CENPF_HUMAN
ID CENPF_HUMAN Reviewed; 3114 AA.
AC P49454; Q13171; Q13246; Q5VVM7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Centromere protein F;
DE Short=CENP-F;
DE AltName: Full=AH antigen;
DE AltName: Full=Kinetochore protein CENPF;
DE AltName: Full=Mitosin;
DE Flags: Precursor;
GN Name=CENPF;
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], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND VARIANTS LEU-250; GLY-272 AND LYS-3106.
RC TISSUE=Mammary carcinoma;
RX PubMed=7542657; DOI=10.1083/jcb.130.3.507;
RA Liao H., Winkfein R.J., Mack G., Rattner J.B., Yen T.J.;
RT "CENP-F is a protein of the nuclear matrix that assembles onto kinetochores
RT at late G2 and is rapidly degraded after mitosis.";
RL J. Cell Biol. 130:507-518(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RB1, SUBCELLULAR
RP LOCATION, AND VARIANT LYS-3106.
RX PubMed=7651420; DOI=10.1128/mcb.15.9.5017;
RA Zhu X., Mancini M.A., Chang K.-H., Liu C.-Y., Chen C.-F., Shan B.,
RA Jones D., Yang-Feng T.L., Lee W.-H.;
RT "Characterization of a novel 350-kilodalton nuclear phosphoprotein that is
RT specifically involved in mitotic-phase progression.";
RL Mol. Cell. Biol. 15:5017-5029(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2098-3114, SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, AND VARIANT LYS-3106.
RX PubMed=7612011; DOI=10.1006/bbrc.1995.1959;
RA Li Q., Ke Y., Kapp J.A., Fertig N., Medsger T.A. Jr., Joshi H.C.;
RT "A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain
RT sufficient for nuclear localization.";
RL Biochem. Biophys. Res. Commun. 212:220-228(1995).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=7642639; DOI=10.1074/jbc.270.33.19545;
RA Zhu X., Chang K.-H., He D., Mancini M.A., Brinkley W.R., Lee W.-H.;
RT "The C-terminus of mitosin is essential for its nuclear localization,
RT centromere/kinetochore targeting, and dimerization.";
RL J. Biol. Chem. 270:19545-19550(1995).
RN [7]
RP INTERACTION WITH BUBR1 AND CENPE, AND SUBCELLULAR LOCATION.
RX PubMed=9763420; DOI=10.1083/jcb.143.1.49;
RA Chan G.K.T., Schaar B.T., Yen T.J.;
RT "Characterization of the kinetochore binding domain of CENP-E reveals
RT interactions with the kinetochore proteins CENP-F and hBUBR1.";
RL J. Cell Biol. 143:49-63(1998).
RN [8]
RP ISOPRENYLATION AT CYS-3111.
RX PubMed=10852915; DOI=10.1074/jbc.m003469200;
RA Ashar H.R., James L., Gray K., Carr D., Black S., Armstrong L.,
RA Bishop W.R., Kirschmeier P.;
RT "Farnesyl transferase inhibitors block the farnesylation of CENP-E and
RT CENP-F and alter the association of CENP-E with the microtubules.";
RL J. Biol. Chem. 275:30451-30457(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12974617; DOI=10.1038/sj.cr.7290172;
RA Yang Z.Y., Guo J., Li N., Qian M., Wang S.N., Zhu X.L.;
RT "Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic
RT dynein-mediated poleward transport.";
RL Cell Res. 13:275-283(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651 AND SER-1654, AND
RP IDENTIFICATION BY 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 [12]
RP FUNCTION, INTERACTION WITH NDEL1 AND NDE1, AND SUBCELLULAR LOCATION.
RX PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
RA Vergnolle M.A.S., Taylor S.S.;
RT "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
RT complexes.";
RL Curr. Biol. 17:1173-1179(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3023, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3054, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-144; SER-834;
RP SER-1248; SER-1651; SER-1652; SER-1654; SER-2416; SER-2417; SER-2900;
RP SER-2911; SER-3023; SER-3026; SER-3054; SER-3079 AND SER-3083, AND
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2900 AND SER-2911, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2779, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-151; THR-154; TYR-158;
RP SER-276; SER-773; SER-783; SER-821; SER-876; SER-1248; SER-1255; SER-1259;
RP SER-1651; SER-1654; SER-1892; SER-2417; SER-2900; SER-2911; SER-2922;
RP THR-2949; SER-2952; SER-2998; SER-3023; SER-3026; SER-3054; SER-3079 AND
RP SER-3083, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3023 AND SER-3054, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-154; SER-242;
RP SER-276; SER-821; SER-838; SER-876; SER-1255; SER-1651; SER-1654; SER-1726;
RP THR-1862; SER-1868; SER-2936; THR-2949; SER-2998; SER-3023; SER-3054 AND
RP SER-3079, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [24]
RP INVOLVEMENT IN STROMS.
