DR   EMBL; BC114491; AAI14492.1; -; mRNA.
DR   EMBL; AK025658; BAB15207.1; ALT_INIT; mRNA.
DR   EMBL; AK027580; BAB55209.1; ALT_INIT; mRNA.
DR   EMBL; AF155113; AAD42879.1; -; mRNA.
DR   CCDS; CCDS47162.1; -. [Q96PY6-1]
DR   CCDS; CCDS56348.1; -. [Q96PY6-4]
DR   CCDS; CCDS56349.1; -. [Q96PY6-2]
DR   CCDS; CCDS56350.1; -. [Q96PY6-6]
DR   CCDS; CCDS56351.1; -. [Q96PY6-3]
DR   RefSeq; NP_001186326.1; NM_001199397.1. [Q96PY6-3]
DR   RefSeq; NP_001186327.1; NM_001199398.1. [Q96PY6-6]
DR   RefSeq; NP_001186328.1; NM_001199399.1. [Q96PY6-4]
DR   RefSeq; NP_001186329.1; NM_001199400.1. [Q96PY6-2]
DR   RefSeq; NP_036356.1; NM_012224.2. [Q96PY6-1]
DR   RefSeq; XP_011530305.1; XM_011532003.1.
DR   RefSeq; XP_011530306.1; XM_011532004.1. [Q96PY6-2]
DR   PDB; 4APC; X-ray; 2.10 A; A/B=1-328.
DR   PDB; 4B9D; X-ray; 1.90 A; A/B=1-328.
DR   PDBsum; 4APC; -.
DR   PDBsum; 4B9D; -.
DR   SMR; Q96PY6; -.
DR   BioGRID; 110825; 47.
DR   IntAct; Q96PY6; 42.
DR   STRING; 9606.ENSP00000424757; -.
DR   BindingDB; Q96PY6; -.
DR   ChEMBL; CHEMBL5855; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   GuidetoPHARMACOLOGY; 2114; -.
DR   iPTMnet; Q96PY6; -.
DR   PhosphoSitePlus; Q96PY6; -.
DR   BioMuta; NEK1; -.
DR   DMDM; 22256934; -.
DR   jPOST; Q96PY6; -.
DR   MassIVE; Q96PY6; -.
DR   MaxQB; Q96PY6; -.
DR   PaxDb; Q96PY6; -.
DR   PeptideAtlas; Q96PY6; -.
DR   PRIDE; Q96PY6; -.
DR   ProteomicsDB; 34091; -.
DR   ProteomicsDB; 77788; -. [Q96PY6-1]
DR   ProteomicsDB; 77789; -. [Q96PY6-2]
DR   ProteomicsDB; 77790; -. [Q96PY6-3]
DR   ProteomicsDB; 77791; -. [Q96PY6-4]
DR   ProteomicsDB; 77792; -. [Q96PY6-5]
DR   TopDownProteomics; Q96PY6-3; -. [Q96PY6-3]
DR   Antibodypedia; 28454; 151 antibodies.
DR   DNASU; 4750; -.
DR   Ensembl; ENST00000439128; ENSP00000408020; ENSG00000137601. [Q96PY6-1]
DR   Ensembl; ENST00000507142; ENSP00000424757; ENSG00000137601. [Q96PY6-3]
DR   Ensembl; ENST00000510533; ENSP00000427653; ENSG00000137601. [Q96PY6-2]
DR   Ensembl; ENST00000511633; ENSP00000423332; ENSG00000137601. [Q96PY6-6]
DR   Ensembl; ENST00000512193; ENSP00000424938; ENSG00000137601. [Q96PY6-4]
DR   GeneID; 4750; -.
DR   KEGG; hsa:4750; -.
DR   UCSC; uc003isb.3; human. [Q96PY6-1]
DR   CTD; 4750; -.
DR   DisGeNET; 4750; -.
DR   GeneCards; NEK1; -.
DR   GeneReviews; NEK1; -.
DR   HGNC; HGNC:7744; NEK1.
DR   HPA; ENSG00000137601; Low tissue specificity.
DR   MalaCards; NEK1; -.
DR   MIM; 263520; phenotype.
DR   MIM; 604588; gene.
DR   MIM; 617892; phenotype.
DR   neXtProt; NX_Q96PY6; -.
DR   OpenTargets; ENSG00000137601; -.
DR   Orphanet; 803; Amyotrophic lateral sclerosis.
