NEK1_HUMAN
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 03-AUG-2022, entry version 195.
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};
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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 AlphaFoldDB; Q96PY6; -.
DR SMR; Q96PY6; -.
DR BioGRID; 110825; 64.
DR IntAct; Q96PY6; 42.
DR MINT; Q96PY6; -.
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 EPD; Q96PY6; -.
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; 157 antibodies from 27 providers.
DR DNASU; 4750; -.
DR Ensembl; ENST00000439128.6; ENSP00000408020.2; ENSG00000137601.18. [Q96PY6-1]
DR Ensembl; ENST00000507142.6; ENSP00000424757.2; ENSG00000137601.18. [Q96PY6-3]
DR Ensembl; ENST00000510533.5; ENSP00000427653.1; ENSG00000137601.18. [Q96PY6-2]
DR Ensembl; ENST00000511633.5; ENSP00000423332.1; ENSG00000137601.18. [Q96PY6-6]
DR Ensembl; ENST00000512193.5; ENSP00000424938.1; ENSG00000137601.18. [Q96PY6-4]
DR GeneID; 4750; -.
DR KEGG; hsa:4750; -.
DR MANE-Select; ENST00000507142.6; ENSP00000424757.2; NM_001199397.3; NP_001186326.1. [Q96PY6-3]
DR UCSC; uc003isb.3; human. [Q96PY6-1]
DR CTD; 4750; -.
DR DisGeNET; 4750; -.
DR GeneCards; 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; EPKTHPP; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; Q96PY6; -.
DR TreeFam; TF333575; -.
DR PathwayCommons; Q96PY6; -.
DR SignaLink; Q96PY6; -.
DR SIGNOR; Q96PY6; -.
DR BioGRID-ORCS; 4750; 38 hits in 1120 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 secondary oocyte and 211 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:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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: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 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 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