RX PubMed=25564561; DOI=10.1136/jmedgenet-2014-102691;
RA Waters A.M., Asfahani R., Carroll P., Bicknell L., Lescai F., Bright A.,
RA Chanudet E., Brooks A., Christou-Savina S., Osman G., Walsh P.,
RA Bacchelli C., Chapgier A., Vernay B., Bader D.M., Deshpande C.,
RA O'Sullivan M., Ocaka L., Stanescu H., Stewart H.S., Hildebrandt F.,
RA Otto E., Johnson C.A., Szymanska K., Katsanis N., Davis E., Kleta R.,
RA Hubank M., Doxsey S., Jackson A., Stupka E., Winey M., Beales P.L.;
RT "The kinetochore protein, CENPF, is mutated in human ciliopathy and
RT microcephaly phenotypes.";
RL J. Med. Genet. 52:147-156(2015).
RN [25]
RP INVOLVEMENT IN STROMS.
RX PubMed=26820108; DOI=10.1002/humu.22960;
RA Filges I., Bruder E., Brandal K., Meier S., Undlien D.E., Waage T.R.,
RA Hoesli I., Schubach M., de Beer T., Sheng Y., Hoeller S., Schulzke S.,
RA Roesby O., Miny P., Tercanli S., Oppedal T., Meyer P., Selmer K.K.,
RA Stroemme P.;
RT "Stroemme Syndrome Is a Ciliary Disorder Caused by Mutations in CENPF.";
RL Hum. Mutat. 37:359-363(2016).
CC -!- FUNCTION: Required for kinetochore function and chromosome segregation
CC in mitosis. Required for kinetochore localization of dynein, LIS1, NDE1
CC and NDEL1. Regulates recycling of the plasma membrane by acting as a
CC link between recycling vesicles and the microtubule network though its
CC association with STX4 and SNAP25. Acts as a potential inhibitor of
CC pocket protein-mediated cellular processes during development by
CC regulating the activity of RB proteins during cell division and
CC proliferation. May play a regulatory or permissive role in the normal
CC embryonic cardiomyocyte cell cycle and in promoting continued mitosis
CC in transformed, abnormally dividing neonatal cardiomyocytes.
CC Interaction with RB directs embryonic stem cells toward a cardiac
CC lineage. Involved in the regulation of DNA synthesis and hence cell
CC cycle progression, via its C-terminus. Has a potential role regulating
CC skeletal myogenesis and in cell differentiation in embryogenesis.
CC Involved in dendritic cell regulation of T-cell immunity against
CC chlamydia. {ECO:0000269|PubMed:12974617, ECO:0000269|PubMed:17600710,
CC ECO:0000269|PubMed:7542657, ECO:0000269|PubMed:7651420}.
CC -!- SUBUNIT: Interacts with and STX4 (via C-terminus) (By similarity).
CC Interacts (via N-terminus) with RBL1, RBL2 and SNAP25 (By similarity).
CC Self-associates. Interacts with CENP-E and BUBR1 (via C-terminus).
CC Interacts (via C-terminus) with NDE1, NDEL1 and RB1. {ECO:0000250,
CC ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:7642639,
CC ECO:0000269|PubMed:7651420, ECO:0000269|PubMed:9763420}.
CC -!- INTERACTION:
CC P49454; Q9GZM8: NDEL1; NbExp=6; IntAct=EBI-968343, EBI-928842;
CC P49454; Q8WUM0: NUP133; NbExp=2; IntAct=EBI-968343, EBI-295695;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus matrix.
CC Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle.
CC Note=Relocalizes to the kinetochore/centromere (coronal surface of the
CC outer plate) and the spindle during mitosis. Observed in nucleus during
CC interphase but not in the nucleolus. At metaphase becomes localized to
CC areas including kinetochore and mitotic apparatus as well as cytoplasm.
CC By telophase, is concentrated within the intracellular bridge at either
CC side of the mid-body.
CC -!- DEVELOPMENTAL STAGE: Gradually accumulates during the cell cycle,
CC reaching peak levels in G2 and M phase, and is rapidly degraded upon
CC completion of mitosis. {ECO:0000269|PubMed:7542657}.