DR   Orphanet; 2751; Orofaciodigital syndrome type 2.
DR   Orphanet; 93269; Short rib-polydactyly syndrome, Majewski type.
DR   PharmGKB; PA31545; -.
DR   VEuPathDB; HostDB:ENSG00000137601; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   GeneTree; ENSGT00940000158460; -.
DR   HOGENOM; CLU_000288_60_1_1; -.
DR   InParanoid; Q96PY6; -.
DR   OMA; TLMDVPI; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; Q96PY6; -.
DR   TreeFam; TF333575; -.
DR   PathwayCommons; Q96PY6; -.
DR   SignaLink; Q96PY6; -.
DR   SIGNOR; Q96PY6; -.
DR   BioGRID-ORCS; 4750; 34 hits in 1056 CRISPR screens.
DR   ChiTaRS; NEK1; human.
DR   GeneWiki; NEK1; -.
DR   GenomeRNAi; 4750; -.
DR   Pharos; Q96PY6; Tchem.
DR   PRO; PR:Q96PY6; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q96PY6; protein.
DR   Bgee; ENSG00000137601; Expressed in trigeminal ganglion and 245 other tissues.
DR   ExpressionAtlas; Q96PY6; baseline and differential.
DR   Genevisible; Q96PY6; HS.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
DR   GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IMP:CACAO.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106311; F:protein threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0042769; P:DNA damage response, detection of DNA damage; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:CACAO.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amyotrophic lateral sclerosis;
KW   ATP-binding; Cell cycle; Cell division; Ciliopathy;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Kinase; Magnesium;
KW   Metal-binding; Mitosis; Neurodegeneration; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..1258
FT                   /note="Serine/threonine-protein kinase Nek1"
FT                   /id="PRO_0000086418"
FT   DOMAIN          4..258
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         10..18
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          330..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         33
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         156
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         162
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51954"
FT   MOD_RES         653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         661
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         664
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         834
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         868
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         881
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1052
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51954"
FT   VAR_SEQ         398..422
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035435"
FT   VAR_SEQ         477..520
FT                   /note="Missing (in isoform 4 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035436"
FT   VAR_SEQ         478..521
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10508479"
FT                   /id="VSP_004870"
FT   VAR_SEQ         522..527
FT                   /note="QKGQLA -> LDCDDP (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_035437"
FT   VAR_SEQ         528..1258
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_035438"
FT   VAR_SEQ         555
FT                   /note="M -> MGILQNLAAMYGGRPSSSRGGKPRNKEEE (in isoform 3 and
FT                   isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_035439"
FT   VARIANT         10
FT                   /note="I -> F (in dbSNP:rs34214559)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040900"
FT   VARIANT         25
FT                   /note="E -> K (in a lung large cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040901"
FT   VARIANT         76
FT                   /note="L -> V (in dbSNP:rs35093214)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040902"
FT   VARIANT         145
FT                   /note="G -> R (in SRTD6; dbSNP:rs431905508)"
FT                   /evidence="ECO:0000269|PubMed:22499340"
FT                   /id="VAR_069617"
FT   VARIANT         253
FT                   /note="L -> S (in SRTD6)"
FT                   /evidence="ECO:0000269|PubMed:22499340"
FT                   /id="VAR_069618"
FT   VARIANT         261
FT                   /note="R -> H (in ALS24; associated with disease
FT                   susceptibility; dbSNP:rs200161705)"
FT                   /evidence="ECO:0000269|PubMed:27455347"
FT                   /id="VAR_080694"
FT   VARIANT         294
FT                   /note="A -> P (in a lung adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040903"
FT   VARIANT         355