CC -!- PTM: Hyperphosphorylated during mitosis.
CC -!- DISEASE: Stromme syndrome (STROMS) [MIM:243605]: An autosomal recessive
CC congenital disorder characterized by intestinal atresia, ocular
CC anomalies, microcephaly, and renal and cardiac abnormalities in some
CC patients. The disease has features of a ciliopathy, and lethality in
CC early childhood is observed in severe cases.
CC {ECO:0000269|PubMed:25564561, ECO:0000269|PubMed:26820108}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the centromere protein F family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA82889.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CENPFID40057ch1q41.html";
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DR EMBL; U19769; AAA82889.1; ALT_SEQ; mRNA.
DR EMBL; U30872; AAA82935.1; -; mRNA.
DR EMBL; AL445666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC172232; AAI72232.1; -; mRNA.
DR EMBL; U25725; AAA86889.1; -; mRNA.
DR CCDS; CCDS31023.1; -.
DR PIR; PC4035; PC4035.
DR RefSeq; NP_057427.3; NM_016343.3.
DR RefSeq; XP_016855575.1; XM_017000086.1.
DR SMR; P49454; -.
DR BioGRID; 107492; 97.
DR IntAct; P49454; 52.
DR MINT; P49454; -.
DR STRING; 9606.ENSP00000355922; -.
DR CarbonylDB; P49454; -.
DR GlyGen; P49454; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P49454; -.
DR MetOSite; P49454; -.
DR PhosphoSitePlus; P49454; -.
DR BioMuta; CENPF; -.
DR DMDM; 156630875; -.
DR EPD; P49454; -.
DR jPOST; P49454; -.
DR MassIVE; P49454; -.
DR MaxQB; P49454; -.
DR PaxDb; P49454; -.
DR PeptideAtlas; P49454; -.
DR PRIDE; P49454; -.
DR ProteomicsDB; 56015; -.
DR Antibodypedia; 4038; 281 antibodies from 34 providers.
DR DNASU; 1063; -.
DR Ensembl; ENST00000366955.8; ENSP00000355922.3; ENSG00000117724.14.
DR GeneID; 1063; -.
DR KEGG; hsa:1063; -.
DR MANE-Select; ENST00000366955.8; ENSP00000355922.3; NM_016343.4; NP_057427.3.
DR UCSC; uc001hkm.4; human.
DR CTD; 1063; -.
DR DisGeNET; 1063; -.
DR GeneCards; CENPF; -.
DR HGNC; HGNC:1857; CENPF.
DR HPA; ENSG00000117724; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; CENPF; -.
DR MIM; 243605; phenotype.
DR MIM; 600236; gene.
DR neXtProt; NX_P49454; -.
DR OpenTargets; ENSG00000117724; -.
DR Orphanet; 444069; Lethal fetal brain malformation-duodenal atresia-bilateral renal hypoplasia syndrome.
DR Orphanet; 506307; Stromme syndrome.
DR PharmGKB; PA26401; -.
DR VEuPathDB; HostDB:ENSG00000117724; -.
DR eggNOG; ENOG502QVMD; Eukaryota.
DR GeneTree; ENSGT00730000111187; -.
DR HOGENOM; CLU_000551_0_0_1; -.
DR InParanoid; P49454; -.
DR OMA; EQPNEQH; -.
DR OrthoDB; 205405at2759; -.
DR PhylomeDB; P49454; -.
DR TreeFam; TF101133; -.
DR PathwayCommons; P49454; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P49454; -.
DR SIGNOR; P49454; -.
DR BioGRID-ORCS; 1063; 67 hits in 1105 CRISPR screens.
DR ChiTaRS; CENPF; human.
DR GeneWiki; CENPF; -.
DR GenomeRNAi; 1063; -.
DR Pharos; P49454; Tbio.
DR PRO; PR:P49454; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P49454; protein.
DR Bgee; ENSG00000117724; Expressed in ventricular zone and 137 other tissues.
DR ExpressionAtlas; P49454; baseline and differential.
DR Genevisible; P49454; HS.
DR GO; GO:0005930; C:axoneme; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0097539; C:ciliary transition fiber; IMP:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045120; C:pronucleus; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0001822; P:kidney development; IMP:GO_Central.
DR GO; GO:0051382; P:kinetochore assembly; NAS:UniProtKB.
DR GO; GO:0051310; P:metaphase plate congression; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; NAS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; NAS:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IMP:GO_Central.
DR InterPro; IPR043513; Cenp-F.
DR InterPro; IPR018302; CenpF/LEK1_Rb-prot-bd.
DR InterPro; IPR019513; Centromere_CenpF_leu-rich_rpt.
DR InterPro; IPR018463; Centromere_CenpF_N.
DR PANTHER; PTHR18874; PTHR18874; 2.
DR Pfam; PF10490; CENP-F_C_Rb_bdg; 1.
DR Pfam; PF10473; CENP-F_leu_zip; 3.
DR Pfam; PF10481; CENP-F_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Ciliopathy;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; DNA synthesis; Kinetochore; Lipoprotein; Methylation;
KW Mitosis; Myogenesis; Nucleus; Phosphoprotein; Prenylation;
KW Primary ciliary dyskinesia; Reference proteome; Repeat.
FT CHAIN 1..3111
FT /note="Centromere protein F"
FT /id="PRO_0000089477"
FT PROPEP 3112..3114
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396744"
FT REPEAT 2111..2290
FT /note="1"
FT REPEAT 2293..2472
FT /note="2"
FT REGION 1..481
FT /note="Interaction with SNAP25 and required for
FT localization to the cytoplasm"
FT /evidence="ECO:0000250"
FT REGION 211..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2351
FT /note="Interaction with NDE1 and NDEL1"
FT /evidence="ECO:0000269|PubMed:17600710"
FT REGION 2111..2472
FT /note="2 X 177 AA tandem repeats"
FT REGION 2392..3017
FT /note="Sufficient for centromere localization"
FT REGION 2392..2829
FT /note="Sufficient for self-association"
FT REGION 2831..3017
FT /note="Sufficient for nuclear localization"
FT REGION 2891..2977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3024..3114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..131
FT /evidence="ECO:0000255"
FT COILED 280..685
FT /evidence="ECO:0000255"
FT COILED 899..989
FT /evidence="ECO:0000255"
FT COILED 1196..1244
FT /evidence="ECO:0000255"
FT COILED 1549..1646
FT /evidence="ECO:0000255"
FT COILED 1890..2078
FT /evidence="ECO:0000255"
FT COILED 2107..2891
FT /evidence="ECO:0000255"
FT MOTIF 2919..2936
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1722..1746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2916..2953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2962..2977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3029..3080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1862
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2779
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 2911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 2922
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2949
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 3026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 3054
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 3079
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 3083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 3111
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 3111
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:10852915"
FT VARIANT 250
FT /note="Q -> L (in dbSNP:rs1050065)"