FT                   /note="R -> G (in dbSNP:rs35763578)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040904"
FT   VARIANT         463
FT                   /note="A -> V (in dbSNP:rs34540355)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040905"
FT   VARIANT         550..1258
FT                   /note="Missing (in ALS24; associated with disease
FT                   susceptibility)"
FT                   /evidence="ECO:0000269|PubMed:27455347"
FT                   /id="VAR_080695"
FT   VARIANT         598
FT                   /note="A -> T (in dbSNP:rs33933790)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046486"
FT   VARIANT         717
FT                   /note="N -> K (in dbSNP:rs34324114)"
FT                   /id="VAR_061743"
FT   VARIANT         724
FT                   /note="E -> G (in dbSNP:rs34099167)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_051651"
FT   VARIANT         745
FT                   /note="K -> N"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040906"
FT   VARIANT         784..1258
FT                   /note="Missing (in ALS24; associated with disease
FT                   susceptibility)"
FT                   /evidence="ECO:0000269|PubMed:26945885"
FT                   /id="VAR_080696"
FT   VARIANT         883
FT                   /note="Q -> E (in dbSNP:rs6828134)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046488"
FT   VARIANT         1008..1258
FT                   /note="Missing (in ALS24; associated with disease
FT                   susceptibility)"
FT                   /evidence="ECO:0000269|PubMed:26945885"
FT                   /id="VAR_080697"
FT   VARIANT         1180
FT                   /note="D -> N (in dbSNP:rs35503975)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_046489"
FT   CONFLICT        250
FT                   /note="N -> D (in Ref. 2; CAI45943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="R -> RK (in Ref. 2; CAI45943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1232
FT                   /note="G -> E (in Ref. 7; AAD42879)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          18..23
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           42..57
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           88..94
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           102..121
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           155..164
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           182..198
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           208..217
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           229..238
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           243..245
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           249..253
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           256..259
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           260..264
FT                   /evidence="ECO:0007829|PDB:4B9D"
FT   HELIX           268..275
FT                   /evidence="ECO:0007829|PDB:4B9D"
SQ   SEQUENCE   1258 AA;  142828 MW;  339C4BFA56612530 CRC64;
     MEKYVRLQKI GEGSFGKAIL VKSTEDGRQY VIKEINISRM SSKEREESRR EVAVLANMKH
     PNIVQYRESF EENGSLYIVM DYCEGGDLFK RINAQKGVLF QEDQILDWFV QICLALKHVH
     DRKILHRDIK SQNIFLTKDG TVQLGDFGIA RVLNSTVELA RTCIGTPYYL SPEICENKPY
     NNKSDIWALG CVLYELCTLK HAFEAGSMKN LVLKIISGSF PPVSLHYSYD LRSLVSQLFK
     RNPRDRPSVN SILEKGFIAK RIEKFLSPQL IAEEFCLKTF SKFGSQPIPA KRPASGQNSI
     SVMPAQKITK PAAKYGIPLA YKKYGDKKLH EKKPLQKHKQ AHQTPEKRVN TGEERRKISE
     EAARKRRLEF IEKEKKQKDQ IISLMKAEQM KRQEKERLER INRAREQGWR NVLSAGGSGE
     VKAPFLGSGG TIAPSSFSSR GQYEHYHAIF DQMQQQRAED NEAKWKREIY GRGLPERGIL
     PGVRPGFPYG AAGHHHFPDA DDIRKTLKRL KAVSKQANAN RQKGQLAVER AKQVEEFLQR
     KREAMQNKAR AEGHMVYLAR LRQIRLQNFN ERQQIKAKLR GEKKEANHSE GQEGSEEADM
     RRKKIESLKA HANARAAVLK EQLERKRKEA YEREKKVWEE HLVAKGVKSS DVSPPLGQHE
     TGGSPSKQQM RSVISVTSAL KEVGVDSSLT DTRETSEEMQ KTNNAISSKR EILRRLNENL
     KAQEDEKGKQ NLSDTFEINV HEDAKEHEKE KSVSSDRKKW EAGGQLVIPL DELTLDTSFS
     TTERHTVGEV IKLGPNGSPR RAWGKSPTDS VLKILGEAEL QLQTELLENT TIRSEISPEG
     EKYKPLITGE KKVQCISHEI NPSAIVDSPV ETKSPEFSEA SPQMSLKLEG NLEEPDDLET
     EILQEPSGTN KDESLPCTIT DVWISEEKET KETQSADRIT IQENEVSEDG VSSTVDQLSD
     IHIEPGTNDS QHSKCDVDKS VQPEPFFHKV VHSEHLNLVP QVQSVQCSPE ESFAFRSHSH
     LPPKNKNKNS LLIGLSTGLF DANNPKMLRT CSLPDLSKLF RTLMDVPTVG DVRQDNLEID
     EIEDENIKEG PSDSEDIVFE ETDTDLQELQ ASMEQLLREQ PGEEYSEEEE SVLKNSDVEP
     TANGTDVADE DDNPSSESAL NEEWHSDNSD GEIASECECD SVFNHLEELR LHLEQEMGFE
     KFFEVYEKIK AIHEDEDENI EICSKIVQNI LGNEHQHLYA KILHLVMADG AYQEDNDE
//
DBGET integrated database retrieval system