FT /evidence="ECO:0000269|PubMed:7542657"
FT /id="VAR_055049"
FT VARIANT 272
FT /note="D -> G (in dbSNP:rs1050066)"
FT /evidence="ECO:0000269|PubMed:7542657"
FT /id="VAR_055050"
FT VARIANT 300
FT /note="R -> C (in dbSNP:rs17023281)"
FT /id="VAR_034712"
FT VARIANT 494
FT /note="H -> Q (in dbSNP:rs2070065)"
FT /id="VAR_034713"
FT VARIANT 701
FT /note="M -> V (in dbSNP:rs3795524)"
FT /id="VAR_034714"
FT VARIANT 754
FT /note="Q -> E (in dbSNP:rs3795523)"
FT /id="VAR_034715"
FT VARIANT 815
FT /note="R -> H (in dbSNP:rs3795522)"
FT /id="VAR_034716"
FT VARIANT 1018
FT /note="Y -> D (in dbSNP:rs3795519)"
FT /id="VAR_034717"
FT VARIANT 1033
FT /note="G -> R (in dbSNP:rs3795518)"
FT /id="VAR_034718"
FT VARIANT 1105
FT /note="T -> I (in dbSNP:rs12067133)"
FT /id="VAR_034719"
FT VARIANT 1412
FT /note="L -> S (in dbSNP:rs3795517)"
FT /id="VAR_034720"
FT VARIANT 1768
FT /note="D -> N (in dbSNP:rs3748692)"
FT /id="VAR_055638"
FT VARIANT 1915
FT /note="E -> A (in dbSNP:rs3790647)"
FT /id="VAR_034723"
FT VARIANT 3106
FT /note="N -> K (in dbSNP:rs7289)"
FT /evidence="ECO:0000269|PubMed:7542657,
FT ECO:0000269|PubMed:7612011, ECO:0000269|PubMed:7651420"
FT /id="VAR_014839"
FT CONFLICT 16
FT /note="A -> T (in Ref. 1; AAA82889)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="L -> P (in Ref. 1; AAA82889 and 2; AAA82935)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="K -> T (in Ref. 1; AAA82889 and 2; AAA82935)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="Missing (in Ref. 2; AAA82935)"
FT /evidence="ECO:0000305"
FT CONFLICT 1515
FT /note="A -> V (in Ref. 1; AAA82889)"
FT /evidence="ECO:0000305"
FT CONFLICT 1715
FT /note="V -> L (in Ref. 2; AAA82935)"
FT /evidence="ECO:0000305"
FT CONFLICT 2146..2147
FT /note="ER -> DG (in Ref. 5; AAA86889)"
FT /evidence="ECO:0000305"
FT CONFLICT 2239
FT /note="L -> Q (in Ref. 5; AAA86889)"
FT /evidence="ECO:0000305"
FT CONFLICT 2396
FT /note="N -> D (in Ref. 1; AAA82889 and 5; AAA86889)"
FT /evidence="ECO:0000305"
FT CONFLICT 2449..2465
FT /note="ELNERVAALHNDQEACK -> SSMREWQPCIMTKKPVS (in Ref. 5;
FT AAA86889)"
FT /evidence="ECO:0000305"
FT CONFLICT 2943
FT /note="R -> G (in Ref. 1; AAA82889, 2; AAA82935 and 5;
FT AAA86889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3114 AA; 357527 MW; 1FC81972F947B375 CRC64;
MSWALEEWKE GLPTRALQKI QELEGQLDKL KKEKQQRQFQ LDSLEAALQK QKQKVENEKT
EGTNLKRENQ RLMEICESLE KTKQKISHEL QVKESQVNFQ EGQLNSGKKQ IEKLEQELKR
CKSELERSQQ AAQSADVSLN PCNTPQKIFT TPLTPSQYYS GSKYEDLKEK YNKEVEERKR
LEAEVKALQA KKASQTLPQA TMNHRDIARH QASSSVFSWQ QEKTPSHLSS NSQRTPIRRD
FSASYFSGEQ EVTPSRSTLQ IGKRDANSSF FDNSSSPHLL DQLKAQNQEL RNKINELELR
LQGHEKEMKG QVNKFQELQL QLEKAKVELI EKEKVLNKCR DELVRTTAQY DQASTKYTAL
EQKLKKLTED LSCQRQNAES ARCSLEQKIK EKEKEFQEEL SRQQRSFQTL DQECIQMKAR
LTQELQQAKN MHNVLQAELD KLTSVKQQLE NNLEEFKQKL CRAEQAFQAS QIKENELRRS
MEEMKKENNL LKSHSEQKAR EVCHLEAELK NIKQCLNQSQ NFAEEMKAKN TSQETMLRDL
QEKINQQENS LTLEKLKLAV ADLEKQRDCS QDLLKKREHH IEQLNDKLSK TEKESKALLS
ALELKKKEYE ELKEEKTLFS CWKSENEKLL TQMESEKENL QSKINHLETC LKTQQIKSHE
YNERVRTLEM DRENLSVEIR NLHNVLDSKS VEVETQKLAY MELQQKAEFS DQKHQKEIEN
MCLKTSQLTG QVEDLEHKLQ LLSNEIMDKD RCYQDLHAEY ESLRDLLKSK DASLVTNEDH
QRSLLAFDQQ PAMHHSFANI IGEQGSMPSE RSECRLEADQ SPKNSAILQN RVDSLEFSLE
SQKQMNSDLQ KQCEELVQIK GEIEENLMKA EQMHQSFVAE TSQRISKLQE DTSAHQNVVA
ETLSALENKE KELQLLNDKV ETEQAEIQEL KKSNHLLEDS LKELQLLSET LSLEKKEMSS
IISLNKREIE ELTQENGTLK EINASLNQEK MNLIQKSESF ANYIDEREKS ISELSDQYKQ
EKLILLQRCE ETGNAYEDLS QKYKAAQEKN SKLECLLNEC TSLCENRKNE LEQLKEAFAK
EHQEFLTKLA FAEERNQNLM LELETVQQAL RSEMTDNQNN SKSEAGGLKQ EIMTLKEEQN
KMQKEVNDLL QENEQLMKVM KTKHECQNLE SEPIRNSVKE RESERNQCNF KPQMDLEVKE
ISLDSYNAQL VQLEAMLRNK ELKLQESEKE KECLQHELQT IRGDLETSNL QDMQSQEISG
LKDCEIDAEE KYISGPHELS TSQNDNAHLQ CSLQTTMNKL NELEKICEIL QAEKYELVTE
LNDSRSECIT ATRKMAEEVG KLLNEVKILN DDSGLLHGEL VEDIPGGEFG EQPNEQHPVS
LAPLDESNSY EHLTLSDKEV QMHFAELQEK FLSLQSEHKI LHDQHCQMSS KMSELQTYVD
SLKAENLVLS TNLRNFQGDL VKEMQLGLEE GLVPSLSSSC VPDSSSLSSL GDSSFYRALL
EQTGDMSLLS NLEGAVSANQ CSVDEVFCSS LQEENLTRKE TPSAPAKGVE ELESLCEVYR
QSLEKLEEKM ESQGIMKNKE IQELEQLLSS ERQELDCLRK QYLSENEQWQ QKLTSVTLEM
ESKLAAEKKQ TEQLSLELEV ARLQLQGLDL SSRSLLGIDT EDAIQGRNES CDISKEHTSE
TTERTPKHDV HQICDKDAQQ DLNLDIEKIT ETGAVKPTGE CSGEQSPDTN YEPPGEDKTQ
GSSECISELS FSGPNALVPM DFLGNQEDIH NLQLRVKETS NENLRLLHVI EDRDRKVESL
LNEMKELDSK LHLQEVQLMT KIEACIELEK IVGELKKENS DLSEKLEYFS CDHQELLQRV
ETSEGLNSDL EMHADKSSRE DIGDNVAKVN DSWKERFLDV ENELSRIRSE KASIEHEALY
LEADLEVVQT EKLCLEKDNE NKQKVIVCLE EELSVVTSER NQLRGELDTM SKKTTALDQL
SEKMKEKTQE LESHQSECLH CIQVAEAEVK EKTELLQTLS SDVSELLKDK THLQEKLQSL
EKDSQALSLT KCELENQIAQ LNKEKELLVK ESESLQARLS ESDYEKLNVS KALEAALVEK
GEFALRLSST QEEVHQLRRG IEKLRVRIEA DEKKQLHIAE KLKEREREND SLKDKVENLE
RELQMSEENQ ELVILDAENS KAEVETLKTQ IEEMARSLKV FELDLVTLRS EKENLTKQIQ
EKQGQLSELD KLLSSFKSLL EEKEQAEIQI KEESKTAVEM LQNQLKELNE AVAALCGDQE
IMKATEQSLD PPIEEEHQLR NSIEKLRARL EADEKKQLCV LQQLKESEHH ADLLKGRVEN
LERELEIART NQEHAALEAE NSKGEVETLK AKIEGMTQSL RGLELDVVTI RSEKENLTNE
LQKEQERISE LEIINSSFEN ILQEKEQEKV QMKEKSSTAM EMLQTQLKEL NERVAALHND
QEACKAKEQN LSSQVECLEL EKAQLLQGLD EAKNNYIVLQ SSVNGLIQEV EDGKQKLEKK
DEEISRLKNQ IQDQEQLVSK LSQVEGEHQL WKEQNLELRN LTVELEQKIQ VLQSKNASLQ
DTLEVLQSSY KNLENELELT KMDKMSFVEK VNKMTAKETE LQREMHEMAQ KTAELQEELS
GEKNRLAGEL QLLLEEIKSS KDQLKELTLE NSELKKSLDC MHKDQVEKEG KVREEIAEYQ
LRLHEAEKKH QALLLDTNKQ YEVEIQTYRE KLTSKEECLS SQKLEIDLLK SSKEELNNSL
KATTQILEEL KKTKMDNLKY VNQLKKENER AQGKMKLLIK SCKQLEEEKE ILQKELSQLQ
AAQEKQKTGT VMDTKVDELT TEIKELKETL EEKTKEADEY LDKYCSLLIS HEKLEKAKEM
LETQVAHLCS QQSKQDSRGS PLLGPVVPGP SPIPSVTEKR LSSGQNKASG KRQRSSGIWE
NGRGPTPATP ESFSKKSKKA VMSGIHPAED TEGTEFEPEG LPEVVKKGFA DIPTGKTSPY
ILRRTTMATR TSPRLAAQKL ALSPLSLGKE NLAESSKPTA GGSRSQKVKV AQRSPVDSGT
ILREPTTKSV PVNNLPERSP TDSPREGLRV KRGRLVPSPK AGLESNGSEN CKVQ
